|
Name |
Accession |
Description |
Interval |
E-value |
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-241 |
3.77e-103 |
|
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: 299.03 E-value: 3.77e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGVKRqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR--L 78
Cdd:COG1124 1 MLEVRNLSVSYGQGGRR--VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKafR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 79 GKMSVVFQDYKSSLHPYFNVRQILNEALSQCDtpVDDKEAHMTALLERVGLSAAFLNKYPQMMSGGEAQRVAIARAVITN 158
Cdd:COG1124 79 RRVQMVFQDPYASLHPRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 159 PDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQL-KTLQNDYTR 237
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLlAGPKHPYTR 236
|
....
gi 1717358098 238 ELFE 241
Cdd:COG1124 237 ELLA 240
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-241 |
1.06e-88 |
|
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: 271.39 E-value: 1.06e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGvKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC-----QRH 75
Cdd:COG1123 260 LLEVRNLSKRYPVR-GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrrSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRLGKMSVVFQDYKSSLHPYFNVRQILNEALSQC-DTPVDDKEAHMTALLERVGLSAAFLNKYPQMMSGGEAQRVAIARA 154
Cdd:COG1123 339 ELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHgLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 155 VITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQ-LKTLQN 233
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEvFANPQH 498
|
....*...
gi 1717358098 234 DYTRELFE 241
Cdd:COG1123 499 PYTRALLA 506
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-222 |
2.57e-86 |
|
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: 255.89 E-value: 2.57e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPV-----CQRH 75
Cdd:cd03257 1 LLEVKNLSVSFP--TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsrRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRLGKMSVVFQDYKSSLHPYFNVRQILNEALS--QCDTPVDDKEAHMTALLERVGLSAAFLNKYPQMMSGGEAQRVAIAR 153
Cdd:cd03257 79 IRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRihGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717358098 154 AVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQER 222
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-200 |
8.07e-75 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 230.00 E-value: 8.07e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSY--RSGVKRQKRQIVK---QVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqrhT 76
Cdd:COG4608 8 LEVRDLKKHFpvRGGLFGRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI----T 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 77 RLG---------KMSVVFQDYKSSLHPYFNVRQILNEALS-QCDTPVDDKEAHMTALLERVGLSAAFLNKYPQMMSGGEA 146
Cdd:COG4608 84 GLSgrelrplrrRMQMVFQDPYASLNPRMTVGDIIAEPLRiHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1717358098 147 QRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHD 200
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-241 |
1.88e-73 |
|
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: 226.09 E-value: 1.88e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKP---DTGTVMLDGQPVCQ---- 73
Cdd:COG0444 1 LLEVRNLKVYFP--TRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsek 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 74 --RHTRLGKMSVVFQDYKSSLHPYFNVRQILNEALSQCdTPVDDKEAH--MTALLERVGLSAA--FLNKYPQMMSGGEAQ 147
Cdd:COG0444 79 elRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIH-GGLSKAEARerAIELLERVGLPDPerRLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 148 RVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQ 227
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237
|
250
....*....|....*
gi 1717358098 228 L-KTLQNDYTRELFE 241
Cdd:COG0444 238 LfENPRHPYTRALLS 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-241 |
1.55e-72 |
|
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: 230.34 E-value: 1.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSY--RSGV-KRQKRQI--VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEkPDTGTVMLDGQPVCQ--- 73
Cdd:COG4172 276 LEARDLKVWFpiKRGLfRRTVGHVkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGlsr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 74 ---RHTRLgKMSVVFQDYKSSLHPYFNVRQILNEALSQCDTPVDDKE--AHMTALLERVGLSAAFLNKYPQMMSGGEAQR 148
Cdd:COG4172 355 ralRPLRR-RMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAErrARVAEALEEVGLDPAARHRYPHEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 149 VAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQ- 227
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQv 513
|
250
....*....|....
gi 1717358098 228 LKTLQNDYTRELFE 241
Cdd:COG4172 514 FDAPQHPYTRALLA 527
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-245 |
3.16e-69 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 213.55 E-value: 3.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGV---KRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC----QR 74
Cdd:COG4167 5 LEVRNLSKTFKYRTglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygdyKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 75 HTRLGKMsvVFQDYKSSLHPYFNVRQILNEALSqCDTPVDDKEAH--MTALLERVGLSAAFLNKYPQMMSGGEAQRVAIA 152
Cdd:COG4167 85 RCKHIRM--IFQDPNTSLNPRLNIGQILEEPLR-LNTDLTAEEREerIFATLRLVGLLPEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 153 RAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQ-LKTL 231
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEvFANP 241
|
250
....*....|....
gi 1717358098 232 QNDYTRELFEKQFM 245
Cdd:COG4167 242 QHEVTKRLIESHFG 255
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-241 |
1.48e-62 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 196.56 E-value: 1.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGV---KRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR 77
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGlfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 LGK-----MSVVFQDYKSSLHPYFNVRQILNEALSQ-CDTPVDDKEAHMTALLERVGLSAAFLNKYPQMMSGGEAQRVAI 151
Cdd:TIGR02769 82 QRRafrrdVQLVFQDSPSAVNPRMTVRQIIGEPLRHlTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 152 ARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQLKTL 231
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF 241
|
250
....*....|
gi 1717358098 232 QNDYTRELFE 241
Cdd:TIGR02769 242 KHPAGRNLQS 251
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-223 |
2.10e-62 |
|
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: 194.61 E-value: 2.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGkm 81
Cdd:cd03293 1 LEVRNVSKTYGGG--GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 sVVFQDYksSLHPYFNVRQilNEALSQCDTPVDDKEA--HMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVITNP 159
Cdd:cd03293 77 -YVFQQD--ALLPWLTVLD--NVALGLELQGVPKAEAreRAEELLELVGLSG-FENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717358098 160 DYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFN--DGQIQERL 223
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSarPGRIVAEV 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-224 |
1.26e-61 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 194.15 E-value: 1.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGk 80
Cdd:COG1116 7 ALELRGVSKRFPTG--GGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 msVVFQDYksSLHPYFNVRQ--ILneALSQCDTPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVITN 158
Cdd:COG1116 84 --VVFQEP--ALLPWLTVLDnvAL--GLELRGVPKAERRERARELLELVGL-AGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 159 PDYIVLDEAISALD----MSIQSQILDLLTTLRdkyqLSLIFITHDIQAAVYLCEDLIIF--NDGQIQERLN 224
Cdd:COG1116 157 PEVLLMDEPFGALDaltrERLQDELLRLWQETG----KTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEEID 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-221 |
6.93e-61 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 191.02 E-value: 6.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ------- 73
Cdd:COG1136 4 LLELRNLTKSYGTG--EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 74 --RHTRLGkmsVVFQDYKssLHPYFNVRQilNEALSQ--CDTPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRV 149
Cdd:COG1136 82 rlRRRHIG---FVFQFFN--LLPELTALE--NVALPLllAGVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 150 AIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYlCEDLIIFNDGQIQE 221
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-221 |
2.39e-59 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 188.74 E-value: 2.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSG---VKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR 77
Cdd:PRK10419 3 LLNVSGLSHHYAHGglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 LGK-----MSVVFQDYKSSLHPYFNVRQILNEALSQCdTPVD--DKEAHMTALLERVGLSAAFLNKYPQMMSGGEAQRVA 150
Cdd:PRK10419 83 QRKafrrdIQMVFQDSISAVNPRKTVREIIREPLRHL-LSLDkaERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717358098 151 IARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-219 |
3.93e-59 |
|
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: 186.16 E-value: 3.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKRQkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPV-CQRHTRLG- 79
Cdd:cd03255 1 IELKNLSKTYGGGGEKV--QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsKLSEKELAa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 ----KMSVVFQDYKssLHPYFNVRQilNEALSQCDTPVDDKEAHMTA--LLERVGLsAAFLNKYPQMMSGGEAQRVAIAR 153
Cdd:cd03255 79 frrrHIGFVFQSFN--LLPDLTALE--NVELPLLLAGVPKKERRERAeeLLERVGL-GDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717358098 154 AVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYlCEDLIIFNDGQI 219
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-201 |
2.31e-57 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 185.17 E-value: 2.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSY--RSGVKRQKRQI--VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ---- 73
Cdd:PRK11308 6 LQAIDLKKHYpvKRGLFKPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 74 -RHTRLGKMSVVFQDYKSSLHPYFNVRQILNEALsQCDTPVDDKE--AHMTALLERVGLSAAFLNKYPQMMSGGEAQRVA 150
Cdd:PRK11308 86 aQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPL-LINTSLSAAErrEKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1717358098 151 IARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDI 201
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-221 |
8.35e-55 |
|
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: 175.02 E-value: 8.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVkrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGKM 81
Cdd:cd03259 1 LELKGLSKTYGSVR------ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 SVVFQDYksSLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVITNPDY 161
Cdd:cd03259 75 GMVFQDY--ALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEG-LLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 162 IVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-228 |
5.06e-54 |
|
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: 181.25 E-value: 5.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGVKRqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPD---TGTVMLDGQPVCQ--RH 75
Cdd:COG1123 4 LLEVRDLSVRYPGGDVP----AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLElsEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRLGKMSVVFQDYKSSLHPYFNVRQILnEALSQCDTPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIARAV 155
Cdd:COG1123 80 LRGRRIGMVFQDPMTQLNPVTVGDQIA-EALENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 156 ITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQL 228
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-220 |
7.86e-53 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 174.13 E-value: 7.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC-----QRH 75
Cdd:COG3842 5 ALELENVSKRY------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglppeKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 trlgkMSVVFQDYksSLHPYFNVRQilNEA--LSQCDTPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIAR 153
Cdd:COG3842 79 -----VGMVFQDY--ALFPHLTVAE--NVAfgLRMRGVPKAEIRARVAELLELVGL-EGLADRYPHQLSGGQQQRVALAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 154 AVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQ 220
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-244 |
1.26e-52 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 171.51 E-value: 1.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKS--YRSGV-KRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC--QRH 75
Cdd:PRK15112 4 LLEVRNLSKTfrYRTGWfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRLGKMSVVFQDYKSSLHPYFNVRQILNEALS-QCDTPVDDKEAHMTALLERVGLSAAFLNKYPQMMSGGEAQRVAIARA 154
Cdd:PRK15112 84 YRSQRIRMIFQDPSTSLNPRQRISQILDFPLRlNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 155 VITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQ-LKTLQN 233
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADvLASPLH 243
|
250
....*....|.
gi 1717358098 234 DYTRELFEKQF 244
Cdd:PRK15112 244 ELTKRLIAGHF 254
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-239 |
1.42e-52 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 177.98 E-value: 1.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSY--RSGVKRQK---RQIVKQVSFQCSKGQSIAIIGESGSGKST----LARMIlgiekPDTGTVMLDGQPV 71
Cdd:PRK15134 275 LLDVEQLQVAFpiRKGILKRTvdhNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 72 CQRHTRL-----GKMSVVFQDYKSSLHPYFNVRQILNEALS--QCDTPVDDKEAHMTALLERVGLSAAFLNKYPQMMSGG 144
Cdd:PRK15134 350 HNLNRRQllpvrHRIQVVFQDPNSSLNPRLNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 145 EAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLN 224
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
250
....*....|....*.
gi 1717358098 225 -RHQLKTLQNDYTREL 239
Cdd:PRK15134 510 cERVFAAPQQEYTRQL 525
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-240 |
1.71e-50 |
|
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: 164.77 E-value: 1.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC-----QRH 75
Cdd:COG1127 5 MIEVRNLTKSFGD------RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglsekELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRLGKMSVVFQD---YkSSLHPYFNVRQILNEAlsqcdTPVDDKEAHMTAL--LERVGLSAAfLNKYPQMMSGGEAQRVA 150
Cdd:COG1127 79 ELRRRIGMLFQGgalF-DSLTVFENVAFPLREH-----TDLSEAEIRELVLekLELVGLPGA-ADKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 151 IARAVITNPDYIVLDEAISALD--MSIqsQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQL 228
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDpiTSA--VIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
250
....*....|..
gi 1717358098 229 KTLQNDYTRELF 240
Cdd:COG1127 230 LASDDPWVRQFL 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-219 |
2.29e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.47 E-value: 2.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRsgvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR-LGK 80
Cdd:COG1131 1 IEVRGLTKRYG------DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSVVFQDykSSLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVITNPD 160
Cdd:COG1131 75 IGYVPQE--PALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717358098 161 YIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-221 |
3.83e-49 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 164.55 E-value: 3.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC-QRHTRLGK 80
Cdd:COG1118 3 IEVRNISKRFGS------FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSVVFQDYksSLHPYFNVRQilNEA--LSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVITN 158
Cdd:COG1118 77 VGFVFQHY--ALFPHMTVAE--NIAfgLRVRPPSKAEIRARVEELLELVQLEG-LADRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 159 PDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQ 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-219 |
6.30e-49 |
|
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: 161.36 E-value: 6.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRsgvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR-LG 79
Cdd:COG1120 1 MLEAENLSVGYG------GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRReLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 K-MSVVFQDykSSLHPYFNVRQIL-------NEALSQcDTPVDDKEAHmtALLERVGLsAAFLNKYPQMMSGGEAQRVAI 151
Cdd:COG1120 75 RrIAYVPQE--PPAPFGLTVRELValgryphLGLFGR-PSAEDREAVE--EALERTGL-EHLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 152 ARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-219 |
9.90e-49 |
|
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: 160.19 E-value: 9.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR--LG 79
Cdd:COG1122 1 IELENLSFSYPGG-----TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRelRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQDYKSslhpyfnvrQILNE--------ALSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAI 151
Cdd:COG1122 76 KVGLVFQNPDD---------QLFAPtveedvafGPENLGLPREEIRERVEEALELVGLEH-LADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 152 ARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-238 |
1.45e-48 |
|
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: 159.97 E-value: 1.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC------QRH 75
Cdd:cd03261 1 IELRGLTKSFGG------RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseaeLYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRLgKMSVVFQDYK--SSLHPYFNVRQILNEALSQCDTPVDDKeAHMTalLERVGLSAAfLNKYPQMMSGGEAQRVAIAR 153
Cdd:cd03261 75 LRR-RMGMLFQSGAlfDSLTVFENVAFPLREHTRLSEEEIREI-VLEK--LEAVGLRGA-EDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 154 AVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQLKTLQN 233
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
|
....*
gi 1717358098 234 DYTRE 238
Cdd:cd03261 230 PLVRQ 234
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-221 |
1.71e-47 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 160.24 E-value: 1.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSgvKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ------R 74
Cdd:COG1135 1 MIELENLSKTFPT--KGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserelR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 75 HTRLgKMSVVFQdyksslHpyFN------VRQilNEA--LSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEA 146
Cdd:COG1135 79 AARR-KIGMIFQ------H--FNllssrtVAE--NVAlpLEIAGVPKAEIRKRVAELLELVGLSD-KADAYPSQLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717358098 147 QRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVE 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-220 |
6.90e-47 |
|
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: 154.76 E-value: 6.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 25 QVSFQCSkGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQ-----------PVCQRhtrlgKMSVVFQDYksSLH 93
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlPPQQR-----KIGLVFQQY--ALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 94 PYFNVRQILNEALSQCDTPVD-DKEAHMTALLERVGLsaafLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALD 172
Cdd:cd03297 88 PHLNVRENLAFGLKRKRNREDrISVDELLDLLGLDHL----LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1717358098 173 MSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQ 220
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-218 |
7.94e-47 |
|
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: 153.50 E-value: 7.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPV------CQRH 75
Cdd:cd03229 1 LELKNVSKRY------GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdledeLPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRlgKMSVVFQDYksSLHPYFNVRQILNEALSqcdtpvddkeahmtallervglsaaflnkypqmmsGGEAQRVAIARAV 155
Cdd:cd03229 75 RR--RIGMVFQDF--ALFPHLTVLENIALGLS-----------------------------------GGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 156 ITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQ 218
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-218 |
8.99e-47 |
|
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: 154.55 E-value: 8.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 3 EVQNVTKSYrsgvKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPV--CQRHTRLGK 80
Cdd:cd03225 1 ELKNLSFSY----PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtkLSLKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSVVFQDYKSslhpyfnvrQILNE------ALSQCDTPVDDKEAHM--TALLERVGLSaAFLNKYPQMMSGGEAQRVAIA 152
Cdd:cd03225 77 VGLVFQNPDD---------QFFGPtveeevAFGLENLGLPEEEIEErvEEALELVGLE-GLRDRSPFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717358098 153 RAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQ 218
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-241 |
2.32e-46 |
|
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: 161.39 E-value: 2.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGVKRQkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILG-----IEKPdTGTVMLDGQPVCQ-- 73
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTV--EAVKGVSFDIAAGETLALVGESGSGKSVTALSILRllpdpAAHP-SGSILFDGQDLLGls 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 74 ----RHTRLGKMSVVFQDYKSSLHPYFNVRQILNEALsQCDTPVDDKEAHMTA--LLERVGLSAAF--LNKYPQMMSGGE 145
Cdd:COG4172 83 erelRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVL-RLHRGLSGAAARARAleLLERVGIPDPErrLDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 146 AQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNR 225
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPT 241
|
250
....*....|....*..
gi 1717358098 226 HQL-KTLQNDYTRELFE 241
Cdd:COG4172 242 AELfAAPQHPYTRKLLA 258
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-221 |
1.22e-45 |
|
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: 152.35 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ------R 74
Cdd:cd03258 1 MIELKNVSKVFGDT--GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkelR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 75 HTRlGKMSVVFQDYK--SSLHPYFNVR---QILNEALSQCDTPVDDkeahmtaLLERVGLSAaFLNKYPQMMSGGEAQRV 149
Cdd:cd03258 79 KAR-RRIGMIFQHFNllSSRTVFENVAlplEIAGVPKAEIEERVLE-------LLELVGLED-KADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 150 AIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVE 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-221 |
4.36e-45 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 150.91 E-value: 4.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRL-- 78
Cdd:COG1126 1 MIEIENLHKSF------GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 79 --GKMSVVFQDYksSLHPYFNVRQILNEAlsqcdtPV-----DDKEAHMTA--LLERVGLsAAFLNKYPQMMSGGEAQRV 149
Cdd:COG1126 75 lrRKVGMVFQQF--NLFPHLTVLENVTLA------PIkvkkmSKAEAEERAmeLLERVGL-ADKADAYPAQLSGGQQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 150 AIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDI----QAAvylceDLIIF-NDGQIQE 221
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMgfarEVA-----DRVVFmDGGRIVE 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-221 |
6.11e-45 |
|
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: 150.46 E-value: 6.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVkrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ--RHTRlg 79
Cdd:cd03300 1 IELENVSKFYGGFV------ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpPHKR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQDYksSLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVITNP 159
Cdd:cd03300 73 PVNTVFQNY--ALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEG-YANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 160 DYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQ 211
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-201 |
1.10e-44 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 152.55 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 16 KRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTV------MLDGQPVCQRHTRlGKMSVVFQDYK 89
Cdd:PRK15079 30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVawlgkdLLGMKDDEWRAVR-SDIQMIFQDPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 90 SSLHPYFNVRQILNEALS--QCDTPVDDKEAHMTALLERVGLSAAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEA 167
Cdd:PRK15079 109 ASLNPRMTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190
....*....|....*....|....*....|....
gi 1717358098 168 ISALDMSIQSQILDLLTTLRDKYQLSLIFITHDI 201
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-220 |
2.15e-44 |
|
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: 152.56 E-value: 2.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 25 QVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQ-----------PVCQRhtRLGkmsVVFQDykSSLH 93
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiflPPHRR--RIG---YVFQE--ARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 94 PYFNVRQILNEALSQCdtPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDM 173
Cdd:COG4148 90 PHLSVRGNLLYGRKRA--PRAERRISFDEVVELLGI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1717358098 174 SIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQ 220
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-219 |
3.08e-44 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 149.05 E-value: 3.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ------R 74
Cdd:COG3638 2 MLELRNLSKRYPGG-----TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlrgralR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 75 HTRlGKMSVVFQDY-----KSSLHpyfNVrqiLNEALSQCDT--------PVDDKEAHMtALLERVGLsAAFLNKYPQMM 141
Cdd:COG3638 77 RLR-RRIGMIFQQFnlvprLSVLT---NV---LAGRLGRTSTwrsllglfPPEDRERAL-EALERVGL-ADKAYQRADQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 142 SGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-219 |
4.06e-44 |
|
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: 146.43 E-value: 4.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 3 EVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ--RHTRLGK 80
Cdd:cd03214 1 EVENLSVGY------GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlsPKELARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSVVFQdyksslhpyfnvrqilnealsqcdtpvddkeahmtaLLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVITNPD 160
Cdd:cd03214 75 IAYVPQ------------------------------------ALELLGL-AHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717358098 161 YIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-241 |
7.17e-44 |
|
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: 148.95 E-value: 7.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKR---------QKRQI---------VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGT 63
Cdd:cd03294 1 IKIKGLYKIFGKNPQKafkllakgkSKEEIlkktgqtvgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 64 VMLDGQPVCQ------RHTRLGKMSVVFQDYksSLHPYFNVRQilNEALSQCDTPVDDKEAHMTAL--LERVGLsAAFLN 135
Cdd:cd03294 81 VLIDGQDIAAmsrkelRELRRKKISMVFQSF--ALLPHRTVLE--NVAFGLEVQGVPRAEREERAAeaLELVGL-EGWEH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 136 KYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFN 215
Cdd:cd03294 156 KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMK 235
|
250 260
....*....|....*....|....*..
gi 1717358098 216 DGQI-QERLNRHQLKTLQNDYTRELFE 241
Cdd:cd03294 236 DGRLvQVGTPEEILTNPANDYVREFFR 262
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-221 |
1.03e-43 |
|
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: 147.20 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC-----QRH 75
Cdd:COG4181 8 IIELRGLTKTVGTG--AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldedARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 T-RLGKMSVVFQDYksslhpyfnvrQILNE--ALSQCDTP-----VDDKEAHMTALLERVGLSAAfLNKYPQMMSGGEAQ 147
Cdd:COG4181 86 RlRARHVGFVFQSF-----------QLLPTltALENVMLPlelagRRDARARARALLERVGLGHR-LDHYPAQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717358098 148 RVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQ-AAvyLCEDLIIFNDGQIQE 221
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPAlAA--RCDRVLRLRAGRLVE 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-220 |
7.23e-43 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 144.90 E-value: 7.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRsgvkrqkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPvcqrHTRLG- 79
Cdd:COG3840 1 MLRLDDLTYRYG--------DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD----LTALPp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 ---KMSVVFQDYksSLHPYFNVRQilNEAL---SQCDTPVDDKEAhMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIAR 153
Cdd:COG3840 69 aerPVSMLFQEN--NLFPHLTVAQ--NIGLglrPGLKLTAEQRAQ-VEQALERVGL-AGLLDRLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 154 AVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQ 220
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-219 |
1.06e-42 |
|
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: 144.21 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRL--- 78
Cdd:cd03262 1 IEIKNLHKSF------GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNInel 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 79 -GKMSVVFQDYksSLHPYFNVRQILNEALSQC-DTPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVI 156
Cdd:cd03262 75 rQKVGMVFQQF--NLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 157 TNPDYIVLDEAISALDMSIQSQILDLLTTLRdKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-219 |
1.14e-42 |
|
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: 144.79 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVkrqkrqiVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGKM 81
Cdd:cd03299 1 LKVENLSKDWKEFK-------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 SVVFQDYksSLHPYFNVRQILNEALS--QCDTPVDDKEAHMTAllERVGLSAaFLNKYPQMMSGGEAQRVAIARAVITNP 159
Cdd:cd03299 74 SYVPQNY--ALFPHMTVYKNIAYGLKkrKVDKKEIERKVLEIA--EMLGIDH-LLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 160 DYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-246 |
1.30e-42 |
|
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: 144.62 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPV-CQRHTRLG 79
Cdd:COG4555 1 MIEVENLSKKY------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrKEPREARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQDykSSLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLSaAFLNKYPQMMSGGEAQRVAIARAVITNP 159
Cdd:COG4555 75 QIGVLPDE--RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 160 DYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQLKTLqndYTREL 239
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE---IGEEN 227
|
....*..
gi 1717358098 240 FEKQFMN 246
Cdd:COG4555 228 LEDAFVA 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-219 |
1.73e-42 |
|
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: 142.15 E-value: 1.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRsgvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRL-GK 80
Cdd:cd03230 1 IEVRNLSKRYG------KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVkRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSVVFQDykSSLHPYFNVRQILnealsqcdtpvddkeahmtallervglsaaflnkypqMMSGGEAQRVAIARAVITNPD 160
Cdd:cd03230 75 IGYLPEE--PSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717358098 161 YIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-202 |
1.15e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 141.73 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqrhTRLG- 79
Cdd:COG2884 1 MIRFENVSKRYPGG-----REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL----SRLKr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 --------KMSVVFQDYKssLHPYFNVRQilNEALSQ--CDTPVDDKEAHMTALLERVGLSaAFLNKYPQMMSGGEAQRV 149
Cdd:COG2884 72 reipylrrRIGVVFQDFR--LLPDRTVYE--NVALPLrvTGKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 150 AIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQ 202
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLE 198
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-243 |
1.64e-41 |
|
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: 150.37 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRsgvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRL--G 79
Cdd:COG2274 474 IELENVSFRYP----GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQDykSSLhpyFN--VRQilNeaLSQCDTPVDDKEahMTALLERVGLsAAFLNKYPQ-----------MMSGGEA 146
Cdd:COG2274 550 QIGVVLQD--VFL---FSgtIRE--N--ITLGDPDATDEE--IIEAARLAGL-HDFIEALPMgydtvvgeggsNLSGGQR 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 147 QRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyqLSLIFITHDIqAAVYLCEDLIIFNDGQIQERLNRH 226
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHE 694
|
250
....*....|....*..
gi 1717358098 227 QLKTLQNDYtRELFEKQ 243
Cdd:COG2274 695 ELLARKGLY-AELVQQQ 710
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-219 |
1.92e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 142.57 E-value: 1.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLG-- 79
Cdd:TIGR04520 1 IEVENVSFSYPE----SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 -KMSVVFQ-------------DYKSSLH----PYFNVRQILNEALsqcdtpvddkeahmtallERVGLSAaFLNKYPQMM 141
Cdd:TIGR04520 77 kKVGMVFQnpdnqfvgatvedDVAFGLEnlgvPREEMRKRVDEAL------------------KLVGMED-FRDREPHLL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 142 SGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVyLCEDLIIFNDGQI 219
Cdd:TIGR04520 138 SGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKI 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-239 |
3.66e-41 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 147.54 E-value: 3.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILG------IEKPdTGTVMLDGQPVCQ- 73
Cdd:PRK15134 5 LLAIENLSVAFRQQ--QTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRllpsppVVYP-SGDIRFHGESLLHa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 74 -----RHTRLGKMSVVFQDYKSSLHPYFNVRQILNEALS-QCDTPVDDKEAHMTALLERVGL--SAAFLNKYPQMMSGGE 145
Cdd:PRK15134 82 seqtlRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIrqAAKRLTDYPHQLSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 146 AQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNR 225
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRA 241
|
250
....*....|....*
gi 1717358098 226 HQL-KTLQNDYTREL 239
Cdd:PRK15134 242 ATLfSAPTHPYTQKL 256
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-224 |
3.67e-41 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 141.54 E-value: 3.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsGVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGk 80
Cdd:COG4525 3 MLTVRHVSVRY--PGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 msVVFQDYksSLHPYFNVRQilNEALSQCDTPVDDKEAHMTA--LLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVITN 158
Cdd:COG4525 80 --VVFQKD--ALLPWLNVLD--NVAFGLRLRGVPKAERRARAeeLLALVGL-ADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 159 PDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIF--NDGQIQERLN 224
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVERLE 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-219 |
3.73e-41 |
|
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: 140.78 E-value: 3.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRL--- 78
Cdd:cd03256 1 IEVENLSKTYPNG-----KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 79 --GKMSVVFQDY---------KSSLHPYFNVRQILNeALSQCDTPVDDKEAhmTALLERVGLsAAFLNKYPQMMSGGEAQ 147
Cdd:cd03256 76 lrRQIGMIFQQFnlierlsvlENVLSGRLGRRSTWR-SLFGLFPKEEKQRA--LAALERVGL-LDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 148 RVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-219 |
9.10e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.84 E-value: 9.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRsgvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGk 80
Cdd:COG1121 6 AIELENLTVSYG------GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 msvvfqdY---KSSLHPYF--NVRQILneaLSQCDTPV--------DDKEAHMTALlERVGLsAAFLNKYPQMMSGGEAQ 147
Cdd:COG1121 79 -------YvpqRAEVDWDFpiTVRDVV---LMGRYGRRglfrrpsrADREAVDEAL-ERVGL-EDLADRPIGELSGGQQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 148 RVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRdKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-221 |
1.34e-40 |
|
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: 139.40 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKrqkrqiVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGKM 81
Cdd:cd03296 3 IEVRNVSKRFGDFVA------LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 SVVFQDYksSLHPYFNVRQI----LNEALSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVIT 157
Cdd:cd03296 77 GFVFQHY--ALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDW-LADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717358098 158 NPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQ 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-222 |
3.78e-40 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 141.09 E-value: 3.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGvkrqKRQI--VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ----- 73
Cdd:PRK11153 1 MIELKNISKVFPQG----GRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlseke 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 74 -RHTRLgKMSVVFQDYK--SSLHPYFNVRQILNEAlsqcDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVA 150
Cdd:PRK11153 77 lRKARR-QIGMIFQHFNllSSRTVFDNVALPLELA----GTPKAEIKARVTELLELVGLSD-KADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 151 IARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQER 222
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQ 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-215 |
9.20e-40 |
|
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: 136.51 E-value: 9.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 3 EVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGKMS 82
Cdd:cd03235 1 EVEDLTVSYGG------HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 83 vvfQdyKSSLHPYFNVRqILNEALSQCDTPV--------DDKEAHMTALlERVGLSAaFLNKYPQMMSGGEAQRVAIARA 154
Cdd:cd03235 75 ---Q--RRSIDRDFPIS-VRDVVLMGLYGHKglfrrlskADKAKVDEAL-ERVGLSE-LADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717358098 155 VITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFN 215
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
37-219 |
1.01e-39 |
|
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: 140.25 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 37 AIIGESGSGKSTLARMILGIEKPDTGTVMLDG-------QPVC-QRHTRlgKMSVVFQDykSSLHPYFNVRQILNEALSQ 108
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFlPPEKR--RIGYVFQE--ARLFPHLSVRGNLRYGMKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 109 CDtpVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRD 188
Cdd:TIGR02142 103 AR--PSERRISFERVIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHA 179
|
170 180 190
....*....|....*....|....*....|.
gi 1717358098 189 KYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:TIGR02142 180 EFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-219 |
1.10e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.10 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVtksyrsGVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ------RH 75
Cdd:COG4619 1 LELEGL------SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmpppewRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 trlgKMSVVFQDyksslhPYF---NVRQILNEALSQCDTPVDDKEAHmtALLERVGLSAAFLNKYPQMMSGGEAQRVAIA 152
Cdd:COG4619 75 ----QVAYVPQE------PALwggTVRDNLPFPFQLRERKFDRERAL--ELLERLGLPPDILDKPVERLSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 153 RAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-241 |
3.48e-39 |
|
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: 142.60 E-value: 3.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ--RHTRLG 79
Cdd:COG4987 334 LELEDVSFRYPG----AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDldEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQDyksslhPY-FN--VRQIL---NEALSqcdtpvddkEAHMTALLERVGLsAAFLNKYPQ-----------MMS 142
Cdd:COG4987 410 RIAVVPQR------PHlFDttLRENLrlaRPDAT---------DEELWAALERVGL-GDWLAALPDgldtwlgeggrRLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 143 GGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQIL-DLLTTLRDKyqlSLIFITHDiQAAVYLCEDLIIFNDGQIQE 221
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLaDLLEALAGR---TVLLITHR-LAGLERMDRILVLEDGRIVE 549
|
250 260
....*....|....*....|
gi 1717358098 222 RLNRHQLKTLQNDYtRELFE 241
Cdd:COG4987 550 QGTHEELLAQNGRY-RQLYQ 568
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-242 |
1.12e-38 |
|
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: 134.74 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRH-TRLG- 79
Cdd:cd03295 1 IEFENVTKRYGGG-----KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDpVELRr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQdyKSSLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGL-SAAFLNKYPQMMSGGEAQRVAIARAVITN 158
Cdd:cd03295 76 KIGYVIQ--QIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdPAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 159 PDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLN-RHQLKTLQNDYTR 237
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTpDEILRSPANDFVA 233
|
....*
gi 1717358098 238 ELFEK 242
Cdd:cd03295 234 EFVGA 238
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-242 |
1.35e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 137.13 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqrhTRLG- 79
Cdd:COG3839 3 SLELENVSKSY------GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV----TDLPp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 ---KMSVVFQDYksSLHPYFNVRQilNEA--LSQCDTPVDDKEAHMTALLERVGLSaAFLNKYPQMMSGGEAQRVAIARA 154
Cdd:COG3839 73 kdrNIAMVFQSY--ALYPHMTVYE--NIAfpLKLRKVPKAEIDRRVREAAELLGLE-DLLDRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 155 VITNPDYIVLDEAISALD----MSIQSQILDLLTTLRdkyqLSLIFITHDiQA-AVYLCEDLIIFNDGQIQerlnrhqlk 229
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLG----TTTIYVTHD-QVeAMTLADRIAVMNDGRIQ--------- 213
|
250
....*....|...
gi 1717358098 230 tlQNDYTRELFEK 242
Cdd:COG3839 214 --QVGTPEELYDR 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-167 |
1.99e-38 |
|
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: 131.23 E-value: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 23 VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ--RHTRLGKMSVVFQDykSSLHPYFNVRQ 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQD--PQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 101 ILNEALSQCDTPVDDKEAHMTALLERVGLSAA---FLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEA 167
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDARAEEALEKLGLGDLadrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-218 |
2.35e-38 |
|
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: 131.35 E-value: 2.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ--RHTRLG 79
Cdd:cd03228 1 IEFKNVSFSYPGR----PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDldLESLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQDyksslhPY-FN--VRQ-ILnealsqcdtpvddkeahmtallervglsaaflnkypqmmSGGEAQRVAIARAV 155
Cdd:cd03228 77 NIAYVPQD------PFlFSgtIREnIL---------------------------------------SGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 156 ITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyqLSLIFITHDIqAAVYLCEDLIIFNDGQ 218
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKG--KTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-221 |
2.46e-38 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 137.00 E-value: 2.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQ-----PVCQRHt 76
Cdd:PRK09452 15 VELRGISKSFDG------KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvPAENRH- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 77 rlgkMSVVFQDYksSLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVI 156
Cdd:PRK09452 88 ----VNTVFQSY--ALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEE-FAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717358098 157 TNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQ 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-228 |
4.05e-38 |
|
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: 132.69 E-value: 4.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRsgvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMI-----LGIEKPDTGTVMLDGQPVCQRHT 76
Cdd:cd03260 1 IELRDLNVYYG------DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 77 RLG----KMSVVFQdyKSSLHP---YFNVRQILNEALSQCDTPVDDKEAHmtaLLERVGLSAAFLNK-YPQMMSGGEAQR 148
Cdd:cd03260 75 DVLelrrRVGMVFQ--KPNPFPgsiYDNVAYGLRLHGIKLKEELDERVEE---ALRKAALWDEVKDRlHALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 149 VAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYqlSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQL 228
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-221 |
9.35e-38 |
|
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: 131.22 E-value: 9.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGKM 81
Cdd:cd03301 1 VELENVTKRF------GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 SVVFQDYksSLHPYFNVRQILNEALSQCDTPVD--DKEAHMTALLERVGlsaAFLNKYPQMMSGGEAQRVAIARAVITNP 159
Cdd:cd03301 75 AMVFQNY--ALYPHMTVYDNIAFGLKLRKVPKDeiDERVREVAELLQIE---HLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 160 DYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-218 |
4.05e-37 |
|
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: 127.75 E-value: 4.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 3 EVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGK-- 80
Cdd:cd00267 1 EIENLSFRY------GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRrr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSVVFQdyksslhpyfnvrqilnealsqcdtpvddkeahmtallervglsaaflnkypqmMSGGEAQRVAIARAVITNPD 160
Cdd:cd00267 75 IGYVPQ------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 161 YIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQ 218
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-228 |
8.00e-37 |
|
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: 136.04 E-value: 8.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ--RHTRLG 79
Cdd:COG4988 337 IELEDVSFSYPGG-----RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDldPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQdyksslHPY-FN--VRQILneALSQCDTPvddkEAHMTALLERVGLsAAFLNKYPQ-----------MMSGGE 145
Cdd:COG4988 412 QIAWVPQ------NPYlFAgtIRENL--RLGRPDAS----DEELEAALEAAGL-DEFVAALPDgldtplgeggrGLSGGQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 146 AQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTL-RDKyqlSLIFITHDIQAAVYLceDLIIF-NDGQIQERL 223
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLaKGR---TVILITHRLALLAQA--DRILVlDDGRIVEQG 553
|
....*
gi 1717358098 224 NRHQL 228
Cdd:COG4988 554 THEEL 558
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-217 |
1.19e-36 |
|
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: 129.12 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 23 VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqrhTRLG--KMsVVFQDYksSLHPYFNVRQ 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----TEPGpdRM-VVFQNY--SLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 101 ilNEALS----QCDTPVDDKEAHMTALLERVGLSAAfLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQ 176
Cdd:TIGR01184 74 --NIALAvdrvLPDLSKSERRAIVEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1717358098 177 SQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDG 217
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-221 |
1.79e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 129.75 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYrsgvKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQP-----VCQRHT 76
Cdd:PRK13635 6 IRVEHISFRY----PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 77 RLGkmsVVFQDYKSSlhpyF---NVRQILNEALSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIAR 153
Cdd:PRK13635 82 QVG---MVFQNPDNQ----FvgaTVQDDVAFGLENIGVPREEMVERVDQALRQVGMED-FLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 154 AVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYlCEDLIIFNDGQIQE 221
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-243 |
1.45e-35 |
|
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: 126.19 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPV--CQRHTRLG 79
Cdd:cd03253 1 IEFENVTFAYDPG-----RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIreVTLDSLRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQD---YKSSLhpYFNVR---------QILNEALSQC--DTPVDDKEAHMTALLERvGLsaaflnkypqMMSGGE 145
Cdd:cd03253 76 AIGVVPQDtvlFNDTI--GYNIRygrpdatdeEVIEAAKAAQihDKIMRFPDGYDTIVGER-GL----------KLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 146 AQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYqlSLIFITHDIqAAVYLCEDLIIFNDGQIQERLNR 225
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRL-STIVNADKIIVLKDGRIVERGTH 219
|
250
....*....|....*...
gi 1717358098 226 HQLKTLQNDYtRELFEKQ 243
Cdd:cd03253 220 EELLAKGGLY-AEMWKAQ 236
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-200 |
3.45e-35 |
|
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: 124.83 E-value: 3.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKRqkrqiVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRL--- 78
Cdd:cd03292 1 IEFINVTKTYPNGTAA-----LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 79 --GKMSVVFQDYKssLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLSAAfLNKYPQMMSGGEAQRVAIARAVI 156
Cdd:cd03292 76 lrRKIGVVFQDFR--LLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHK-HRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1717358098 157 TNPDYIVLDEAISALDMSIQSQILDLLTTLrDKYQLSLIFITHD 200
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHA 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-239 |
4.21e-35 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 131.90 E-value: 4.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSY--RSGV-KRQKRQI--VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQ-----P 70
Cdd:PRK10261 313 ILQVRNLVTRFplRSGLlNRVTREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 71 VCQRHTRLGKMSVVFQDYKSSLHPYFNVRQILNEALsQCDTPVDDKEA--HMTALLERVGLSAAFLNKYPQMMSGGEAQR 148
Cdd:PRK10261 393 PGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPL-RVHGLLPGKAAaaRVAWLLERVGLLPEHAWRYPHEFSGGQRQR 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 149 VAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQL 228
Cdd:PRK10261 472 ICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
|
250
....*....|..
gi 1717358098 229 -KTLQNDYTREL 239
Cdd:PRK10261 552 fENPQHPYTRKL 563
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-223 |
7.39e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 125.20 E-value: 7.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGk 80
Cdd:PRK11248 1 MLQISHLYADY------GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERG- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 msVVFQDykSSLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVITNPD 160
Cdd:PRK11248 74 --VVFQN--EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717358098 161 YIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIF--NDGQIQERL 223
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVERL 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-219 |
1.42e-34 |
|
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: 122.99 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 27 SFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGKMSVVFQDykSSLHPYFNVRQILNEAL 106
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE--NNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 107 SQCD--TPVDDKEAHmtALLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLT 184
Cdd:cd03298 96 SPGLklTAEDRQAIE--VALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*
gi 1717358098 185 TLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-246 |
2.34e-34 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 129.51 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ--RHTRLG 79
Cdd:COG1132 340 IEFENVSFSYPGD-----RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDltLESLRR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQDykSSLhpyFN--VRQilNEALSQCDtpVDDKEahMTALLERVGLsAAFLNKYPQ-----------MMSGGEA 146
Cdd:COG1132 415 QIGVVPQD--TFL---FSgtIRE--NIRYGRPD--ATDEE--VEEAAKAAQA-HEFIEALPDgydtvvgergvNLSGGQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 147 QRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTL-RDKyqlSLIFITHD---IQAAvylceDLII-FNDGQIQE 221
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLmKGR---TTIVIAHRlstIRNA-----DRILvLDDGRIVE 554
|
250 260
....*....|....*....|....*..
gi 1717358098 222 RLNRHQLktLQND--YtRELFEKQFMN 246
Cdd:COG1132 555 QGTHEEL--LARGglY-ARLYRLQFGE 578
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-220 |
1.22e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.41 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ---RHTR 77
Cdd:PRK13632 7 MIKVENVSFSYPN----SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenlKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 lGKMSVVFQDYKSSlhpyF---NVRQILNEALSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARA 154
Cdd:PRK13632 83 -KKIGIIFQNPDNQ----FigaTVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMED-YLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717358098 155 VITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVyLCEDLIIFNDGQIQ 220
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLI 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
2.49e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 122.14 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHT-RLG 79
Cdd:COG4152 1 MLELKGLTKRFGD------KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRrRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 ----------KMSVVFQ-DYKSSLHpyfnvrqilnealsqcdtPVDDKEAH--MTALLERVGLsAAFLNKYPQMMSGGEA 146
Cdd:COG4152 75 ylpeerglypKMKVGEQlVYLARLK------------------GLSKAEAKrrADEWLERLGL-GDRANKKVEELSKGNQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717358098 147 QRVAIARAVITNPDYIVLDEAISALDmSIQSQIL-DLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:COG4152 136 QKVQLIAALLHDPELLILDEPFSGLD-PVNVELLkDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-220 |
8.84e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 119.49 E-value: 8.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTksyrsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPV-----CQRH 75
Cdd:PRK13548 2 MLEARNLS------VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLadwspAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRLGKMSvvfQdyKSSLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLsAAFLNK-YPQmMSGGEAQRVAIAR- 153
Cdd:PRK13548 76 RRRAVLP---Q--HSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDL-AHLAGRdYPQ-LSGGEQQRVQLARv 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 154 -AVITNPD----YIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDI-QAAVYlCEDLIIFNDGQIQ 220
Cdd:PRK13548 149 lAQLWEPDgpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLnLAARY-ADRIVLLHQGRLV 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-219 |
1.05e-32 |
|
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: 118.15 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRH-TRLG- 79
Cdd:cd03269 1 LEVENVTKRFGR------VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArNRIGy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 ---------KMSVVFQ-DYKSSLHPYfNVRQILNEALSqcdtpvddkeahmtaLLERVGLSaAFLNKYPQMMSGGEAQRV 149
Cdd:cd03269 75 lpeerglypKMKVIDQlVYLAQLKGL-KKEEARRRIDE---------------WLERLELS-EYANKRVEELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 150 AIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-221 |
4.16e-32 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 120.19 E-value: 4.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGKM 81
Cdd:PRK10851 3 IEIANIKKSF------GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 SVVFQDYksSLHPYFNV-------------RQILNEALsqcdtpVDDKeahMTALLERVGLSAaFLNKYPQMMSGGEAQR 148
Cdd:PRK10851 77 GFVFQHY--ALFRHMTVfdniafgltvlprRERPNAAA------IKAK---VTQLLEMVQLAH-LADRYPAQLSGGQKQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 149 VAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:PRK10851 145 VALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQ 217
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-239 |
5.07e-32 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 117.49 E-value: 5.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 20 RQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDT----GTVMLDGQPVCQRHTRLGKMSVVFQDYKSSLHPY 95
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVrqtaGRVLLDGKPVAPCALRGRKIATIMQNPRSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 96 FNVRQILNEALSQCDTPVDDkeAHMTALLERVGLS--AAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDM 173
Cdd:PRK10418 96 HTMHTHARETCLALGKPADD--ATLTAALEAVGLEnaARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 174 SIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQL-KTLQNDYTREL 239
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLfNAPKHAVTRSL 240
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-221 |
6.35e-32 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 116.80 E-value: 6.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHT---- 76
Cdd:PRK10584 6 IVEVHHLKKSVGQG--EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEeara 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 77 --RLGKMSVVFQDYKssLHPYFNVRQILN-EALSQCDTPVDDKEaHMTALLERVGLSAAfLNKYPQMMSGGEAQRVAIAR 153
Cdd:PRK10584 84 klRAKHVGFVFQSFM--LIPTLNALENVElPALLRGESSRQSRN-GAKALLEQLGLGKR-LDHLPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 154 AVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYlCEDLIIFNDGQIQE 221
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-221 |
6.79e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 119.94 E-value: 6.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGK 80
Cdd:PRK11607 19 LLEIRNLTKSF------DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSVVFQDYksSLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLSaAFLNKYPQMMSGGEAQRVAIARAVITNPD 160
Cdd:PRK11607 93 INMMFQSY--ALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 161 YIVLDEAISALDMSI----QSQILDLLttlrDKYQLSLIFITHDIQAAVYLCEDLIIFNDG---QIQE 221
Cdd:PRK11607 170 LLLLDEPMGALDKKLrdrmQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGkfvQIGE 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-219 |
6.97e-32 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 117.47 E-value: 6.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPV--CQRHTRLg 79
Cdd:PRK11247 13 LLLNAVSKRYGE------RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLaeAREDTRL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 kmsvVFQDykSSLHPYFNVrqILNEALSqcdTPVDDKEAHMTALlERVGLsAAFLNKYPQMMSGGEAQRVAIARAVITNP 159
Cdd:PRK11247 86 ----MFQD--ARLLPWKKV--IDNVGLG---LKGQWRDAALQAL-AAVGL-ADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 160 DYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
7.65e-32 |
|
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: 115.65 E-value: 7.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSyrsgvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPV-CQRHTRLG 79
Cdd:COG4133 2 MLEAENLSCR------RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIrDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQDykSSLHPYFNVRQILNEALSQCDTPVDDKEAHmtALLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVITNP 159
Cdd:COG4133 76 RLAYLGHA--DGLKPELTVRENLRFWAALYGLRADREAID--EALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1717358098 160 DYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHD 200
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-220 |
8.78e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 117.53 E-value: 8.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSgvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ------R 74
Cdd:PRK13650 4 IIEVKNLTFKYKE---DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenvwdiR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 75 HtrlgKMSVVFQDYKSSlhpyF---NVRQILNEALSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAI 151
Cdd:PRK13650 81 H----KIGMVFQNPDNQ----FvgaTVEDDVAFGLENKGIPHEEMKERVNEALELVGMQD-FKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717358098 152 ARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQaAVYLCEDLIIFNDGQIQ 220
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLD-EVALSDRVLVMKNGQVE 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-220 |
9.87e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 116.75 E-value: 9.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTksyrsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ-RHTRLG 79
Cdd:COG4559 1 MLEAENLS------VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwSPWELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KM-SVVFQDykSSLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIARA---- 154
Cdd:COG4559 75 RRrAVLPQH--SSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGL-AHLAGRSYQTLSGGEQQRVQLARVlaql 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717358098 155 ---VITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQIQ 220
Cdd:COG4559 152 wepVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-219 |
1.96e-31 |
|
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: 113.29 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYrSGVKrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqrhtrlgkm 81
Cdd:cd03216 1 LELRGITKRF-GGVK-----ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 svvfqdyksslhpyfnvrqilnealsqcdTPVDDKEAHmtalleRVGLSAAFlnkypQmMSGGEAQRVAIARAVITNPDY 161
Cdd:cd03216 65 -----------------------------SFASPRDAR------RAGIAMVY-----Q-LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 162 IVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-240 |
3.80e-31 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 118.60 E-value: 3.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 23 VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ------RHTRLGKMSVVFQDYksSLHPYF 96
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelREVRRKKIAMVFQSF--ALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 97 NVRQILNEALSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQ 176
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLEN-YAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717358098 177 SQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQ-IQERLNRHQLKTLQNDYTRELF 240
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEvVQVGTPDEILNNPANDYVRTFF 265
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
23-221 |
6.87e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 116.38 E-value: 6.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 23 VKQVSFQCSKGQSIAIIGESGSGKSTLARMILG-IEKPdtGTVM-----LDGQPVC-----QRHTRLG-KMSVVFQDYKS 90
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlIDYP--GRVMaekleFNGQDLQrisekERRNLVGaEVAMIFQDPMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 91 SLHPYFNVRQILNEALsQCDTPVDDKEAHMTA--LLERVGLS--AAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDE 166
Cdd:PRK11022 101 SLNPCYTVGFQIMEAI-KVHQGGNKKTRRQRAidLLNQVGIPdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1717358098 167 AISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-220 |
7.76e-31 |
|
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: 113.37 E-value: 7.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKrqkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC-QRHTRLGK 80
Cdd:cd03263 1 LQIRNLTKTYKKGTK----PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRtDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSVVFQDykSSLHPYFNVRQILN-EALSQCdTPVDDKEAHMTALLERVGLSaAFLNKYPQMMSGGEAQRVAIARAVITNP 159
Cdd:cd03263 77 LGYCPQF--DALFDELTVREHLRfYARLKG-LPKSEIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717358098 160 DYIVLDEAISALDMSIQSQILDLLTTLRDkyQLSLIFITHDIQAAVYLCEDLIIFNDGQIQ 220
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-228 |
1.89e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 113.26 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC-----QRH 75
Cdd:PRK09493 1 MIEFKNVSKHF------GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkvdERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRLgKMSVVFQDYksSLHPY--------FNVRQIlnEALSQCDTpvddkEAHMTALLERVGLsAAFLNKYPQMMSGGEAQ 147
Cdd:PRK09493 75 IRQ-EAGMVFQQF--YLFPHltalenvmFGPLRV--RGASKEEA-----EKQARELLAKVGL-AERAHHYPSELSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 148 RVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQ 227
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQV 222
|
.
gi 1717358098 228 L 228
Cdd:PRK09493 223 L 223
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
21-204 |
1.97e-30 |
|
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: 111.75 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 21 QIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqRHTRLG------KMSVVFQDYKSSLHp 94
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL--DYSRKGllerrqRVGLVFQDPDDQLF- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 95 YFNVRQ-----ILNEALSQcdtpvDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAIS 169
Cdd:TIGR01166 83 AADVDQdvafgPLNLGLSE-----AEVERRVREALTAVGASG-LRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1717358098 170 ALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAA 204
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRAE-GMTVVISTHDVDLA 190
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-221 |
2.17e-30 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 113.18 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDG------QPVCQRH 75
Cdd:COG4161 3 IQLKNINCFYGS------HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRL--GKMSVVFQDYksSLHPYFNVRQILNEAlsqcdtPV-----DDKEAHMTA--LLERVGLsAAFLNKYPQMMSGGEA 146
Cdd:COG4161 77 IRLlrQKVGMVFQQY--NLWPHLTVMENLIEA------PCkvlglSKEQAREKAmkLLARLRL-TDKADRFPLHLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717358098 147 QRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-219 |
2.41e-30 |
|
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: 112.30 E-value: 2.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYrsgvKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRH--TRLG 79
Cdd:cd03245 3 IEFRNVSFSY----PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDpaDLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQDykSSLHpYFNVRQilNEALSqcDTPVDDKEahMTALLERVGLSaAFLNKYP---QMM--------SGGEAQR 148
Cdd:cd03245 79 NIGYVPQD--VTLF-YGTLRD--NITLG--APLADDER--ILRAAELAGVT-DFVNKHPnglDLQigergrglSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 149 VAIARAVITNPDYIVLDEAISALDMSIQSQILDLL-TTLRDKyqlSLIFITHDiQAAVYLCEDLIIFNDGQI 219
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLrQLLGDK---TLIIITHR-PSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-219 |
3.02e-30 |
|
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: 110.77 E-value: 3.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqrhtrlgkm 81
Cdd:cd03246 1 LEVENVSFRYPGA----EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 svvfqdykSSLHPyfnvrqilnealsqcdtpvDDKEAHMTALLERVGLSAAFLNKypQMMSGGEAQRVAIARAVITNPDY 161
Cdd:cd03246 67 --------SQWDP-------------------NELGDHVGYLPQDDELFSGSIAE--NILSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 162 IVLDEAISALDMSIQSQILDLLTTLRdKYQLSLIFITHDIqAAVYLCEDLIIFNDGQI 219
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-204 |
3.68e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 111.42 E-value: 3.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTksyrsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPD---TGTVMLDGQPVCQRHTR 77
Cdd:COG4136 1 MLSLENLT------ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 LGKMSVVFQDykSSLHPYFNVRQILNEALSQcDTPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVIT 157
Cdd:COG4136 75 QRRIGILFQD--DLLFPHLSVGENLAFALPP-TIGRAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1717358098 158 NPDYIVLDEAISALDMSIQSQILDL-LTTLRDKyQLSLIFITHDIQAA 204
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREFvFEQIRQR-GIPALLVTHDEEDA 197
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-219 |
4.39e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.04 E-value: 4.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRsgvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQ-----PVCQRh 75
Cdd:COG1137 3 TLEAENLVKSYG------KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlPMHKR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRLG------------KMSVvfQDyksslhpyfNVRQILnEAlsqcdTPVDDKE--AHMTALLERVGLSAafLNKYPQM- 140
Cdd:COG1137 76 ARLGigylpqeasifrKLTV--ED---------NILAVL-EL-----RKLSKKEreERLEELLEEFGITH--LRKSKAYs 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 141 MSGGEAQRVAIARAVITNPDYIVLDEAISALD-MSIqSQILDLLTTLRDKyQLSlIFIT-HDIQAAVYLCEDLIIFNDGQ 218
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLKER-GIG-VLITdHNVRETLGICDRAYIISEGK 213
|
.
gi 1717358098 219 I 219
Cdd:COG1137 214 V 214
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-228 |
4.76e-30 |
|
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: 111.93 E-value: 4.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 3 EVQNVTKSYRSgvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ--RHTRLGK 80
Cdd:cd03254 4 EFENVNFSYDE-----KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDisRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSVVFQDyksslhPYFNVRQIL-NEALSQCDTPVDD-----KEAHMTALLERV--GLSAAfLNKYPQMMSGGEAQRVAIA 152
Cdd:cd03254 79 IGVVLQD------TFLFSGTIMeNIRLGRPNATDEEvieaaKEAGAHDFIMKLpnGYDTV-LGENGGNLSQGERQLLAIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 153 RAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDkyQLSLIFITH---DIQAAvylceDLIIF-NDGQIQERLNRHQL 228
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHrlsTIKNA-----DKILVlDDGKIIEEGTHDEL 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
6.16e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.86 E-value: 6.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGVkrqkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRL-- 78
Cdd:PRK13639 1 ILETRDLKYSYPDGT-----EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLle 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 79 --GKMSVVFQDYKSSLH-PyfNVRQ-----ILNEALSQcdtpvDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVA 150
Cdd:PRK13639 76 vrKTVGIVFQNPDDQLFaP--TVEEdvafgPLNLGLSK-----EEVEKRVKEALKAVGMEG-FENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717358098 151 IARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-221 |
6.36e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.54 E-value: 6.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 23 VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRH-TRLGK-MSVVFQD------------- 87
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfEKLRKhIGIVFQNpdnqfvgsivkyd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 88 ----YKSSLHPYFNVRQILNEALSQCDtpvddkeahmtaLLERVglsaaflNKYPQMMSGGEAQRVAIARAVITNPDYIV 163
Cdd:PRK13648 105 vafgLENHAVPYDEMHRRVSEALKQVD------------MLERA-------DYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 164 LDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYlCEDLIIFNDGQIQE 221
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYK 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-219 |
7.72e-30 |
|
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: 110.92 E-value: 7.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSgvKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ--RHTRL 78
Cdd:cd03266 1 MITADALTKRFRD--VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 79 gKMSVVFQdyKSSLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVITN 158
Cdd:cd03266 79 -RLGFVSD--STGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717358098 159 PDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-219 |
1.26e-29 |
|
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: 110.04 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 3 EVQNVTKSYRSGVKrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRhTRLGKMS 82
Cdd:cd03226 1 RIENISFSYKKGTE-----ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK-ERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 83 VVFQDYKSSLhpYFN-VRqilnEALSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVITNPDY 161
Cdd:cd03226 75 YVMQDVDYQL--FTDsVR----EELLLGLKELDAGNEQAETVLKDLDLYA-LKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 162 IVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIfITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIV-ITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-222 |
1.27e-29 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 110.00 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGKM 81
Cdd:cd03268 1 LKTNDLTKTY------GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 SVVFqDYkSSLHPYFNVRQilNEALSQCDTPVDDKEAHmtALLERVGLSAAFLNKYPQmMSGGEAQRVAIARAVITNPDY 161
Cdd:cd03268 75 GALI-EA-PGFYPNLTARE--NLRLLARLLGIRKKRID--EVLDVVGLKDSAKKKVKG-FSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717358098 162 IVLDEAISALDMSIQSQILDLLTTLRDkYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQER 222
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-219 |
1.77e-29 |
|
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: 110.94 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTksyrsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTG-TVMLDGQpvcqrhtRLG 79
Cdd:COG1119 3 LLELRNVT------VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGE-------RRG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVvfQDYK-------SSLHPYFNVRQ-ILNEALS----------QCdTPVDDKEAHmtALLERVGLsAAFLNKYPQMM 141
Cdd:COG1119 70 GEDV--WELRkriglvsPALQLRFPRDEtVLDVVLSgffdsiglyrEP-TDEQRERAR--ELLELLGL-AHLADRPFGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 142 SGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITH---DIQAAVYlceDLIIFNDGQ 218
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHhveEIPPGIT---HVLLLKDGR 220
|
.
gi 1717358098 219 I 219
Cdd:COG1119 221 V 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-219 |
2.04e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 114.73 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrSGVKrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR--- 77
Cdd:COG1129 4 LLEMRGISKSF-GGVK-----ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 -LGkMSVVFQDykSSLHPYFNV-------RQILNEALsqcdtpVDDKEAH--MTALLERVGLSaafLNkyPQM----MSG 143
Cdd:COG1129 78 aAG-IAIIHQE--LNLVPNLSVaeniflgREPRRGGL------IDWRAMRrrARELLARLGLD---ID--PDTpvgdLSV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 144 GEAQRVAIARAVITNPDYIVLDEAISALDMSiQSQIL-DLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:COG1129 144 AQQQLVEIARALSRDARVLILDEPTASLTER-EVERLfRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-219 |
2.16e-29 |
|
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: 110.22 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRsGVKrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQR--H--TR 77
Cdd:cd03219 1 LEVRGLTKRFG-GLV-----ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLppHeiAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 LGkMSVVFQdyKSSLHPYFNVRQ--------ILNEALSQCDTPVDDKEAHMTA--LLERVGLsAAFLNKYPQMMSGGEAQ 147
Cdd:cd03219 75 LG-IGRTFQ--IPRLFPELTVLEnvmvaaqaRTGSGLLLARARREEREARERAeeLLERVGL-ADLADRPAGELSYGQQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 148 RVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-245 |
2.38e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.43 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYrsgvKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDT---GTVMLDGQPVCQR---H 75
Cdd:PRK13640 6 VEFKHVSFTY----PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKtvwD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRlGKMSVVFQDYKSSlhpyF---NVRQILNEALSQCDTPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIA 152
Cdd:PRK13640 82 IR-EKVGIVFQNPDNQ----FvgaTVGDDVAFGLENRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 153 RAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVyLCEDLIIFNDGQIqerlnrhqlktLQ 232
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKL-----------LA 223
|
250
....*....|...
gi 1717358098 233 NDYTRELFEKQFM 245
Cdd:PRK13640 224 QGSPVEIFSKVEM 236
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-221 |
2.67e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 110.40 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTV---MLDGQPVC----- 72
Cdd:PRK11701 6 LLSVRGLTKLY------GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrMRDGQLRDlyals 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 73 ---QRH---TRLGkmsVVFQDYKSSLHP-------------------YFNVRQilnealsqcdtpvddkeahmTAL--LE 125
Cdd:PRK11701 80 eaeRRRllrTEWG---FVHQHPRDGLRMqvsaggnigerlmavgarhYGDIRA--------------------TAGdwLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 126 RVGLSAAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAV 205
Cdd:PRK11701 137 RVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVAR 216
|
250
....*....|....*.
gi 1717358098 206 YLCEDLIIFNDGQIQE 221
Cdd:PRK11701 217 LLAHRLLVMKQGRVVE 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-246 |
2.77e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 110.22 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTV-----MLDG-QPVCQR 74
Cdd:PRK11264 3 AIEVKNLVKKFHG------QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 75 HTRLGKM----SVVFQDYksSLHPYFNV-RQILNEALSQCDTPVDDKEAHMTALLERVGLSAAfLNKYPQMMSGGEAQRV 149
Cdd:PRK11264 77 KGLIRQLrqhvGFVFQNF--NLFPHRTVlENIIEGPVIVKGEPKEEATARARELLAKVGLAGK-ETSYPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 150 AIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQAAVYLCEDLIIFNDGQIQErlnRHQLK 229
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVE---QGPAK 229
|
250 260
....*....|....*....|.
gi 1717358098 230 TL----QNDYTRELFEKQFMN 246
Cdd:PRK11264 230 ALfadpQQPRTRQFLEKFLLQ 250
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-239 |
2.86e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 115.34 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSgvKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDG------------ 68
Cdd:PRK10261 12 VLAVENLNIAFMQ--EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvie 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 69 ---QPVCQ-RHTRLGKMSVVFQDYKSSLHPYFNVRQILNEALsQCDTPVDDKEAHMTA--LLERVGL--SAAFLNKYPQM 140
Cdd:PRK10261 90 lseQSAAQmRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESI-RLHQGASREEAMVEAkrMLDQVRIpeAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 141 MSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQ 220
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260
....*....|....*....|
gi 1717358098 221 ERLNRHQL-KTLQNDYTREL 239
Cdd:PRK10261 249 ETGSVEQIfHAPQHPYTRAL 268
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-240 |
2.95e-29 |
|
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: 109.94 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRsgvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQ-----PVCQRhT 76
Cdd:cd03218 1 LRAENLSKRYG------KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklPMHKR-A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 77 RLGkMSVVFQDykSSLHPYFNVRQILNEALSQcdTPVDDKEAH--MTALLERVGLsAAFLNKYPQMMSGGEAQRVAIARA 154
Cdd:cd03218 74 RLG-IGYLPQE--ASIFRKLTVEENILAVLEI--RGLSKKEREekLEELLEEFHI-THLRKSKASSLSGGERRRVEIARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 155 VITNPDYIVLDEAISALD-MSIQSqILDLLTTLRDKyQLSlIFIT-HDIQAAVYLCEDLIIFNDGQIQERLNRHQLktLQ 232
Cdd:cd03218 148 LATNPKFLLLDEPFAGVDpIAVQD-IQKIIKILKDR-GIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEI--AA 222
|
....*...
gi 1717358098 233 NDYTRELF 240
Cdd:cd03218 223 NELVRKVY 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
23-221 |
3.75e-29 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 111.74 E-value: 3.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 23 VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPD---TGTVMLDGQPVC---QRH---TRLGKMSVVFQDYKSSLH 93
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILnlpEKElnkLRAEQISMIFQDPMTSLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 94 PYFNVRQILNEALsQCDTPVDDKEAHMTA--LLERVGLSAAF--LNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAIS 169
Cdd:PRK09473 112 PYMRVGEQLMEVL-MLHKGMSKAEAFEESvrMLDAVKMPEARkrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 170 ALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:PRK09473 191 ALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-245 |
1.45e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 110.58 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVkrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGKM 81
Cdd:PRK11432 7 VVLKNITKRFGSNT------VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 SVVFQDYksSLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVITNPDY 161
Cdd:PRK11432 81 CMVFQSY--ALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDL-AGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 162 IVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQerlnrhQLKTLQNDYTR--EL 239
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM------QIGSPQELYRQpaSR 231
|
....*.
gi 1717358098 240 FEKQFM 245
Cdd:PRK11432 232 FMASFM 237
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-219 |
1.56e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 107.75 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRsgvkrqkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQ-----PVCQRh 75
Cdd:PRK10771 1 MLKLTDITWLYH--------HLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttPPSRR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 trlgKMSVVFQDykSSLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAV 155
Cdd:PRK10771 72 ----PVSMLFQE--NNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIED-LLARLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717358098 156 ITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-223 |
1.57e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 107.98 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ------- 73
Cdd:PRK11629 5 LLQCDNLCKRYQEG--SVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaaka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 74 --RHTRLGkmsVVFQDYKssLHPYFNVRQilNEALSQCDTPVDDKEAHMTAL--LERVGLsAAFLNKYPQMMSGGEAQRV 149
Cdd:PRK11629 83 elRNQKLG---FIYQFHH--LLPDFTALE--NVAMPLLIGKKKPAEINSRALemLAAVGL-EHRANHRPSELSGGERQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717358098 150 AIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIfNDGQIQERL 223
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEM-RDGRLTAEL 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-219 |
2.00e-28 |
|
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: 108.20 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrSGVKrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPV--------C 72
Cdd:COG0411 4 LLEVRGLTKRF-GGLV-----AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpphriA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 73 QR-------HTRL-GKMSVvFQdyksslhpyfNVR---------QILNEALSQCDTPVDDKEAHMTA--LLERVGLsAAF 133
Cdd:COG0411 78 RLgiartfqNPRLfPELTV-LE----------NVLvaaharlgrGLLAALLRLPRARREEREARERAeeLLERVGL-ADR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 134 LNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLII 213
Cdd:COG0411 146 ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVV 225
|
....*.
gi 1717358098 214 FNDGQI 219
Cdd:COG0411 226 LDFGRV 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-221 |
2.37e-28 |
|
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: 105.86 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYrsgvKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqrhtrlgkm 81
Cdd:cd03247 1 LSINNVSFSY----PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 svvfQDYKSSLHPYFNVrqilneaLSQcdtpvddkEAHM--TALLERVGLSaaflnkypqmMSGGEAQRVAIARAVITNP 159
Cdd:cd03247 67 ----SDLEKALSSLISV-------LNQ--------RPYLfdTTLRNNLGRR----------FSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717358098 160 DYIVLDEAISALDMSIQSQILDLL-TTLRDKyqlSLIFITHDIQAAVYLceDLIIF-NDGQIQE 221
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIfEVLKDK---TLIWITHHLTGIEHM--DKILFlENGKIIM 176
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-235 |
2.40e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 112.89 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ-------R 74
Cdd:TIGR00958 479 IEFQDVSFSYPN---RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhhylhR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 75 HTRL-GKMSVVFQDyksslhpyfNVRQILNEALSQCDtpvddkEAHMTALLERVGlSAAFLNKYPQ-----------MMS 142
Cdd:TIGR00958 556 QVALvGQEPVLFSG---------SVRENIAYGLTDTP------DEEIMAAAKAAN-AHDFIMEFPNgydtevgekgsQLS 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 143 GGEAQRVAIARAVITNPDYIVLDEAISALDmsiqSQILDLLTTLRDKYQLSLIFITHDIQaAVYLCEDLIIFNDGQIQER 222
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLS-TVERADQILVLKKGSVVEM 694
|
250
....*....|...
gi 1717358098 223 LNRHQLKTLQNDY 235
Cdd:TIGR00958 695 GTHKQLMEDQGCY 707
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-221 |
4.95e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.31 E-value: 4.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVmldgqpvcQRHTRLgK 80
Cdd:COG0488 315 VLELEGLSKSY------GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------KLGETV-K 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSVVFQDYkSSLHPYFNVRQILNEALSqcdtpvDDKEAHMTALLERVGLSAAFLNKYPQMMSGGEAQRVAIARAVITNPD 160
Cdd:COG0488 380 IGYFDQHQ-EELDPDKTVLDELRDGAP------GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717358098 161 YIVLDEAISALDmsIQSqiLDLLTTLRDKYQLSLIFITHD---IQAavyLCEDLIIFNDGQIQE 221
Cdd:COG0488 453 VLLLDEPTNHLD--IET--LEALEEALDDFPGTVLLVSHDryfLDR---VATRILEFEDGGVRE 509
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-243 |
1.13e-27 |
|
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: 105.70 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 3 EVQNVTKSYRSgvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ---RHTRlG 79
Cdd:cd03249 2 EFKNVSFRYPS---RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlnlRWLR-S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQD---YKSSLhpYFNVRQILNEAlsqcdTPVDDKEAHMTALLERvglsaaFLNKYPQ-----------MMSGGE 145
Cdd:cd03249 78 QIGLVSQEpvlFDGTI--AENIRYGKPDA-----TDEEVEEAAKKANIHD------FIMSLPDgydtlvgergsQLSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 146 AQRVAIARAVITNPDYIVLDEAISALDMSIQSQI---LDLLTTLRdkyqlSLIFITH---DIQAAvylceDLII-FNDGQ 218
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAESEKLVqeaLDRAMKGR-----TTIVIAHrlsTIRNA-----DLIAvLQNGQ 214
|
250 260
....*....|....*....|....*
gi 1717358098 219 IQERLNRHQLKTLQNDYtRELFEKQ 243
Cdd:cd03249 215 VVEQGTHDELMAQKGVY-AKLVKAQ 238
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-221 |
1.97e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 105.82 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 19 KRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGKMSV--------------- 83
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVadknqlrllrtrltm 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 84 VFQDYksSLHPYFNVRQILNEALSQCdTPVDDKEAHMTAL--LERVGLSAAFLNKYPQMMSGGEAQRVAIARAVITNPDY 161
Cdd:PRK10619 97 VFQHF--NLWSHMTVLENVMEAPIQV-LGLSKQEARERAVkyLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 162 IVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-204 |
2.40e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 105.10 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDG------QPVCQRH 75
Cdd:PRK11124 3 IQLNGINCFYGA------HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRLGKMSV--VFQDYksSLHPYFNVRQILNEAlsqcdtP-----VDDKEAHMTA--LLERVGLsAAFLNKYPQMMSGGEA 146
Cdd:PRK11124 77 IRELRRNVgmVFQQY--NLWPHLTVQQNLIEA------PcrvlgLSKDQALARAekLLERLRL-KPYADRFPLHLSGGQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 147 QRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAA 204
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVA 204
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
21-241 |
5.14e-27 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 106.14 E-value: 5.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 21 QIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTgTV-----MLDGQ-----PVCQRHTRLGK-MSVVFQDYK 89
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNW-HVtadrfRWNGIdllklSPRERRKIIGReIAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 90 SSLHPYFNVRQILNEALSQCDTPV------DDKEAHMTALLERVGL--SAAFLNKYPQMMSGGEAQRVAIARAVITNPDY 161
Cdd:COG4170 100 SCLDPSAKIGDQLIEAIPSWTFKGkwwqrfKWRKKRAIELLHRVGIkdHKDIMNSYPHELTEGECQKVMIAMAIANQPRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 162 IVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQ-LKTLQNDYTRELF 240
Cdd:COG4170 180 LIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQiLKSPHHPYTKALL 259
|
.
gi 1717358098 241 E 241
Cdd:COG4170 260 R 260
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-219 |
1.25e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.08 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTksyrsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR-LG 79
Cdd:PRK09536 3 MIDVSDLS------VEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARaAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 K-MSVVFQDykSSLHPYFNVRQILNEA----LSQCDTPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIARA 154
Cdd:PRK09536 77 RrVASVPQD--TSLSFEFDVRQVVEMGrtphRSRFDTWTETDRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717358098 155 VITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFItHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRV 217
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-219 |
2.28e-26 |
|
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: 101.09 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILG--IEKPDTGTVMLDGQPVCQRHTRlG 79
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFR-K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQDykSSLHPYFNVRqilnEALsqcdtpvddkeaHMTALLERVglsaaflnkypqmmSGGEAQRVAIARAVITNP 159
Cdd:cd03213 83 IIGYVPQD--DILHPTLTVR----ETL------------MFAAKLRGL--------------SGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717358098 160 DYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVY-LCEDLIIFNDGQI 219
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSEIFeLFDKLLLLSQGRV 190
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-217 |
3.62e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 104.14 E-value: 3.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVkrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRhTRLGKM 81
Cdd:PRK13536 42 IDLAGVSKSYGDKA------VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR-ARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 SVVFQDYKSSLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLSAAfLNKYPQMMSGGEAQRVAIARAVITNPDY 161
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESK-ADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 162 IVLDEAISALDMSIQSQILDLLTTL--RDKyqlSLIFITHDIQAAVYLCEDLIIFNDG 217
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLlaRGK---TILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-219 |
5.94e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 103.77 E-value: 5.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGVkrqkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGK 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKT-----QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSVVFQDYksSLHPYFNVRQILNEALSQCDTPVDDKEahmtallERVGLSA------AFLNKYPQMMSGGEAQRVAIARA 154
Cdd:PRK11650 78 IAMVFQNY--ALYPHMSVRENMAYGLKIRGMPKAEIE-------ERVAEAArilelePLLDRKPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 155 VITNPDYIVLDEAISALD------MSIQSQILD--LLTTlrdkyqlSLiFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDaklrvqMRLEIQRLHrrLKTT-------SL-YVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-199 |
1.30e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.50 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 20 RQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILG--------IEKPDTGTVMLdgqpVCQRhtrlgkmsvvfqdykss 91
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwpygsgrIARPAGARVLF----LPQR----------------- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 92 lhPYF---NVRQILneALSQCDTPVDDKEahMTALLERVGLsAAFLNKY------PQMMSGGEAQRVAIARAVITNPDYI 162
Cdd:COG4178 435 --PYLplgTLREAL--LYPATAEAFSDAE--LREALEAVGL-GHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWL 507
|
170 180 190
....*....|....*....|....*....|....*...
gi 1717358098 163 VLDEAISALDMSIQSQILDLL-TTLRDkyqLSLIFITH 199
Cdd:COG4178 508 FLDEATSALDEENEAALYQLLrEELPG---TTVISVGH 542
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-219 |
1.64e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.93 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC-QRHT--- 76
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdEENLwdi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 77 RlGKMSVVFQDYKSSLhpyfnVRQILNE--ALSQCDTPVDDKE--AHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIA 152
Cdd:PRK13633 84 R-NKAGMVFQNPDNQI-----VATIVEEdvAFGPENLGIPPEEirERVDESLKKVGMYE-YRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 153 RAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYlCEDLIIFNDGQI 219
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-219 |
1.77e-25 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 102.26 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 37 AIIGESGSGKSTLARMILGIEKPDTGTVMLDGQ-----------PVCQRHtrlgkMSVVFQDykSSLHPYFNVRQILNEA 105
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclPPEKRR-----IGYVFQD--ARLFPHYKVRGNLRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 106 LSQCDTPVDDKeahMTALLervGLsAAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTT 185
Cdd:PRK11144 101 MAKSMVAQFDK---IVALL---GI-EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190
....*....|....*....|....*....|....
gi 1717358098 186 LRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK11144 174 LAREINIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-219 |
2.31e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.89 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKRQKRQIvKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLG-- 79
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKKAL-DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 --KMSVVFQDYKSSLHPYFNVRQI----LNEALSQCDTPVDDKEAhmtalLERVGLS-AAFLNKYPQMMSGGEAQRVAIA 152
Cdd:PRK13637 82 rkKVGLVFQYPEYQLFEETIEKDIafgpINLGLSEEEIENRVKRA-----MNIVGLDyEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 153 RAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
6-228 |
2.32e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.01 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 6 NVTKSYRSGVKRQKrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ-------RHTRl 78
Cdd:PRK13646 7 NVSYTYQKGTPYEH-QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyiRPVR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 79 GKMSVVFQDYKSSLHPYFNVRQILNeALSQCDTPVDDKEAHMTALLERVGLSAAFLNKYPQMMSGGEAQRVAIARAVITN 158
Cdd:PRK13646 85 KRIGMVFQFPESQLFEDTVEREIIF-GPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 159 PDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQL 228
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
3.35e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.78 E-value: 3.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGVKRQKRqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQR--HTRL 78
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKR-ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpeYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 79 GKMSVVFQDYKS----------------------SLHPYFN--VRQILNEALSQCDTpvdDKEAHMTAlleRVGLsaafl 134
Cdd:COG1101 80 KYIGRVFQDPMMgtapsmtieenlalayrrgkrrGLRRGLTkkRRELFRELLATLGL---GLENRLDT---KVGL----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 135 nkypqmMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIF 214
Cdd:COG1101 149 ------LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMM 222
|
....*
gi 1717358098 215 NDGQI 219
Cdd:COG1101 223 HEGRI 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-220 |
3.93e-25 |
|
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: 98.42 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRsgvkrqKRQIVKQVSFQCSKGQsIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC-QRHTRLGK 80
Cdd:cd03264 1 LQLENLTKRYG------KKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLkQPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSVVFQDYksSLHPYFNVRQILN--EALSQCDTPVDDKEAHMtaLLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVITN 158
Cdd:cd03264 74 IGYLPQEF--GVYPNFTVREFLDyiAWLKGIPSKEVKARVDE--VLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 159 PDYIVLDEAISALDMSIQSQILDLLTTL-RDKyqlSLIFITHDIQAAVYLCEDLIIFNDGQIQ 220
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELgEDR---IVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
33-220 |
1.25e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 98.94 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 33 GQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLdGQPVCQRHTR-------LGKMSVVFQdyksslhpyFNVRQILNEA 105
Cdd:PRK13634 33 GSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKnkklkplRKKVGIVFQ---------FPEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 106 LSQ--CDTP----VDDKEAHMTA--LLERVGLSAAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQS 177
Cdd:PRK13634 103 VEKdiCFGPmnfgVSEEDAKQKAreMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1717358098 178 QILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQ 220
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-219 |
1.31e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.85 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR-LG 79
Cdd:COG4604 1 MIEIKNVSKRY------GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSReLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 K-MSVVFQDykSSLHPYFNVRQILN--------EALSQCDtpvddkEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVA 150
Cdd:COG4604 75 KrLAILRQE--NHINSRLTVRELVAfgrfpyskGRLTAED------REIIDEAIAYLDLED-LADRYLDELSGGQRQRAF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717358098 151 IARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDI-QAAVYlcEDLII-FNDGQI 219
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDInFASCY--ADHIVaMKDGRV 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-219 |
1.42e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.72 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARmILG-IEKPDTGTVMLDGQPVCQRHT--- 76
Cdd:PRK10535 4 LLELKDIRRSYPSG--EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGcLDKPTSGTYRVAGQDVATLDAdal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 77 ---RLGKMSVVFQDYKssLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIAR 153
Cdd:PRK10535 81 aqlRREHFGFIFQRYH--LLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717358098 154 AVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQAAVYlCEDLIIFNDGQI 219
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-219 |
1.46e-24 |
|
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: 101.42 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTV----------MLDGQP 70
Cdd:TIGR03269 279 IIKVRNVSKRYIS-VDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 71 VCQ-RHTRLgkMSVVFQDYksSLHPYFNVRQILNEALSqCDTPvdDKEAHMTAL--LERVGLS----AAFLNKYPQMMSG 143
Cdd:TIGR03269 358 DGRgRAKRY--IGILHQEY--DLYPHRTVLDNLTEAIG-LELP--DELARMKAVitLKMVGFDeekaEEILDKYPDELSE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717358098 144 GEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-221 |
1.90e-24 |
|
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: 96.83 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKRQ----------------KRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVm 65
Cdd:cd03220 1 IELENVSKSYPTYKGGSsslkklgilgrkgevgEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 66 ldgqpvcqrhTRLGKMSVVFqDYKSSLHPYFNVRQ--ILNEALSQCDTpvDDKEAHMTALLERVGLsAAFLNKYPQMMSG 143
Cdd:cd03220 80 ----------TVRGRVSSLL-GLGGGFNPELTGREniYLNGRLLGLSR--KEIDEKIDEIIEFSEL-GDFIDLPVKTYSS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 144 GEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
1.92e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 98.34 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGVKrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGK 80
Cdd:PRK13652 3 LIETRDLCYSYSGSKE-----ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSV--VFQDYKSSLhpyFNVRQILNEALSQCDTPVDDK--EAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVI 156
Cdd:PRK13652 78 KFVglVFQNPDDQI---FSPTVEQDIAFGPINLGLDEEtvAHRVSSALHMLGLEE-LRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 157 TNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
2.03e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 99.01 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSY-------------RSGVKRQKRQI--VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVM 65
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkgalKGLFRREYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 66 LDG-QPVCQRHTRLGKMSVVF-QdyKSSLHPYFNVRQI--LNEALSQcdtpVDDKE-----AHMTALLErVGlsaAFLNK 136
Cdd:COG4586 81 VLGyVPFKRRKEFARRIGVVFgQ--RSQLWWDLPAIDSfrLLKAIYR----IPDAEykkrlDELVELLD-LG---ELLDT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 137 YPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFND 216
Cdd:COG4586 151 PVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH 230
|
...
gi 1717358098 217 GQI 219
Cdd:COG4586 231 GRI 233
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-200 |
2.43e-24 |
|
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: 100.90 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ-RHTRLGK 80
Cdd:TIGR02868 335 LELRDLSAGYPGA-----PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 -MSVVFQD---YKSSlhpyfnVRQilNEALSQCDtpVDDKEahMTALLERVGLsAAFLNKYP-----------QMMSGGE 145
Cdd:TIGR02868 410 rVSVCAQDahlFDTT------VRE--NLRLARPD--ATDEE--LWAALERVGL-ADWLRALPdgldtvlgeggARLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1717358098 146 AQRVAIARAVITNPDYIVLDEAISALDMSIQSQIL-DLLTTLRDKyqlSLIFITHD 200
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLeDLLAALSGR---TVVLITHH 529
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-218 |
4.27e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.95 E-value: 4.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRhTRLGKM 81
Cdd:PRK13537 8 IDFRNVEKRY------GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR-ARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 SVVFQDYKSSLHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLSAAFLNKYPQmMSGGEAQRVAIARAVITNPDY 161
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE-LSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717358098 162 IVLDEAISALDMSIQSQILDLLTTL--RDKyqlSLIFITHDIQAAVYLCEDLIIFNDGQ 218
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLlaRGK---TILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-221 |
4.46e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 96.30 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGVKRQKR----------------QIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTV 64
Cdd:COG1134 4 MIEVENVSKSYRLYHEPSRSlkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 65 mldgqpvcqrhTRLGKMSVVFqDYKSSLHPYFNVRQ--ILNEAL---SQCDtpvddkeahMTALLERV----GLSAAF-- 133
Cdd:COG1134 84 -----------EVNGRVSALL-ELGAGFHPELTGREniYLNGRLlglSRKE---------IDEKFDEIvefaELGDFIdq 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 134 -LNKYpqmmSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQAAVYLCEDLI 212
Cdd:COG1134 143 pVKTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAI 217
|
....*....
gi 1717358098 213 IFNDGQIQE 221
Cdd:COG1134 218 WLEKGRLVM 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-220 |
4.70e-24 |
|
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: 100.21 E-value: 4.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTksYRSGvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ-RHTRLGK 80
Cdd:COG4618 331 LSVENLT--VVPP--GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 M------SVVFqdyksslhpyFN--VRQ-I--LNEAlsqcdtpvDDKEAHMTAllERVGLSAAFLnKYPQ---------- 139
Cdd:COG4618 407 HigylpqDVEL----------FDgtIAEnIarFGDA--------DPEKVVAAA--KLAGVHEMIL-RLPDgydtrigegg 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 140 -MMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDiQAAVYLCEDLIIFNDGQ 218
Cdd:COG4618 466 aRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHR-PSLLAAVDKLLVLRDGR 543
|
..
gi 1717358098 219 IQ 220
Cdd:COG4618 544 VQ 545
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-201 |
5.22e-24 |
|
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: 100.05 E-value: 5.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ--RHTRLG 79
Cdd:TIGR02857 322 LEFSGVSVAYPG-----RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADadADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQdyksslHPYFNVRQIL-NEALSQCDTPvddkEAHMTALLERVGLsAAFLNKYPQM-----------MSGGEAQ 147
Cdd:TIGR02857 397 QIAWVPQ------HPFLFAGTIAeNIRLARPDAS----DAEIREALERAGL-DEFVAALPQGldtpigeggagLSGGQAQ 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1717358098 148 RVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYqlSLIFITHDI 201
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRL 517
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-219 |
8.50e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.70 E-value: 8.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRsgvKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHT--RL 78
Cdd:PRK13642 4 ILEVENLVFKYE---KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwnLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 79 GKMSVVFQDYKSSLHPYfNVRQILNEALSQCDTPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVITN 158
Cdd:PRK13642 81 RKIGMVFQNPDNQFVGA-TVEDDVAFGMENQGIPREEMIKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717358098 159 PDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYlCEDLIIFNDGQI 219
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-219 |
1.04e-23 |
|
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: 94.81 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRsgvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPV----CQRHTR 77
Cdd:cd03224 1 LEVENLNAGYG------KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItglpPHERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 LGkMSVVFQDykSSLHPYFNVRQ-ILNEALSQCDTPVDDKEAHMTALLERVglsAAFLNKYPQMMSGGEAQRVAIARAVI 156
Cdd:cd03224 75 AG-IGYVPEG--RRIFPELTVEEnLLLGAYARRRAKRKARLERVYELFPRL---KERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 157 TNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-219 |
1.14e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 97.79 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 6 NVTKSYRSGVkrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQ-----PVCQRhtrlgK 80
Cdd:PRK11000 8 NVTKAYGDVV------ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvPPAER-----G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSVVFQDYksSLHPYFNVRQilNEA----LSQCDTPVDDKEAHMTAllERVGLsAAFLNKYPQMMSGGEAQRVAIARAVI 156
Cdd:PRK11000 77 VGMVFQSY--ALYPHLSVAE--NMSfglkLAGAKKEEINQRVNQVA--EVLQL-AHLLDRKPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 157 TNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-200 |
1.37e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 4 VQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLdgqpvcQRHTRLGKMS- 82
Cdd:COG0488 1 LENLSKSF------GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI------PKGLRIGYLPq 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 83 -VVFQDYKS-------SLHPYFNVRQILNEALSQCDTPVDDK------------------EAHMTALLERVGLSAAFLNK 136
Cdd:COG0488 69 ePPLDDDLTvldtvldGDAELRALEAELEELEAKLAEPDEDLerlaelqeefealggweaEARAEEILSGLGFPEEDLDR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717358098 137 YPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDmsIQSqILDLLTTLRDkYQLSLIFITHD 200
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LES-IEWLEEFLKN-YPGTVLVVSHD 208
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-201 |
1.47e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 94.56 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR--- 77
Cdd:PRK10908 1 MIRFEHVSKAYLGG-----RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 --LGKMSVVFQDYKSSLHP--YFNVRQILNEAlsqcDTPVDDKEAHMTALLERVGLsaafLNK---YPQMMSGGEAQRVA 150
Cdd:PRK10908 76 flRRQIGMIFQDHHLLMDRtvYDNVAIPLIIA----GASGDDIRRRVSAALDKVGL----LDKaknFPIQLSGGEQQRVG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1717358098 151 IARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLrDKYQLSLIFITHDI 201
Cdd:PRK10908 148 IARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDI 197
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
1.71e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.68 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGVkrqkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqRHTRLGK 80
Cdd:PRK13636 5 ILKVEELNYNYSDGT-----HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI--DYSRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MS------VVFQDYKSSLHPYfNVRQILNEALSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARA 154
Cdd:PRK13636 78 MKlresvgMVFQDPDNQLFSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717358098 155 VITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-228 |
1.97e-23 |
|
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: 98.35 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQP---VCQRHTRl 78
Cdd:COG5265 358 VRFENVSFGYDPE-----RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDirdVTQASLR- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 79 GKMSVVFQD---YKSSLhpYFNVR------------------QILN--EALSQ-CDTPVDdkeahmtallERvGLsaafl 134
Cdd:COG5265 432 AAIGIVPQDtvlFNDTI--AYNIAygrpdaseeeveaaaraaQIHDfiESLPDgYDTRVG----------ER-GL----- 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 135 nkypqMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLL-------TTLRDKYQLSLIfithdIQAavyl 207
Cdd:COG5265 494 -----KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALrevargrTTLVIAHRLSTI-----VDA---- 559
|
250 260
....*....|....*....|..
gi 1717358098 208 ceDLII-FNDGQIQERLNRHQL 228
Cdd:COG5265 560 --DEILvLEAGRIVERGTHAEL 579
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-188 |
3.59e-23 |
|
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: 93.49 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 16 KRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILG-IEKPDT--GTVMLDGQPVcQRHTRLGKMSVVFQDykSSL 92
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGTtsGQILFNGQPR-KPDQFQKCVAYVRQD--DIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 93 HPYFNVRQILNEAlSQCDTPVDDKEAHMTALLERVGLSAAFL----NKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAI 168
Cdd:cd03234 93 LPGLTVRETLTYT-AILRLPRKSSDAIRKKRVEDVLLRDLALtrigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180
....*....|....*....|
gi 1717358098 169 SALDMSIQsqiLDLLTTLRD 188
Cdd:cd03234 172 SGLDSFTA---LNLVSTLSQ 188
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-202 |
3.74e-23 |
|
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: 93.69 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ-RHTRL-G 79
Cdd:cd03248 12 VKFQNVTFAYPT---RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLhS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQDyksslhPYFNVRQILNE---ALSQCDTPvDDKEAHMTAllervgLSAAFLNKYPQ-----------MMSGGE 145
Cdd:cd03248 89 KVSLVGQE------PVLFARSLQDNiayGLQSCSFE-CVKEAAQKA------HAHSFISELASgydtevgekgsQLSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 146 AQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTtlRDKYQLSLIFITHDIQ 202
Cdd:cd03248 156 KQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALY--DWPERRTVLVIAHRLS 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-187 |
9.07e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.57 E-value: 9.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 3 EVQNVTKSYRSgvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ------RHT 76
Cdd:PRK13657 336 EFDDVSFSYDN-----SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvtraslRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 77 rlgkMSVVFQDykSSLhpyFNvRQIlNEALSQCDTpvDDKEAHMTALLERvglSAA--FLNKYPQ-----------MMSG 143
Cdd:PRK13657 411 ----IAVVFQD--AGL---FN-RSI-EDNIRVGRP--DATDEEMRAAAER---AQAhdFIERKPDgydtvvgergrQLSG 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1717358098 144 GEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLR 187
Cdd:PRK13657 475 GERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELM 518
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-235 |
1.47e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 95.66 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYrsgvKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ------RH 75
Cdd:PRK11160 339 LTLNNVSFTY----PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADyseaalRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TrlgkMSVVFQdyksSLHpyfnvrqILNEALSQ-----CDTPVDDKeahMTALLERVGLSA---------AFLNKYPQMM 141
Cdd:PRK11160 415 A----ISVVSQ----RVH-------LFSATLRDnlllaAPNASDEA---LIEVLQQVGLEKlleddkglnAWLGEGGRQL 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 142 SGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTL-RDKyqlSLIFITHDIQAAVYLceDLI-IFNDGQI 219
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaQNK---TVLMITHRLTGLEQF--DRIcVMDNGQI 551
|
250
....*....|....*.
gi 1717358098 220 QERLNRHQLKTLQNDY 235
Cdd:PRK11160 552 IEQGTHQELLAQQGRY 567
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-237 |
2.33e-22 |
|
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: 91.52 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqRHTRLG-- 79
Cdd:cd03251 1 VEFKNVTFRYPG----DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV--RDYTLAsl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 --KMSVVFQDyksslhPY-FN--VRQilNEALSQCDTPVDDKE--AHMTALLErvglsaaFLNKYPQ-----------MM 141
Cdd:cd03251 75 rrQIGLVSQD------VFlFNdtVAE--NIAYGRPGATREEVEeaARAANAHE-------FIMELPEgydtvigergvKL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 142 SGGEAQRVAIARAVITNPDYIVLDEAISALD----MSIQSQILDLL---TTLRDKYQLSLIFITHDIqaavylcedlIIF 214
Cdd:cd03251 140 SGGQRQRIAIARALLKDPPILILDEATSALDteseRLVQAALERLMknrTTFVIAHRLSTIENADRI----------VVL 209
|
250 260
....*....|....*....|...
gi 1717358098 215 NDGQIQERLNRHQLKTLQNDYTR 237
Cdd:cd03251 210 EDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-243 |
3.79e-22 |
|
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: 91.01 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQ------PVCQRH 75
Cdd:cd03252 1 ITFEHVRFRYKP----DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaladPAWLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 trlgKMSVVFQDyksslHPYFNVRQILNEALSqcdtpvdDKEAHMTALLERVGLSAA--FLNKYPQ-----------MMS 142
Cdd:cd03252 77 ----QVGVVLQE-----NVLFNRSIRDNIALA-------DPGMSMERVIEAAKLAGAhdFISELPEgydtivgeqgaGLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 143 GGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYqlSLIFITHDIqAAVYLCEDLIIFNDGQIQER 222
Cdd:cd03252 141 GGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRL-STVKNADRIIVMEKGRIVEQ 217
|
250 260
....*....|....*....|.
gi 1717358098 223 lNRHQLKTLQNDYTRELFEKQ 243
Cdd:cd03252 218 -GSHDELLAENGLYAYLYQLQ 237
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-218 |
4.11e-22 |
|
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: 90.96 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSY----RSGVKRQkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVML--DGQPV--C 72
Cdd:COG4778 4 LLEVENLSKTFtlhlQGGKRLP---VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 73 Q---------RHTRLGKMS----VVfqdyksslhPYFNVRQILNEALsqCDTPVDDKEAHMTA--LLERVGLSAAFLNKY 137
Cdd:COG4778 81 QaspreilalRRRTIGYVSqflrVI---------PRVSALDVVAEPL--LERGVDREEARARAreLLARLNLPERLWDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 138 PQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDG 217
Cdd:COG4778 150 PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
.
gi 1717358098 218 Q 218
Cdd:COG4778 229 S 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-243 |
4.63e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.81 E-value: 4.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKRQKrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLG-- 79
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEK-KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 ----KMSVVFQDYKSSLHPYFNVRQI----LNEALSqcdtpvdDKEAHMTAL--LERVGLSAAFLNKYPQMMSGGEAQRV 149
Cdd:PRK13641 82 klrkKVSLVFQFPEAQLFENTVLKDVefgpKNFGFS-------EDEAKEKALkwLKKVGLSEDLISKSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 150 AIARAVITNPDYIVLDEAISALDMSIQSQILDLLTtlrdKYQL---SLIFITHDIQAAVYLCEDLIIFNDGqiqeRLNRH 226
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFK----DYQKaghTVILVTHNMDDVAEYADDVLVLEHG----KLIKH 226
|
250
....*....|....*..
gi 1717358098 227 qlktlqnDYTRELFEKQ 243
Cdd:PRK13641 227 -------ASPKEIFSDK 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-244 |
7.61e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 93.63 E-value: 7.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqRHTRLG-- 79
Cdd:TIGR02203 331 VEFRNVTFRYPG----RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL--ADYTLAsl 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 --KMSVVFQDYKsslhpYFNVRQILNEALSQCDTpVDDKEahmtalLERVgLSAA----FLNKYPQ-----------MMS 142
Cdd:TIGR02203 405 rrQVALVSQDVV-----LFNDTIANNIAYGRTEQ-ADRAE------IERA-LAAAyaqdFVDKLPLgldtpigengvLLS 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 143 GGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLL-------TTLRDKYQLSlifithDIQAAvylcEDLIIFN 215
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALerlmqgrTTLVIAHRLS------TIEKA----DRIVVMD 541
|
250 260
....*....|....*....|....*....
gi 1717358098 216 DGQIQERLNRHQLKTLQNDYTReLFEKQF 244
Cdd:TIGR02203 542 DGRIVERGTHNELLARNGLYAQ-LHNMQF 569
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-220 |
1.05e-21 |
|
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: 90.08 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYR-------------SGVKRQKRQI--VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVML 66
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligslkSLFKRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 67 DGQ-PVCQRHTRLGKMSVVFQDyKSSLHPYFNVRQ--ILNEALSQCDtPVDDKE--AHMTALLErvglSAAFLNKYPQMM 141
Cdd:cd03267 81 AGLvPWKRRKKFLRRIGVVFGQ-KTQLWWDLPVIDsfYLLAAIYDLP-PARFKKrlDELSELLD----LEELLDTPVRQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717358098 142 SGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQ 220
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
1.27e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.92 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKRQkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLdgqpvCQRHTRLGKM 81
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTE-LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW-----IFKDEKNKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 SVVFQDYKSSL---HPYF----NVRQI--------------LNEALSQCDT-------PVDDKEAHMTAL--LERVGLSA 131
Cdd:PRK13651 77 TKEKEKVLEKLviqKTRFkkikKIKEIrrrvgvvfqfaeyqLFEQTIEKDIifgpvsmGVSKEEAKKRAAkyIELVGLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 132 AFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQAAVYLCEDL 211
Cdd:PRK13651 157 SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRT 235
|
....*...
gi 1717358098 212 IIFNDGQI 219
Cdd:PRK13651 236 IFFKDGKI 243
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
17-201 |
3.18e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.44 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 17 RQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQ--PVCQRhTRL----GKMSVVFQDYK- 89
Cdd:PRK11831 17 RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEniPAMSR-SRLytvrKRMSMLFQSGAl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 90 -SSLHPYFNVRQILNEalsqcDTPVDDKEAHMTAL--LERVGLSAAfLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDE 166
Cdd:PRK11831 96 fTDMNVFDNVAYPLRE-----HTQLPAPLLHSTVMmkLEAVGLRGA-AKLMPSELSGGMARRAALARAIALEPDLIMFDE 169
|
170 180 190
....*....|....*....|....*....|....*
gi 1717358098 167 AISALDMSIQSQILDLLTTLRDKYQLSLIFITHDI 201
Cdd:PRK11831 170 PFVGQDPITMGVLVKLISELNSALGVTCVVVSHDV 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-219 |
4.02e-21 |
|
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: 88.20 E-value: 4.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKrqkrqiVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGK- 80
Cdd:cd03265 1 IEVENLVKKYGDFEA------VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSVVFQDyksslhpyfnvrQILNEALSQCDT----------PVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVA 150
Cdd:cd03265 75 IGIVFQD------------LSVDDELTGWENlyiharlygvPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLE 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717358098 151 IARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-199 |
4.81e-21 |
|
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: 86.44 E-value: 4.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVmldgqpvcqrhTRLGKM 81
Cdd:cd03223 1 IELENLSLATPDG-----RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 SVVF--QdyksslHPYF---NVRQILNealsqcdtpvddkeahmtallervglsaaflnkYP--QMMSGGEAQRVAIARA 154
Cdd:cd03223 65 DLLFlpQ------RPYLplgTLREQLI---------------------------------YPwdDVLSGGEQQRLAFARL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1717358098 155 VITNPDYIVLDEAISALDMSIQSQILDLLTTLRdkyqLSLIFITH 199
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-219 |
5.11e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.53 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR-LG 79
Cdd:PRK11231 2 TLRTENLTVGY------GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRqLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 K-MSVVFQ--------------DYKSSlhPYFNvrqiLNEALSQCDtpvddkEAHMTALLERVGLSaAFLNKYPQMMSGG 144
Cdd:PRK11231 76 RrLALLPQhhltpegitvrelvAYGRS--PWLS----LWGRLSAED------NARVNQAMEQTRIN-HLADRRLTDLSGG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717358098 145 EAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-240 |
5.53e-21 |
|
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: 91.34 E-value: 5.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ--RHTRLG 79
Cdd:TIGR01193 474 IVINDVSYSYGYG-----SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDidRHTLRQ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQDyksslhPYFNVRQILNEALSQCDTPVDDKE-------AHMTALLERVGLS-AAFLNKYPQMMSGGEAQRVAI 151
Cdd:TIGR01193 549 FINYLPQE------PYIFSGSILENLLLGAKENVSQDEiwaaceiAEIKDDIENMPLGyQTELSEEGSSISGGQKQRIAL 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 152 ARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyqlSLIFITHDIQAAvYLCEDLIIFNDGQIQERLNRHQLkTL 231
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL-LD 697
|
....*....
gi 1717358098 232 QNDYTRELF 240
Cdd:TIGR01193 698 RNGFYASLI 706
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-199 |
8.83e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.47 E-value: 8.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrSGVKrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR--- 77
Cdd:COG3845 5 ALELRGITKRF-GGVV-----ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdai 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 -LG-KMsvVFQDYksSLHPYFNVRQilNEALSQCDTP---VDDKEAH--MTALLERVGLSAAfLNKYPQMMSGGEAQRVA 150
Cdd:COG3845 79 aLGiGM--VHQHF--MLVPNLTVAE--NIVLGLEPTKggrLDRKAARarIRELSERYGLDVD-PDAKVEDLSVGEQQRVE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1717358098 151 IARAVITNPDYIVLDEAISALdmSIQsQILDLLTTLRdkyQL-----SLIFITH 199
Cdd:COG3845 152 ILKALYRGARILILDEPTAVL--TPQ-EADELFEILR---RLaaegkSIIFITH 199
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-218 |
1.79e-20 |
|
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: 84.42 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDgqpvcqRHTRLGkm 81
Cdd:cd03221 1 IELENLSKTY------GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------STVKIG-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 svvfqdyksslhpYFnvrqilnealsqcdtpvddkeahmtallervglsaaflnkyPQmMSGGEAQRVAIARAVITNPDY 161
Cdd:cd03221 67 -------------YF-----------------------------------------EQ-LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 162 IVLDEAISALDMSIQSQILDLLTtlrdKYQLSLIFITHD---IQAavyLCEDLIIFNDGQ 218
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALK----EYPGTVILVSHDryfLDQ---VATKIIELEDGK 144
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-229 |
2.23e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.49 E-value: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQ-----PVCQRHT 76
Cdd:PRK10895 4 LTAKNLAKAYKG------RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 77 R----LGKMSVVFQdyksSLHPYFNVRQILNealSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIA 152
Cdd:PRK10895 78 RgigyLPQEASIFR----RLSVYDNLMAVLQ---IRDDLSAEQREDRANELMEEFHIEH-LRDSMGQSLSGGERRRVEIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 153 RAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDkYQLSLIFITHDIQAAVYLCEDLIIFNDGQI------QERLNRH 226
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLiahgtpTEILQDE 228
|
...
gi 1717358098 227 QLK 229
Cdd:PRK10895 229 HVK 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-200 |
4.02e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 85.54 E-value: 4.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 20 RQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC--------QRHTRLGKMSVVFQD--YK 89
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlkpeiyrQQVSYCAQTPTLFGDtvYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 90 SSLHPYfnvrQILNealsqcDTPvddKEAHMTALLERVGLSAAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAIS 169
Cdd:PRK10247 100 NLIFPW----QIRN------QQP---DPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190
....*....|....*....|....*....|.
gi 1717358098 170 ALDMSIQSQILDLLTTLRDKYQLSLIFITHD 200
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
5.76e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.94 E-value: 5.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRL--G 79
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-----ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQDYKSSLhpyFNVRQILNEALSQCDTPVDDKEahmtaLLERVG--LSA----AFLNKYPQMMSGGEAQRVAIAR 153
Cdd:PRK13647 80 KVGLVFQDPDDQV---FSSTVWDDVAFGPVNMGLDKDE-----VERRVEeaLKAvrmwDFRDKPPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717358098 154 AVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-199 |
1.48e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 84.35 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTksyrsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEK--PDTGTVMLDGQ-----PVCQR 74
Cdd:COG0396 1 LEIKNLH------VSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEdilelSPDER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 75 hTRLGkMSVVFQdyksslHPY----FNVRQILNEAL-SQCDTPVDDKEAH--MTALLERVGLSAAFLNKYPQM-MSGGEA 146
Cdd:COG0396 75 -ARAG-IFLAFQ------YPVeipgVSVSNFLRTALnARRGEELSAREFLklLKEKMKELGLDEDFLDRYVNEgFSGGEK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1717358098 147 QRVAIARAVITNPDYIVLDEAISALDmsIQS-QIL-DLLTTLRDKyQLSLIFITH 199
Cdd:COG0396 147 KRNEILQMLLLEPKLAILDETDSGLD--IDAlRIVaEGVNKLRSP-DRGILIITH 198
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-204 |
1.56e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.05 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 20 RQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVmldgqpvcqRHTRLGKMSVVFQdyKSSLHPYF--N 97
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------RRAGGARVAYVPQ--RSEVPDSLplT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 98 VRQILNEALSQCDTPV-----DDKEAhMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALD 172
Cdd:NF040873 74 VRDLVAMGRWARRGLWrrltrDDRAA-VDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|..
gi 1717358098 173 MSIQSQILDLLTTLRDKyQLSLIFITHDIQAA 204
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELV 182
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-219 |
2.15e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.45 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 20 RQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGKMSVVFQDYKSSLHPYFNVR 99
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 100 QIL-------NEALSQCDtpVDDKEaHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALD 172
Cdd:PRK10575 104 ELVaigrypwHGALGRFG--AADRE-KVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1717358098 173 MSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-219 |
2.16e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGVKrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLG- 79
Cdd:PRK13644 1 MIRLENVSYSYPDGTP-----ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 --KMSVVFQDYKSSLhpyfnVRQILNEALS-----QCDTPVDDKEAHMTALLErVGLSaAFLNKYPQMMSGGEAQRVAIA 152
Cdd:PRK13644 76 rkLVGIVFQNPETQF-----VGRTVEEDLAfgpenLCLPPIEIRKRVDRALAE-IGLE-KYRHRSPKTLSGGQGQCVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 153 RAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQaAVYLCEDLIIFNDGQI 219
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLE-ELHDADRIIVMDRGKI 213
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-185 |
3.67e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.61 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTksyrsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPvcQRHTRLGK 80
Cdd:PRK13539 2 MLEGEDLA------CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD--IDDPDVAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 mSVVFQDYKSSLHPYFNVRQILN---EALSQCDTPVDdkeahmtALLERVGLSAAFLNKYpQMMSGGEAQRVAIARAVIT 157
Cdd:PRK13539 74 -ACHYLGHRNAMKPALTVAENLEfwaAFLGGEELDIA-------AALEAVGLAPLAHLPF-GYLSAGQKRRVALARLLVS 144
|
170 180
....*....|....*....|....*...
gi 1717358098 158 NPDYIVLDEAISALDMSIQSQILDLLTT 185
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAVALFAELIRA 172
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-209 |
4.43e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.01 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGVKRQKRQIVkQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLdGQPVCQRHTRLG- 79
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 ------KMSVVFQDYKSSLhpyFNVRQILNEALSQCDTPVDDKEAHMTAL--LERVGLSAAFLNKYPQMMSGGEAQRVAI 151
Cdd:PRK13643 79 ikpvrkKVGVVFQFPESQL---FEETVLKDVAFGPQNFGIPKEKAEKIAAekLEMVGLADEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717358098 152 ARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITH------DIQAAVYLCE 209
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHlmddvaDYADYVYLLE 218
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-239 |
6.32e-19 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 84.08 E-value: 6.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGVKRQKrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKpDTGTV-----------MLDGQ 69
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVK--AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVtadrmrfddidLLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 70 PVcQRHTRLG-KMSVVFQDYKSSLHPYFNVRQILNEAL------SQCDTPVDDKEAHMTALLERVGLSA--AFLNKYPQM 140
Cdd:PRK15093 80 PR-ERRKLVGhNVSMIFQEPQSCLDPSERVGRQLMQNIpgwtykGRWWQRFGWRKRRAIELLHRVGIKDhkDAMRSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 141 MSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQ 220
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250 260
....*....|....*....|
gi 1717358098 221 ERLNRHQL-KTLQNDYTREL 239
Cdd:PRK15093 239 ETAPSKELvTTPHHPYTQAL 258
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-219 |
6.69e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 82.95 E-value: 6.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTksyrsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGiEKPD---------TGTVMLDGQPV 71
Cdd:PRK13547 1 MLTADHLH------VARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGggaprgarvTGDVTLNGEPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 72 -CQRHTRLGKMSVVFQDYKSSLHPyFNVRQILN-----EALSQCDTPVDDKEAHMTALlERVGlSAAFLNKYPQMMSGGE 145
Cdd:PRK13547 74 aAIDAPRLARLRAVLPQAAQPAFA-FSAREIVLlgrypHARRAGALTHRDGEIAWQAL-ALAG-ATALVGRDVTTLSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 146 AQRVAIARAV---------ITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFND 216
Cdd:PRK13547 151 LARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLAD 230
|
...
gi 1717358098 217 GQI 219
Cdd:PRK13547 231 GAI 233
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-214 |
7.01e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.93 E-value: 7.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 6 NVTKSYRSGVKR-----------------QKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEK--PDTGTVML 66
Cdd:COG2401 12 RVTKVYSSVLDLservaivleafgvelrvVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 67 DGQPvcqrhtrlgkmsvvfqdyksslhpyFNVRQILNEALSQCDTPVDDKEahmtaLLERVGLSAA--FLNKYPQmMSGG 144
Cdd:COG2401 92 PDNQ-------------------------FGREASLIDAIGRKGDFKDAVE-----LLNAVGLSDAvlWLRRFKE-LSTG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717358098 145 EAQRVAIARAVITNPDYIVLDEAISALDMSiQSQILDL-LTTLRDKYQLSLIFITHDIQAAVYLCEDLIIF 214
Cdd:COG2401 141 QKFRFRLALLLAERPKLLVIDEFCSHLDRQ-TAKRVARnLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-200 |
8.97e-19 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 84.94 E-value: 8.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLdgqpvcQRHTRLGKM 81
Cdd:PRK15064 320 LEVENLTKGF------DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW------SENANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 SvvfQDYKSslhpYFNVRQILNEALSQCDTPVDDKEAhMTALLERVGLSAAFLNKYPQMMSGGEAQRVAIARAVITNPDY 161
Cdd:PRK15064 388 A---QDHAY----DFENDLTLFDWMSQWRQEGDDEQA-VRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1717358098 162 IVLDEAISALDM-SIQSqildlLTTLRDKYQLSLIFITHD 200
Cdd:PRK15064 460 LVMDEPTNHMDMeSIES-----LNMALEKYEGTLIFVSHD 494
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-188 |
1.04e-18 |
|
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: 81.95 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsGvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHT---- 76
Cdd:COG0410 3 MLEVENLHAGY--G----GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhria 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 77 RLGkMSVVFQDyksslhpyfnvRQI-----------LNEALSQCDTPVDDKEAHMTA----LLERVGLSAAFLnkypqmm 141
Cdd:COG0410 77 RLG-IGYVPEG-----------RRIfpsltveenllLGAYARRDRAEVRADLERVYElfprLKERRRQRAGTL------- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1717358098 142 SGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRD 188
Cdd:COG0410 138 SGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR 184
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-228 |
2.40e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 81.36 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 19 KRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMI-----LGIEKPDTGTVMLDGQPVCQRHT---RLGK-MSVVFQD-- 87
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSPRTdtvDLRKeIGMVFQQpn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 88 -YKSSLhpYFNV-----------RQILNEA----LSQCDT--PVDDKeAHMTALlervGLSaaflnkypqmmsGGEAQRV 149
Cdd:PRK14239 97 pFPMSI--YENVvyglrlkgikdKQVLDEAveksLKGASIwdEVKDR-LHDSAL----GLS------------GGQQQRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717358098 150 AIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYqlSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQL 228
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-218 |
2.78e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.42 E-value: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYrSGVKrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR---L 78
Cdd:PRK11288 5 LSFDGIGKTF-PGVK-----ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaalA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 79 GKMSVVFQDykssLH--PYFNVRQilNEALSQCDTP---VDDKEAHMTAL--LERVGLS---AAFLnKYpqmMSGGEAQR 148
Cdd:PRK11288 79 AGVAIIYQE----LHlvPEMTVAE--NLYLGQLPHKggiVNRRLLNYEAReqLEHLGVDidpDTPL-KY---LSIGQRQM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 149 VAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLsLIFITHDIQAAVYLCEDLIIFNDGQ 218
Cdd:PRK11288 149 VEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-244 |
3.92e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 83.14 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqRHTRLGKM 81
Cdd:PRK11176 342 IEFRNVTFTYPG----KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL--RDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 ----SVVFQDykssLHpYFN---VRQILNEALSQCDTPVDDKEAHMTALLErvglsaaFLNKYPQ-----------MMSG 143
Cdd:PRK11176 416 rnqvALVSQN----VH-LFNdtiANNIAYARTEQYSREQIEEAARMAYAMD-------FINKMDNgldtvigengvLLSG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 144 GEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRdKYQLSLIfITH---DIQAAvylcEDLIIFNDGQIQ 220
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQ-KNRTSLV-IAHrlsTIEKA----DEILVVEDGEIV 557
|
250 260
....*....|....*....|....
gi 1717358098 221 ERLNRHQLKTLQNDYtRELFEKQF 244
Cdd:PRK11176 558 ERGTHAELLAQNGVY-AQLHKMQF 580
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-200 |
7.00e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.03 E-value: 7.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 23 VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ---------------RHTRLGK-MSVV-- 84
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlpghqiarmgvvrtfQHVRLFReMTVIen 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 85 -----FQDYKSS-LHPYFNV---RQILNEALsqcdtpvdDKEAHMtalLERVGLSAaFLNKYPQMMSGGEAQRVAIARAV 155
Cdd:PRK11300 101 llvaqHQQLKTGlFSGLLKTpafRRAESEAL--------DRAATW---LERVGLLE-HANRQAGNLAYGQQRRLEIARCM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1717358098 156 ITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHD 200
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-204 |
7.72e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.08 E-value: 7.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRsgvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLA----RMILGIekPD---TGTVMLDGQPVCQR 74
Cdd:COG1117 12 IEVRNLNVYYG------DKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMNDLI--PGarvEGEILLDGEDIYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 75 HT-------RLGkMsvVFQdyKSSLHP---YFNV-----------RQILNEALSQCdtpvddkeahmtalLERVGL---- 129
Cdd:COG1117 84 DVdvvelrrRVG-M--VFQ--KPNPFPksiYDNVayglrlhgiksKSELDEIVEES--------------LRKAALwdev 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 130 ------SAAFLnkypqmmSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYqlSLIFITHDI-Q 202
Cdd:COG1117 145 kdrlkkSALGL-------SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMqQ 215
|
..
gi 1717358098 203 AA 204
Cdd:COG1117 216 AA 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-219 |
8.74e-18 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 78.24 E-value: 8.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRsgvkrqkrqiVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR--- 77
Cdd:cd03215 4 VLEVRGLSVKGA----------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdai 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 -LGkMSVVFQDYKSS-LHPYFNVRQilNEALsqcdtpvddkeahmtallervglsaaflnkyPQMMSGGEAQRVAIARAV 155
Cdd:cd03215 74 rAG-IAYVPEDRKREgLVLDLSVAE--NIAL-------------------------------SSLLSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717358098 156 ITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-221 |
1.82e-17 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 77.84 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKrqkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqRHTRLG-- 79
Cdd:cd03369 7 IEVENLSVRYAPDLP----PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI--STIPLEdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 --KMSVVFQD-------YKSSLHPYfnvrqilNEalsqcdtpVDDKEAhMTALleRVglSAAFLNkypqmMSGGEAQRVA 150
Cdd:cd03369 81 rsSLTIIPQDptlfsgtIRSNLDPF-------DE--------YSDEEI-YGAL--RV--SEGGLN-----LSQGQRQLLC 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 151 IARAVITNPDYIVLDEAISALDMSIQSQILDlltTLRDKYQLSLIF-ITHDIQaAVYLCEDLIIFNDGQIQE 221
Cdd:cd03369 136 LARALLKRPRVLVLDEATASIDYATDALIQK---TIREEFTNSTILtIAHRLR-TIIDYDKILVMDAGEVKE 203
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-221 |
6.74e-17 |
|
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: 76.76 E-value: 6.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKrqkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ--RHTRLG 79
Cdd:cd03244 3 IEFKNVSLRYRPNLP----PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKigLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQDyksslhPY-FN--VRQILnEALSQCdtpvDDKEAHmtALLERVGLSAAFLNKYPQM----------MSGGEA 146
Cdd:cd03244 79 RISIIPQD------PVlFSgtIRSNL-DPFGEY----SDEELW--QALERVGLKEFVESLPGGLdtvveeggenLSVGQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717358098 147 QRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLL-TTLRDKyqlSLIFITHDIQaAVYLCEDLIIFNDGQIQE 221
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIrEAFKDC---TVLTIAHRLD-TIIDSDRILVLDKGRVVE 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-201 |
6.83e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 6.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVmldgqpvcqrhTRLGK 80
Cdd:PRK09544 4 LVSLENVSVSFGQ------RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSVVFQDYKSSLHPY--FNVRQILnealsQCDTPVddKEAHMTALLERVglSAAFLNKYP-QMMSGGEAQRVAIARAVIT 157
Cdd:PRK09544 67 LRIGYVPQKLYLDTTlpLTVNRFL-----RLRPGT--KKEDILPALKRV--QAGHLIDAPmQKLSGGETQRVLLARALLN 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1717358098 158 NPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDI 201
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-199 |
7.12e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.86 E-value: 7.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKRQKRQIVkQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ-------R 74
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdiK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 75 HTRlGKMSVVFQDYKSSLhpyFNVRQILNEALSQCDTPVDDKEAHMTAL--LERVGLSAAFLNKYPQMMSGGEAQRVAIA 152
Cdd:PRK13649 82 QIR-KKVGLVFQFPESQL---FEETVLKDVAFGPQNFGVSQEEAEALARekLALVGISESLFEKNPFELSGGQMRRVAIA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1717358098 153 RAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITH 199
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTH 203
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
1.32e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.58 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSgvkRQKRQIV--KQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTV-------------- 64
Cdd:PRK13631 21 ILRVKNLYCVFDE---KQENELValNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 65 ---MLDGQPVCQRHTRLGK-MSVVFQdyksslhpyFNVRQILNEALSQ------CDTPVDDKEAHMTA--LLERVGLSAA 132
Cdd:PRK13631 98 eliTNPYSKKIKNFKELRRrVSMVFQ---------FPEYQLFKDTIEKdimfgpVALGVKKSEAKKLAkfYLNKMGLDDS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 133 FLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRdKYQLSLIFITHDIQAAVYLCEDLI 212
Cdd:PRK13631 169 YLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVLEVADEVI 247
|
....*..
gi 1717358098 213 IFNDGQI 219
Cdd:PRK13631 248 VMDKGKI 254
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-219 |
1.42e-16 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 76.15 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTksyrsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGieKPDT----GTVMLDGQ-----PVC 72
Cdd:TIGR01978 1 LKIKDLH------VSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSYevtsGTILFKGQdllelEPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 73 QRhTRLGkmsvVFQDYKSSLH-PYFNVRQILNEALSQC-----DTPVD--DKEAHMTALLERVGLSAAFLNKYPQM-MSG 143
Cdd:TIGR01978 73 ER-ARAG----LFLAFQYPEEiPGVSNLEFLRSALNARrsargEEPLDllDFEKLLKEKLALLDMDEEFLNRSVNEgFSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 144 GEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLI-IFNDGQI 219
Cdd:TIGR01978 148 GEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREP-DRSFLIITHYQRLLNYIKPDYVhVLLDGRI 223
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-195 |
2.38e-16 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 75.25 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSY-RSgvkrqkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPV-----CQRh 75
Cdd:TIGR03410 1 LEVSNLNVYYgQS-------HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklppHER- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRLGkMSVVFQDYKSslHPYFNVRQILN---EALSQCDTPVDDKeahmtaLLERVGLSAAFLNKYPQMMSGGEAQRVAIA 152
Cdd:TIGR03410 73 ARAG-IAYVPQGREI--FPRLTVEENLLtglAALPRRSRKIPDE------IYELFPVLKEMLGRRGGDLSGGQQQQLAIA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1717358098 153 RAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLI 195
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAIL 186
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-228 |
2.91e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.37 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKsyrsgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR--- 77
Cdd:COG1129 256 VLEVEGLSV----------GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdai 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 -LGkMSVVFQDYKSS-LHPYFNVRQilNEALSQCDT-----PVDDKEAHMTA--LLERVGLSAAFLNKYPQMMSGGEAQR 148
Cdd:COG1129 326 rAG-IAYVPEDRKGEgLVLDLSIRE--NITLASLDRlsrggLLDRRRERALAeeYIKRLRIKTPSPEQPVGNLSGGNQQK 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 149 VAIARAVITNPDYIVLDEA-----ISAldmsiQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERL 223
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPtrgidVGA-----KAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGEL 476
|
....*
gi 1717358098 224 NRHQL 228
Cdd:COG1129 477 DREEA 481
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-219 |
5.06e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.05 E-value: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGI---EKPDTGTVMLDGQPVcQRHTR 77
Cdd:PRK09984 4 IIRVEKLAKTF------NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTV-QREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 LGKMSVVFQDYKSSLHPYFNV-------RQILNEALSQCD---------TPVDDKEAHMTalLERVGLsAAFLNKYPQMM 141
Cdd:PRK09984 77 LARDIRKSRANTGYIFQQFNLvnrlsvlENVLIGALGSTPfwrtcfswfTREQKQRALQA--LTRVGM-VHFAHQRVSTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 142 SGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDlltTLRDKYQ---LSLIFITHDIQAAVYLCEDLIIFNDGQ 218
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMD---TLRDINQndgITVVVTLHQVDYALRYCERIVALRQGH 230
|
.
gi 1717358098 219 I 219
Cdd:PRK09984 231 V 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-219 |
6.91e-16 |
|
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: 73.33 E-value: 6.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTksyrsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIE--KPDTGTVMLDGQ-----PVCQR 74
Cdd:cd03217 1 LEIKDLH------VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEditdlPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 75 hTRLGkMSVVFQDyksslhpyfnvrqilnealsqcdtPVDDKEAHMTALLERVGLSaaflnkypqmMSGGEAQRVAIARA 154
Cdd:cd03217 75 -ARLG-IFLAFQY------------------------PPEIPGVKNADFLRYVNEG----------FSGGEKKRNEILQL 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717358098 155 VITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQAAVYLCEDLI-IFNDGQI 219
Cdd:cd03217 119 LLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGK-SVLIITHYQRLLDYIKPDRVhVLYDGRI 183
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-235 |
9.30e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.91 E-value: 9.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPV-CQRHTRLGK 80
Cdd:PRK10790 341 IDIDNVSFAYRDD-----NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 -MSVVFQDYKSSLHPYFNvrqilNEALSQcdtpvDDKEAHMTALLERVGLsAAFLNKYPQ-----------MMSGGEAQR 148
Cdd:PRK10790 416 gVAMVQQDPVVLADTFLA-----NVTLGR-----DISEEQVWQALETVQL-AELARSLPDglytplgeqgnNLSVGQKQL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 149 VAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDkyQLSLIFITHDIQAAVYlCEDLIIFNDGQIQERLNRHQL 228
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
....*..
gi 1717358098 229 KTLQNDY 235
Cdd:PRK10790 562 LAAQGRY 568
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-172 |
1.49e-15 |
|
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: 75.36 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLdGQPVcqrhtrlgKM 81
Cdd:TIGR03719 323 IEAENLTKAFGD------KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 SVVFQDyKSSLHPYFNVRQILNEALSQCDtpVDDKEAHMTALLERVGLSAAFLNKYPQMMSGGEAQRVAIARAVITNPDY 161
Cdd:TIGR03719 388 AYVDQS-RDALDPNKTVWEEISGGLDIIK--LGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNV 464
|
170
....*....|.
gi 1717358098 162 IVLDEAISALD 172
Cdd:TIGR03719 465 LLLDEPTNDLD 475
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-184 |
2.60e-15 |
|
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: 72.01 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTksyrsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGKm 81
Cdd:TIGR01189 1 LAARNLA------CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 SVVFQDYKSSLHPYFNVR---QILNEALSQCDTPVDDkeahmtaLLERVGLS------AAFLnkypqmmSGGEAQRVAIA 152
Cdd:TIGR01189 74 NILYLGHLPGLKPELSALenlHFWAAIHGGAQRTIED-------ALAAVGLTgfedlpAAQL-------SAGQQRRLALA 139
|
170 180 190
....*....|....*....|....*....|..
gi 1717358098 153 RAVITNPDYIVLDEAISALDMSIQSQILDLLT 184
Cdd:TIGR01189 140 RLWLSRRPLWILDEPTTALDKAGVALLAGLLR 171
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-216 |
3.14e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 74.68 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILG-----------IEKPDTGTVMLDGQP 70
Cdd:PTZ00265 1166 IEIMDVNFRYIS---RPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivFKNEHTNDMTNEQDY 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 71 VCQRHTRLGKMSV-VFQDYKSSLHP-----YFNVRQILNEALSQCDTPVDD-----------------------KEAHMT 121
Cdd:PTZ00265 1243 QGDEEQNVGMKNVnEFSLTKEGGSGedstvFKNSGKILLDGVDICDYNLKDlrnlfsivsqepmlfnmsiyeniKFGKED 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 122 ALLERVGLSAAFL----------NKYP-------QMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLT 184
Cdd:PTZ00265 1323 ATREDVKRACKFAaidefieslpNKYDtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402
|
250 260 270
....*....|....*....|....*....|..
gi 1717358098 185 TLRDKYQLSLIFITHDIqAAVYLCEDLIIFND 216
Cdd:PTZ00265 1403 DIKDKADKTIITIAHRI-ASIKRSDKIVVFNN 1433
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-172 |
4.38e-15 |
|
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: 71.37 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTksyrsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQrhtrlgkm 81
Cdd:cd03231 1 LEADELT------CERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 svVFQDYKSSLHpYFNVRQILNEALSQCDT-----PVDDKEAHMTAlLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVI 156
Cdd:cd03231 67 --QRDSIARGLL-YLGHAPGIKTTLSVLENlrfwhADHSDEQVEEA-LARVGL-NGFEDRPVAQLSAGQQRRVALARLLL 141
|
170
....*....|....*.
gi 1717358098 157 TNPDYIVLDEAISALD 172
Cdd:cd03231 142 SGRPLWILDEPTTALD 157
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-201 |
6.72e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.80 E-value: 6.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 26 VSFQCSKGQSIAIIGESGSGKSTLARMILGIEkPDTGTVMLDGQPV---------------CQRHTRLGKMSVvFQdyks 90
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLsdwsaaelarhraylSQQQSPPFAMPV-FQ---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 91 slhpYFnvrqilneALSQCDTPVDDK-EAHMTALLERVGLSaaflNKYPQMM---SGGEAQRVAIARAVI-----TNPD- 160
Cdd:COG4138 89 ----YL--------ALHQPAGASSEAvEQLLAQLAEALGLE----DKLSRPLtqlSGGEWQRVRLAAVLLqvwptINPEg 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1717358098 161 -YIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDI 201
Cdd:COG4138 153 qLLLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDL 193
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-243 |
1.13e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.96 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 21 QIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIeKPDTGTVMLDGQPVCQ---RHTRlGKMSVVFQDyksSLHPYFN 97
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREldpESWR-KHLSWVGQN---PQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 98 VRQilNEALSQcdtpVDDKEAHMTALLERVGLSAaFLNKYPQ-----------MMSGGEAQRVAIARAVITNPDYIVLDE 166
Cdd:PRK11174 439 LRD--NVLLGN----PDASDEQLQQALENAWVSE-FLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 167 AISALDMSIQSQILDLLTTLRDkyQLSLIFITHDIQaAVYLCEDLIIFNDGQIQERLNRHQLKTLQNDYTRELFEKQ 243
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLE-DLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQ 585
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-189 |
1.13e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.99 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 18 QKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPD--TGTVML-DGQPVCQRHTRLGkmsVVFQDykSSLHP 94
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILAnNRKPTKQILKRTG---FVTQD--DILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 95 YFNVRQIL--------NEALSQcdtpvDDKEAHMTALLERVGLS----AAFLNKYPQMMSGGEAQRVAIARAVITNPDYI 162
Cdd:PLN03211 154 HLTVRETLvfcsllrlPKSLTK-----QEKILVAESVISELGLTkcenTIIGNSFIRGISGGERKRVSIAHEMLINPSLL 228
|
170 180
....*....|....*....|....*..
gi 1717358098 163 VLDEAISALDMSIQSQILDLLTTLRDK 189
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAQK 255
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-209 |
1.26e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 4 VQNVTKSYRSGvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcQRHTRLGKMSV 83
Cdd:PRK15056 9 VNDVTVTWRNG-----HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-RQALQKNLVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 84 VFQDYKSSLHPYFNVRQILNEA----LSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVITNP 159
Cdd:PRK15056 83 VPQSEEVDWSFPVLVEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVE-FRHRQIGELSGGQKKRVFLARAIAQQG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1717358098 160 DYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIfITHDIQAAVYLCE 209
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLV-STHNLGSVTEFCD 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-221 |
1.55e-14 |
|
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: 72.53 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIE--KPDTGTVM-------------- 65
Cdd:TIGR03269 1 IEVKNLTKKFDG------KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyver 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 66 --LDGQ--PVCQ-----------------RHTRLGKMSVVFQdykSSLHPYFNVRQILN--EALSQCDTPVDDKEAHMTA 122
Cdd:TIGR03269 75 psKVGEpcPVCGgtlepeevdfwnlsdklRRRIRKRIAIMLQ---RTFALYGDDTVLDNvlEALEEIGYEGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 123 LLERVGLSAAFLNkYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQ 202
Cdd:TIGR03269 152 LIEMVQLSHRITH-IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
250
....*....|....*....
gi 1717358098 203 AAVYLCEDLIIFNDGQIQE 221
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKE 249
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-218 |
3.05e-14 |
|
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: 69.74 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 31 SKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRL-GKMSVVFQDYKSSL------HPYFNVrQILN 103
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIkADYEGTVRDLLSSItkdfytHPYFKT-EIAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 104 ealsqcdtPVddkeaHMTALLERVglsaafLNKypqmMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLL 183
Cdd:cd03237 102 --------PL-----QIEQILDRE------VPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1717358098 184 TTLRDKYQLSLIFITHDIQAAVYLCEDLIIFnDGQ 218
Cdd:cd03237 159 RRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGE 192
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-219 |
3.39e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.42 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 4 VQNVTKSYRSGVKRQKRQIvKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTG-TVMLD-----GQPVCQRHTR 77
Cdd:PRK13645 9 LDNVSYTYAKKTPFEFKAL-NNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDyaipaNLKKIKEVKR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 LGK-MSVVFQdyksslHPYFNVRQILNE---ALSQCDTPVDDKEAH--MTALLERVGLSAAFLNKYPQMMSGGEAQRVAI 151
Cdd:PRK13645 88 LRKeIGLVFQ------FPEYQLFQETIEkdiAFGPVNLGENKQEAYkkVPELLKLVQLPEDYVKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 152 ARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-243 |
5.88e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.21 E-value: 5.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDG----QPVCQRHTR 77
Cdd:PTZ00265 383 IQFKNVRFHYDT---RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 lGKMSVVFQD-----------YKSSLHPYFNVRQILNE-----------------ALSQCDTPVDDKEAHMTA--LL--- 124
Cdd:PTZ00265 460 -SKIGVVSQDpllfsnsiknnIKYSLYSLKDLEALSNYynedgndsqenknkrnsCRAKCAGDLNDMSNTTDSneLIemr 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 125 ---------ERVGLS---------AAFLNKYPQM-------MSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQI 179
Cdd:PTZ00265 539 knyqtikdsEVVDVSkkvlihdfvSALPDKYETLvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717358098 180 LDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNdgqiQERLNRHQLKTLQNDYTRELFEKQ 243
Cdd:PTZ00265 619 QKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSN----RERGSTVDVDIIGEDPTKDNKENN 678
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-228 |
6.95e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.35 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 20 RQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKP-----DTGTVMLDGQPVCQRHTRLG---KMSVVFQdyKSS 91
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLEfrrRVGMLFQ--RPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 92 LHPYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGLSAAF---LNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAI 168
Cdd:PRK14271 112 PFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVkdrLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 169 SALDMSIQSQILDLLTTLRDKyqLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQL 228
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-201 |
7.37e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.91 E-value: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKST----LARMI-LGIEKPDTGTVMLDGQPVCQRHT 76
Cdd:PRK14258 8 IKVNNLSFYYDT------QKILEGVSMEIYQSKVTAIIGPSGCGKSTflkcLNRMNeLESEVRVEGRVEFFNQNIYERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 77 RLGKM----SVVFQD-------------YKSSL---HPYFNVRQILNEALSQCDTPVDDK-EAHMTALlervglsaafln 135
Cdd:PRK14258 82 NLNRLrrqvSMVHPKpnlfpmsvydnvaYGVKIvgwRPKLEIDDIVESALKDADLWDEIKhKIHKSAL------------ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717358098 136 kypqMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHDI 201
Cdd:PRK14258 150 ----DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNL 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-172 |
8.12e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 8.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTksyrsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqRHTR--- 77
Cdd:PRK13538 1 MLEARNLA------CERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--RRQRdey 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 ------LGKMSVVfqdyKSSLHPYFNVRqiLNEALSQCdtpVDDkEAHMTAlLERVGLS------AAFLnkypqmmSGGE 145
Cdd:PRK13538 73 hqdllyLGHQPGI----KTELTALENLR--FYQRLHGP---GDD-EALWEA-LAQVGLAgfedvpVRQL-------SAGQ 134
|
170 180
....*....|....*....|....*..
gi 1717358098 146 AQRVAIARAVITNPDYIVLDEAISALD 172
Cdd:PRK13538 135 QRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-243 |
9.76e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.13 E-value: 9.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 18 QKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQrhTRL----GKMSVVFQDyksslh 93
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK--LQLdswrSRLAVVSQT------ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 94 PY-FNVRQILNEALSQCD-TPVDDKEAHMTALLERVGLsaaflnKYPQ-----------MMSGGEAQRVAIARAVITNPD 160
Cdd:PRK10789 398 PFlFSDTVANNIALGRPDaTQQEIEHVARLASVHDDIL------RLPQgydtevgergvMLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 161 YIVLDEAISALDMSIQSQILDLLTTLRDkyQLSLIFITHDIQAAVYLCEDLIIfNDGQIQERlNRHQLKTLQNDYTRELF 240
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTEASEILVM-QHGHIAQR-GNHDQLAQQSGWYRDMY 547
|
...
gi 1717358098 241 EKQ 243
Cdd:PRK10789 548 RYQ 550
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-215 |
2.15e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.88 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKrqkrqiVKQVSFQCSKGQSIAIIGESGSGKSTLAR-------MILGIEKpdTGTVMLDGQ----- 69
Cdd:PRK14243 11 LRTENLNVYYGSFLA------VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKnlyap 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 70 ---PVCQRHtRLGkmsVVFQdyksslHPYFNVRQIL-NEALSqcdTPVDDKEAHMTALLERVGLSAAF-------LNKYP 138
Cdd:PRK14243 83 dvdPVEVRR-RIG---MVFQ------KPNPFPKSIYdNIAYG---ARINGYKGDMDELVERSLRQAALwdevkdkLKQSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 139 QMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYqlSLIFITHDIQAAVYLCEDLIIFN 215
Cdd:PRK14243 150 LSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFN 224
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-219 |
2.19e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.74 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVtksyRSGVKrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGieKPD----TGTVMLDGQPVCQ--- 73
Cdd:CHL00131 7 ILEIKNL----HASVN--ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDlep 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 74 -RHTRLGkMSVVFQ-----------DYkssLHPYFNVRQILNEaLSQCDtPVDDKEAhMTALLERVGLSAAFLNKY-PQM 140
Cdd:CHL00131 79 eERAHLG-IFLAFQypieipgvsnaDF---LRLAYNSKRKFQG-LPELD-PLEFLEI-INEKLKLVGMDPSFLSRNvNEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 141 MSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQAAVYLCEDLI-IFNDGQI 219
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQRLLDYIKPDYVhVMQNGKI 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-218 |
4.92e-13 |
|
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: 65.57 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKRQKRqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDG-------QPVCQR 74
Cdd:cd03250 1 ISVEDASFTWDSGEQETSF-TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGsiayvsqEPWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 75 HTRlgKMSVVFqdykssLHPYFNVRqiLNEALSQC----DT---PVDDkeahMTALLERvGLSaaflnkypqmMSGGEAQ 147
Cdd:cd03250 80 GTI--RENILF------GKPFDEER--YEKVIKACalepDLeilPDGD----LTEIGEK-GIN----------LSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 148 RVAIARAVITNPDYIVLDEAISALDMSIQSQILD--LLTTLRDKYqlSLIFITHDIQAAVYlCEDLIIFNDGQ 218
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-219 |
8.22e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.16 E-value: 8.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 19 KRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcQRHT------RLGKMSvvfqdyKSSL 92
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI-QHYAskevarRIGLLA------QNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 93 HPYFNVRQILNEALSQCDTPV------DDKEAhMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDE 166
Cdd:PRK10253 92 TPGDITVQELVARGRYPHQPLftrwrkEDEEA-VTKAMQATGITH-LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 167 AISALDMSIQSQILDLLTTLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-219 |
9.21e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 9.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrSGVkrqkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC-----QRH 75
Cdd:PRK15439 11 LLCARSISKQY-SGV-----EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArltpaKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 tRLGkMSVVFQDykSSLHPYFNVRQilNEALSQCDTPVDDKEahMTALLERVGLSaafLNkyPQMMSG----GEAQRVAI 151
Cdd:PRK15439 85 -QLG-IYLVPQE--PLLFPNLSVKE--NILFGLPKRQASMQK--MKQLLAALGCQ---LD--LDSSAGslevADRQIVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 152 ARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-217 |
9.85e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 9.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrSGVkrqkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGK 80
Cdd:PRK09700 5 YISMAGIGKSF-GPV-----HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 ---MSVVFQ-----DYKSSLHPYFNVRQILNEAlsqCDTP-VDDKEAHMTA--LLERVGLSAAfLNKYPQMMSGGEAQRV 149
Cdd:PRK09700 79 qlgIGIIYQelsviDELTVLENLYIGRHLTKKV---CGVNiIDWREMRVRAamMLLRVGLKVD-LDEKVANLSISHKQML 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 150 AIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRdKYQLSLIFITHDIQAAVYLCEDLIIFNDG 217
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-183 |
1.09e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.72 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 26 VSFQCSKGQSIAIIGESGSGKSTLARMILGIeKPDTGTVMLDGQPVCQ-RHTRLGKMSVVFQDYKSslhPYFN--VRQIL 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAwSAAELARHRAYLSQQQT---PPFAmpVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 103 neALSQCD-TPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIArAVI------TNPD--YIVLDEAISALDM 173
Cdd:PRK03695 91 --TLHQPDkTRTEAVASALNEVAEALGL-DDKLGRSVNQLSGGEWQRVRLA-AVVlqvwpdINPAgqLLLLDEPMNSLDV 166
|
170
....*....|
gi 1717358098 174 SiQSQILDLL 183
Cdd:PRK03695 167 A-QQAALDRL 175
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-130 |
1.82e-12 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 66.36 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRsGVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcQRHTRLG-- 79
Cdd:COG4615 328 LELRGVTYRYP-GEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV-TADNREAyr 405
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 80 -KMSVVFQDYksslHpyfnvrqiLNEALSQCDTPVDDKEAHmtALLERVGLS 130
Cdd:COG4615 406 qLFSAVFSDF----H--------LFDRLLGLDGEADPARAR--ELLERLELD 443
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-202 |
1.87e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 3 EVQNVtkSYRSGVKrqkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVmldgqpvcqrhtRLG-KM 81
Cdd:PRK11147 321 EMENV--NYQIDGK----QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------------HCGtKL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 SVV-FQDYKSSLHPYFNVrqILNEALSQCDTPVDDKEAHMTALLERvglsaaFLnkYPQM--------MSGGEAQRVAIA 152
Cdd:PRK11147 383 EVAyFDQHRAELDPEKTV--MDNLAEGKQEVMVNGRPRHVLGYLQD------FL--FHPKramtpvkaLSGGERNRLLLA 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1717358098 153 RAVITNPDYIVLDEAISALDMsiqsQILDLLTTLRDKYQLSLIFITHDIQ 202
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHDRQ 498
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-189 |
3.76e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.45 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 15 VKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDT---GTVMLDGQPVCQRHTRlgKMSV-VFQDykS 90
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPIDAKEMR--AISAyVQQD--D 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 91 SLHPYFNVRQILN---EALSQCDTPVDDKEAHMTALLERVGLS--AAFLNKYPQMM---SGGEAQRVAIARAVITNPDYI 162
Cdd:TIGR00955 109 LFIPTLTVREHLMfqaHLRMPRRVTKKEKRERVDEVLQALGLRkcANTRIGVPGRVkglSGGERKRLAFASELLTDPPLL 188
|
170 180
....*....|....*....|....*..
gi 1717358098 163 VLDEAISALDMSIQSQILDLLTTLRDK 189
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQK 215
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-223 |
4.01e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTksyrsgvkRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRH----T 76
Cdd:PRK09700 265 VFEVRNVT--------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldaV 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 77 RLGKMSVVFQDYKSSLHPYFNVRQilNEALSQCDTP---------VDDKEAHMTALLER--VGLSAAFLNKYPQMMSGGE 145
Cdd:PRK09700 337 KKGMAYITESRRDNGFFPNFSIAQ--NMAISRSLKDggykgamglFHEVDEQRTAENQRelLALKCHSVNQNITELSGGN 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 146 AQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQAAVYLCEDLIIFNDGQIQERL 223
Cdd:PRK09700 415 QQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLTQIL 491
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-219 |
4.64e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.26 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 14 GVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqRHTRLG------KMSVVFQD 87
Cdd:PRK13638 8 WFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL--DYSKRGllalrqQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 88 YKSSLHpYFNVRQILNEALSQCDTPVDDKEAHMTALLERVGlSAAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEA 167
Cdd:PRK13638 86 PEQQIF-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 168 ISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-200 |
5.36e-12 |
|
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: 64.96 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 5 QNVTKSYRSgvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLdgQPvcqrhtrlgKMSVV 84
Cdd:TIGR03719 8 NRVSKVVPP-----KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--QP---------GIKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 85 FQDYKSSLHPYFNVRQILNEALSQCDTPVD----------DKEAHMTALLERVG-----LSAAFL----NKYPQMM---- 141
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEEGVAEIKDALDrfneisakyaEPDADFDKLAAEQAelqeiIDAADAwdldSQLEIAMdalr 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 142 -----------SGGEAQRVAIARAVITNPDYIVLDEAISALDmsiqSQILDLLTTLRDKYQLSLIFITHD 200
Cdd:TIGR03719 152 cppwdadvtklSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-199 |
8.79e-12 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 64.38 E-value: 8.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 22 IVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDgqpvcqrhtRLGKMSVVFQdyksslHPYFNVRQi 101
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP---------AKGKLFYVPQ------RPYMTLGT- 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 102 LNEALSQCDTPVDDKE--------------AHMTALLER-VGLSAafLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDE 166
Cdd:TIGR00954 531 LRDQIIYPDSSEDMKRrglsdkdleqildnVQLTHILEReGGWSA--VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|...
gi 1717358098 167 AISALDMSIQSQILDLLTtlrdKYQLSLIFITH 199
Cdd:TIGR00954 609 CTSAVSVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-218 |
1.00e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.08 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrSGVKrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDT--GTVMLDGQPVCQRH--- 75
Cdd:TIGR02633 1 LLEMKGIVKTF-GGVK-----ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNird 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRLGKMSVVFQDYksSLHPYFNVRQ--ILNEALSQCDTPVDDKEAHMTA--LLERVGLSAAFLNKYPQMMSGGEAQRVAI 151
Cdd:TIGR02633 75 TERAGIVIIHQEL--TLVPELSVAEniFLGNEITLPGGRMAYNAMYLRAknLLRELQLDADNVTRPVGDYGGGQQQLVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 152 ARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQ 218
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-218 |
1.22e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrSGVKrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDT--GTVMLDGQPVCQRHTR- 77
Cdd:PRK13549 5 LLEMKNITKTF-GGVK-----ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 ---LGkMSVVFQDYksSLHPYFNVRQilNEALSQCDTP---VDDKEAHMTA--LLERVGLSaafLNKYPQMM--SGGEAQ 147
Cdd:PRK13549 79 terAG-IAIIHQEL--ALVKELSVLE--NIFLGNEITPggiMDYDAMYLRAqkLLAQLKLD---INPATPVGnlGLGQQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717358098 148 RVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQ 218
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-222 |
1.28e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrSGVKrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC---QRHTR 77
Cdd:PRK10762 4 LLQLKGIDKAF-PGVK-----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPKSSQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 LGKMSVVFQDYksSLHPYFNV-------RQILNeALSQCDTPVDDKEAhmTALLERVGLSAAflnkyPQMMSG----GEA 146
Cdd:PRK10762 78 EAGIGIIHQEL--NLIPQLTIaeniflgREFVN-RFGRIDWKKMYAEA--DKLLARLNLRFS-----SDKLVGelsiGEQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 147 QRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQ-IQER 222
Cdd:PRK10762 148 QMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQfIAER 223
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-172 |
1.38e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSgvkrqkRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLdGQPVcqrhtrlgKM 81
Cdd:PRK11819 325 IEAENLSKSFGD------RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--------KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 82 SVVFQDyKSSLHPYFNVRQILNEALSQCDtpVDDKEAHMTALLERVGLSAAFLNKYPQMMSGGEAQRVAIARAVITNPDY 161
Cdd:PRK11819 390 AYVDQS-RDALDPNKTVWEEISGGLDIIK--VGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNV 466
|
170
....*....|.
gi 1717358098 162 IVLDEAISALD 172
Cdd:PRK11819 467 LLLDEPTNDLD 477
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-214 |
1.40e-11 |
|
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: 63.65 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 32 KGQSIAIIGESGSGKSTLARMILGIEKPDTGTVmldgqpvcqrHTRLgKMSvvfqdYKSS-LHPYFN--VRQILNEALSQ 108
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV----------DEDL-KIS-----YKPQyISPDYDgtVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 109 cdtPVDDKeAHMTALLERVGLSaAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMS---IQSQILDLLTT 185
Cdd:COG1245 429 ---DFGSS-YYKTEIIKPLGLE-KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRFAE 503
|
170 180
....*....|....*....|....*....
gi 1717358098 186 LRDKyqlSLIFITHDIQAAVYLCEDLIIF 214
Cdd:COG1245 504 NRGK---TAMVVDHDIYLIDYISDRLMVF 529
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-219 |
1.43e-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: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHT-RLG 79
Cdd:PRK11614 5 MLSFDKVSAHY------GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQDYKSSLHPYFNVRQilNEALSQCdtpVDDKEAHMTALLERVGLSAAFLNKYPQ---MMSGGEAQRVAIARAVI 156
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEE--NLAMGGF---FAERDQFQERIKWVYELFPRLHERRIQragTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 157 TNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-230 |
2.29e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.15 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 24 KQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHT--RLGKMSVVF-QDYKSS-LH---P-Y 95
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqRLARGLVYLpEDRQSSgLYldaPlA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 96 FNVrqilnEALSQCDTPVDDKEAHMTALLER----VGLSAAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISAL 171
Cdd:PRK15439 360 WNV-----CALTHNRRGFWIKPARENAVLERyrraLNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717358098 172 DMSIQSQILDLLTTLRdKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQLKT 230
Cdd:PRK15439 435 DVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINV 492
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-219 |
2.34e-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: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 20 RQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPV-------------CQRHtrlgkmSVVFQ 86
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetnldavrqslgmCPQH------NILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 87 DYKSSLHPYFNVRQilnEALSQcdtpvDDKEAHMTALLERVGLSAAfLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDE 166
Cdd:TIGR01257 1017 HLTVAEHILFYAQL---KGRSW-----EEAQLEMEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 167 AISALDMSIQSQILDLLttLRDKYQLSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
26-238 |
2.35e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.99 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 26 VSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGqpvcqrhtrlgkmSVVFQDYKSSLHPYFN-VRQILNE 104
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-------------SAALIAISSGLNGQLTgIENIELK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 105 ALSQCDTPVDDKEahMTALLERVGLSAAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLT 184
Cdd:PRK13545 110 GLMMGLTKEKIKE--IIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMN 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1717358098 185 TLRDKYQlSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQLKTLQNDYTRE 238
Cdd:PRK13545 188 EFKEQGK-TIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKK 240
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-221 |
2.49e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.85 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 21 QIVKQVSFQCSKGQSIAIIGESGSGKSTLARMI-----LGIEKPDTGTVMLDGQ-----PVCQRHTRLgkmSVVFQdyks 90
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQdifkmDVIELRRRV---QMVFQ---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 91 SLHPYFNVRQILNEALS-QCDTPVDDK---EAHMTALLERVGLSAAF---LNKYPQMMSGGEAQRVAIARAVITNPDYIV 163
Cdd:PRK14247 90 IPNPIPNLSIFENVALGlKLNRLVKSKkelQERVRWALEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 164 LDEAISALDMSIQSQILDLLTTLrdKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVE 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-221 |
1.78e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.37 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYrsgvkrQKRQI-VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC--QRHTRL 78
Cdd:PRK10522 323 LELRNVTFAY------QDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaeQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 79 GKMSVVFQDYksslHPYfnvrqilNEALSQCDTPVDDKEAHmtALLERVGLS-------AAFLNkypQMMSGGEAQRVAI 151
Cdd:PRK10522 397 KLFSAVFTDF----HLF-------DQLLGPEGKPANPALVE--KWLERLKMAhkleledGRISN---LKLSKGQKKRLAL 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 152 ARAVITNPDYIVLDEAisALDMSIQSQ---ILDLLTTLRDKYQlSLIFITHD----IQAavylcEDLIIFNDGQIQE 221
Cdd:PRK10522 461 LLALAEERDILLLDEW--AADQDPHFRrefYQVLLPLLQEMGK-TIFAISHDdhyfIHA-----DRLLEMRNGQLSE 529
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-189 |
1.83e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.43 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKRqkrqiVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR---- 77
Cdd:COG3845 258 LEVENLSVRDDRGVPA-----LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRerrr 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 78 LGkMSVVFQD-YKSSLHPYFNVRQilNEALSQCDTP-------VDDKE--AHMTALLERVGLSAAFLNKYPQMMSGGEAQ 147
Cdd:COG3845 333 LG-VAYIPEDrLGRGLVPDMSVAE--NLILGRYRRPpfsrggfLDRKAirAFAEELIEEFDVRTPGPDTPARSLSGGNQQ 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1717358098 148 RVAIARAVITNPDYIV-------LDE-AISAldmsIQSQILDllttLRDK 189
Cdd:COG3845 410 KVILARELSRDPKLLIaaqptrgLDVgAIEF----IHQRLLE----LRDA 451
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-172 |
2.53e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLGK 80
Cdd:PRK13540 1 MLDVIELDFDY------HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 mSVVFQDYKSSLHPYFNVRQILNEALSQCDTPVDDKEahmtalLERVgLSAAFLNKYP-QMMSGGEAQRVAIARAVITNP 159
Cdd:PRK13540 75 -QLCFVGHRSGINPYLTLRENCLYDIHFSPGAVGITE------LCRL-FSLEHLIDYPcGLLSSGQKRQVALLRLWMSKA 146
|
170
....*....|...
gi 1717358098 160 DYIVLDEAISALD 172
Cdd:PRK13540 147 KLWLLDEPLVALD 159
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-214 |
3.29e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 32 KGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDgqpvcqrhtrlGKMSV----VFQDYKSSlhpyfnVRQILNEALS 107
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-----------LKISYkpqyIKPDYDGT------VEDLLRSITD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 108 QCDTPVDDKEahmtaLLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMS---IQSQILDLLT 184
Cdd:PRK13409 427 DLGSSYYKSE-----IIKPLQL-ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRIA 500
|
170 180 190
....*....|....*....|....*....|
gi 1717358098 185 TLRDKyqlSLIFITHDIQAAVYLCEDLIIF 214
Cdd:PRK13409 501 EEREA---TALVVDHDIYMIDYISDRLMVF 527
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-232 |
3.71e-10 |
|
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: 59.45 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGI-EKPDTGTVMLDGQPV----CQRH 75
Cdd:TIGR02633 257 ILEARNLTCWD---VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdirnPAQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRLGKMSVVFQDYKSSLHPYFNVRQILNEALSQ--CDTPVDDKEAHMTALLE---RVGLSAAFLNKYPQMMSGGEAQRVA 150
Cdd:TIGR02633 334 IRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKsfCFKMRIDAAAELQIIGSaiqRLKVKTASPFLPIGRLSGGNQQKAV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 151 IARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQLKT 230
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQ 492
|
..
gi 1717358098 231 LQ 232
Cdd:TIGR02633 493 EQ 494
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-204 |
5.00e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.93 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 21 QIVKQVSFQCSKGQSIAIIGESGSGKSTLARMI-----LGIEKPDTGTVMLDGQ--------PVCQRHtrlgKMSVVFQd 87
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRniyspdvdPIEVRR----EVGMVFQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 88 YKSS---LHPYFNVrqILNEALSQCDTPVDDKEAHMTALLERVGLSAAF---LNKYPQMMSGGEAQRVAIARAVITNPDY 161
Cdd:PRK14267 93 YPNPfphLTIYDNV--AIGVKLNGLVKSKKELDERVEWALKKAALWDEVkdrLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1717358098 162 IVLDEAISALDMSIQSQILDLLTTLRDKYqlSLIFITHD-IQAA 204
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSpAQAA 212
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-221 |
5.75e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.13 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 20 RQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILG-IEKPDT-----GTVMLDGQPVCQ-RHTRLGK-MSVVFQdyksS 91
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlIEIYDSkikvdGKVLYFGKDIFQiDAIKLRKeVGMVFQ----Q 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 92 LHPYFNVRQILNEALSQCDTPVDDK---EAHMTALLERVGLSAAF---LNKYPQMMSGGEAQRVAIARAVITNPDYIVLD 165
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKSHGIKEKreiKKIVEECLRKVGLWKEVydrLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1717358098 166 EAISALDMSIQSQILDLLTTLrdKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQE 221
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-219 |
8.77e-10 |
|
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: 56.50 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 10 SYRSGVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGI----EKPDtGTVMLDGQPV---CQRHTRlgkmS 82
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSVE-GDIHYNGIPYkefAEKYPG----E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 83 VVFQDYKSSLHPYFNVRQILNEALSQCDtpvddkeahmtallervglsaaflNKYPQMMSGGEAQRVAIARAVITNPDYI 162
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETLDFALRCKG------------------------NEFVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 163 VLDEAISALDMSIQSQILDLLTTLRDKYQLSLIFITHdiQAA---VYLCEDLIIFNDGQI 219
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLY--QASdeiYDLFDKVLVLYEGRQ 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-218 |
1.47e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 6 NVTKSYrSGVKrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqrhtrlgkmsvvf 85
Cdd:PRK10982 3 NISKSF-PGVK-----ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 86 qDYKSSLHPYFN----VRQILNEALsQCDT---------P-----VDDKEAH--MTALLERVGLSAAFLNKYPQmMSGGE 145
Cdd:PRK10982 63 -DFKSSKEALENgismVHQELNLVL-QRSVmdnmwlgryPtkgmfVDQDKMYrdTKAIFDELDIDIDPRAKVAT-LSVSQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 146 AQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFNDGQ 218
Cdd:PRK10982 140 MQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-221 |
1.51e-09 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 56.84 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKrqkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ--RHTRLG 79
Cdd:cd03288 20 IKIHDLCVRYENNLK----PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlpLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 KMSVVFQD---YKSSLHpyFNVrqilnEALSQCdtpVDDK--EAHMTALLERV------GLSaAFLNKYPQMMSGGEAQR 148
Cdd:cd03288 96 RLSIILQDpilFSGSIR--FNL-----DPECKC---TDDRlwEALEIAQLKNMvkslpgGLD-AVVTEGGENFSVGQRQL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717358098 149 VAIARAVITNPDYIVLDEAISALDMSIQSqILD--LLTTLRDKYQLSLIFITHDIQAAvylcEDLIIFNDGQIQE 221
Cdd:cd03288 165 FCLARAFVRKSSILIMDEATASIDMATEN-ILQkvVMTAFADRTVVTIAHRVSTILDA----DLVLVLSRGILVE 234
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
31-214 |
4.47e-09 |
|
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: 54.12 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 31 SKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGqpvcqrhtrlgkMSVVFQDYKSSLhpyfnvrqilnealsqcd 110
Cdd:cd03222 23 KEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG------------ITPVYKPQYIDL------------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 111 tpvddkeahmtallervglsaaflnkypqmmSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKY 190
Cdd:cd03222 73 -------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
170 180
....*....|....*....|....
gi 1717358098 191 QLSLIFITHDIQAAVYLCEDLIIF 214
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-227 |
5.38e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 23 VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTRLG-KMSVVF--QDYK-SSLHPYFNV 98
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYisEDRKrDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 99 RQILN----EALSQCDTPVDDKEAHMtALLERVGLsaaFLNKYPQM------MSGGEAQRVAIARAVITNPDYIVLDEAI 168
Cdd:PRK10762 348 KENMSltalRYFSRAGGSLKHADEQQ-AVSDFIRL---FNIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717358098 169 SALDMSIQSQILDLLTTLRdKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQ 227
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFK-AEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQ 481
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
4-221 |
6.14e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.82 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 4 VQNVTKSYR---SGVKRQKRQIV-----------KQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVmldgq 69
Cdd:PRK13546 7 IKNVTKEYRiyrTNKERMKDALIpkhknktffalDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 70 pvcqrhTRLGKMSVVfqdyksslhpyfnvrqILNEALSQCDTPVDDKEAHMTAL-LERVGLSA------------AFLNK 136
Cdd:PRK13546 82 ------DRNGEVSVI----------------AISAGLSGQLTGIENIEFKMLCMgFKRKEIKAmtpkiiefselgEFIYQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 137 YPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQAAVYLCEDLIIFND 216
Cdd:PRK13546 140 PVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNK-TIFFVSHNLGQVRQFCTKIAWIEG 218
|
....*
gi 1717358098 217 GQIQE 221
Cdd:PRK13546 219 GKLKD 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-172 |
6.52e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 23 VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPV-----CQRHtRLGKMSVVFqdyksSLHPYFN 97
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdagdiATRR-RVGYMSQAF-----SLYGELT 355
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 98 VRQ--ILNEALSQcdTPVDDKEAHMTALLERVGLsAAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALD 172
Cdd:NF033858 356 VRQnlELHARLFH--LPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-221 |
7.82e-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: 55.72 E-value: 7.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 26 VSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDG-------QPVCQRHTRlgKMSVVFQdyKSSLHPYFnv 98
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGsvayvpqQAWIQNDSL--RENILFG--KALNEKYY-- 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 99 RQILNEALSQCDT---PVDDKeahmTALLERvGLSaaflnkypqmMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSI 175
Cdd:TIGR00957 731 QQVLEACALLPDLeilPSGDR----TEIGEK-GVN----------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 176 QSQILDLLT----TLRDKYQlslIFITHDIQaavYLCE-DLII-FNDGQIQE 221
Cdd:TIGR00957 796 GKHIFEHVIgpegVLKNKTR---ILVTHGIS---YLPQvDVIIvMSGGKISE 841
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-200 |
9.86e-09 |
|
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: 52.76 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 32 KGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMldgqpvcqrhtrlgkmsvvfqdyksslhpYFNVRQILNEALSQCDT 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI-----------------------------YIDGEDILEEVLDQLLL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 112 PVDDKEAHMTallervglsaaflnkypqmmSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDK-- 189
Cdd:smart00382 52 IIVGGKKASG--------------------SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLll 111
|
170
....*....|....
gi 1717358098 190 ---YQLSLIFITHD 200
Cdd:smart00382 112 kseKNLTVILTTND 125
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-200 |
1.01e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 5 QNVTKSYRsgvkrQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLdgqpvcQRHTRLGKMSvv 84
Cdd:PRK11819 10 NRVSKVVP-----PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP------APGIKVGYLP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 85 fQDYKssLHPYFNVRQILNEALSQCDTPVD----------DKEAHMTALLERVG-----LSAAFL----NKYPQMM---- 141
Cdd:PRK11819 77 -QEPQ--LDPEKTVRENVEEGVAEVKAALDrfneiyaayaEPDADFDALAAEQGelqeiIDAADAwdldSQLEIAMdalr 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717358098 142 -----------SGGEAQRVAIARAVITNPDYIVLDEAISALDM-SIQSqildLLTTLRDkYQLSLIFITHD 200
Cdd:PRK11819 154 cppwdakvtklSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAeSVAW----LEQFLHD-YPGTVVAVTHD 219
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
10-172 |
1.15e-08 |
|
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: 53.40 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 10 SYRSGVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTL-----ARMILGIEkpdTGTVMLDGQPVCQRHTRlgKMSVV 84
Cdd:cd03232 10 NYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLldvlaGRKTAGVI---TGEILINGRPLDKNFQR--STGYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 85 FQDYkssLH-PYFNVRqilnEALSqcdtpvddkeahMTALLErvGLSAAflnkypqmmsggEAQRVAIARAVITNPDYIV 163
Cdd:cd03232 85 EQQD---VHsPNLTVR----EALR------------FSALLR--GLSVE------------QRKRLTIGVELAAKPSILF 131
|
....*....
gi 1717358098 164 LDEAISALD 172
Cdd:cd03232 132 LDEPTSGLD 140
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
26-202 |
1.48e-08 |
|
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: 53.49 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 26 VSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTV----MLDGQPVCQRHTRLGKMSVVFQDYKSSL--------- 92
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLlnatveeni 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 93 ---HPYFNVR-QILNEALS-QCDT---PVDDKeahmTALLERvGLSaaflnkypqmMSGGEAQRVAIARAVITNPDYIVL 164
Cdd:cd03290 100 tfgSPFNKQRyKAVTDACSlQPDIdllPFGDQ----TEIGER-GIN----------LSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1717358098 165 DEAISALDMSIQSQILD--LLTTLRDKYQlSLIFITHDIQ 202
Cdd:cd03290 165 DDPFSALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQ 203
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-221 |
3.62e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYRSGVKrqkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqrhTRLG- 79
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLP----PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV----AKFGl 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 80 -----KMSVVFQD-------YKSSLHPYFNVRQI-LNEALSQcdtpvddkeAHMTALLER--VGLSAAfLNKYPQMMSGG 144
Cdd:PLN03232 1306 tdlrrVLSIIPQSpvlfsgtVRFNIDPFSEHNDAdLWEALER---------AHIKDVIDRnpFGLDAE-VSEGGENFSVG 1375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 145 EAQRVAIARAVITNPDYIVLDEAISALDMSIQSQIldlLTTLRDKYQ-LSLIFITHDIQAAVYlCEDLIIFNDGQIQE 221
Cdd:PLN03232 1376 QRQLLSLARALLRRSKILVLDEATASVDVRTDSLI---QRTIREEFKsCTMLVIAHRLNTIID-CDKILVLSSGQVLE 1449
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-200 |
3.79e-08 |
|
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: 51.55 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 23 VKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEkpdtGTVMLDGQPvcqrhTRLGKMSVVFqdyksslhpyfnvrqil 102
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYAS----GKARLISFL-----PKFSRNKLIF----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 103 neaLSQCDTPVDdkeahmtallerVGLSAAFLNKYPQMMSGGEAQRVAIAR--AVITNPDYIVLDEAISALDMSIQSQIL 180
Cdd:cd03238 65 ---IDQLQFLID------------VGLGYLTLGQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLL 129
|
170 180
....*....|....*....|
gi 1717358098 181 DLLTTLRDKYQlSLIFITHD 200
Cdd:cd03238 130 EVIKGLIDLGN-TVILIEHN 148
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-195 |
6.50e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 27 SFQCSKGQSIAIIGESGSGKSTLARMILGiekpdtGTVMLDGQPVC--QRHTRLG-----KM-SVVFQDYKSS-LHPY-- 95
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG------ELPLLSGERQSqfSHITRLSfeqlqKLvSDEWQRNNTDmLSPGed 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 96 ---FNVRQILNEALSqcDTPVDDKEA---HMTALLERvglsaAFlnKYpqmMSGGEAQRVAIARAVITNPDYIVLDEAIS 169
Cdd:PRK10938 97 dtgRTTAEIIQDEVK--DPARCEQLAqqfGITALLDR-----RF--KY---LSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180
....*....|....*....|....*..
gi 1717358098 170 ALDMSIQSQILDLLTTL-RDKYQLSLI 195
Cdd:PRK10938 165 GLDVASRQQLAELLASLhQSGITLVLV 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-172 |
7.40e-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: 52.48 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 32 KGQSIAIIGESGSGKSTLARMILGIEKPDTGtvMLDGQP----VCQRH--TRLgkmsvvfQDY---------KSSLHP-- 94
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLG--DYDEEPswdeVLKRFrgTEL-------QDYfkklangeiKVAHKPqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 95 ------YF--NVRQILNEalsqcdtpVDDKEAhMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDE 166
Cdd:COG1245 169 vdlipkVFkgTVRELLEK--------VDERGK-LDELAEKLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
....*.
gi 1717358098 167 AISALD 172
Cdd:COG1245 239 PSSYLD 244
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-226 |
9.21e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrSGVKrqkrqIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDT--GTVMLDGQpVCQrhtrl 78
Cdd:NF040905 1 ILEMRGITKTF-PGVK-----ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGE-VCR----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 79 gkmsvvFQDYKSS-------------LHPYFNVRQIL---NEALSQcdTPVDDKEAHMTA--LLERVGLSAAflnkyPQM 140
Cdd:NF040905 69 ------FKDIRDSealgiviihqelaLIPYLSIAENIflgNERAKR--GVIDWNETNRRAreLLAKVGLDES-----PDT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 141 MSG----GEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQLSLIFITHDIQAAVYLCEDLIIFND 216
Cdd:NF040905 136 LVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRD 214
|
250
....*....|
gi 1717358098 217 GQIQERLNRH 226
Cdd:NF040905 215 GRTIETLDCR 224
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-173 |
1.07e-07 |
|
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: 51.21 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 33 GQSIAIIGESGSGKSTLARMILGIEKPDTGtvmldgqpvcqRHTRLGKMSVVFQDYK-SSLHPYFnvRQILNEALSQCDT 111
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLG-----------KFDDPPDWDEILDEFRgSELQNYF--TKLLEGDVKVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 112 P--VD-----------------DKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALD 172
Cdd:cd03236 93 PqyVDlipkavkgkvgellkkkDERGKLDELVDQLELRH-VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
.
gi 1717358098 173 M 173
Cdd:cd03236 172 I 172
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-181 |
1.25e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.22 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 22 IVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVmldgqpvcqRHTrlGKMSvvFQDYKSSLHPYfNVRQI 101
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI---------KHS--GRIS--FSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 102 LNEALSQcdtpvddKEAHMTALLERVGLSAAfLNKYPQ-----------MMSGGEAQRVAIARAVITNPDYIVLDEAISA 170
Cdd:TIGR01271 507 IIFGLSY-------DEYRYTSVIKACQLEED-IALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170
....*....|.
gi 1717358098 171 LDMSIQSQILD 181
Cdd:TIGR01271 579 LDVVTEKEIFE 589
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-246 |
1.28e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 33 GQSIAIIGESGSGKSTLARMILG-IEKPDTGTVMLDGQ-----PVCQRHTRLGKMSVVF-QDYKSSLHpyfnVRQILNEA 105
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSvayvpQVSWIFNATVRENILFgSDFESERY----WRAIDVTA 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 106 LsQCDtpVDDKEAH-MTALLERvGLSaaflnkypqmMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDllT 184
Cdd:PLN03232 719 L-QHD--LDLLPGRdLTEIGER-GVN----------ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD--S 782
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 185 TLRDKYQ-LSLIFITHDIQaAVYLCEDLIIFNDGQIQERLNRHQLKTlqndyTRELFEKQFMN 246
Cdd:PLN03232 783 CMKDELKgKTRVLVTNQLH-FLPLMDRIILVSEGMIKEEGTFAELSK-----SGSLFKKLMEN 839
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-219 |
1.34e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 19 KRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMIL----GIEKPDTGTVMLDGQPV--CQRHTRlgkMSVVFQDYKSSL 92
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPeeIKKHYR---GDVVYNAETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 93 HPYFNVRQILNEAlSQCDTP------VDDKE--AHMTALLERV-GLSAAFL----NKYPQMMSGGEAQRVAIARAVITNP 159
Cdd:TIGR00956 150 FPHLTVGETLDFA-ARCKTPqnrpdgVSREEyaKHIADVYMATyGLSHTRNtkvgNDFVRGVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717358098 160 DYIVLDEAISALDMSIQSQILDLLTTLRDKYQLS-LIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTSANILDTTpLVAIYQCSQDAYELFDKVIVLYEGYQ 289
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-228 |
1.92e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGI-EKPDTGTVMLDGQPV----CQRH 75
Cdd:PRK13549 259 ILEVRNLTAWD---PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVkirnPQQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRLGkMSVVFQDYKS-SLHPYFNVRQ-ILNEALSQ-CDTPVDDKEAHMTALLE-----RVGLSAAFLNKypQMMSGGEAQ 147
Cdd:PRK13549 336 IAQG-IAMVPEDRKRdGIVPVMGVGKnITLAALDRfTGGSRIDDAAELKTILEsiqrlKVKTASPELAI--ARLSGGNQQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 148 RVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRdKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQ 227
Cdd:PRK13549 413 KAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLV-QQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHN 491
|
.
gi 1717358098 228 L 228
Cdd:PRK13549 492 L 492
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-181 |
3.34e-07 |
|
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: 49.86 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 22 IVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQ-----------PVCQRHTRLgkMSVVFQDYKs 90
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRisfssqfswimPGTIKENII--FGVSYDEYR- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 91 slhpYFNVRQI--LNEALSQcdTPVDDKeahmTALLERvGLSaaflnkypqmMSGGEAQRVAIARAVITNPDYIVLDEAI 168
Cdd:cd03291 129 ----YKSVVKAcqLEEDITK--FPEKDN----TVLGEG-GIT----------LSGGQRARISLARAVYKDADLYLLDSPF 187
|
170
....*....|...
gi 1717358098 169 SALDMSIQSQILD 181
Cdd:cd03291 188 GYLDVFTEKEIFE 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-172 |
3.52e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 32 KGQSIAIIGESGSGKSTLARMILGIEKPDTGtvmldgqpvcqRHTRLGKMSVVFQDYK-SSLHPYF-------------- 96
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLG-----------DYEEEPSWDEVLKRFRgTELQNYFkklyngeikvvhkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 97 ------------NVRQILNEAlsqcdtpvdDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIARAVITNPDYIVL 164
Cdd:PRK13409 167 qyvdlipkvfkgKVRELLKKV---------DERGKLDEVVERLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
....*...
gi 1717358098 165 DEAISALD 172
Cdd:PRK13409 237 DEPTSYLD 244
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-203 |
5.00e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.29 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDtGTVMLDG---QPVCQRHTRL 78
Cdd:TIGR01271 1218 MDVQGLTAKYTEA----GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvswNSVTLQTWRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 79 G------KMSVVFQDYKSSLHPYfnvrqilnEALSqcdtpvdDKEAHMTAllERVGLSAAfLNKYPQ-----------MM 141
Cdd:TIGR01271 1293 AfgvipqKVFIFSGTFRKNLDPY--------EQWS-------DEEIWKVA--EEVGLKSV-IEQFPDkldfvlvdggyVL 1354
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 142 SGGEAQRVAIARAVITNPDYIVLDEAISALDmSIQSQILDllTTLRDKY-QLSLIFITHDIQA 203
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLD-PVTLQIIR--KTLKQSFsNCTVILSEHRVEA 1414
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-199 |
1.85e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTksyrsgVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIE--KPDTGTVMLDGQPVCQ--RHT 76
Cdd:PRK09580 1 MLSIKDLH------VSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLElsPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 77 RLGK-MSVVFQdYKSSLhPYFNVRQILNEALSQC-----DTPVD--DKEAHMTALLERVGLSAAFLNKYPQM-MSGGEAQ 147
Cdd:PRK09580 75 RAGEgIFMAFQ-YPVEI-PGVSNQFFLQTALNAVrsyrgQEPLDrfDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 148 RVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITH 199
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTH 203
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
141-191 |
1.98e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 1.98e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1717358098 141 MSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDllTTLRDKYQ 191
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELR 789
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
124-200 |
2.42e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 2.42e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717358098 124 LERVGLSA-AFLNKypqmMSGGEAQRVAIARAVITNPDYIVLDEAISALDMsiqsQILDLLTTLRDKYQLSLIFITHD 200
Cdd:PRK11147 143 LAQLGLDPdAALSS----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHD 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-237 |
4.43e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKsyrsgvKRQKRqiVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVC-------- 72
Cdd:PRK10982 250 ILEVRNLTS------LRQPS--IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhnaneai 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 73 ----------QRHTRL-GKMSVVFQDYKSSLHPYFNVRQILNEALSQCDTP--VDDKEAHMTALLERVGlsaaflnkypq 139
Cdd:PRK10982 322 nhgfalvteeRRSTGIyAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQwvIDSMRVKTPGHRTQIG----------- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 140 MMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQAAVYLCEDLIIFNDGQI 219
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLV 469
|
250
....*....|....*...
gi 1717358098 220 QERLNRHqlKTLQNDYTR 237
Cdd:PRK10982 470 AGIVDTK--TTTQNEILR 485
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
30-76 |
5.40e-06 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 46.47 E-value: 5.40e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1717358098 30 CSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLD---GqpvcqRHT 76
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVREDdskG-----RHT 236
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
24-207 |
5.48e-06 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.10 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 24 KQVSFQCSKGQSIAIIGESGSGKSTLA--------------------RMILG-IEKPD----TG---TVMLDgqpvcQRH 75
Cdd:cd03270 12 KNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayaRQFLGqMDKPDvdsiEGlspAIAID-----QKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 76 TRLGKMSVVfqDYKSSLHPYFNV---RQILNEALSQcdtpvddkeahmtalLERVGLSAAFLNKYPQMMSGGEAQRVAIA 152
Cdd:cd03270 87 TSRNPRSTV--GTVTEIYDYLRLlfaRVGIRERLGF---------------LVDVGLGYLTLSRSAPTLSGGEAQRIRLA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 153 RAVITNPDYI--VLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHD---IQAAVYL 207
Cdd:cd03270 150 TQIGSGLTGVlyVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDedtIRAADHV 208
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-221 |
8.43e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 45.62 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGvkrqKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDtGTVMLDG-----QPVCQRHT 76
Cdd:cd03289 3 MTVKDLTAKYTEG----GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGvswnsVPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 77 RLG----KMSVVFQDYKSSLHPYfnvrqilnealsqcdTPVDDKEAHMTAllERVGLSAAfLNKYPQ-----------MM 141
Cdd:cd03289 78 AFGvipqKVFIFSGTFRKNLDPY---------------GKWSDEEIWKVA--EEVGLKSV-IEQFPGqldfvlvdggcVL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 142 SGGEAQRVAIARAVITNPDYIVLDEAISALDmSIQSQILDllTTLRDKYQ-LSLIFITHDIQAAVYlCEDLIIFNDGQIQ 220
Cdd:cd03289 140 SHGHKQLMCLARSVLSKAKILLLDEPSAHLD-PITYQVIR--KTLKQAFAdCTVILSEHRIEAMLE-CQRFLVIEENKVR 215
|
.
gi 1717358098 221 E 221
Cdd:cd03289 216 Q 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-77 |
2.60e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 2.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 26 VSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQRHTR 77
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPR 323
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
5-191 |
7.51e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.56 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 5 QNVTksYRSGVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTL-----ARMILGIekPDTGTVMLDGQP--------- 70
Cdd:TIGR00956 763 RNLT--YEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLlnvlaERVTTGV--ITGGDRLVNGRPldssfqrsi 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 71 --VCQRHTRLGKMSVvfqdyKSSLHPYFNVRQILNEALSQCDTPVDD--KEAHMTALLER-VGLSAAFLNKYpqmmsggE 145
Cdd:TIGR00956 839 gyVQQQDLHLPTSTV-----RESLRFSAYLRQPKSVSKSEKMEYVEEviKLLEMESYADAvVGVPGEGLNVE-------Q 906
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1717358098 146 AQRVAIARAVITNPDYIV-LDEAISALDMSIQSQILDLLTTLRDKYQ 191
Cdd:TIGR00956 907 RKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQ 953
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
23-230 |
7.60e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.19 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 23 VKQVSFQCSKGQSIAIIGESGSG--KSTLARMILGiekPDTGTVMLDGQPVCQRHTRLGKMSVVFQDYKSSLHPYFNVRQ 100
Cdd:NF000106 29 VDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*HRPVR*GRRESFSGRE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 101 ILNEALSQCDTPVDDKEAHMTALLERVGLSAAfLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQIL 180
Cdd:NF000106 106 NLYMIGR*LDLSRKDARARADELLERFSLTEA-AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1717358098 181 DLLTTL-RDKyqLSLIFITHDIQAAVYLCEDLIIFNDGQIQERLNRHQLKT 230
Cdd:NF000106 185 DEVRSMvRDG--ATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
141-201 |
1.42e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 1.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717358098 141 MSGGEAQRVAIARAVITNPDYIVLDEAISALDMSIQSQILD--LLTTLRDKYQlslIFITHDI 201
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecFLGALAGKTR---VLATHQV 842
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
33-134 |
1.48e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.92 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 33 GQSIAIIGESGSGKSTLARMILgiekpdtgtvmldgQPVCQRHTRLgkMSVVFQDYKSSLhPYFNVRQILNEALSQCDTp 112
Cdd:COG3899 311 GELVLVSGEAGIGKSRLVRELA--------------RRARARGGRV--LRGKCDQLERGV-PYAPLAQALRALLGQLPE- 372
|
90 100
....*....|....*....|..
gi 1717358098 113 vDDKEAHMTALLERVGLSAAFL 134
Cdd:COG3899 373 -DELAAWRARLLAALGANGRLL 393
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
11-53 |
2.11e-04 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 42.10 E-value: 2.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1717358098 11 YRSGVKRQKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMI 53
Cdd:COG5635 158 YVPLNLLERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYL 200
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-221 |
2.79e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.07 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 2 LEVQNVTKSYRSGVKrqkrQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVCQ---RHTRL 78
Cdd:PTZ00243 1309 LVFEGVQMRYREGLP----LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAyglRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 79 gKMSVVFQDyksslhPYF---NVRQILN---EALSqcdtpvddkeAHMTALLERVGLSAAFLNKYPQM----------MS 142
Cdd:PTZ00243 1385 -QFSMIPQD------PVLfdgTVRQNVDpflEASS----------AEVWAALELVGLRERVASESEGIdsrvleggsnYS 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 143 GGEAQRVAIARAVIT-NPDYIVLDEAISALDMSIQSQILDLLTTLRDKYqlSLIFITHDIQaAVYLCEDLIIFNDGQIQE 221
Cdd:PTZ00243 1448 VGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLH-TVAQYDKIIVMDHGAVAE 1524
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-220 |
4.65e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 41.15 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 1 MLEVQNVTKSYrSGVKRQKrqiVKQVSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDGQPVcqrhtrLGK 80
Cdd:TIGR01257 1937 ILRLNELTKVY-SGTSSPA---VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI------LTN 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 81 MSVVFQDYKSSlhPYFNV-------RQILNEALSQCDTPVDDKEAHMTALLERVGLSAaFLNKYPQMMSGGEAQRVAIAR 153
Cdd:TIGR01257 2007 ISDVHQNMGYC--PQFDAiddlltgREHLYLYARLRGVPAEEIEKVANWSIQSLGLSL-YADRLAGTYSGGNKRKLSTAI 2083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717358098 154 AVITNPDYIVLDEAISALDMSIQSQILDLLTTLRdKYQLSLIFITHDIQAAVYLCEDLIIFNDGQIQ 220
Cdd:TIGR01257 2084 ALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII-REGRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| PRK07261 |
PRK07261 |
DNA topology modulation protein; |
36-53 |
5.27e-04 |
|
DNA topology modulation protein;
Pssm-ID: 180911 [Multi-domain] Cd Length: 171 Bit Score: 39.70 E-value: 5.27e-04
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
35-89 |
7.15e-04 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 39.88 E-value: 7.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717358098 35 SIAIIGESGSGKSTLARMIL----GIEKP---DTGTVMLDGQPVCQRHTRLGKMSVVFQDYK 89
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLyatgAIDRLgrvEDGNTVSDYDPEEKKRKMSIETSVAPLEWN 62
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
32-199 |
7.68e-04 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 39.88 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 32 KGQSIAIIGESGSGKSTLARMIlgiekpdtGTVMLDGQPVCQRHTRLGKmsVVFQ---DYKSSLHPyfnvRqiLNEALSQ 108
Cdd:COG3598 12 EGGVTLLAGPPGTGKSFLALQL--------AAAVAAGGPWLGRRVPPGK--VLYLaaeDDRGELRR----R--LKALGAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 109 CDTPVDDKEAHMTALLERVGLSAAFLnkypqmmsggeaqRVAIARAVIT-NPDYIVLD--------EAISALDMsiqSQI 179
Cdd:COG3598 76 LGLPFADLDGRLRLLSLAGDLDDTDD-------------LEALERAIEEeGPDLVVIDplarvfggDENDAEEM---RAF 139
|
170 180
....*....|....*....|
gi 1717358098 180 LDLLTTLRDKYQLSLIFITH 199
Cdd:COG3598 140 LNPLDRLAERTGAAVLLVHH 159
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-209 |
7.93e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.51 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 37 AIIGESGSGKSTL---ARMILGIEKPDTGTVMLDGQPVCQRHTRLGKMSVVFQDYKSslHPYFNVRQIlnEALSQCdtpv 113
Cdd:cd03240 26 LIVGQNGAGKTTIieaLKYALTGELPPNSKGGAHDPKLIREGEVRAQVKLAFENANG--KKYTITRSL--AILENV---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 114 ddkeahmtaLLERVGLSAAFLNKYPQMMSGGE------AQRVAIARAVITNPDYIVLDEAISALDM-SIQSQILDLLTTL 186
Cdd:cd03240 98 ---------IFCHQGESNWPLLDMRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEER 168
|
170 180
....*....|....*....|....*.
gi 1717358098 187 RDKYQLSLIFITHD---IQAAVYLCE 209
Cdd:cd03240 169 KSQKNFQLIVITHDeelVDAADHIYR 194
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
117-199 |
9.56e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 117 EAHMTALLERVGLSAAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLDEAISALDMsiqSQILDLLTTLRdKYQLSLIF 196
Cdd:PLN03073 321 EARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL---HAVLWLETYLL-KWPKTFIV 396
|
...
gi 1717358098 197 ITH 199
Cdd:PLN03073 397 VSH 399
|
|
| DUF87 |
pfam01935 |
Helicase HerA, central domain; This entry represents the central domain found in archaeal ... |
34-67 |
9.67e-04 |
|
Helicase HerA, central domain; This entry represents the central domain found in archaeal proteins such as DNA double-strand break repair helicase HerA (EC:3.6.4.12). HerA is a helicase which is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding. It forms a complex with NurA nuclease, this complex has the 5'-3' DNA end resection activity and is essential for cell viability in the crenarchaeon Sulfolobus islandicus. This domain includes the the central RecA-like catalytic core and a flanking four-helix bundle. The function of this prokaryotic domain is unknown. It contains several conserved aspartates and histidines that could be metal ligands.
Pssm-ID: 376671 [Multi-domain] Cd Length: 220 Bit Score: 39.27 E-value: 9.67e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1717358098 34 QSIAIIGESGSGKSTLARMILG--IEKPDTGTVMLD 67
Cdd:pfam01935 24 RHFAILGSTGSGKSNTVAVLLEelLEKKGATVLIFD 59
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
30-54 |
1.27e-03 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 38.88 E-value: 1.27e-03
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
34-204 |
1.34e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 39.66 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 34 QSIAIIGESGSGK-STLARMI--LGIEKPDTGTVMLDgqpvcqrHTRLGKMSVVfQDYksslhpyfnVRQILNEALSQCD 110
Cdd:PRK11889 242 QTIALIGPTGVGKtTTLAKMAwqFHGKKKTVGFITTD-------HSRIGTVQQL-QDY---------VKTIGFEVIAVRD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 111 tpvddkEAHMTALL----ERVGLSAAFLNKYPQMMSGGEAQRVAIARAVITNPDYIVLdeaisALDMSIQSQ-ILDLLTT 185
Cdd:PRK11889 305 ------EAAMTRALtyfkEEARVDYILIDTAGKNYRASETVEEMIETMGQVEPDYICL-----TLSASMKSKdMIEIITN 373
|
170
....*....|....*....
gi 1717358098 186 LRDKYQLSLIFITHDIQAA 204
Cdd:PRK11889 374 FKDIHIDGIVFTKFDETAS 392
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
36-62 |
1.69e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 37.85 E-value: 1.69e-03
10 20 30
....*....|....*....|....*....|
gi 1717358098 36 IAIIGESGSGKSTLARMI---LGIEKPDTG 62
Cdd:cd02020 2 IAIDGPAGSGKSTVAKLLakkLGLPYLDTG 31
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-71 |
2.25e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.62 E-value: 2.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 18 QKRQIVKQVSFQCSKGQSIAIIGESGSGKSTLARMILG------IekpdTGTVMLDGQPV 71
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsygrnI----SGTVFKDGKEV 326
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
126-213 |
2.70e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 126 RVGLSAAFLnkypqmmSGGEAQRVAIAR---AVITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKYQlSLIFITHDIQ 202
Cdd:TIGR00630 822 RLGQPATTL-------SGGEAQRIKLAKelsKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLD 893
|
90
....*....|.
gi 1717358098 203 aaVYLCEDLII 213
Cdd:TIGR00630 894 --VIKTADYII 902
|
|
| Cmk |
COG0283 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
36-62 |
2.76e-03 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440052 [Multi-domain] Cd Length: 220 Bit Score: 37.70 E-value: 2.76e-03
10 20 30
....*....|....*....|....*....|
gi 1717358098 36 IAIIGESGSGKSTLARMI---LGIEKPDTG 62
Cdd:COG0283 3 IAIDGPAGSGKSTVAKALakrLGYHYLDTG 32
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
37-200 |
5.21e-03 |
|
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: 36.57 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 37 AIIGESGSGKSTLARMILGIekpdtgtvmldgqpVCQRHTRLGKMSVVFQDYKSSLhpyfnvrqilnealsqcdtpvddk 116
Cdd:cd03227 25 IITGPNGSGKSTILDAIGLA--------------LGGAQSATRRRSGVKAGCIVAA------------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 117 eAHMTALLERVGLSaaflnkypqmmsGGEAQRVAIARAV----ITNPDYIVLDEAISALDMSIQSQILDLLTTLRDKyQL 192
Cdd:cd03227 67 -VSAELIFTRLQLS------------GGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK-GA 132
|
....*...
gi 1717358098 193 SLIFITHD 200
Cdd:cd03227 133 QVIVITHL 140
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
26-200 |
6.09e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 37.56 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 26 VSFQCSKGQSIAIIGESGSGKSTLARMILGIEKPDTGTVMLDgqpvcqRHTRLGKMS---VVFQDYkSSL-------HPY 95
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD------PNERLGKLRqdqFAFEEF-TVLdtvimghTEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717358098 96 FNVRQILNEALSQCDTPVDD---------KEAHM---TA------LLERVGLSAAFLNKYPQMMSGGEAQRVAIARAVIT 157
Cdd:PRK15064 93 WEVKQERDRIYALPEMSEEDgmkvadlevKFAEMdgyTAearageLLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1717358098 158 NPDYIVLDEAISALDMSIQSQILDLLTtlrdKYQLSLIFITHD 200
Cdd:PRK15064 173 NPDILLLDEPTNNLDINTIRWLEDVLN----ERNSTMIIISHD 211
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
30-53 |
7.30e-03 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 36.77 E-value: 7.30e-03
|
| |
