|
Name |
Accession |
Description |
Interval |
E-value |
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-250 |
1.03e-160 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 445.67 E-value: 1.03e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVEnpaeadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHVTSGTITLDGADVLAMSIDE 83
Cdd:COG0396 1 LEIKNLHVSVE-------GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGEDILELSPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RARAGLFLAMQYPVEVPGVSMSNFLRSAATAIRGEPPKLRHWVKEVKAAMAALDIDPAFAERSVNEGFSGGEKKRHEILQ 163
Cdd:COG0396 74 RARAGIFLAFQYPVEIPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEGFSGGEKKRNEILQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 164 LELLKPKIAILDETDSGLDVDALRVVSEGVNRYAeSQHGGILLITHYTRILRYIHPEYVHVFVGGRIVESGGSELADELD 243
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIDALRIVAEGVNKLR-SPDRGILIITHYQRILDYIKPDFVHVLVDGRIVKSGGKELALELE 232
|
....*..
gi 950436399 244 QNGYVGF 250
Cdd:COG0396 233 EEGYDWL 239
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
4-248 |
1.00e-144 |
|
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: 405.11 E-value: 1.00e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVEnpaeadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHVTSGTITLDGADVLAMSIDE 83
Cdd:TIGR01978 1 LKIKDLHVSVE-------DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILFKGQDLLELEPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RARAGLFLAMQYPVEVPGVSMSNFLRSAATAIR---GEPP-KLRHWVKEVKAAMAALDIDPAFAERSVNEGFSGGEKKRH 159
Cdd:TIGR01978 74 RARAGLFLAFQYPEEIPGVSNLEFLRSALNARRsarGEEPlDLLDFEKLLKEKLALLDMDEEFLNRSVNEGFSGGEKKRN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 160 EILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAEsQHGGILLITHYTRILRYIHPEYVHVFVGGRIVESGGSELA 239
Cdd:TIGR01978 154 EILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLRE-PDRSFLIITHYQRLLNYIKPDYVHVLLDGRIVKSGDVELA 232
|
....*....
gi 950436399 240 DELDQNGYV 248
Cdd:TIGR01978 233 KELEAKGYD 241
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-247 |
1.55e-112 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 323.90 E-value: 1.55e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 2 TILEIKDLHVSVEnpaeadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHVTSGTITLDGADVLAMSI 81
Cdd:CHL00131 6 PILEIKNLHASVN-------ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGESILDLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 82 DERARAGLFLAMQYPVEVPGVSMSNFLRSAATAIRG-------EPPKLRHWVKEvkaAMAALDIDPAFAERSVNEGFSGG 154
Cdd:CHL00131 79 EERAHLGIFLAFQYPIEIPGVSNADFLRLAYNSKRKfqglpelDPLEFLEIINE---KLKLVGMDPSFLSRNVNEGFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 155 EKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHgGILLITHYTRILRYIHPEYVHVFVGGRIVESG 234
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQRLLDYIKPDYVHVMQNGKIIKTG 234
|
250
....*....|...
gi 950436399 235 GSELADELDQNGY 247
Cdd:CHL00131 235 DAELAKELEKKGY 247
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-247 |
6.38e-109 |
|
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: 312.92 E-value: 6.38e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVEnpaeadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHVTSGTITLDGADVLAMSIDE 83
Cdd:cd03217 1 LEIKDLHVSVG-------GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDITDLPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RARAGLFLAMQYPVEVPGVSMSNFLrsaatairgeppklrhwvkevkaamaaldidpafaeRSVNEGFSGGEKKRHEILQ 163
Cdd:cd03217 74 RARLGIFLAFQYPPEIPGVKNADFL------------------------------------RYVNEGFSGGEKKRNEILQ 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 164 LELLKPKIAILDETDSGLDVDALRVVSEGVNRYAEsQHGGILLITHYTRILRYIHPEYVHVFVGGRIVESGGSELADELD 243
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLRE-EGKSVLIITHYQRLLDYIKPDRVHVLYDGRIVKSGDKELALEIE 196
|
....
gi 950436399 244 QNGY 247
Cdd:cd03217 197 KKGY 200
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-247 |
2.93e-89 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 264.73 E-value: 2.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVEnpaeadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHVTSGTITLDGADVLAMSID 82
Cdd:PRK09580 1 MLSIKDLHVSVE-------DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLELSPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 83 ERARAGLFLAMQYPVEVPGVSMSNFLRSAATAI---RGEPPKLRHWVKE-VKAAMAALDIDPAFAERSVNEGFSGGEKKR 158
Cdd:PRK09580 74 DRAGEGIFMAFQYPVEIPGVSNQFFLQTALNAVrsyRGQEPLDRFDFQDlMEEKIALLKMPEDLLTRSVNVGFSGGEKKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 159 HEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGIlLITHYTRILRYIHPEYVHVFVGGRIVESGGSEL 238
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFI-IVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTL 232
|
....*....
gi 950436399 239 ADELDQNGY 247
Cdd:PRK09580 233 VKQLEEQGY 241
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-209 |
5.14e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.84 E-value: 5.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVENPaeadheiPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG-HPkyhVTSGTITLDGADVLAMSID 82
Cdd:COG4619 1 LELEGLSFRVGGK-------PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADlDP---PTSGEIYLDGKPLSAMPPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 83 E-RARAGLFlaMQYPVEVPGVSMSNFLRsaATAIRGEPPKLrhwvKEVKAAMAALDIDPAFAERSVNEgFSGGEKKRHEI 161
Cdd:COG4619 71 EwRRQVAYV--PQEPALWGGTVRDNLPF--PFQLRERKFDR----ERALELLERLGLPPDILDKPVER-LSGGERQRLAL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 950436399 162 LQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITH 209
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSH 189
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-234 |
1.52e-30 |
|
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: 113.75 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVENPaeaDHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSID 82
Cdd:cd03257 1 LLEVKNLSVSFPTG---GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK--PTSGSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 83 ERARAGLFLAM--QYPvevpgvsMS--NFLRSAATAIRgEPpkLRHWVKEVKAA---------MAALDIDPAFAERSVNE 149
Cdd:cd03257 76 LRKIRRKEIQMvfQDP-------MSslNPRMTIGEQIA-EP--LRIHGKLSKKEarkeavlllLVGVGLPEEVLNRYPHE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 150 gFSGGEKKRHEI---LqleLLKPKIAILDETDSGLDVDA----LRVVSEgvnryAESQHG-GILLITHYTRILRYIhPEY 221
Cdd:cd03257 146 -LSGGQRQRVAIaraL---ALNPKLLIADEPTSALDVSVqaqiLDLLKK-----LQEELGlTLLFITHDLGVVAKI-ADR 215
|
250
....*....|...
gi 950436399 222 VHVFVGGRIVESG 234
Cdd:cd03257 216 VAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-237 |
3.02e-29 |
|
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: 115.39 E-value: 3.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MT-ILEIKDLHVSVenpaeADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG-HPKYHVTSGTITLDGADVLA 78
Cdd:COG1123 1 MTpLLEVRDLSVRY-----PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGlLPHGGRISGEVLLDGRDLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 79 MSIDERARAglfLAMqypveVPGVSMSNFLRSA-------ATAIRGEPPKLRHwvKEVKAAMAALDIDpAFAERSVNEgF 151
Cdd:COG1123 76 LSEALRGRR---IGM-----VFQDPMTQLNPVTvgdqiaeALENLGLSRAEAR--ARVLELLEAVGLE-RRLDRYPHQ-L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 152 SGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHYTRILRYIhPEYVHVFVGGRIV 231
Cdd:COG1123 144 SGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEI-ADRVVVMDDGRIV 222
|
....*.
gi 950436399 232 ESGGSE 237
Cdd:COG1123 223 EDGPPE 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-234 |
8.46e-29 |
|
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: 113.84 E-value: 8.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 2 TILEIKDLHVSveNPAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG-HPkyhVTSGTITLDGADVLAMS 80
Cdd:COG1123 259 PLLEVRNLSKR--YPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGlLR---PTSGSILFDGKDLTKLS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 81 IDERARAGLFLAM--QYPvevpgVSMSNFLRSAATAIrGEPPKLRHWV------KEVKAAMAALDIDPAFAERSVNEgFS 152
Cdd:COG1123 334 RRSLRELRRRVQMvfQDP-----YSSLNPRMTVGDII-AEPLRLHGLLsraerrERVAELLERVGLPPDLADRYPHE-LS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 153 GGEKKRHEI---LqleLLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHYTRILRYIhPEYVHVFVGGR 229
Cdd:COG1123 407 GGQRQRVAIaraL---ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYI-ADRVAVMYDGR 482
|
....*
gi 950436399 230 IVESG 234
Cdd:COG1123 483 IVEDG 487
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-249 |
3.48e-27 |
|
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: 105.06 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MTILEIKDLHVSVenpaeadHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMS 80
Cdd:COG0410 1 MPMLEVENLHAGY-------GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP--PRSGSIRFDGEDITGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 81 IDERARAGLFLamqypveVP---GV--SMS---NfLRSAATAIRGEPPklRHWVKEvkaamAALDIDPAFAERSVNEG-- 150
Cdd:COG0410 72 PHRIARLGIGY-------VPegrRIfpSLTveeN-LLLGAYARRDRAE--VRADLE-----RVYELFPRLKERRRQRAgt 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 151 FSGGEKKrheilQLEL-----LKPKIAILDETDSGL------DV-DALR-VVSEGVnryaesqhgGILLITHYTR-ILRY 216
Cdd:COG0410 137 LSGGEQQ-----MLAIgralmSRPKLLLLDEPSLGLapliveEIfEIIRrLNREGV---------TILLVEQNARfALEI 202
|
250 260 270
....*....|....*....|....*....|....*
gi 950436399 217 IHpeYVHVFVGGRIVESGGSE--LADELDQNGYVG 249
Cdd:COG0410 203 AD--RAYVLERGRIVLEGTAAelLADPEVREAYLG 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-237 |
5.05e-27 |
|
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: 104.89 E-value: 5.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVenpAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG-HPkyhVTSGTITLDGADVlamsiD 82
Cdd:COG1124 2 LEVRNLSVSY---GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGlER---PWSGEVTFDGRPV-----T 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 83 ERARAGLFLAMQYPVEVPGVSMsNFLRSAATAIRgEPPKLRH---WVKEVKAAMAALDIDPAFAERSVNEgFSGGEKKRH 159
Cdd:COG1124 71 RRRRKAFRRRVQMVFQDPYASL-HPRHTVDRILA-EPLRIHGlpdREERIAELLEQVGLPPSFLDRYPHQ-LSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 160 EILQLELLKPKIAILDETDSGLDV----DALRVvsegVNRYAESQHGGILLITHYTRILRYIhPEYVHVFVGGRIVESGG 235
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVsvqaEILNL----LKDLREERGLTYLFVSHDLAVVAHL-CDRVAVMQNGRIVEELT 222
|
..
gi 950436399 236 SE 237
Cdd:COG1124 223 VA 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-176 |
5.20e-27 |
|
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: 101.96 E-value: 5.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIdERARAGLFLAMQYPVEVPGVSMS 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGL--LSPTEGTILLDGQDLTDDER-KSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 950436399 106 NFLRsaaTAIRGEPPKLRHWVKEVKAAMAALDIDPaFAERSVNEG---FSGGEKKRHEILQLELLKPKIAILDE 176
Cdd:pfam00005 78 ENLR---LGLLLKGLSKREKDARAEEALEKLGLGD-LADRPVGERpgtLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-229 |
1.17e-26 |
|
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: 102.93 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 5 EIKDLHVSVEnpaeaDHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDER 84
Cdd:cd03225 1 ELKNLSFSYP-----DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLG--PTSGEVLVDGKDLTKLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 85 AR-AGlfLAMQYP----------VEVpGVSMSNflrsaataiRGEPPKLRhwVKEVKAAMAALDIDpAFAERSVNEgFSG 153
Cdd:cd03225 74 RRkVG--LVFQNPddqffgptveEEV-AFGLEN---------LGLPEEEI--EERVEEALELVGLE-GLRDRSPFT-LSG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 950436399 154 GEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHgGILLITHYTRILRYIhPEYVHVFVGGR 229
Cdd:cd03225 138 GQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLEL-ADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-234 |
6.11e-26 |
|
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: 101.64 E-value: 6.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVENpaeadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMSI 81
Cdd:COG1122 1 IELENLSFSYPG------GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGllKP----TSGEVLVDGKDITKKNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 82 DE-RARAGL-FlamQYP----VEvPGV------SMSNFLRSAATAIRgeppklrhwvkEVKAAMAALDIDpAFAERSVNE 149
Cdd:COG1122 71 RElRRKVGLvF---QNPddqlFA-PTVeedvafGPENLGLPREEIRE-----------RVEEALELVGLE-HLADRPPHE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 150 gFSGGEKKRheilqLEL-----LKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHgGILLITHYTRILRYIhPEYVHV 224
Cdd:COG1122 135 -LSGGQKQR-----VAIagvlaMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLDLVAEL-ADRVIV 206
|
250
....*....|
gi 950436399 225 FVGGRIVESG 234
Cdd:COG1122 207 LDDGRIVADG 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-241 |
7.01e-26 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 101.36 E-value: 7.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVEnpaeadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDE 83
Cdd:cd03224 1 LEVENLNAGYG-------KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGL--LPPRSGSIRFDGRDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RARAGLFLAMQ----YPvevpgvSMS---NfLRSAATAIRGEPPKlrhWVKEvkaamAALDIDPAFAERSVNEG--FSGG 154
Cdd:cd03224 72 RARAGIGYVPEgrriFP------ELTveeN-LLLGAYARRRAKRK---ARLE-----RVYELFPRLKERRKQLAgtLSGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 155 EKKrheilQLE-----LLKPKIAILDETDSGLDVDALRVVSEGVNRYAESqhG-GILLITHYTRILRYIhPEYVHVFVGG 228
Cdd:cd03224 137 EQQ-----MLAiaralMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE--GvTILLVEQNARFALEI-ADRAYVLERG 208
|
250
....*....|....
gi 950436399 229 RIVESG-GSELADE 241
Cdd:cd03224 209 RVVLEGtAAELLAD 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-234 |
3.09e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 99.75 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVENpaeadheIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDE 83
Cdd:COG1131 1 IEVRGLTKRYGD-------KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL--LRPTSGEVRVLGEDVARDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RARAGLFLamQYPVEVPGVSMSNFLRSAAtAIRGEPPKLRHwvKEVKAAMAALDIDPaFAERSVnEGFSGGEKKRHEILQ 163
Cdd:COG1131 72 RRRIGYVP--QEPALYPDLTVRENLRFFA-RLYGLPRKEAR--ERIDELLELFGLTD-AADRKV-GTLSGGMKQRLGLAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 950436399 164 LELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHgGILLITHYTRILRYIhPEYVHVFVGGRIVESG 234
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGK-TVLLSTHYLEEAERL-CDRVAIIDKGRIVADG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-234 |
4.67e-25 |
|
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: 99.73 E-value: 4.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVenpaeadHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMS 80
Cdd:COG1120 1 MLEAENLSVGY-------GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGllKP----SSGEVLLDGRDLASLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 81 IDERARAglfLAM--QYPVEVPG------VSMSnflRSAATAIRGEPPKlrHWVKEVKAAMAALDIDpAFAERSVNEgFS 152
Cdd:COG1120 70 RRELARR---IAYvpQEPPAPFGltvrelVALG---RYPHLGLFGRPSA--EDREAVEEALERTGLE-HLADRPVDE-LS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 153 GGEKkrheilQLELL------KPKIAILDETDSGLD----VDALRVVSegvnRYAESQHGGILLITHY-TRILRYIHpeY 221
Cdd:COG1120 140 GGER------QRVLIaralaqEPPLLLLDEPTSHLDlahqLEVLELLR----RLARERGRTVVMVLHDlNLAARYAD--R 207
|
250
....*....|...
gi 950436399 222 VHVFVGGRIVESG 234
Cdd:COG1120 208 LVLLKDGRIVAQG 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-209 |
1.44e-24 |
|
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: 98.39 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVenpaeadHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSIDE 83
Cdd:COG4555 2 IEVENLSKKY-------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAG--LLKPDSGSILIDGEDVRKEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RARAGLFlamqyPVEV---PGVSMSNFLRSAAtAIRGEPPKLRHwvKEVKAAMAALDIDPaFAERSVnEGFSGGEKKRHE 160
Cdd:COG4555 73 RRQIGVL-----PDERglyDRLTVRENIRYFA-ELYGLFDEELK--KRIEELIELLGLEE-FLDRRV-GELSTGMKKKVA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 950436399 161 ILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHgGILLITH 209
Cdd:COG4555 143 LARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGK-TVLFSSH 190
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-234 |
1.86e-24 |
|
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: 96.35 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 5 EIKDLHVSVENPaeadheiPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDER 84
Cdd:cd03214 1 EVENLSVGYGGR-------TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK--PSSGEILLDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 85 ARAGLFLAmQypvevpgvsmsnflrsaatairgeppklrhwvkevkaAMAALDIDpAFAERSVNEgFSGGEKKRHEILQL 164
Cdd:cd03214 72 ARKIAYVP-Q-------------------------------------ALELLGLA-HLADRPFNE-LSGGERQRVLLARA 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 950436399 165 ELLKPKIAILDETDSGLDVD-ALRVVSEgVNRYAESQHGGILLITHY-TRILRYIHpeyvHVFV--GGRIVESG 234
Cdd:cd03214 112 LAQEPPILLLDEPTSHLDIAhQIELLEL-LRRLARERGKTVVMVLHDlNLAARYAD----RVILlkDGRIVAQG 180
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
26-234 |
5.09e-24 |
|
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: 96.74 E-value: 5.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSIDERARAGLFLAMQYPVEVPGVSMS 105
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISG--FLRPTSGSVLFDGEDITGLPPHEIARLGIGRTFQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 106 NFLRSAATAIRGEPPKLRHWVKEVKA----AMAALDID--PAFAERSVnEGFSGGEKKRHEILQLELLKPKIAILDETDS 179
Cdd:cd03219 94 ENVMVAAQARTGSGLLLARARREEREarerAEELLERVglADLADRPA-GELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 950436399 180 GLDVDALRVVSEGVNRYAESQHgGILLITHYTRILRYIhPEYVHVFVGGRIVESG 234
Cdd:cd03219 173 GLNPEETEELAELIRELRERGI-TVLLVEHDMDVVMSL-ADRVTVLDQGRVIAEG 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-229 |
2.95e-22 |
|
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: 90.00 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 5 EIKDLHVSVenpaeadHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIdER 84
Cdd:cd00267 1 EIENLSFRY-------GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGL--LKPTSGEILIDGKDIAKLPL-EE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 85 ARAGLFLAMQypvevpgvsmsnflrsaatairgeppklrhwvkevkaamaaldidpafaersvnegFSGGEKKRHEILQL 164
Cdd:cd00267 71 LRRRIGYVPQ--------------------------------------------------------LSGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 950436399 165 ELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHgGILLITHYTRILRYIhPEYVHVFVGGR 229
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGR-TVIIVTHDPELAELA-ADRVIVLKDGK 157
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
19-234 |
1.23e-21 |
|
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: 93.75 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 19 ADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDE-RARAGLflamqypv 97
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL--YEPTSGRILIDGIDLRQIDPASlRRQIGV-------- 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 98 evpgVSMSNFLRSaATaIR-----GEPPKLRHWVKEVkAAMAALDidpAFAER-------SVNEG---FSGGEKKRHEIL 162
Cdd:COG2274 554 ----VLQDVFLFS-GT-IRenitlGDPDATDEEIIEA-ARLAGLH---DFIEAlpmgydtVVGEGgsnLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 950436399 163 QLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQhgGILLITHYTRILRyiHPEYVHVFVGGRIVESG 234
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIR--LADRIIVLDKGRIVEDG 691
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
24-249 |
1.59e-21 |
|
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: 89.91 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDERARAGL-FLAMQypvevpgv 102
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVK--PDSGKILLDGQDITKLPMHKRARLGIgYLPQE-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 103 sMSNFLR-------SAATAIRGEPPKLRHwvKEVKAAMAALDIDPafAERSVNEGFSGGEKKRHEILQLELLKPKIAILD 175
Cdd:cd03218 84 -ASIFRKltveeniLAVLEIRGLSKKERE--EKLEELLEEFHITH--LRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 950436399 176 ETDSGLDVDALRVVSEGVNRYAESQHGgiLLIT-HYTR-ILRYIHPEYVhVFvGGRIVESGGSE--LADELDQNGYVG 249
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIG--VLITdHNVReTLSITDRAYI-IY-EGKVLAEGTPEeiAANELVRKVYLG 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-208 |
1.93e-21 |
|
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: 89.08 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVenpaeadHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLamSIDE 83
Cdd:COG4133 3 LEAENLSCRR-------GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGL--LPPSAGEVLWNGEPIR--DARE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RARAGLFLAMQYPVEVPGVSMSNFLRSAAtAIRGEPPKLRhwvkEVKAAMAALDIDPaFAERSVNEgFSGGEKKRHEILQ 163
Cdd:COG4133 72 DYRRRLAYLGHADGLKPELTVRENLRFWA-ALYGLRADRE----AIDEALEAVGLAG-LADLPVRQ-LSAGQKRRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 950436399 164 LELLKPKIAILDETDSGLDVDALRVVSEGVNRYAesQHGGILLIT 208
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAHL--ARGGAVLLT 187
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-237 |
4.67e-21 |
|
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: 90.11 E-value: 4.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVENPaeaDHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG-HPKYHVTSGTITLDGADVLAMSI 81
Cdd:COG0444 1 LLEVRNLKVYFPTR---RGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGlLPPPGITSGEILFDGEDLLKLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 82 DE-RARAGLFLAM--QYPvevpgvsMS--NFLRSAATAIrGEPPKLRHWV------KEVKAAMAALDIDPafAERSVNE- 149
Cdd:COG0444 78 KElRKIRGREIQMifQDP-------MTslNPVMTVGDQI-AEPLRIHGGLskaearERAIELLERVGLPD--PERRLDRy 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 150 --GFSGGEKKRHEI---LqleLLKPKIAILDETDSGLDV-------DALRvvsegvnRYAESQHGGILLITHYTRILRYI 217
Cdd:COG0444 148 phELSGGMRQRVMIaraL---ALEPKLLIADEPTTALDVtiqaqilNLLK-------DLQRELGLAILFITHDLGVVAEI 217
|
250 260
....*....|....*....|
gi 950436399 218 hPEYVHVFVGGRIVESGGSE 237
Cdd:COG0444 218 -ADRVAVMYAGRIVEEGPVE 236
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-183 |
5.61e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 89.02 E-value: 5.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVenpaeadHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMSI 81
Cdd:COG4559 2 LEAENLSVRL-------GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGelTP----SSGEVRLNGRPLAAWSP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 82 DERA--RAGL----FLAMQYPV-EVpgVSMSnflRSAATAIRGEPPKLrhwvkeVKAAMAALDIDpAFAERSVNEgFSGG 154
Cdd:COG4559 71 WELArrRAVLpqhsSLAFPFTVeEV--VALG---RAPHGSSAAQDRQI------VREALALVGLA-HLAGRSYQT-LSGG 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 950436399 155 EKKR-------HEILQLELLKPKIAILDETDSGLDV 183
Cdd:COG4559 138 EQQRvqlarvlAQLWEPVDGGPRWLFLDEPTSALDL 173
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-209 |
1.15e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 88.17 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MTILEIKDLHVS----VenpaeadheipILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADV 76
Cdd:COG0411 2 DPLLEVRGLTKRfgglV-----------AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF--YRPTSGRILFDGRDI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 77 LAMSIDERARAGLFLAMQYPVEVPGvsMS---NfLRSAATAIRGE--------PPKLRHWVKEVKA-AMAALD---IDpA 141
Cdd:COG0411 69 TGLPPHRIARLGIARTFQNPRLFPE--LTvleN-VLVAAHARLGRgllaallrLPRARREEREARErAEELLErvgLA-D 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 950436399 142 FAERSVNEgFSGGEKKRheilqLEL-----LKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITH 209
Cdd:COG0411 145 RADEPAGN-LSYGQQRR-----LEIaralaTEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEH 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-209 |
3.21e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 86.68 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MTILEIKDLHVSVENPaeadheiPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG-HPkyhVTSGTITLDGADVLAm 79
Cdd:COG1121 4 MPAIELENLTVSYGGR-------PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGlLP---PTSGTVRLFGKPPRR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 80 sidERARAG-----LFLAMQYPV---EVpgVSMSNFLRSAATAIRGeppklRHWVKEVKAAMAALDIDpAFAERSVNEgF 151
Cdd:COG1121 73 ---ARRRIGyvpqrAEVDWDFPItvrDV--VLMGRYGRRGLFRRPS-----RADREAVDEALERVGLE-DLADRPIGE-L 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 950436399 152 SGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAesQHG-GILLITH 209
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR--REGkTILVVTH 197
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-234 |
3.67e-20 |
|
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: 86.68 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MTILEIKDLHVSVEnpaeadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPKYhvtSGTITLDGADVLA 78
Cdd:COG1119 1 DPLLELRNVTVRRG-------GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdlPPTY---GNDVRLFGERRGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 79 MSIDE-RARAGLF---LAMQYPVEVPGVSMsnfLRSAATAIRGEPPKLRHWVKE-VKAAMAALDIDpAFAERSVNEgFSG 153
Cdd:COG1119 71 EDVWElRKRIGLVspaLQLRFPRDETVLDV---VLSGFFDSIGLYREPTDEQRErARELLELLGLA-HLADRPFGT-LSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 154 GEKKRheilqleLL-------KPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHYtriLRYIHPEYVHV-- 224
Cdd:COG1119 146 GEQRR-------VLiaralvkDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHH---VEEIPPGITHVll 215
|
250
....*....|
gi 950436399 225 FVGGRIVESG 234
Cdd:COG1119 216 LKDGRVVAAG 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-209 |
6.67e-20 |
|
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: 84.89 E-value: 6.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 5 EIKDLHVSVENPaeadheiPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG-HPKyhvTSGTITLDGADVLamsiDE 83
Cdd:cd03235 1 EVEDLTVSYGGH-------PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGlLKP---TSGSIRVFGKPLE----KE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RARAGlFLAMQYPVE--VPgVSMSNFLRSAATAIRGEPPKLRHWVKE-VKAAMAALDIDpAFAERSVNEgFSGGEKKRHE 160
Cdd:cd03235 67 RKRIG-YVPQRRSIDrdFP-ISVRDVVLMGLYGHKGLFRRLSKADKAkVDEALERVGLS-ELADRQIGE-LSGGQQQRVL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 950436399 161 ILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHgGILLITH 209
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGM-TILVVTH 190
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-89 |
6.79e-20 |
|
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: 85.56 E-value: 6.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 2 TILEIKDLHVSVenpAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAM 79
Cdd:COG4181 7 PIIELRGLTKTV---GTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGldRP----TSGTVRLAGQDLFAL 79
|
90
....*....|
gi 950436399 80 siDERARAGL 89
Cdd:COG4181 80 --DEDARARL 87
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
26-210 |
7.15e-20 |
|
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: 85.11 E-value: 7.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDERARAGlfLAMQYPVEVPGVS-M 104
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK--PTSGRATVAGHDVVREPREVRRRIG--IVFQDLSVDDELTgW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 105 SNFLRSAatAIRGEP-PKLRHWVKEVKAAMAALDidpaFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDETDSGLDV 183
Cdd:cd03265 92 ENLYIHA--RLYGVPgAERRERIDELLDFVGLLE----AADRLVKT-YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180
....*....|....*....|....*..
gi 950436399 184 DALRVVSEGVNRYAESQHGGILLITHY 210
Cdd:cd03265 165 QTRAHVWEYIEKLKEEFGMTILLTTHY 191
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
24-232 |
9.50e-20 |
|
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: 85.63 E-value: 9.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDERARAGLFLAMQYPVEVPGVS 103
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEK--PAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQDSPSAVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 104 MsnflRSAATAIRGEPpkLRHWVK----EVKAAMAAL----DIDPAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILD 175
Cdd:TIGR02769 103 P----RMTVRQIIGEP--LRHLTSldesEQKARIAELldmvGLRSEDADKLPRQ-LSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 950436399 176 ETDSGLDvdalRVVSEGVNRYAES--QHGGI--LLITHYTRILRYIHPEyVHVFVGGRIVE 232
Cdd:TIGR02769 176 EAVSNLD----MVLQAVILELLRKlqQAFGTayLFITHDLRLVQSFCQR-VAVMDKGQIVE 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-234 |
1.18e-19 |
|
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: 84.86 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVEnpaeadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMSI 81
Cdd:cd03261 1 IELRGLTKSFG-------GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGllRP----DSGEVLIDGEDISGLSE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 82 DE----RARAG-------LFLAM------QYPVEVpgvsMSNFLRSAATAIrgeppklrhwVKEvKAAMAALdidPAFAE 144
Cdd:cd03261 70 AElyrlRRRMGmlfqsgaLFDSLtvfenvAFPLRE----HTRLSEEEIREI----------VLE-KLEAVGL---RGAED 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 145 RSVNEgFSGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHYTRILRYIhPEYVHV 224
Cdd:cd03261 132 LYPAE-LSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAI-ADRIAV 209
|
250
....*....|
gi 950436399 225 FVGGRIVESG 234
Cdd:cd03261 210 LYDGKIVAEG 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-209 |
2.76e-19 |
|
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: 83.08 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 5 EIKDLHVSVEnpaeadHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHvtSGTITLDGADVlamSIDER 84
Cdd:cd03226 1 RIENISFSYK------KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES--SGSILLNGKPI---KAKER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 85 ARAGlFLAMQYP-VEVPGVSMSNFLRSAATAIRGEPPKLRHwvkevkaAMAALDIDpAFAERSVNEgFSGGEKKRHEILQ 163
Cdd:cd03226 70 RKSI-GYVMQDVdYQLFTDSVREELLLGLKELDAGNEQAET-------VLKDLDLY-ALKERHPLS-LSGGQKQRLAIAA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 950436399 164 LELLKPKIAILDETDSGLDVDALRVVSEGVNRYAEsQHGGILLITH 209
Cdd:cd03226 140 ALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAA-QGKAVIVITH 184
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-209 |
3.45e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 82.91 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVenpaeadHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHVT-SGTITLDGADVLAMSID 82
Cdd:COG4136 2 LSLENLTITL-------GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSaSGEVLLNGRRLTALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 83 ERaRAGLFlaMQYPVEVPGVSMSNFLrsaATAIRGEPPK-LRHwvKEVKAAMAALDIDpAFAERSVNEgFSGGEKKRHEI 161
Cdd:COG4136 75 QR-RIGIL--FQDDLLFPHLSVGENL---AFALPPTIGRaQRR--ARVEQALEEAGLA-GFADRDPAT-LSGGQRARVAL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 950436399 162 LQLELLKPKIAILDETDSGLDVdALRV-VSEGVNRYAESQHGGILLITH 209
Cdd:COG4136 145 LRALLAEPRALLLDEPFSKLDA-ALRAqFREFVFEQIRQRGIPALLVTH 192
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-232 |
7.08e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 82.40 E-value: 7.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 2 TILEIKDLHVSVEnpaEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAM 79
Cdd:COG1136 3 PLLELRNLTKSYG---TGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGldRP----TSGEVLIDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 80 SIDERAR------------AGLFlamqyP-------VEVPGVsmsnflrsaataIRGEPPKLRHwvKEVKAAMAALDIDp 140
Cdd:COG1136 76 SERELARlrrrhigfvfqfFNLL-----PeltalenVALPLL------------LAGVSRKERR--ERARELLERVGLG- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 141 AFAERSVNEgFSGGEKKRHEI---LqleLLKPKIAILDE------TDSGLDV-DALRvvsegvnRYAESQHGGILLITHY 210
Cdd:COG1136 136 DRLDHRPSQ-LSGGQQQRVAIaraL---VNRPKLILADEptgnldSKTGEEVlELLR-------ELNRELGTTIVMVTHD 204
|
250 260
....*....|....*....|..
gi 950436399 211 TRILRYIHpeYVHVFVGGRIVE 232
Cdd:COG1136 205 PELAARAD--RVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-218 |
7.15e-19 |
|
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: 82.54 E-value: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVENPAEadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDE 83
Cdd:cd03255 1 IELKNLSKTYGGGGE---KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR--PTSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RAR-----AGlFLAMQY---P-------VEVPGVsmsnflrsaataIRGEPPKLRHwvKEVKAAMAALDIDpAFAERSVN 148
Cdd:cd03255 76 LAAfrrrhIG-FVFQSFnllPdltalenVELPLL------------LAGVPKKERR--ERAEELLERVGLG-DRLNHYPS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 149 EgFSGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHYTRILRYIH 218
Cdd:cd03255 140 E-LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYAD 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-209 |
8.23e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.90 E-value: 8.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 2 TILEIKDLHVSVenpaeadHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAM 79
Cdd:PRK13548 1 AMLEARNLSVRL-------GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGelSP----DSGEVRLNGRPLADW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 80 SIDERA--RAGL----FLAMQYPV-EVpgVSMSnflRSAATAIRGEPPKLrhwvkeVKAAMAALDIDpAFAERSVNEgFS 152
Cdd:PRK13548 70 SPAELArrRAVLpqhsSLSFPFTVeEV--VAMG---RAPHGLSRAEDDAL------VAAALAQVDLA-HLAGRDYPQ-LS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 153 GGEKKRheiLQL---------ELLKPKIAILDETDSGLDV----DALRVVSegvnRYAESQHGGILLITH 209
Cdd:PRK13548 137 GGEQQR---VQLarvlaqlwePDGPPRWLLLDEPTSALDLahqhHVLRLAR----QLAHERGLAVIVVLH 199
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-209 |
1.28e-18 |
|
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: 80.50 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVEnpaeaDHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDE 83
Cdd:cd03228 1 IEFKNVSFSYP-----GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRL--YDPTSGEILIDGVDLRDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 raraglflamqypvevpgvsmsnfLRSaatairgeppklrhwvkevkaAMAALDIDPAFAERSVNE-GFSGGEKKRHEIL 162
Cdd:cd03228 74 ------------------------LRK---------------------NIAYVPQDPFLFSGTIREnILSGGQRQRIAIA 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 950436399 163 QLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQhgGILLITH 209
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAH 153
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-247 |
1.42e-18 |
|
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: 81.89 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 20 DHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIaghPK-YHVTSGTITLDGADVLAMSIDE-RARAGLflamqypv 97
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI---PRfYDVDSGRILIDGHDVRDYTLASlRRQIGL-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 98 evpgVSMSNFLRSAATA--IR-GEPPKLRHWVKEVKAAMAALDI--------DPAFAERSVNegFSGGEKKRHEILQLEL 166
Cdd:cd03251 81 ----VSQDVFLFNDTVAenIAyGRPGATREEVEEAARAANAHEFimelpegyDTVIGERGVK--LSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 167 LKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGgiLLITHytRILRYIHPEYVHVFVGGRIVESGGSElaDELDQNG 246
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMKNRTT--FVIAH--RLSTIENADRIVVLEDGKIVERGTHE--ELLAQGG 228
|
.
gi 950436399 247 Y 247
Cdd:cd03251 229 V 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-234 |
1.91e-18 |
|
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: 81.09 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVENPAeadheipILRGVDLTVKSGeTHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMSI 81
Cdd:cd03264 1 LQLENLTKRYGKKR-------ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATltPP----SSGTIRIDGQDVLKQPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 82 DERARAGlFLAMQYPVeVPGVSMSNFLRSAAtAIRGEPPKLRHwvKEVKAAMAALDIDPaFAERSVNeGFSGGEKKRHEI 161
Cdd:cd03264 69 KLRRRIG-YLPQEFGV-YPNFTVREFLDYIA-WLKGIPSKEVK--ARVDEVLELVNLGD-RAKKKIG-SLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 950436399 162 LQLELLKPKIAILDETDSGLDVD---ALR--VVSEGVNRYaesqhggILLITHYTRILRYIHPEyVHVFVGGRIVESG 234
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEeriRFRnlLSELGEDRI-------VILSTHIVEDVESLCNQ-VAVLNKGKLVFEG 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-209 |
2.66e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.91 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVEnpaeadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMS 80
Cdd:PRK10247 7 LLQLQNVGYLAG-------DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASliSP----TSGTLLFEGEDISTLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 81 iDERARAGLFLAMQYPVEVPGVSMSNFLrsAATAIRGEPPKLRHWVKEvkaaMAALDIDPAFAERSVNEgFSGGEKKRHE 160
Cdd:PRK10247 76 -PEIYRQQVSYCAQTPTLFGDTVYDNLI--FPWQIRNQQPDPAIFLDD----LERFALPDTILTKNIAE-LSGGEKQRIS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 950436399 161 ILQ-LELLkPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITH 209
Cdd:PRK10247 148 LIRnLQFM-PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTH 196
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-234 |
2.71e-18 |
|
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: 84.04 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSvenpaeADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDE 83
Cdd:COG4988 337 IELEDVSFS------YPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF--LPPYSGSILINGVDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RaRAGLFLAMQYPVEVPGVSMSNFLRSAATAIRgeppklrhwvKEVKAAMAALDIDpAFAER-------SVNE---GFSG 153
Cdd:COG4988 409 W-RRQIAWVPQNPYLFAGTIRENLRLGRPDASD----------EELEAALEAAGLD-EFVAAlpdgldtPLGEggrGLSG 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 154 GEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQhgGILLITHytRILRYIHPEYVHVFVGGRIVES 233
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITH--RLALLAQADRILVLDDGRIVEQ 552
|
.
gi 950436399 234 G 234
Cdd:COG4988 553 G 553
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-234 |
3.49e-18 |
|
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: 81.05 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 22 EIPILRGVDLTVKSGETHALMGPNGSGKST-----LSYaiaghpkYHVTSGTITLDGADVLAMSIDERaRAGLFLAMQYP 96
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTvvsllERF-------YDPTSGEILLDGVDIRDLNLRWL-RSQIGLVSQEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 97 VEVPGVSMSNFLRSAATAIrgeppklrhwVKEVKAAMAALDIDpAFAErSVNEGF-----------SGGEKKRHEILQLE 165
Cdd:cd03249 87 VLFDGTIAENIRYGKPDAT----------DEEVEEAAKKANIH-DFIM-SLPDGYdtlvgergsqlSGGQKQRIAIARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 950436399 166 LLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQhgGILLITHytRILRYIHPEYVHVFVGGRIVESG 234
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAH--RLSTIRNADLIAVLQNGQVVEQG 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
24-210 |
3.76e-18 |
|
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: 79.36 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMSIDERARAGlflamqYPVEVPG 101
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGllKP----DSGEIKVLGKDIKKEPEEVKRRIG------YLPEEPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 102 VsmsnflrsaatairgePPKLRhwVKEVkaamaaLDidpafaersvnegFSGGEKKRHEILQLELLKPKIAILDETDSGL 181
Cdd:cd03230 84 L----------------YENLT--VREN------LK-------------LSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180
....*....|....*....|....*....
gi 950436399 182 DVDALRVVSEGVNRYAEsQHGGILLITHY 210
Cdd:cd03230 127 DPESRREFWELLRELKK-EGKTILLSSHI 154
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-234 |
6.64e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 82.91 E-value: 6.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 20 DHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDE-RARAGLflamqypve 98
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF--YDPTSGRILIDGVDIRDLTLESlRRQIGV--------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 99 vpgVSMSNFL--RSAATAIR-GEPPKLRhwvKEVKAAMAALDIDPaFAER-------SVNEG---FSGGEKKRHEILQLE 165
Cdd:COG1132 419 ---VPQDTFLfsGTIRENIRyGRPDATD---EEVEEAAKAAQAHE-FIEAlpdgydtVVGERgvnLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 950436399 166 LLKPKIAILDETDSGLDVDALRVVSEGVNRYAEsqhgG--ILLITH-------YTRILryihpeyvhVFVGGRIVESG 234
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEALERLMK----GrtTIVIAHrlstirnADRIL---------VLDDGRIVEQG 556
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-234 |
8.30e-18 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 80.02 E-value: 8.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVEnpaeaDHeiPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMS 80
Cdd:COG1127 5 MIEVRNLTKSFG-----DR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGllRP----DSGEILVDGQDITGLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 81 IDERAR-----------AGLFLAM------QYPvevpgvsmsnfLRsaatAIRGEPPKLRHwvKEVKAAMAALDIDPAfA 143
Cdd:COG1127 74 EKELYElrrrigmlfqgGALFDSLtvfenvAFP-----------LR----EHTDLSEAEIR--ELVLEKLELVGLPGA-A 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 144 ERSVNEgFSGGEKKRHEI---LQLEllkPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHYTRILRYIhPE 220
Cdd:COG1127 136 DKMPSE-LSGGMRKRVALaraLALD---PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAI-AD 210
|
250
....*....|....
gi 950436399 221 YVHVFVGGRIVESG 234
Cdd:COG1127 211 RVAVLADGKIIAEG 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-209 |
1.78e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.60 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDERARAGLFLAMQYPVEVPGVS-M 104
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGV--YQPDSGEILLDGEPVRFRSPRDAQAAGIAIIHQELNLVPNLSvA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 105 SN-FLrsaatairGEPPKLRHWV------KEVKAAMAAL--DIDPafaERSVnEGFSGGEKKRHEILQLELLKPKIAILD 175
Cdd:COG1129 98 ENiFL--------GREPRRGGLIdwramrRRARELLARLglDIDP---DTPV-GDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 950436399 176 ETDSGL---DVDAL-RVV----SEGVnryaesqhgGILLITH 209
Cdd:COG1129 166 EPTASLterEVERLfRIIrrlkAQGV---------AIIYISH 198
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
25-234 |
2.28e-17 |
|
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: 78.38 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTL-------SYAIAGHPkyhvTSGTITLDGADVLAMSIDE---RARAGlfLAMQ 94
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLlrllnrlNDLIPGAP----DEGEVLLDGKDIYDLDVDVlelRRRVG--MVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 95 YPVEVPGVSMSNFlrSAATAIRGEppKLRHWVKE-VKAAMAALDIDPAFAERSVNEGFSGGEKKRHEILQLELLKPKIAI 173
Cdd:cd03260 89 KPNPFPGSIYDNV--AYGLRLHGI--KLKEELDErVEEALRKAALWDEVKDRLHALGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 950436399 174 LDETDSGLDVDALRVVSEGVNRYAESQhgGILLITH----YTRIlryihPEYVHVFVGGRIVESG 234
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHnmqqAARV-----ADRTAFLLNGRLVEFG 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-209 |
5.77e-17 |
|
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: 77.17 E-value: 5.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVenpaeadHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMSI 81
Cdd:cd03259 1 LELKGLSKTY-------GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGleRP----DSGEILIDGRDVTGVPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 82 DERARAGLFlamQYPVEVPgvSMSNFlRSAATAIRGEPPKLRHWVKEVKAAMAALDIDPaFAERSVNEgFSGGEKKRHEI 161
Cdd:cd03259 70 ERRNIGMVF---QDYALFP--HLTVA-ENIAFGLKLRGVPKAEIRARVRELLELVGLEG-LLNRYPHE-LSGGQQQRVAL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 950436399 162 LQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITH 209
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTH 189
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-212 |
8.90e-17 |
|
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: 76.99 E-value: 8.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 22 EIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMSIDERARAGLFLAM--QYPV 97
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGllQP----TSGEVRVAGLVPWKRRKKFLRRIGVVFGQktQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 98 EVPGVSMSNFLRsaatAIRGEPPklRHWVKEVKAAMAALDIDPaFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDET 177
Cdd:cd03267 109 DLPVIDSFYLLA----AIYDLPP--ARFKKRLDELSELLDLEE-LLDTPVRQ-LSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190
....*....|....*....|....*....|....*
gi 950436399 178 DSGLDVDALRVVSEGVNRYAESQHGGILLITHYTR 212
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMK 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-246 |
1.12e-16 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 76.50 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 20 DHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDE-RARAGLFLamQYPVE 98
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF--YDPQKGQILIDGIDIRDISRKSlRSMIGVVL--QDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 99 VPGVSMSNFLRSAATAIRGEppklrhWVKEVKAAMAALDID--PAFAERSVNEG---FSGGEKKRHEILQLELLKPKIAI 173
Cdd:cd03254 89 FSGTIMENIRLGRPNATDEE------VIEAAKEAGAHDFIMklPNGYDTVLGENggnLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 174 LDETDSGLDV-------DALRVVSEGvnRYAesqhggiLLITHYTRILRyiHPEYVHVFVGGRIVESGG-SELadeLDQN 245
Cdd:cd03254 163 LDEATSNIDTetekliqEALEKLMKG--RTS-------IIIAHRLSTIK--NADKILVLDDGKIIEEGThDEL---LAKK 228
|
.
gi 950436399 246 G 246
Cdd:cd03254 229 G 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
10-247 |
1.30e-16 |
|
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: 78.99 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 10 HVSVENPaeaDHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIaghPK-YHVTSGTITLDGADVLAMSIDErARAG 88
Cdd:TIGR02203 335 NVTFRYP---GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI---PRfYEPDSGQILLDGHDLADYTLAS-LRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 89 LFLAMQYPVEVPGVSMSNFlrsaATAIRGEPPKLRhwVKEVKAAMAALD--------IDPAFAERSVNegFSGGEKKRHE 160
Cdd:TIGR02203 408 VALVSQDVVLFNDTIANNI----AYGRTEQADRAE--IERALAAAYAQDfvdklplgLDTPIGENGVL--LSGGQRQRLA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 161 ILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGgiLLITHytRILRYIHPEYVHVFVGGRIVESGGSElaD 240
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT--LVIAH--RLSTIEKADRIVVMDDGRIVERGTHN--E 553
|
....*..
gi 950436399 241 ELDQNGY 247
Cdd:TIGR02203 554 LLARNGL 560
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-247 |
2.12e-16 |
|
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: 78.27 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVENPAEadheiPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDE 83
Cdd:COG4987 334 LELEDVSFRYPGAGR-----PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF--LDPQSGSITLGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 -RARAGLFlamqyPVEVPGVSMS---NFL--RSAATAirgeppklrhwvKEVKAAMAALDIDPAFAER------SVNEG- 150
Cdd:COG4987 407 lRRRIAVV-----PQRPHLFDTTlreNLRlaRPDATD------------EELWAALERVGLGDWLAALpdgldtWLGEGg 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 151 --FSGGEKKRheiLQLE--LLKPK-IAILDETDSGLDVDALRVVSEGVNRYAesQHGGILLITHYTRILRYIHPeyVHVF 225
Cdd:COG4987 470 rrLSGGERRR---LALAraLLRDApILLLDEPTEGLDAATEQALLADLLEAL--AGRTVLLITHRLAGLERMDR--ILVL 542
|
250 260
....*....|....*....|...
gi 950436399 226 VGGRIVESGG-SELadeLDQNGY 247
Cdd:COG4987 543 EDGRIVEQGThEEL---LAQNGR 562
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-97 |
2.37e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 74.39 E-value: 2.37e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 950436399 23 IPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSIDERARAGLFLAMQYPV 97
Cdd:cd03216 13 VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSG--LYKPDSGEILVDGKEVSFASPRDARRAGIAMVYQLSV 85
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-237 |
4.59e-16 |
|
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: 77.42 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 2 TILEIKDLHVSVENPA-----EADHeIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG-HPkyhvTSGTITLDGAD 75
Cdd:COG4172 274 PLLEARDLKVWFPIKRglfrrTVGH-VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRlIP----SEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 76 VLAMSidERARAGLFLAMQypveV----PGVSMSNflRSAATAIRGEP-----PKL----RHwvKEVKAAMAALDIDPAF 142
Cdd:COG4172 349 LDGLS--RRALRPLRRRMQ----VvfqdPFGSLSP--RMTVGQIIAEGlrvhgPGLsaaeRR--ARVAEALEEVGLDPAA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 143 AERSVNEgFSGGEKKRHEILQLELLKPKIAILDETDSGLDV-------DALRVVSEgvnryaesQHG-GILLITHYTRIL 214
Cdd:COG4172 419 RHRYPHE-FSGGQRQRIAIARALILEPKLLVLDEPTSALDVsvqaqilDLLRDLQR--------EHGlAYLFISHDLAVV 489
|
250 260
....*....|....*....|....
gi 950436399 215 RYI-HpeYVHVFVGGRIVESGGSE 237
Cdd:COG4172 490 RALaH--RVMVMKDGKVVEQGPTE 511
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
24-246 |
4.71e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 77.31 E-value: 4.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLsyaIA-GHPKYHVTSGTITLDGADVLAMSideraRAGLFLAMQYPVEVPGV 102
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTL---INlLQRVFDPQSGRILIDGTDIRTVT-----RASLRRNIAVVFQDAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 103 smsnFLRSAATAIR-GEPPKLRHWVKEVKAAMAALDidpaFAERSVNeGF-----------SGGEKKRHEILQLELLKPK 170
Cdd:PRK13657 421 ----FNRSIEDNIRvGRPDATDEEMRAAAERAQAHD----FIERKPD-GYdtvvgergrqlSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 950436399 171 IAILDETDSGLDVDALRVVSEGVNryaESQHG-GILLITHYTRILRyiHPEYVHVFVGGRIVESGGselADELDQNG 246
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALD---ELMKGrTTFIIAHRLSTVR--NADRILVFDNGRVVESGS---FDELVARG 560
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-234 |
5.80e-16 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 74.55 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 20 DHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSIDERaRAGLFLAMQYPVEV 99
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAG--LYKPTSGSVLLDGTDIRQLDPADL-RRNIGYVPQDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 100 PGVSMSNfLRSAATAIRGEppklrhwvKEVKAAMAA-----LDIDPAFAERSVNE---GFSGGEKKRHEILQLELLKPKI 171
Cdd:cd03245 91 YGTLRDN-ITLGAPLADDE--------RILRAAELAgvtdfVNKHPNGLDLQIGErgrGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 950436399 172 AILDETDSGLDVDALRVVSEGVNRYAESQhgGILLITHYTRIL----RYIhpeyvhVFVGGRIVESG 234
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLdlvdRII------VMDSGRIVADG 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-234 |
8.48e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.56 E-value: 8.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MTILEIKDLHVSVENpaeadheIPILRGVDLTVKSGETHALMGPNGSGKSTL----SYAIAGHPKYHVtSGTITLDGADV 76
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ-------VEVLDGVNLEIPDNTITALMGPSGSGKSTLlrvfNRLIELYPEARV-SGEVYLDGQDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 77 LAMSIDErARAGLFLAMQYPVEVP----------GVSMSNFLRSAA---TAIRGEPPKLRHWvKEVKAAMAAldidPAfa 143
Cdd:PRK14247 73 FKMDVIE-LRRRVQMVFQIPNPIPnlsifenvalGLKLNRLVKSKKelqERVRWALEKAQLW-DEVKDRLDA----PA-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 144 ersvnEGFSGGEKKRHEILQLELLKPKIAILDETDSGLD-VDALRVVSEGVNRYAESQhggILLITHYTRILRYIhPEYV 222
Cdd:PRK14247 145 -----GKLSGGQQQRLCIARALAFQPEVLLADEPTANLDpENTAKIESLFLELKKDMT---IVLVTHFPQQAARI-SDYV 215
|
250
....*....|..
gi 950436399 223 HVFVGGRIVESG 234
Cdd:PRK14247 216 AFLYKGQIVEWG 227
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-86 |
8.98e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.74 E-value: 8.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVeNPAEADhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSID 82
Cdd:COG1101 1 MLELKNLSKTF-NPGTVN-EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAG--SLPPDSGSILIDGKDVTKLPEY 76
|
....
gi 950436399 83 ERAR 86
Cdd:COG1101 77 KRAK 80
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-183 |
1.21e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.13 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDL--HVSVEN----PAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADV 76
Cdd:PRK15079 8 LLEVADLkvHFDIKDgkqwFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK--ATDGEVAWLGKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 77 LAMSIDER--ARAGLFLAMQYPVevpgVSMSNflRSAATAIRGEP-----PKL-RHWVKE-VKAAMAALDIDPAFAERSV 147
Cdd:PRK15079 86 LGMKDDEWraVRSDIQMIFQDPL----ASLNP--RMTIGEIIAEPlrtyhPKLsRQEVKDrVKAMMLKVGLLPNLINRYP 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 950436399 148 NEgFSGGEKKRHEILQLELLKPKIAILDETDSGLDV 183
Cdd:PRK15079 160 HE-FSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-255 |
1.29e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.65 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MTILEIKDLHVSVEnpaeadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMS 80
Cdd:PRK09536 1 MPMIDVSDLSVEFG-------DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAING--TLTPTAGTVLVAGDDVEALS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 81 iderARAglflAMQYPVEVP-GVSMSNFLRSAATAIRGEPPKLRHW-------VKEVKAAMAALDIDpAFAERSVNEgFS 152
Cdd:PRK09536 72 ----ARA----ASRRVASVPqDTSLSFEFDVRQVVEMGRTPHRSRFdtwtetdRAAVERAMERTGVA-QFADRPVTS-LS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 153 GGEKKRHEILQLELLKPKIAILDETDSGLDVD-ALRVVsEGVNRYAESQHGGILLITHYTRILRYIhpEYVHVFVGGRIV 231
Cdd:PRK09536 142 GGERQRVLLARALAQATPVLLLDEPTASLDINhQVRTL-ELVRRLVDDGKTAVAAIHDLDLAARYC--DELVLLADGRVR 218
|
250 260 270
....*....|....*....|....*....|.
gi 950436399 232 ESGGSE-------LADELDQNGYVGFSPASG 255
Cdd:PRK09536 219 AAGPPAdvltadtLRAAFDARTAVGTDPATG 249
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
24-246 |
2.06e-15 |
|
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: 73.42 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDE-RARAGLflamqypveVPGV 102
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRF--YDVSSGSILIDGQDIREVTLDSlRRAIGV---------VPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 103 S-------MSN--FLRSAATAIrgeppklrhwvkEVKAAMAALDIDPAFaeRSVNEGF-----------SGGEKKRHEIL 162
Cdd:cd03253 84 TvlfndtiGYNirYGRPDATDE------------EVIEAAKAAQIHDKI--MRFPDGYdtivgerglklSGGEKQRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 163 QLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGgiLLITHytRILRYIHPEYVHVFVGGRIVESGG-SELade 241
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTT--IVIAH--RLSTIVNADKIIVLKDGRIVERGThEEL--- 222
|
....*
gi 950436399 242 LDQNG 246
Cdd:cd03253 223 LAKGG 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-209 |
3.19e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 74.68 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDERARAGlfLAM--QYPVEVPgvS 103
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGL--YQPDSGEILIDGKPVRIRSPRDAIALG--IGMvhQHFMLVP--N 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 104 MS---NFLRSAATAiRGEPPKLRHWVKEVKAAMAA--LDIDP-AFAER-SVnegfsgGEKKRHEILQLELLKPKIAILDE 176
Cdd:COG3845 95 LTvaeNIVLGLEPT-KGGRLDRKAARARIRELSERygLDVDPdAKVEDlSV------GEQQRVEILKALYRGARILILDE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 950436399 177 TDSGL---DVDAL-----RVVSEGVnryaesqhgGILLITH 209
Cdd:COG3845 168 PTAVLtpqEADELfeilrRLAAEGK---------SIIFITH 199
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-209 |
3.46e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.88 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDERAraglfLAMQYPVEVPG-V 102
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR--PTSGTVRRAGGARVAYVPQRSE-----VPDSLPLTVRDlV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 103 SMSNFLRsaataiRGEPPKL-RHWVKEVKAAMAALDIDpAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDETDSGL 181
Cdd:NF040873 79 AMGRWAR------RGLWRRLtRDDRAAVDDALERVGLA-DLAGRQLGE-LSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180
....*....|....*....|....*...
gi 950436399 182 DVDALRVVSEGVNRYAESQhGGILLITH 209
Cdd:NF040873 151 DAESRERIIALLAEEHARG-ATVVVVTH 177
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
25-209 |
5.41e-15 |
|
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: 71.30 E-value: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHvtSGTITLDGADV-LAMSIDERARAGLFLAMQYP-VEVPGV 102
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQ--SGAVLIDGEPLdYSRKGLLERRQRVGLVFQDPdDQLFAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 103 SMSNFLRSAATAIRGEPPKLRHWVKEvkaAMAALDIDpAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDETDSGLD 182
Cdd:TIGR01166 85 DVDQDVAFGPLNLGLSEAEVERRVRE---ALTAVGAS-GLRERPTHC-LSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180
....*....|....*....|....*..
gi 950436399 183 VDALRVVSEGVNRYAEsQHGGILLITH 209
Cdd:TIGR01166 160 PAGREQMLAILRRLRA-EGMTVVISTH 185
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-232 |
5.63e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.80 E-value: 5.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSideRARAGLFLAMQYPVEVPGVSM 104
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLES--PSQGNVSWRGEPLAKLN---RAQRKAFRRDIQMVFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 105 SNfLRSAATAIRGEPpkLRHWVKEVKAAMAA--------LDIDPAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDE 176
Cdd:PRK10419 102 VN-PRKTVREIIREP--LRHLLSLDKAERLArasemlraVDLDDSVLDKRPPQ-LSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 177 TDSGLDvdalRVVSEGVNRYAES--QHGGI--LLITHYTRILRYIhPEYVHVFVGGRIVE 232
Cdd:PRK10419 178 AVSNLD----LVLQAGVIRLLKKlqQQFGTacLFITHDLRLVERF-CQRVMVMDNGQIVE 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-216 |
5.69e-15 |
|
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: 71.43 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVENPAEADHEiPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHVTSGTITLDGADVLAMSIde 83
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGK-QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPLDKRSF-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RARAGlfLAMQYPVEVPGVSMSNFLRSAAtairgeppKLRhwvkevkaamaaldidpafaersvneGFSGGEKKRHEIlQ 163
Cdd:cd03213 81 RKIIG--YVPQDDILHPTLTVRETLMFAA--------KLR--------------------------GLSGGERKRVSI-A 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 950436399 164 LELL-KPKIAILDETDSGLD-VDALRVVSEgVNRYAeSQHGGILLITHYTRILRY 216
Cdd:cd03213 124 LELVsNPSLLFLDEPTSGLDsSSALQVMSL-LRRLA-DTGRTIICSIHQPSSEIF 176
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-182 |
6.37e-15 |
|
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: 71.92 E-value: 6.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 18 EADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGH-PKYHVTSGTITLDGAdvlAMSIDERARAGLFLAmQYP 96
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvEGGGTTSGQILFNGQ---PRKPDQFQKCVAYVR-QDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 97 VEVPGVSMSNFLRSAATaIRGEppklRHWVKEVKAAMAALDIDPAFAERSVN----EGFSGGEKKRHEIlQLELLK-PKI 171
Cdd:cd03234 91 ILLPGLTVRETLTYTAI-LRLP----RKSSDAIRKKRVEDVLLRDLALTRIGgnlvKGISGGERRRVSI-AVQLLWdPKV 164
|
170
....*....|.
gi 950436399 172 AILDETDSGLD 182
Cdd:cd03234 165 LILDEPTSGLD 175
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-84 |
7.47e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 73.21 E-value: 7.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MTILEIKDLHVSVEnpaeadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMS 80
Cdd:COG3842 3 MPALELENVSKRYG-------DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGF--ETPDSGRILLDGRDVTGLP 73
|
....
gi 950436399 81 IDER 84
Cdd:COG3842 74 PEKR 77
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
10-234 |
9.70e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.60 E-value: 9.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 10 HVSVENPAEADheIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVlamsideraragl 89
Cdd:TIGR00958 483 DVSFSYPNRPD--VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL--YQPTGGQVLLDGVPL------------- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 90 flaMQYPvevpgvsmSNFLRSAATAIRGEPPKLRHWVKE--------------VKAAMAAL----------DIDPAFAER 145
Cdd:TIGR00958 546 ---VQYD--------HHYLHRQVALVGQEPVLFSGSVREniaygltdtpdeeiMAAAKAANahdfimefpnGYDTEVGEK 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 146 SVNegFSGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESqhggILLITHYTRILRYIHpeyvHVF 225
Cdd:TIGR00958 615 GSQ--LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRT----VLLIAHRLSTVERAD----QIL 684
|
250
....*....|.
gi 950436399 226 V--GGRIVESG 234
Cdd:TIGR00958 685 VlkKGSVVEMG 695
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-234 |
1.06e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 73.18 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MTILEIKDLHVSVENPaeaDHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPKYHVTSGTITLDGADVLA 78
Cdd:COG4172 4 MPLLSVEDLSVAFGQG---GGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRllPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 79 MSIDE-RARAGLFLAM--QYPvevpgvsMS--NFLRSAATAIrGEPPKLRHWVKEVKAAMAALDI-------DPAFAERS 146
Cdd:COG4172 81 LSERElRRIRGNRIAMifQEP-------MTslNPLHTIGKQI-AEVLRLHRGLSGAAARARALELlervgipDPERRLDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 147 VNEGFSGGEKKRHEILQLELLKPKIAILDETDSGLDV-------DALRVVSEgvnryaesQHG-GILLITHYTRILRYIh 218
Cdd:COG4172 153 YPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvqaqilDLLKDLQR--------ELGmALLLITHDLGVVRRF- 223
|
250
....*....|....*.
gi 950436399 219 PEYVHVFVGGRIVESG 234
Cdd:COG4172 224 ADRVAVMRQGEIVEQG 239
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
21-234 |
1.33e-14 |
|
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: 70.71 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 21 HEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAmSIDERARAGLFLamQYPVEVP 100
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILG--LIKPDSGEITFDGKSYQK-NIEALRRIGALI--EAPGFYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 101 GVSMSNFLRSAATAIRgeppkLRHwvKEVKAAMAALDIDpAFAERSVnEGFSGGEKKRHEILQLELLKPKIAILDETDSG 180
Cdd:cd03268 86 NLTARENLRLLARLLG-----IRK--KRIDEVLDVVGLK-DSAKKKV-KGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 950436399 181 LDVDALRVVSEGVNRYAEsQHGGILLITHytrILRYIHPEYVHVFV--GGRIVESG 234
Cdd:cd03268 157 LDPDGIKELRELILSLRD-QGITVLISSH---LLSEIQKVADRIGIinKGKLIEEG 208
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-158 |
1.41e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 72.41 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MTILEIKDLHVSVenpaeadHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMS 80
Cdd:COG3839 1 MASLELENVSKSY-------GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG--LEDPTSGEILIGGRDVTDLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 81 IDERaraglFLAM--Q----YPvevpgvSMSNF------LRsaataIRGEPPKLRHwvKEVKAAMAALDIDPaFAERSVN 148
Cdd:COG3839 72 PKDR-----NIAMvfQsyalYP------HMTVYeniafpLK-----LRKVPKAEID--RRVREAAELLGLED-LLDRKPK 132
|
170
....*....|
gi 950436399 149 EgFSGGEKKR 158
Cdd:COG3839 133 Q-LSGGQRQR 141
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-209 |
4.84e-14 |
|
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: 69.32 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVENPAEADHeipILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSID 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQ---AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLE--PDAGFATVDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 83 ERARAGLFLAmqypvevpgvSMSNFLRSAATAIRGEPPKLrHWVK--EVKAAM----AALDIDPaFAERSVnEGFSGGEK 156
Cdd:cd03266 76 ARRRLGFVSD----------STGLYDRLTARENLEYFAGL-YGLKgdELTARLeelaDRLGMEE-LLDRRV-GGFSTGMR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 950436399 157 KRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHgGILLITH 209
Cdd:cd03266 143 QKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTH 194
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
14-249 |
6.35e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 6.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 14 ENPAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG-HPKyhvTSGTITLDGADVLAMSIDERARAGLFLA 92
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGiVPR---DAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 93 MQYPVEVPGVSMSNFLRsAATAIRGEppkLRHWVKEVKAAMAALDIDPAFAERSVNEGFSGGEKKRHEILQLELLKPKIA 172
Cdd:PRK10895 84 PQEASIFRRLSVYDNLM-AVLQIRDD---LSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 173 ILDETDSGldVDALRVVS-EGVNRYAESQHGGILLITHYTRILRYIhPEYVHVFVGGRIVESGGSE--LADELDQNGYVG 249
Cdd:PRK10895 160 LLDEPFAG--VDPISVIDiKRIIEHLRDSGLGVLITDHNVRETLAV-CERAYIVSQGHLIAHGTPTeiLQDEHVKRVYLG 236
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-187 |
1.34e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.22 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLhvSVENPAEAdheiPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYhvTSGTITL-DGADVLamsid 82
Cdd:COG4178 363 LALEDL--TLRTPDGR----PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPY--GSGRIARpAGARVL----- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 83 eraraglFLAMQ-YpveVPGVSmsnfLRSAATairgePPKLRHWV--KEVKAAMAALDIdPAFAERsVNEG------FSG 153
Cdd:COG4178 430 -------FLPQRpY---LPLGT----LREALL-----YPATAEAFsdAELREALEAVGL-GHLAER-LDEEadwdqvLSL 488
|
170 180 190
....*....|....*....|....*....|....
gi 950436399 154 GEKKRHEILQLELLKPKIAILDETDSGLDVDALR 187
Cdd:COG4178 489 GEQQRLAFARLLLHKPDWLFLDEATSALDEENEA 522
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-209 |
1.44e-13 |
|
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: 70.08 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVENPAEAdheipiLRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHvtSGTITLDGADVLAMSIDE 83
Cdd:TIGR02868 335 LELRDLSAGYPGAPPV------LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL--QGEVTLDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RARAGLFLAMQypVEVPGVSMSNFLRSAATAIRGEppklrhwvkEVKAAMAA------LDIDPAFAERSVNEG---FSGG 154
Cdd:TIGR02868 407 VRRRVSVCAQD--AHLFDTTVRENLRLARPDATDE---------ELWAALERvgladwLRALPDGLDTVLGEGgarLSGG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 950436399 155 EKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNryAESQHGGILLITH 209
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLL--AALSGRTVVLITH 528
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-183 |
1.73e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.12 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 2 TILEIKDLHVSVENPaeadheiPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSI 81
Cdd:PRK11231 1 MTLRTENLTVGYGTK-------RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLT--PQSGTVFLGDKPISMLSS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 82 DERARAGLFLAMQYPveVP-GVSMSNFLRsaataiRGEPPKLRHWVK-------EVKAAMAALDIDpAFAERSVNEgFSG 153
Cdd:PRK11231 72 RQLARRLALLPQHHL--TPeGITVRELVA------YGRSPWLSLWGRlsaednaRVNQAMEQTRIN-HLADRRLTD-LSG 141
|
170 180 190
....*....|....*....|....*....|
gi 950436399 154 GEKKRHEILQLELLKPKIAILDETDSGLDV 183
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-227 |
2.12e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.29 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 22 EIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHVTSGTITLDgadvlamsideraraglflAMQYPVEVPG 101
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVP-------------------DNQFGREASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 102 VSmsNFLRsaatairgeppklrhwVKEVKAAMAALDI----DPAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDET 177
Cdd:COG2401 103 ID--AIGR----------------KGDFKDAVELLNAvglsDAVLWLRRFKE-LSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 950436399 178 DSGLDVDALRVVSEGVNRYAESQHGGILLITHYTRILRYIHPEYVhVFVG 227
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLL-IFVG 212
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
24-247 |
3.19e-13 |
|
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: 69.00 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDERARAGLFLAmQYPVEVPGVS 103
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGF--FQARSGEILLNGFSLKDIDRHTLRQFINYLP-QEPYIFSGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 104 MSNFLRSAATAIRGEppklrhwvkEVKAAMAALDIDP-------AFAERSVNEGF--SGGEKKRHEILQLELLKPKIAIL 174
Cdd:TIGR01193 565 LENLLLGAKENVSQD---------EIWAACEIAEIKDdienmplGYQTELSEEGSsiSGGQKQRIALARALLTDSKVLIL 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 950436399 175 DETDSGLDVDALRVVsegVNRYAESQHGGILLITHYTRILRYIHPeyVHVFVGGRIVESGgsELADELDQNGY 247
Cdd:TIGR01193 636 DESTSNLDTITEKKI---VNNLLNLQDKTIIFVAHRLSVAKQSDK--IIVLDHGKIIEQG--SHDELLDRNGF 701
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
28-183 |
3.45e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 68.22 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 28 GVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSidERARAGLFLAMQ------------- 94
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLR--LEEPTSGEILFDGQDITGLS--GRELRPLRRRMQmvfqdpyaslnpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 95 YPVEvpgvsmsnflrsaatAIRGEPPKL-----RHWVKE-VKAAMAALDIDPAFAERSVNEgFSGGEKKRHEILQLELLK 168
Cdd:COG4608 112 MTVG---------------DIIAEPLRIhglasKAERRErVAELLELVGLRPEHADRYPHE-FSGGQRQRIGIARALALN 175
|
170
....*....|....*
gi 950436399 169 PKIAILDETDSGLDV 183
Cdd:COG4608 176 PKLIVCDEPVSALDV 190
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-246 |
4.23e-13 |
|
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: 68.69 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDE-RARAGLflamqypveVP-G 101
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF--YDVTSGRILIDGQDIRDVTQASlRAAIGI---------VPqD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 102 VSMSN--------FLRSAATAirgeppklrhwvKEVKAA--MAALDidpAFAErSVNEGF-----------SGGEKKRHE 160
Cdd:COG5265 441 TVLFNdtiayniaYGRPDASE------------EEVEAAarAAQIH---DFIE-SLPDGYdtrvgerglklSGGEKQRVA 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 161 ILQLELLKPKIAILDETDSGLD-------VDALRVVSEGvnRYAesqhggiLLITHytRILRYIHPEYVHVFVGGRIVES 233
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDsrteraiQAALREVARG--RTT-------LVIAH--RLSTIVDADEILVLEAGRIVER 573
|
250
....*....|....
gi 950436399 234 GG-SELadeLDQNG 246
Cdd:COG5265 574 GThAEL---LAQGG 584
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
22-234 |
4.75e-13 |
|
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: 67.07 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 22 EIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYhvTSGTITLDGADVLamsiDE------RARAGL-FlamQ 94
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLP--TSGKVTVDGLDTL----DEenlweiRKKVGMvF---Q 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 95 YP--------VE--VpGVSMSNflrsaataiRGEPPKLrhWVKEVKAAMAALDIDpAFAERSVNEgFSGGEKKRHEILQL 164
Cdd:TIGR04520 85 NPdnqfvgatVEddV-AFGLEN---------LGVPREE--MRKRVDEALKLVGME-DFRDREPHL-LSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 165 ELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHYtrILRYIHPEYVHVFVGGRIVESG 234
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHD--MEEAVLADRVIVMNKGKIVAEG 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-234 |
4.90e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.32 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 22 EIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSIDErARAGLFLAMQYPvevpg 101
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTG--LLKPQSGEIKIDGITISKENLKE-IRKKIGIIFQNP----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 102 vsMSNFLRSAATA--------IRGEPPKLRHWVKEV--KAAMA-ALDIDPAFaersvnegFSGGEKKRHEILQLELLKPK 170
Cdd:PRK13632 93 --DNQFIGATVEDdiafglenKKVPPKKMKDIIDDLakKVGMEdYLDKEPQN--------LSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 950436399 171 IAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHytRILRYIHPEYVHVFVGGRIVESG 234
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITH--DMDEAILADKVIVFSEGKLIAQG 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
21-209 |
5.78e-13 |
|
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: 65.29 E-value: 5.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 21 HEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDERA-RAGLFLAMQYPVEV 99
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE--PDSGSILIDGEDLTDLEDELPPlRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 100 PGvsmsnflrsaatairgeppklrhwvkevkaaMAALDIdpafaersVNEGFSGGEKKRHEILQLELLKPKIAILDETDS 179
Cdd:cd03229 89 PH-------------------------------LTVLEN--------IALGLSGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190
....*....|....*....|....*....|
gi 950436399 180 GLDVDALRVVSEGVNRYAESQHGGILLITH 209
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQLGITVVLVTH 159
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-182 |
6.64e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 66.99 E-value: 6.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSI---DERARAGlfLAMQYPvevpgv 102
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLK--PTSGKIIIDGVDITDKKVklsDIRKKVG--LVFQYP------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 103 SMSNFLRSAATAIRGEPPKL----RHWVKEVKAAMAALDID-PAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDET 177
Cdd:PRK13637 93 EYQLFEETIEKDIAFGPINLglseEEIENRVKRAMNIVGLDyEDYKDKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEP 171
|
....*
gi 950436399 178 DSGLD 182
Cdd:PRK13637 172 TAGLD 176
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-182 |
8.85e-13 |
|
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: 65.63 E-value: 8.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVenpaeADHEIpiLRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYhvTSGTITLDGADVLAMSID- 82
Cdd:cd03262 1 IEIKNLHKSF-----GDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEP--DSGTIIIDGLKLTDDKKNi 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 83 --ERARAG-------LF----------LAmqyPVEVPGVSmsnflRSAATAIrgeppklrhwvkevkaAMAALD------ 137
Cdd:cd03262 72 neLRQKVGmvfqqfnLFphltvlenitLA---PIKVKGMS-----KAEAEER----------------ALELLEkvglad 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 950436399 138 -ID--PAFaersvnegFSGGEKKRHEILQLELLKPKIAILDETDSGLD 182
Cdd:cd03262 128 kADayPAQ--------LSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
24-209 |
9.05e-13 |
|
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: 67.70 E-value: 9.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDERaRAGLFLAMQYPVEVPGvs 103
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD--PTEGSIAVNGVPLADADADSW-RDQIAWVPQHPFLFAG-- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 104 msnflrSAATAIR-GEPPKLRHWVKEVKAAMAALDID---PAFAERSVNE---GFSGGEKKRHEILQLELLKPKIAILDE 176
Cdd:TIGR02857 411 ------TIAENIRlARPDASDAEIREALERAGLDEFVaalPQGLDTPIGEggaGLSGGQAQRLALARAFLRDAPLLLLDE 484
|
170 180 190
....*....|....*....|....*....|...
gi 950436399 177 TDSGLDVDALRVVSEGVNRYAESQhgGILLITH 209
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALAQGR--TVLLVTH 515
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-234 |
1.10e-12 |
|
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: 64.64 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVEnpaeaDHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVlamSIDE 83
Cdd:cd03247 1 LSINNVSFSYP-----EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQQGEITLDGVPV---SDLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RARAGLFLAMQYPVEVpgvsmsnFlrsaATAIRgeppklrhwvkevkaamaaldidpafaeRSVNEGFSGGEKKRHEILQ 163
Cdd:cd03247 71 KALSSLISVLNQRPYL-------F----DTTLR----------------------------NNLGRRFSGGERQRLALAR 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 950436399 164 LELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQhgGILLITHytRILRYIHPEYVHVFVGGRIVESG 234
Cdd:cd03247 112 ILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITH--HLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
25-247 |
1.16e-12 |
|
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: 65.59 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADvLAMSIDERARAGLFLAMQYPVEvpgvsm 104
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF--YVPENGRVLVDGHD-LALADPAWLRRQVGVVLQENVL------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 105 snFLRSAATAIR-GEPPKLRHWVKEVKAAMAALDI--------DPAFAERSVneGFSGGEKKRHEILQLELLKPKIAILD 175
Cdd:cd03252 88 --FNRSIRDNIAlADPGMSMERVIEAAKLAGAHDFiselpegyDTIVGEQGA--GLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 950436399 176 ETDSGLDVDALRVVSEGVNRYAESQhgGILLITHYTRILRYIHpeYVHVFVGGRIVESGGSElaDELDQNGY 247
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKNAD--RIIVMEKGRIVEQGSHD--ELLAENGL 229
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-209 |
1.97e-12 |
|
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: 64.30 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 12 SVENPAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADvLAMSIDERARAGL 89
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGllRP----DSGEVRWNGTP-LAEQRDEPHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 90 FLAMQypvevPGvsMSNFLrSAATAIRGEPPKLRHWVKEVKAAMAALDIDpAFAERSVNEgFSGGEKKRHEILQLELLKP 169
Cdd:TIGR01189 77 YLGHL-----PG--LKPEL-SALENLHFWAAIHGGAQRTIEDALAAVGLT-GFEDLPAAQ-LSAGQQRRLALARLWLSRR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 950436399 170 KIAILDETDSGLDVDALRVVSEGVNRYAESQhGGILLITH 209
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLLRAHLARG-GIVLLTTH 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-209 |
2.04e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.63 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGadvlamsideRARAGlFLAmQYPVEVPGVS 103
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG--ELEPDSGEVSIPK----------GLRIG-YLP-QEPPLDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 104 -----MSNF---------LRSAATAIRGEPPKLRHWVK---------------EVKAAMAALDIDPAFAERSVNEgFSGG 154
Cdd:COG0488 78 vldtvLDGDaelraleaeLEELEAKLAEPDEDLERLAElqeefealggweaeaRAEEILSGLGFPEEDLDRPVSE-LSGG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 950436399 155 EKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAesqhGGILLITH 209
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP----GTVLVVSH 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-228 |
2.10e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.63 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 2 TILEIKDLHVSVEnpaeadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLdGadvlamsi 81
Cdd:COG0488 314 KVLELEGLSKSYG-------DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG--ELEPDSGTVKL-G-------- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 82 deraraglflamqypvevPGVSMSNF------LRSAAT---AIRGEPPKLRHwvKEVKAAMAALDIDPAFAERSVnEGFS 152
Cdd:COG0488 376 ------------------ETVKIGYFdqhqeeLDPDKTvldELRDGAPGGTE--QEVRGYLGRFLFSGDDAFKPV-GVLS 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 153 GGEKKRheiLQLELL---KPKIAILDE-T-DsgLDVDALRVVSEGVNRYAesqhGGILLITH--Y------TRILrYIHP 219
Cdd:COG0488 435 GGEKAR---LALAKLllsPPNVLLLDEpTnH--LDIETLEALEEALDDFP----GTVLLVSHdrYfldrvaTRIL-EFED 504
|
....*....
gi 950436399 220 EYVHVFVGG 228
Cdd:COG0488 505 GGVREYPGG 513
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
29-209 |
2.36e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.90 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 29 VDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDER------ARAGLFLAMQYPVEVP-G 101
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEK--PTEGQIFIDGEDVTHRSIQQRdicmvfQSYALFPHMSLGENVGyG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 102 VSMsnfLRSAATAIRgeppklrhwvKEVKAAMAALDIDpAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDETDSGL 181
Cdd:PRK11432 103 LKM---LGVPKEERK----------QRVKEALELVDLA-GFEDRYVDQ-ISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190
....*....|....*....|....*....|
gi 950436399 182 DVDALRVVSEGVNRYaeSQHGGI--LLITH 209
Cdd:PRK11432 168 DANLRRSMREKIREL--QQQFNItsLYVTH 195
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-209 |
2.41e-12 |
|
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: 64.42 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVENpaeADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGAdvlamSI 81
Cdd:cd03293 1 LEVRNVSKTYGG---GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGleRP----TSGEVLVDGE-----PV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 82 DERARAGLFLAMQY---P-------VEVPgvsmsnfLRsaataIRGEPPKLRHwvKEVKAAMAALDIDpAFAERSVNEgF 151
Cdd:cd03293 69 TGPGPDRGYVFQQDallPwltvldnVALG-------LE-----LQGVPKAEAR--ERAEELLELVGLS-GFENAYPHQ-L 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 950436399 152 SGGEKKRHEILQLELLKPKIAILDETDSGLDV--------DALRVVSEgvnryaesQHGGILLITH 209
Cdd:cd03293 133 SGGMRQRVALARALAVDPDVLLLDEPFSALDAltreqlqeELLDIWRE--------TGKTVLLVTH 190
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
26-234 |
2.63e-12 |
|
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: 64.66 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDERARA------GLFLAMqypvev 99
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGF--IKPDSGKILLNGKDITNLPPEKRDISyvpqnyALFPHM------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 100 pgvsmsNFLRSAATAIRGEPPKLRHWVKEVKAAMAALDIDpAFAERSVnEGFSGGEKKRHEILQLELLKPKIAILDETDS 179
Cdd:cd03299 87 ------TVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGID-HLLNRKP-ETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 950436399 180 GLDVDALRVVSEGVNRYAESQHGGILLITH-YTRILryIHPEYVHVFVGGRIVESG 234
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHdFEEAW--ALADKVAIMLNGKLIQVG 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
24-209 |
2.71e-12 |
|
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: 64.45 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG-HPKyhvTSGTITLDGADVLamSIDERARAGLFLAMQYPVEVPGV 102
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGeLRP---TSGTAYINGYSIR--TDRKAARQSLGYCPQFDALFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 103 SMSNFLRSAAtAIRGEPPKLRHwvKEVKAAMAALDIDPaFAERSVNEgFSGGEKKRheiLQLELL---KPKIAILDETDS 179
Cdd:cd03263 91 TVREHLRFYA-RLKGLPKSEIK--EEVELLLRVLGLTD-KANKRART-LSGGMKRK---LSLAIAligGPSVLLLDEPTS 162
|
170 180 190
....*....|....*....|....*....|
gi 950436399 180 GLDVDALRVVSEGVNRyaESQHGGILLITH 209
Cdd:cd03263 163 GLDPASRRAIWDLILE--VRKGRSIILTTH 190
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-209 |
3.93e-12 |
|
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: 62.08 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVENPaeadheiPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDgadvlamside 83
Cdd:cd03221 1 IELENLSKTYGGK-------LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG--ELEPDEGIVTWG----------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 raraglflamqypvevPGVSMSNFlrsaatairgeppklrhwvkevkaamaaldidpafaersvnEGFSGGEKKRHEILQ 163
Cdd:cd03221 61 ----------------STVKIGYF-----------------------------------------EQLSGGEKMRLALAK 83
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 950436399 164 LELLKPKIAILDETDSGLDVDALRVVSEGVNRYaesqHGGILLITH 209
Cdd:cd03221 84 LLLENPNLLLLDEPTNHLDLESIEALEEALKEY----PGTVILVSH 125
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-234 |
4.00e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 64.71 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVENPAEAdheipiLRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGAdvlAMSID 82
Cdd:PRK13639 1 ILETRDLKYSYPDGTEA------LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNG--ILKPTSGEVLIKGE---PIKYD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 83 ER----ARAGLFLAMQYP---VEVPGVSMSNFLRSAATAIRGEPPKlrhwvKEVKAAMAALDIDPafAERSVNEGFSGGE 155
Cdd:PRK13639 70 KKslleVRKTVGIVFQNPddqLFAPTVEEDVAFGPLNLGLSKEEVE-----KRVKEALKAVGMEG--FENKPPHHLSGGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 156 KKRHEILQLELLKPKIAILDETDSGLDVdalRVVSEGVNRYAESQHGGILLI--THYTRiLRYIHPEYVHVFVGGRIVES 233
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLDP---MGASQIMKLLYDLNKEGITIIisTHDVD-LVPVYADKVYVMSDGKIIKE 218
|
.
gi 950436399 234 G 234
Cdd:PRK13639 219 G 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
11-230 |
4.12e-12 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 64.03 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 11 VSVENPAEADHeiPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADvLAMSIDERARAGLF 90
Cdd:cd03248 17 VTFAYPTRPDT--LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENF--YQPQGGQVLLDGKP-ISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 91 LAMQYPVEvpgvsmsnFLRSAATAIR-GEPPKLRHWVKEVKAAMAALDIDPAFAERSVNEG------FSGGEKKRHEILQ 163
Cdd:cd03248 92 LVGQEPVL--------FARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVgekgsqLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 950436399 164 LELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHggILLITHytRILRYIHPEYVHVFVGGRI 230
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRT--VLVIAH--RLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-237 |
4.34e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 64.82 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKdlHVSVENPaeaDHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHVTSGT-ITLDGADVLAMSI 81
Cdd:PRK13640 5 IVEFK--HVSFTYP---DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSkITVDGITLTAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 82 -DERARAGLflAMQYP-VEVPGVSMSNflrSAATAI--RGEP-PKLRHWVKEVKAAMAALDI---DPAFaersvnegFSG 153
Cdd:PRK13640 80 wDIREKVGI--VFQNPdNQFVGATVGD---DVAFGLenRAVPrPEMIKIVRDVLADVGMLDYidsEPAN--------LSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 154 GEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHytRILRYIHPEYVHVFVGGRIVES 233
Cdd:PRK13640 147 GQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITH--DIDEANMADQVLVLDDGKLLAQ 224
|
....
gi 950436399 234 GGSE 237
Cdd:PRK13640 225 GSPV 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
26-234 |
5.41e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.42 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDE-----RARAGLflAMQYPvevp 100
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLK--PTTGTVTVDDITITHKTKDKyirpvRKRIGM--VFQFP---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 101 gvSMSNFLRSAATAIRGEPPKLRHWVKEVKAAMAALDIDPAFaERSVNE----GFSGGEKKRHEILQLELLKPKIAILDE 176
Cdd:PRK13646 95 --ESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGF-SRDVMSqspfQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 950436399 177 TDSGLDVDALRVVSEGVNRYAESQHGGILLITH-YTRILRYIhpEYVHVFVGGRIVESG 234
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHdMNEVARYA--DEVIVMKEGSIVSQT 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
30-90 |
5.46e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 63.62 E-value: 5.46e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 950436399 30 DLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDERARAGLF 90
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGF--LPPDSGRILWNGQDLTALPPAERPVSMLF 77
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
12-215 |
6.71e-12 |
|
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: 62.23 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 12 SVEN----PAEADHeiPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVlaMSIDERARA 87
Cdd:cd03246 2 EVENvsfrYPGAEP--PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR--PTSGRVRLDGADI--SQWDPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 88 GLFLAMQYPVEVpgvsmsnFLRSAATAIrgeppklrhwvkevkaamaaldidpafaersvnegFSGGEKKRheILQLELL 167
Cdd:cd03246 76 DHVGYLPQDDEL-------FSGSIAENI-----------------------------------LSGGQRQR--LGLARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 950436399 168 --KPKIAILDETDSGLDVDALRVVSEGVNRyAESQHGGILLITHYTRILR 215
Cdd:cd03246 112 ygNPRILVLDEPNSHLDVEGERALNQAIAA-LKAAGATRIVIAHRPETLA 160
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
24-183 |
7.89e-12 |
|
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: 63.41 E-value: 7.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDERARAGLFlamQYPVEVPgvS 103
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFET--PTSGEILLDGKDITNLPPHKRPVNTVF---QNYALFP--H 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 104 MSNFLRSA-ATAIRGEPPKLRHwvKEVKAAMAALDIDpAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDETDSGLD 182
Cdd:cd03300 87 LTVFENIAfGLRLKKLPKAEIK--ERVAEALDLVQLE-GYANRKPSQ-LSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
.
gi 950436399 183 V 183
Cdd:cd03300 163 L 163
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-234 |
8.63e-12 |
|
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: 62.98 E-value: 8.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVENPAEadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYhvTSGTITLDGADVLAMSID 82
Cdd:cd03258 1 MIELKNVSKVFGDTGG---KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERP--TSGSVLVDGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 83 E----RARAGL-------------FLAMQYPVEVPGVSMSNFLRsaatairgeppKLRHWVKEVKAAMAAlDIDPAfaer 145
Cdd:cd03258 76 ElrkaRRRIGMifqhfnllssrtvFENVALPLEIAGVPKAEIEE-----------RVLELLELVGLEDKA-DAYPA---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 146 svneGFSGGEKKRHEILQLELLKPKIAILDETDSGLD-------VDALRvvseGVNRyaesQHG-GILLITHYTRILRYI 217
Cdd:cd03258 140 ----QLSGGQKQRVGIARALANNPKVLLCDEATSALDpettqsiLALLR----DINR----ELGlTIVLITHEMEVVKRI 207
|
250
....*....|....*..
gi 950436399 218 hPEYVHVFVGGRIVESG 234
Cdd:cd03258 208 -CDRVAVMEKGEVVEEG 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-241 |
8.66e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.08 E-value: 8.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpkyhVTS---GTITLDGADVLAMSIDERARAGLF-----LAMQY 95
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILG-----MTSpdaGKITVLGVPVPARARLARARIGVVpqfdnLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 96 PVEVPGVSMSNFLRSAATAIRGEPPKLRHWVK-EVKAAMAALDIdpafaersvnegfSGGEKKRHEILQLELLKPKIAIL 174
Cdd:PRK13536 130 TVRENLLVFGRYFGMSTREIEAVIPSLLEFARlESKADARVSDL-------------SGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 950436399 175 DETDSGLDVDALRVVSEGVnRYAESQHGGILLITHYTRILRYIHPEYVHVFVGGRIVESGGSELADE 241
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERL-RSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-234 |
1.74e-11 |
|
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: 61.93 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 29 VDLTVkSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGA------DVLAMSIDERARAGLFlaMQYPVeVPGV 102
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEK--PDGGTIVLNGTvlfdsrKKINLPPQQRKIGLVF--QQYAL-FPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 103 SMSNFLrsAATAIRGEPPKLRHWVKEVkaaMAALDIDPaFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDETDSGLD 182
Cdd:cd03297 91 NVRENL--AFGLKRKRNREDRISVDEL---LDLLGLDH-LLNRYPAQ-LSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 950436399 183 vDALRVVSEG-VNRYAESQHGGILLITHYTRILRYIHPEYVhVFVGGRIVESG 234
Cdd:cd03297 164 -RALRLQLLPeLKQIKKNLNIPVIFVTHDLSEAEYLADRIV-VMEDGRLQYIG 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
11-240 |
2.40e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.34 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 11 VSVENPAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG------HPKYHVTSGTITLDGADVLAMSI-DE 83
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdkSAGSHIELLGRTVQREGRLARDIrKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RARAGlFLAMQYPVEVPGVSMSNFLRSAAtairGEPPKLR---HW---VKEVKAAMAALDIDPA-FAERSVNEgFSGGEK 156
Cdd:PRK09984 85 RANTG-YIFQQFNLVNRLSVLENVLIGAL----GSTPFWRtcfSWftrEQKQRALQALTRVGMVhFAHQRVST-LSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 157 KRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYaeSQHGGILLITHYTRI---LRYIhpEYVHVFVGGRIVES 233
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDI--NQNDGITVVVTLHQVdyaLRYC--ERIVALRQGHVFYD 234
|
....*..
gi 950436399 234 GGSELAD 240
Cdd:PRK09984 235 GSSQQFD 241
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-89 |
2.45e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.12 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 2 TILEIKDLHVsvenpaEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSI 81
Cdd:COG3845 256 VVLEVENLSV------RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP--PASGSIRLDGEDITGLSP 327
|
....*...
gi 950436399 82 DERARAGL 89
Cdd:COG3845 328 RERRRLGV 335
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-89 |
3.46e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.33 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVenpAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMsiD 82
Cdd:PRK10584 6 IVEVHHLKKSV---GQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDD--GSSGEVSLVGQPLHQM--D 78
|
....*..
gi 950436399 83 ERARAGL 89
Cdd:PRK10584 79 EEARAKL 85
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
22-73 |
4.12e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 61.01 E-value: 4.12e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 950436399 22 EIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDG 73
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAG--IYPPDSGTVTVRG 83
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-189 |
5.50e-11 |
|
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: 61.04 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVENPAEAdheipiLRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMSI 81
Cdd:cd03256 1 IEVENLSKTYPNGKKA------LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlvEP----TSGSVLIDGTDINKLKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 82 DE----RARAGlFLAMQYPVeVPGVS-MSNFL------RSAATAIRGEPPKlrhwvKEVKAAMAALD---IDPaFAERSV 147
Cdd:cd03256 71 KAlrqlRRQIG-MIFQQFNL-IERLSvLENVLsgrlgrRSTWRSLFGLFPK-----EEKQRALAALErvgLLD-KAYQRA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 950436399 148 NEgFSGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVV 189
Cdd:cd03256 143 DQ-LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQV 183
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-234 |
6.25e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.99 E-value: 6.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 23 IPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG-HPKyhvTSGTITLDGADVLAMSIDERARAGLFLAMQYPVEVPG 101
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGiVPP---DSGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 102 VSM-SNFL----RSAATAIRgeppklrhwVKEVKAAMAA-LDIDPAFAERSVnegfsgGEKKRHEILQLELLKPKIAILD 175
Cdd:PRK15439 101 LSVkENILfglpKRQASMQK---------MKQLLAALGCqLDLDSSAGSLEV------ADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 950436399 176 ETDSGL---DVDAL-----RVVSEGVnryaesqhgGILLITHYTRILRYIhPEYVHVFVGGRIVESG 234
Cdd:PRK15439 166 EPTASLtpaETERLfsrirELLAQGV---------GIVFISHKLPEIRQL-ADRISVMRDGTIALSG 222
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
22-73 |
8.19e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.48 E-value: 8.19e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 950436399 22 EIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDG 73
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGilEP----TSGRVEVNG 87
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-209 |
1.16e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.49 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVENPAEADHeipiLRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSI- 81
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQ----LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDG--LFEEFEGKVKIDGELLTAENVw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 82 DERARAGLflAMQYP-VEVPGVSMSNflrSAATAIRGEPPKLRHWVKEVKAAMAALDIdPAFAERSVNEgFSGGEKKRHE 160
Cdd:PRK13642 78 NLRRKIGM--VFQNPdNQFVGATVED---DVAFGMENQGIPREEMIKRVDEALLAVNM-LDFKTREPAR-LSGGQKQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 950436399 161 ILQLELLKPKIAILDETDSGLD----VDALRVVSEGVNRYaesqHGGILLITH 209
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKY----QLTVLSITH 199
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-209 |
1.19e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.41 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 2 TILEIKdlHVSVENPaeaDHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAM 79
Cdd:PRK13635 4 EIIRVE--HISFRYP---DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGllLP----EAGTITVGGMVLSEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 80 SI-DERARAGlfLAMQYP--------VE-----------VPGVSMsnflrsaatairgeppklrhwVKEVKAAMAALDID 139
Cdd:PRK13635 75 TVwDVRRQVG--MVFQNPdnqfvgatVQddvafglenigVPREEM---------------------VERVDQALRQVGME 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 140 PaFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITH 209
Cdd:PRK13635 132 D-FLNREPHR-LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITH 199
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-234 |
1.31e-10 |
|
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: 59.43 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 30 DLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDERARAGLFlamqypvevpgvsMSNFLR 109
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFET--PQSGRVLINGVDVTAAPPADRPVSMLF-------------QENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 110 SAATAIR----GEPPKLR---HWVKEVKAAMAALDIDPAFAERSvnEGFSGGEKKRHEILQLELLKPKIAILDETDSGLD 182
Cdd:cd03298 83 AHLTVEQnvglGLSPGLKltaEDRQAIEVALARVGLAGLEKRLP--GELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 950436399 183 vDALRV-VSEGVNRYAESQHGGILLITHYTRILRYIHPEYVHVfVGGRIVESG 234
Cdd:cd03298 161 -PALRAeMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFL-DNGRIAAQG 211
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-262 |
1.70e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.05 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 22 EIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHVTSGTITLDGADVLAMSIderARAGlFLA---MQYP-- 96
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQIL---KRTG-FVTqddILYPhl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 97 -VEVPGVSMSnFLRSAATAIRGEPPKLrhwVKEVKAAMAALDIDPAFAERSVNEGFSGGEKKRHEILQLELLKPKIAILD 175
Cdd:PLN03211 156 tVRETLVFCS-LLRLPKSLTKQEKILV---AESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 176 ETDSGLD-VDALRVVSEgvnrYAESQHGGILLITHY----TRILRYIHPeyVHVFVGGRIVESGgsELADELDQNGYVGF 250
Cdd:PLN03211 232 EPTSGLDaTAAYRLVLT----LGSLAQKGKTIVTSMhqpsSRVYQMFDS--VLVLSEGRCLFFG--KGSDAMAYFESVGF 303
|
250
....*....|..
gi 950436399 251 SPAsgrYPHQPA 262
Cdd:PLN03211 304 SPS---FPMNPA 312
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-76 |
1.89e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 60.16 E-value: 1.89e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 950436399 1 MTIlEIKDLHVSVENpaeadheIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADV 76
Cdd:COG1118 1 MSI-EVRNISKRFGS-------FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGleTP----DSGRIVLNGRDL 66
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
10-209 |
2.71e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.35 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 10 HVSVENPAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADvlamSIDERARAgl 89
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP--PAAGTIKLDGGD----IDDPDVAE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 90 flAMQYpvevpgVSMSNFLRSAAT---------AIRGEPPklrhwvKEVKAAMAALDIDPAfAERSVNEgFSGGEKKRHE 160
Cdd:PRK13539 74 --ACHY------LGHRNAMKPALTvaenlefwaAFLGGEE------LDIAAALEAVGLAPL-AHLPFGY-LSAGQKRRVA 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 950436399 161 ILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESqhGGILLI-TH 209
Cdd:PRK13539 138 LARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQ--GGIVIAaTH 185
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
22-182 |
2.72e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.95 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 22 EIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDERA---RAG-------LFL 91
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEE--ITSGDLIVDGLKVNDPKVDERLirqEAGmvfqqfyLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 92 AMQY-------PVEVPGVSmsnflRSAATAIrgeppklrhwvkevkaAMAALDiDPAFAERS---VNEgFSGGEKKRHEI 161
Cdd:PRK09493 91 HLTAlenvmfgPLRVRGAS-----KEEAEKQ----------------ARELLA-KVGLAERAhhyPSE-LSGGQQQRVAI 147
|
170 180
....*....|....*....|.
gi 950436399 162 LQLELLKPKIAILDETDSGLD 182
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALD 168
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-213 |
3.08e-10 |
|
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: 58.57 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 21 HEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADV--LAMSIDERARAGLFLAMQypvE 98
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEEL--PTSGTIRVNGQDVsdLRGRAIPYLRRKIGVVFQ---D 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 99 VPGVSMSNFLRSAATAIR--GEPPKLrhWVKEVKAAMAALDIdpAFAERSVNEGFSGGEKKRHEILQLELLKPKIAILDE 176
Cdd:cd03292 87 FRLLPDRNVYENVAFALEvtGVPPRE--IRKRVPAALELVGL--SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 950436399 177 TDSGLDVD-ALRVVS--EGVNRYAESqhggILLITHYTRI 213
Cdd:cd03292 163 PTGNLDPDtTWEIMNllKKINKAGTT----VVVATHAKEL 198
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
11-209 |
3.23e-10 |
|
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: 58.45 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 11 VSVENPAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSID-------E 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG--IILPDSGEVLFDGKPLDIAARNrigylpeE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RaraGLFLAMQYpvevpgVSMSNFLRSaataIRGEPPK-LRHWVKEVkaaMAALDIDPaFAERSVNEgFSGGEKKRHEIL 162
Cdd:cd03269 79 R---GLYPKMKV------IDQLVYLAQ----LKGLKKEeARRRIDEW---LERLELSE-YANKRVEE-LSKGNQQKVQFI 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 950436399 163 QLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHgGILLITH 209
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGK-TVILSTH 186
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
11-84 |
3.60e-10 |
|
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: 58.50 E-value: 3.60e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 950436399 11 VSVENPAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMSIDER 84
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGleRP----DSGTILFGGEDATDVPVQER 74
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
24-209 |
3.63e-10 |
|
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: 58.47 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMSIDERAR--------AGLFLAM 93
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRliEP----TSGEIFIDGEDIREQDPVELRRkigyviqqIGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 94 QYPVEVPGVsmsnflrsaatairgepPKLRHWVKE-----VKAAMAALDIDPA-FAERSVNEgFSGGEKKRHEILQLELL 167
Cdd:cd03295 91 TVEENIALV-----------------PKLLKWPKEkirerADELLALVGLDPAeFADRYPHE-LSGGQQQRVGVARALAA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 950436399 168 KPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITH 209
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTH 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-247 |
4.10e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.68 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGH-PKYHVTSGTITLDGadvlaMSIDE---RARAGlfLAMQYPVEVP 100
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRsPKGVKGSGSVLLNG-----MPIDAkemRAISA--YVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 101 GVSMSNFL---------RSAATAIRgeppklRHWVKEVKAAMAALDI-DPAFAERSVNEGFSGGEKKRHEIlQLELLK-P 169
Cdd:TIGR00955 113 TLTVREHLmfqahlrmpRRVTKKEK------RERVDEVLQALGLRKCaNTRIGVPGRVKGLSGGERKRLAF-ASELLTdP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 170 KIAILDETDSGLD-------VDALRVVsegvnryaeSQHGGILLIThytrilryIHPEYVHVF---------VGGRIVES 233
Cdd:TIGR00955 186 PLLFCDEPTSGLDsfmaysvVQVLKGL---------AQKGKTIICT--------IHQPSSELFelfdkiilmAEGRVAYL 248
|
250
....*....|....*
gi 950436399 234 G-GSELADELDQNGY 247
Cdd:TIGR00955 249 GsPDQAVPFFSDLGH 263
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
25-182 |
5.25e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 58.94 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPkyHVTSGTITLDGADVLAMSIDERaRAG-------LFLAMqypv 97
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLE--HQTSGHIRFHGTDVSRLHARDR-KVGfvfqhyaLFRHM---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 98 evpgvsmsNFLRSAATAIRGEPPKLRHWVKEVKA-AMAALDID--PAFAERSVNEgFSGGEKKRHEILQLELLKPKIAIL 174
Cdd:PRK10851 90 --------TVFDNIAFGLTVLPRRERPNAAAIKAkVTQLLEMVqlAHLADRYPAQ-LSGGQKQRVALARALAVEPQILLL 160
|
....*...
gi 950436399 175 DETDSGLD 182
Cdd:PRK10851 161 DEPFGALD 168
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-238 |
6.31e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 58.21 E-value: 6.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVENPAEAdheipiLRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSID 82
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKA------LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNG--IYLPQRGRVKVMGREVNAENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 83 E-RARAGlfLAMQYPVEvpgvsmSNFLRSAATAIRGEPPKLRHWVKEVK----AAMAALDIDpAFAERSVNEgFSGGEKK 157
Cdd:PRK13647 76 WvRSKVG--LVFQDPDD------QVFSSTVWDDVAFGPVNMGLDKDEVErrveEALKAVRMW-DFRDKPPYH-LSYGQKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 158 RHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYaeSQHGGILLITHYTRILRYIHPEYVHVFVGGRIVESGGSE 237
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRL--HNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
.
gi 950436399 238 L 238
Cdd:PRK13647 224 L 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
26-237 |
8.47e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.05 E-value: 8.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIA--GHPkyhvTSGTITLDGADVLAMsiDERARAGLFLAMQYPVEVPGVS 103
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTmiETP----TGGELYYQGQDLLKA--DPEAQKLLRQKIQIVFQNPYGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 104 MSNflRSAATAIRGEPPKL-----RHWVKE-VKAAMAALDIDPAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDET 177
Cdd:PRK11308 105 LNP--RKKVGQILEEPLLIntslsAAERREkALAMMAKVGLRPEHYDRYPHM-FSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 950436399 178 DSGLDVDalrVVSEGVNRYAESQ---HGGILLITHYTRILRYIHPEyVHVFVGGRIVESGGSE 237
Cdd:PRK11308 182 VSALDVS---VQAQVLNLMMDLQqelGLSYVFISHDLSVVEHIADE-VMVMYLGRCVEKGTKE 240
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
10-187 |
8.77e-10 |
|
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: 56.39 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 10 HVSVENPAEadheIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITL-DGADVlamsiderarag 88
Cdd:cd03223 5 NLSLATPDG----RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG--LWPWGSGRIGMpEGEDL------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 89 LFLAmQYPVEVPGVsmsnfLRSAatairgeppkLRH-WVKEvkaamaaldidpafaersvnegFSGGEKKRHEILQLELL 167
Cdd:cd03223 67 LFLP-QRPYLPLGT-----LREQ----------LIYpWDDV----------------------LSGGEQQRLAFARLLLH 108
|
170 180
....*....|....*....|
gi 950436399 168 KPKIAILDETDSGLDVDALR 187
Cdd:cd03223 109 KPKFVFLDEATSALDEESED 128
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-183 |
1.26e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.25 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 32 TVKSGETHALMGPNGSGKSTLSYAIAGHPKYhvtSGTITLDGADVLAMSIDERARAGLFLAMQYPvevPGVSMSNF---- 107
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLPG---SGSIQFAGQPLEAWSAAELARHRAYLSQQQT---PPFAMPVFqylt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 108 LRSAATAIRGEPPKLRHWVKEvkaamaALDIDPaFAERSVNEgFSGGEKKRHE----ILQL-ELLKP--KIAILDETDSG 180
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEVAE------ALGLDD-KLGRSVNQ-LSGGEWQRVRlaavVLQVwPDINPagQLLLLDEPMNS 163
|
...
gi 950436399 181 LDV 183
Cdd:PRK03695 164 LDV 166
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-182 |
1.32e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.19 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 20 DHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDE-RARaglfLAMqypve 98
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRH--FDVSEGDIRFHDIPLTKLQLDSwRSR----LAV----- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 99 vpgVSMSNFLRS---AATAIRGEPPKLRHWVKEVkAAMAAL--DI-------DPAFAERSVNegFSGGEKKRHEILQLEL 166
Cdd:PRK10789 394 ---VSQTPFLFSdtvANNIALGRPDATQQEIEHV-ARLASVhdDIlrlpqgyDTEVGERGVM--LSGGQKQRISIARALL 467
|
170
....*....|....*.
gi 950436399 167 LKPKIAILDETDSGLD 182
Cdd:PRK10789 468 LNAEILILDDALSAVD 483
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
24-86 |
1.36e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 57.02 E-value: 1.36e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG-HPKyhvTSGTITLDGADVLAMSIDERAR 86
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRlLPP---DSGEVLVDGLDVATTPSRELAK 75
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-234 |
1.52e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSIDERARAGLFLAMQYPVEVPGVSMS 105
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG--IHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 106 NFL---RSAATAIRGEPpkLRHWVK-EVKAAMAALDIDpafAERSVNE---GFSGGEKKRHEILQLELLKPKIAILDETD 178
Cdd:PRK09700 99 ENLyigRHLTKKVCGVN--IIDWREmRVRAAMMLLRVG---LKVDLDEkvaNLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 950436399 179 SGL---DVDALRVVSegvnRYAESQHGGILLITHYTRILRYIHPEYVhVFVGGRIVESG 234
Cdd:PRK09700 174 SSLtnkEVDYLFLIM----NQLRKEGTAIVYISHKLAEIRRICDRYT-VMKDGSSVCSG 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-209 |
1.62e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.71 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 2 TILEIKDLHVSVeNPAEAdheipiLRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG----HPKYHVTsGTITLDGADVL 77
Cdd:PRK14239 4 PILQVSDLSVYY-NKKKA------LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndlNPEVTIT-GSIVYNGHNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 78 AMSIDE-RARAGLFLAMQYPVEVPgvsMSNF------LRsaataIRGEPPK--LRHWV-KEVKAAMAALDIDPAFAERSV 147
Cdd:PRK14239 76 SPRTDTvDLRKEIGMVFQQPNPFP---MSIYenvvygLR-----LKGIKDKqvLDEAVeKSLKGASIWDEVKDRLHDSAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 950436399 148 neGFSGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVnrYAESQHGGILLITH 209
Cdd:PRK14239 148 --GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETL--LGLKDDYTMLLVTR 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-237 |
1.75e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.79 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAghpKYHVTSGTITLDGadvlaMSIDERARAGLfLAMQYPVEV----P 100
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALL---RLINSQGEIWFDG-----QPLHNLNRRQL-LPVRHRIQVvfqdP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 101 GVSMS---NFLRSAATAIRGEPPKLRHWVKE--VKAAMAALDIDPAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILD 175
Cdd:PRK15134 372 NSSLNprlNVLQIIEEGLRVHQPTLSAAQREqqVIAVMEEVGLDPETRHRYPAE-FSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 950436399 176 ETDSGLDVDALRVVSEGVNRYAESQHGGILLITHYTRILRYI-HPeyVHVFVGGRIVESGGSE 237
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALcHQ--VIVLRQGEVVEQGDCE 511
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-235 |
1.83e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 57.17 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 2 TILEIKDLHVSVENPAEAdheipiLRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVlamsi 81
Cdd:PRK13636 4 YILKVEELNYNYSDGTHA------LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILK--PSSGRILFDGKPI----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 82 dERARAGLfLAMQYPVEVPGVSMSNFLRSAAT-------AIRGEPPKlRHWVKEVKAAMAALDIDPafAERSVNEGFSGG 154
Cdd:PRK13636 71 -DYSRKGL-MKLRESVGMVFQDPDNQLFSASVyqdvsfgAVNLKLPE-DEVRKRVDNALKRTGIEH--LKDKPTHCLSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 155 EKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHYTRILRyIHPEYVHVFVGGRIVESG 234
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVP-LYCDNVFVMKEGRVILQG 224
|
.
gi 950436399 235 G 235
Cdd:PRK13636 225 N 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-181 |
2.03e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.53 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHVTSGTITLDGADVLAMSIDERARAGLFLAMQYPVEVPGVS-M 104
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTERAGIVIIHQELTLVPELSvA 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 950436399 105 SNFLRSAATAIRGEPPKLRHWVKEVKAAMAALDIDPAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDETDSGL 181
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGD-YGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-234 |
2.10e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.68 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 22 EIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpkYHV-TSGTITLDGADVLAMSIDE-----RARAGlfLAMQY 95
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNG---LHVpTQGSVRVDDTLITSTSKNKdikqiRKKVG--LVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 96 P---------VEVPGVSMSNFLRSAATAIRGEPPKLrhwvkevkaamAALDIDPAFAERSVNEgFSGGEKKRHEILQLEL 166
Cdd:PRK13649 94 PesqlfeetvLKDVAFGPQNFGVSQEEAEALAREKL-----------ALVGISESLFEKNPFE-LSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 950436399 167 LKPKIAILDETDSGLDVDALRvvsEGVNRYAESQHGG--ILLITHYT-RILRYihPEYVHVFVGGRIVESG 234
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRK---ELMTLFKKLHQSGmtIVLVTHLMdDVANY--ADFVYVLEKGKLVLSG 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
28-209 |
2.53e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.15 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 28 GVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDERARAG---------LFLAMQYpVE 98
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGF--YKPTGGTILLRGQHIEGLPGHQIARMGvvrtfqhvrLFREMTV-IE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 99 VPGVSM-----SNFL----------RSAATAIRgeppKLRHWVKEVKAAmaaldidpAFAERSVNEgFSGGEKKRHEILQ 163
Cdd:PRK11300 100 NLLVAQhqqlkTGLFsgllktpafrRAESEALD----RAATWLERVGLL--------EHANRQAGN-LAYGQQRRLEIAR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 950436399 164 LELLKPKIAILDETDSGLD----------VDALRvvsegvnryaeSQHG-GILLITH 209
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNpketkeldelIAELR-----------NEHNvTVLLIEH 212
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-190 |
2.65e-09 |
|
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: 55.73 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 21 HEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGH-PKYHVTSGTITLDGadvlaMSIDERARaglflamQYPVEV 99
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtEGNVSVEGDIHYNG-----IPYKEFAE-------KYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 100 PGVSMSNFlrsaatairgEPPKLRhwVKEVkaamaaLDidpaFAERSVNE----GFSGGEKKRHEILQLELLKPKIAILD 175
Cdd:cd03233 86 IYVSEEDV----------HFPTLT--VRET------LD----FALRCKGNefvrGISGGERKRVSIAEALVSRASVLCWD 143
|
170
....*....|....*.
gi 950436399 176 ETDSGLDVD-ALRVVS 190
Cdd:cd03233 144 NSTRGLDSStALEILK 159
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-181 |
3.10e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHVTSGTITLDGADVLAMSIDERARAGLFLAMQYPVEVPGVSMS 105
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEELQASNIRDTERAGIAIIHQELALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 106 N--FLRS----------AATAIRGEppklrHWVKEVKaamaaLDIDPafAERSVNEGfsGGEKKRHEILQLELLKPKIAI 173
Cdd:PRK13549 101 EniFLGNeitpggimdyDAMYLRAQ-----KLLAQLK-----LDINP--ATPVGNLG--LGQQQLVEIAKALNKQARLLI 166
|
....*...
gi 950436399 174 LDETDSGL 181
Cdd:PRK13549 167 LDEPTASL 174
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-183 |
3.24e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 56.00 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHvtsGTITLDGADVLAMSIDERARAGLFLAMQypvEVPGVSMS 105
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ---GEILLNGRPLSDWSAAELARHRAYLSQQ---QSPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 106 NF--LRsaataiRGEPPKLRHwvKEVKAAMA----ALDIDPAFAeRSVNEgFSGGEKKRHEI----LQL--------ELL 167
Cdd:COG4138 86 VFqyLA------LHQPAGASS--EAVEQLLAqlaeALGLEDKLS-RPLTQ-LSGGEWQRVRLaavlLQVwptinpegQLL 155
|
170
....*....|....*.
gi 950436399 168 kpkiaILDETDSGLDV 183
Cdd:COG4138 156 -----LLDEPMNSLDV 166
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-87 |
3.41e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 56.62 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVENpaeADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMS 80
Cdd:COG1135 1 MIELENLSKTFPT---KGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLleRP----TSGSVLVDGVDLTALS 73
|
....*..
gi 950436399 81 IDERARA 87
Cdd:COG1135 74 ERELRAA 80
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-182 |
3.79e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHP-KYHVT-SGTITLDGADvlAMSIDERARAGLFLAMQYPVEVPGV 102
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdGFHIGvEGVITYDGIT--PEEIKKHYRGDVVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 103 SMSNFLRsaaTAIRGEPPKLR--------HWVKEVKAAMAALDIDPAFAERSVNE---GFSGGEKKRHEILQLELLKPKI 171
Cdd:TIGR00956 154 TVGETLD---FAARCKTPQNRpdgvsreeYAKHIADVYMATYGLSHTRNTKVGNDfvrGVSGGERKRVSIAEASLGGAKI 230
|
170
....*....|.
gi 950436399 172 AILDETDSGLD 182
Cdd:TIGR00956 231 QCWDNATRGLD 241
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-237 |
4.15e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 55.62 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTLSYA----IAGHPKYHVtSGTITLDGADVLAMSIDE-RARAGLFLAMQYPVEV 99
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlLELNEEARV-EGEVRLFGRNIYSPDVDPiEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 100 P----------GVSMSNFLRSaataiRGEPPKLRHWVkeVKAAMAALDIDPAFAERSVNegFSGGEKKRHEILQLELLKP 169
Cdd:PRK14267 98 PhltiydnvaiGVKLNGLVKS-----KKELDERVEWA--LKKAALWDEVKDRLNDYPSN--LSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 950436399 170 KIAILDETDSGLDVDALRVVSEGVnrYAESQHGGILLITHY----TRILRYIHPEYVhvfvgGRIVESGGSE 237
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELL--FELKKEYTIVLVTHSpaqaARVSDYVAFLYL-----GKLIEVGPTR 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-234 |
5.11e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 55.89 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADvlaMSIDERARAGlflamqY-PVEvpgv 102
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGilAP----DSGEVLWDGEP---LDPEDRRRIG------YlPEE---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 103 smsnflrsaataiRGEPPKLRhwVKEVKAAMAAL-DIDPAFAERSVNEGFsggekKRHEI------------------LQ 163
Cdd:COG4152 80 -------------RGLYPKMK--VGEQLVYLARLkGLSKAEAKRRADEWL-----ERLGLgdrankkveelskgnqqkVQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 164 L--ELL-KPKIAILDETDSGLDVDALRVVSEGVNRYAESqhgG--ILLITHytRIlryihpEYV-----HVFV--GGRIV 231
Cdd:COG4152 140 LiaALLhDPELLILDEPFSGLDPVNVELLKDVIRELAAK---GttVIFSSH--QM------ELVeelcdRIVIinKGRKV 208
|
...
gi 950436399 232 ESG 234
Cdd:COG4152 209 LSG 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-254 |
7.43e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.99 E-value: 7.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHvtSGTITLDGADVLAMSIDERARAGLFLAMQYP-VEVPGV 102
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ--KGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPeTQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 103 SMSNFLRSAATAIRGEPPKLRhwvKEVKAAMAALDIDpAFAERSvNEGFSGGEKKRHEILQLELLKPKIAILDETDSGLD 182
Cdd:PRK13644 94 TVEEDLAFGPENLCLPPIEIR---KRVDRALAEIGLE-KYRHRS-PKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 950436399 183 VDALRVVSEGVNRYAEsQHGGILLITHYtriLRYIH-PEYVHVFVGGRIVESGGSE--LADELDQngYVGFSPAS 254
Cdd:PRK13644 169 PDSGIAVLERIKKLHE-KGKTIVYITHN---LEELHdADRIIVMDRGKIVLEGEPEnvLSDVSLQ--TLGLTPPS 237
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-234 |
8.14e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.71 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPKYHVTSGTITLDGADVLAMSIDERARAglfLAMQYPvevpg 101
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGilPAGVRQTAGRVLLDGKPVAPCALRGRKIA---TIMQNP----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 102 VSMSNFLRSAAT------AIRGEPPKLRhwvkEVKAAMAALDI-DPAFAERSVNEGFSGGEKKRHEILQLELLKPKIAIL 174
Cdd:PRK10418 89 RSAFNPLHTMHTharetcLALGKPADDA----TLTAALEAVGLeNAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 950436399 175 DETDSGLDVDALRVVSEGVNRYAESQHGGILLITHYTRIL-RYIHPeyVHVFVGGRIVESG 234
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVaRLADD--VAVMSHGRIVEQG 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
26-234 |
8.68e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.93 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGA-----DVLAMSIDER---ARAGLFLAMQYPV 97
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLA--PDAGEVHYRMRdgqlrDLYALSEAERrrlLRTEWGFVHQHPR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 98 EvpGVSMSnflRSAATAIrGEPP---------KLR----HWVKEVKAAMAALDIDPAfaersvneGFSGGEKKRHEILQL 164
Cdd:PRK11701 100 D--GLRMQ---VSAGGNI-GERLmavgarhygDIRatagDWLERVEIDAARIDDLPT--------TFSGGMQQRLQIARN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 165 ELLKPKIAILDETDSGLDV-------DALR-VVSEgvnryaesQHGGILLITH---YTRILryihPEYVHVFVGGRIVES 233
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVsvqarllDLLRgLVRE--------LGLAVVIVTHdlaVARLL----AHRLLVMKQGRVVES 233
|
.
gi 950436399 234 G 234
Cdd:PRK11701 234 G 234
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
25-188 |
9.06e-09 |
|
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: 54.18 E-value: 9.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDERARAGLF--LAMqYPvevpgv 102
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEE--PTSGRIYIGGRDVTDLPPKDRDIAMVFqnYAL-YP------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 103 SMSNFLRSA-ATAIRGEPPklRHWVKEVKAAMAALDIDpAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDETDSGL 181
Cdd:cd03301 86 HMTVYDNIAfGLKLRKVPK--DEIDERVREVAELLQIE-HLLDRKPKQ-LSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
....*..
gi 950436399 182 DVdALRV 188
Cdd:cd03301 162 DA-KLRV 167
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-237 |
1.09e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.81 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MTILEIKDLHVSVENPAEAdheipiLRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMS 80
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEA------LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILK--PTSGSVLIRGEPITKEN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 81 IDErARAGLFLAMQYP---VEVPGVSMSNFLRSAATAIRGEPPKLRhwvkeVKAAMAALDIDpAFAERsVNEGFSGGEKK 157
Cdd:PRK13652 73 IRE-VRKFVGLVFQNPddqIFSPTVEQDIAFGPINLGLDEETVAHR-----VSSALHMLGLE-ELRDR-VPHHLSGGEKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 158 RHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHYTRILRYIhPEYVHVFVGGRIVESGGSE 237
Cdd:PRK13652 145 RVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEM-ADYIYVMDKGRIVAYGTVE 223
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-234 |
1.46e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 54.83 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVEnpaeaDHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSidE 83
Cdd:PRK11160 339 LTLNNVSFTYP-----DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRA--WDPQQGEILLNGQPIADYS--E 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RA-RAGLFLAMQYpVEVPGVSMSNFLRSAATAIRGEppKLRHWVKEVkaAMAALDIDPAFAERSVNEG---FSGGEKKRH 159
Cdd:PRK11160 410 AAlRQAISVVSQR-VHLFSATLRDNLLLAAPNASDE--ALIEVLQQV--GLEKLLEDDKGLNAWLGEGgrqLSGGEQRRL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 950436399 160 EILQLeLLKPK-IAILDETDSGLDVDALRVVSEGVNRYAesQHGGILLITHytRILRYIHPEYVHVFVGGRIVESG 234
Cdd:PRK11160 485 GIARA-LLHDApLLLLDEPTEGLDAETERQILELLAEHA--QNKTVLMITH--RLTGLEQFDRICVMDNGQIIEQG 555
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-234 |
1.56e-08 |
|
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: 53.57 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVenpaeADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIagHPKYHVTSGTITLDGADVlaMSID- 82
Cdd:cd03369 7 IEVENLSVRY-----APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILAL--FRFLEAEEGKIEIDGIDI--STIPl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 83 ERARAGLFLAMQYPVEVPGVSMSNFlrsaatairgePPKLRHWVKEVKAAMaaldidpafaerSVNEG---FSGGEKKRH 159
Cdd:cd03369 78 EDLRSSLTIIPQDPTLFSGTIRSNL-----------DPFDEYSDEEIYGAL------------RVSEGglnLSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 950436399 160 EILQLELLKPKIAILDETDSGLDV--DAL--RVVSEgvnryaESQHGGILLITHytRILRYIHPEYVHVFVGGRIVESG 234
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYatDALiqKTIRE------EFTNSTILTIAH--RLRTIIDYDKILVMDAGEVKEYD 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
10-86 |
1.58e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 53.52 E-value: 1.58e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 950436399 10 HVSVENPAEadheIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSIDERAR 86
Cdd:COG2884 6 NVSKRYPGG----REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG--EERPTSGQVLVNGQDLSRLKRREIPY 76
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-232 |
1.94e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.71 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MTILEIKDLHVSVENpaeADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG---HPKYHVTSGTITLDGADVL 77
Cdd:PRK15134 3 QPLLAIENLSVAFRQ---QQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRllpSPPVVYPSGDIRFHGESLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 78 amSIDERARAGLF---LAMQYpvEVPGVSMsNFLR----------SAATAIRGEPPKlrhwvKEVKAAMAALDIDPAfAE 144
Cdd:PRK15134 80 --HASEQTLRGVRgnkIAMIF--QEPMVSL-NPLHtlekqlyevlSLHRGMRREAAR-----GEILNCLDRVGIRQA-AK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 145 RSVN--EGFSGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHYTRILRYIhPEYV 222
Cdd:PRK15134 149 RLTDypHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKL-ADRV 227
|
250
....*....|
gi 950436399 223 HVFVGGRIVE 232
Cdd:PRK15134 228 AVMQNGRCVE 237
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
22-249 |
1.96e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.73 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 22 EIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVL----------AMSIDERARAgLFL 91
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPR--ATSGRIVFDGKDITdwqtakimreAVAIVPEGRR-VFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 92 AMQypVEvPGVSMSNFLrsaatairGEPPKLRHWVKEVkaamaaLDIDPAFAERSVNEG--FSGGEKKRHEILQLELLKP 169
Cdd:PRK11614 94 RMT--VE-ENLAMGGFF--------AERDQFQERIKWV------YELFPRLHERRIQRAgtMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 170 KIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHYTRILRYIHPEYvhVFVGGRIV--ESGGSELADELDQNGY 247
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGY--VLENGHVVleDTGDALLANEAVRSAY 234
|
..
gi 950436399 248 VG 249
Cdd:PRK11614 235 LG 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
11-234 |
2.20e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.60 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 11 VSVENPAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTL--SYAIAGHPKY-HVTSGTITLDGADVLamsideRARA 87
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrCINLLEQPEAgTIRVGDITIDTARSL------SQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 88 GLFLAMQYPVevpGVSMSNF----LRSAATAIRGEPPKLRhwvKEVKAAMAAL------DIDPAFAERSVNEGFSGGEKK 157
Cdd:PRK11264 78 GLIRQLRQHV---GFVFQNFnlfpHRTVLENIIEGPVIVK---GEPKEEATARarellaKVGLAGKETSYPRRLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 950436399 158 RHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHgGILLITHYTRILRYIhPEYVHVFVGGRIVESG 234
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDV-ADRAIFMDQGRIVEQG 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-210 |
2.44e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 53.66 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPKyhvtSGTITLDGADVLAMSIDERARAGlfLAMQYPVEVPGV 102
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGltHPD----AGSISLCGEPVPSRARHARQRVG--VVPQFDNLDPDF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 103 SMSNFLR--------SAATAIRGEPPKLRHWVKEVKaamaaldidpafAERSVNEgFSGGEKKRHEILQLELLKPKIAIL 174
Cdd:PRK13537 96 TVRENLLvfgryfglSAAAARALVPPLLEFAKLENK------------ADAKVGE-LSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 950436399 175 DETDSGLDVDALRVVSEGVnRYAESQHGGILLITHY 210
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERL-RSLLARGKTILLTTHF 197
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-182 |
2.50e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 54.18 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MTILEIKDLHVSVENPaeadheiPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPkyHVTSGTITLDGADVLAMS 80
Cdd:PRK09452 12 SPLVELRGISKSFDGK-------EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFE--TPDSGRIMLDGQDITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 81 IDERARAGLFlaMQYPVeVPgvSMSNF------LRSAATAirgePPKLRHWVKEVkAAMAALDidpAFAERSVNEgFSGG 154
Cdd:PRK09452 83 AENRHVNTVF--QSYAL-FP--HMTVFenvafgLRMQKTP----AAEITPRVMEA-LRMVQLE---EFAQRKPHQ-LSGG 148
|
170 180
....*....|....*....|....*...
gi 950436399 155 EKKRHEILQLELLKPKIAILDETDSGLD 182
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-209 |
2.65e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.96 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MTILEIKDLHVSVENPaeaDHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG-HPKYHVTSGTITLDGADVLAM 79
Cdd:PRK09473 10 DALLDVKDLRVTFSTP---DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGlLAANGRIGGSATFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 80 SIDE--RARAGLfLAMQYpvEVPGVSMSNFLR---------------SAATAIRgEPPKLRHWVK--EVKAAMaaldidp 140
Cdd:PRK09473 87 PEKElnKLRAEQ-ISMIF--QDPMTSLNPYMRvgeqlmevlmlhkgmSKAEAFE-ESVRMLDAVKmpEARKRM------- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 950436399 141 afaeRSVNEGFSGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITH 209
Cdd:PRK09473 156 ----KMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITH 220
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-209 |
3.02e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 52.50 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG-HPKyhvTSGTITLDGADvLAMSIDERARAGLFLAMQypvevPGVs 103
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGlSPP---LAGRVLLNGGP-LDFQRDSIARGLLYLGHA-----PGI- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 104 msnflRSAATAIRgeppKLRHW-----VKEVKAAMAALDIDpAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDETD 178
Cdd:cd03231 85 -----KTTLSVLE----NLRFWhadhsDEQVEEALARVGLN-GFEDRPVAQ-LSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 950436399 179 SGLDVdalrvvsEGVNRYAE--SQH----GGILLITH 209
Cdd:cd03231 154 TALDK-------AGVARFAEamAGHcargGMVVLTTH 183
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-210 |
3.10e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.17 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 17 AEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTlsyaIAGH------PkyhvTSGTITLDGADVLAMS--IDERARAG 88
Cdd:PRK13633 17 NEESTEKLALDDVNLEVKKGEFLVILGRNGSGKST----IAKHmnalliP----SEGKVYVDGLDTSDEEnlWDIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 89 lfLAMQYPvevpgvsmSNFLrsAATAIR----------GEPPK-LRHWVKEVKAAMAALDIdpafaERSVNEGFSGGEKK 157
Cdd:PRK13633 89 --MVFQNP--------DNQI--VATIVEedvafgpenlGIPPEeIRERVDESLKKVGMYEY-----RRHAPHLLSGGQKQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 950436399 158 RHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHY 210
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHY 204
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-209 |
3.12e-08 |
|
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: 53.42 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSiDERARA-------------GLFLA 92
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINR--LIEPTSGKVLIDGQDIAAMS-RKELRElrrkkismvfqsfALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 93 MqypvevpgvsmsNFLRSAATA--IRGEPPKLRHwvkevKAAMAALDID--PAFAERSVNEgFSGGEKKRHEILQLELLK 168
Cdd:cd03294 117 R------------TVLENVAFGleVQGVPRAERE-----ERAAEALELVglEGWEHKYPDE-LSGGMQQRVGLARALAVD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 950436399 169 PKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITH 209
Cdd:cd03294 179 PDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITH 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-209 |
3.44e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 52.80 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 32 TVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVlamsiderARAGLFLAMQYPVEVpgvsmSNFLRSa 111
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLK--PDEGDIEIELDTV--------SYKPQYIKADYEGTV-----RDLLSS- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 112 ATAIRGEPPklrHWVKEVkaaMAALDIDPAFaERSVNEgFSGGEKKRHEILqLELLKP-KIAILDETDSGLDVDALRVVS 190
Cdd:cd03237 85 ITKDFYTHP---YFKTEI---AKPLQIEQIL-DREVPE-LSGGELQRVAIA-ACLSKDaDIYLLDEPSAYLDVEQRLMAS 155
|
170
....*....|....*....
gi 950436399 191 EGVNRYAESQHGGILLITH 209
Cdd:cd03237 156 KVIRRFAENNEKTAFVVEH 174
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-89 |
3.54e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 53.12 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 2 TILEIKDLHVSVenpaeADHEIpiLRGVDLTVKSGETHALMGPNGSGKSTL---------SYaiaghPKYHVTsGTITLD 72
Cdd:COG1117 10 PKIEVRNLNVYY-----GDKQA--LKDINLDIPENKVTALIGPSGCGKSTLlrclnrmndLI-----PGARVE-GEILLD 76
|
90 100
....*....|....*....|
gi 950436399 73 GADVLAMSID---ERARAGL 89
Cdd:COG1117 77 GEDIYDPDVDvveLRRRVGM 96
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-209 |
1.09e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.66 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MTILEIKDLHVSVENpaeaDHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMS 80
Cdd:PRK13650 2 SNIIEVKNLTFKYKE----DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLE--AESGQIIIDGDLLTEEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 81 I-DERARAGlfLAMQYP-VEVPGVSMSNflrSAATAIRGEPPKLRHWVKEVKAAMAALDIDpAFAERSVNEgFSGGEKKR 158
Cdd:PRK13650 76 VwDIRHKIG--MVFQNPdNQFVGATVED---DVAFGLENKGIPHEEMKERVNEALELVGMQ-DFKEREPAR-LSGGQKQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 950436399 159 HEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITH 209
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITH 199
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-76 |
1.41e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.77 E-value: 1.41e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 950436399 1 MTILEIKDLHVSVENPaeadheIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADV 76
Cdd:PRK11650 1 MAGLKLQAVRKSYDGK------TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLER--ITSGEIWIGGRVV 68
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-246 |
1.53e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.94 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 22 EIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIdERARAGLFLAMQyPVEVPG 101
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRF--YDIDEGEILLDGHDLRDYTL-ASLRNQVALVSQ-NVHLFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 102 VSMSNFLRSAATairgeppklRHWVKE--VKAA-MA-ALD--------IDPAFAERSVNegFSGGEKKRHEILQLELLKP 169
Cdd:PRK11176 431 DTIANNIAYART---------EQYSREqiEEAArMAyAMDfinkmdngLDTVIGENGVL--LSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 950436399 170 KIAILDETDSGLDVDALRVVSEGVNRYAESQhgGILLITHytRILRYIHPEYVHVFVGGRIVESGGSelADELDQNG 246
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNR--TSLVIAH--RLSTIEKADEILVVEDGEIVERGTH--AELLAQNG 570
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
28-237 |
1.93e-07 |
|
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: 51.73 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 28 GVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HP---KYHVTSGTitlDGADVLAMSIDERARAGLFLAMQYPvEVPGV 102
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGvlEPtsgEVNVRVGD---EWVDMTKPGPDGRGRAKRYIGILHQ-EYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 103 SMSNFLRSAATAIRGEPPKLRHWVKEVkAAMAALDIDPAFAERSVN---EGFSGGEKKRHEILQLELLKPKIAILDETDS 179
Cdd:TIGR03269 378 PHRTVLDNLTEAIGLELPDELARMKAV-ITLKMVGFDEEKAEEILDkypDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 950436399 180 GLDVDALRVVSEGVNRYAESQHGGILLITHYTRILRYIhPEYVHVFVGGRIVESGGSE 237
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDV-CDRAALMRDGKIVKIGDPE 513
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-182 |
2.07e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 51.37 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVENPAEADHeipilrgVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPkyHVTSGTITLDGADVLAMSID 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDD-------VSLTIYKGEIFALLGASGCGKSTLLRMLAGFE--QPTAGQIMLDGVDLSHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 83 ERARAGLFlamQYPVEVPGVSMSNFLRSAATAIRGEPPKLRHWVKEvkaaMAALDIDPAFAERSVNEgFSGGEKKRHEIL 162
Cdd:PRK11607 90 QRPINMMF---QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNE----MLGLVHMQEFAKRKPHQ-LSGGQRQRVALA 161
|
170 180
....*....|....*....|
gi 950436399 163 QLELLKPKIAILDETDSGLD 182
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALD 181
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
29-243 |
2.33e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.89 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 29 VDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLdgADVLAMSIDER-----ARAGLFLAMQYPvevpgvs 103
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNG--LLQPTEGKVTV--GDIVVSSTSKQkeikpVRKKVGVVFQFP------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 104 MSNFLRSAATAIRGEPPKLRHWVKEVKAAMAA-----LDIDPAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDETD 178
Cdd:PRK13643 94 ESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAeklemVGLADEFWEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 950436399 179 SGLDVDA---LRVVSEGVNRYAESqhggILLITHYTRILRYiHPEYVHVFVGGRIVESGG-SELADELD 243
Cdd:PRK13643 173 AGLDPKArieMMQLFESIHQSGQT----VVLVTHLMDDVAD-YADYVYLLEKGHIISCGTpSDVFQEVD 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-73 |
2.54e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 2.54e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDG 73
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSG--NYQPDAGSILIDG 65
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
10-76 |
2.91e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.08 E-value: 2.91e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 950436399 10 HVSVENPAEadheiPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYhvTSGTITLDGADV 76
Cdd:PRK11248 6 HLYADYGGK-----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPY--QHGSITLDGKPV 65
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-236 |
3.21e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.05 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVENPAeadheipILRGVDLTVKSGETHALMGPNGSGKST----LSYAIAGHPKYHVTSGTITLDGADVLA 78
Cdd:PRK14246 10 VFNISRLYLYINDKA-------ILKDITIKIPNNSIFGIMGPSGSGKSTllkvLNRLIEIYDSKIKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 79 M-SIDERARAGlfLAMQYPVEVPGVSMSNflrSAATAIRGEPPKLRHWVKE-VKAAMAALDIDPAFAER--SVNEGFSGG 154
Cdd:PRK14246 83 IdAIKLRKEVG--MVFQQPNPFPHLSIYD---NIAYPLKSHGIKEKREIKKiVEECLRKVGLWKEVYDRlnSPASQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 155 EKKRHEILQLELLKPKIAILDETDSGLDV----DALRVVSEGVNRYAesqhggILLITHYTRILRYIhPEYVHVFVGGRI 230
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIvnsqAIEKLITELKNEIA------IVIVSHNPQQVARV-ADYVAFLYNGEL 230
|
....*.
gi 950436399 231 VESGGS 236
Cdd:PRK14246 231 VEWGSS 236
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-234 |
3.40e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.21 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGH------PKYHVTSGTITLDGADVLAMSIDERARAGLFLAMQ---- 94
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggaPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLPQAaqpa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 95 YPVEVPG-VSMSNF---LRSAATAIRGeppklrhwvKEVKAAMAALDIDPAFAERSVNEgFSGGEKKRHE----ILQL-- 164
Cdd:PRK13547 96 FAFSAREiVLLGRYphaRRAGALTHRD---------GEIAWQALALAGATALVGRDVTT-LSGGELARVQfarvLAQLwp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 950436399 165 ---ELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHYTRiLRYIHPEYVHVFVGGRIVESG 234
Cdd:PRK13547 166 phdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPN-LAARHADRIAMLADGAIVAHG 237
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
29-83 |
4.06e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.74 E-value: 4.06e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 950436399 29 VDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSIDE 83
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTG--LYQPQSGEILLDGKPVTAEQPED 394
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-90 |
4.82e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 49.58 E-value: 4.82e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 950436399 30 DLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSIDERARAGLF 90
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGF--LTPASGSLTLNGQDHTTTPPSRRPVSMLF 77
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
26-183 |
5.30e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.50 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITldgadVLAMSIDERARAGLF--------LAMQYPV 97
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGF--VRLASGKIS-----ILGQPTRQALQKNLVayvpqseeVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 98 EVPGVSM------SNFLRSAATAIRgeppklrhwvKEVKAAMAALDIdPAFAERSVNEgFSGGEKKRHEILQLELLKPKI 171
Cdd:PRK15056 96 LVEDVVMmgryghMGWLRRAKKRDR----------QIVTAALARVDM-VEFRHRQIGE-LSGGQKKRVFLARAIAQQGQV 163
|
170
....*....|..
gi 950436399 172 AILDETDSGLDV 183
Cdd:PRK15056 164 ILLDEPFTGVDV 175
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-210 |
5.82e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 49.70 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 21 HEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITldgadVLAMSIDERARAglfLAMQYpve 98
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGilVP----TSGEVR-----VLGYVPFKRRKE---FARRI--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 99 vpGVSMSN---------------FLRsaatAIRGEPPK-LRHWVKEVkAAMaaLDIDPaFAERSVNEgFSGGEKKRHEIL 162
Cdd:COG4586 98 --GVVFGQrsqlwwdlpaidsfrLLK----AIYRIPDAeYKKRLDEL-VEL--LDLGE-LLDTPVRQ-LSLGQRMRCELA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 950436399 163 qLELL-KPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHY 210
Cdd:COG4586 167 -AALLhRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHD 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-73 |
7.14e-07 |
|
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: 48.62 E-value: 7.14e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 950436399 6 IKDLHVSVENPAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDG 73
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG--ELEKLSGSVSVPG 66
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-209 |
8.85e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.31 E-value: 8.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 22 EIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVlamSIDERARaglflAMQYPVEVPG 101
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAG--LLHVESGQIQIDGKTA---TRGDRSR-----FMAYLGHLPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 102 V-----SMSN--FLrsaaTAIRGEPPKlrhwvKEVKAAMAALDIdpAFAERSVNEGFSGGEKKRHEILQLELLKPKIAIL 174
Cdd:PRK13543 93 LkadlsTLENlhFL----CGLHGRRAK-----QMPGSALAIVGL--AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 950436399 175 DETDSGLDVDALRVVSEGVNRYAESQhGGILLITH 209
Cdd:PRK13543 162 DEPYANLDLEGITLVNRMISAHLRGG-GAALVTTH 195
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
24-199 |
1.01e-06 |
|
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: 48.01 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHVTSGTITLDGadvLAMSIDERARAGlfLAMQYPVEVPGVS 103
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILING---RPLDKNFQRSTG--YVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 104 MSNFLRSAAtairgeppKLRhwvkevkaamaaldidpafaersvneGFSGGEKKRHEIlQLELL-KPKIAILDETDSGLD 182
Cdd:cd03232 96 VREALRFSA--------LLR--------------------------GLSVEQRKRLTI-GVELAaKPSILFLDEPTSGLD 140
|
170
....*....|....*..
gi 950436399 183 VDALRVVSEGVNRYAES 199
Cdd:cd03232 141 SQAAYNIVRFLKKLADS 157
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-234 |
1.05e-06 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 48.26 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 20 DHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSIdERARAGLFLAMQYPVEV 99
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFR--LVELSSGSILIDGVDISKIGL-HDLRSRISIIPQDPVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 100 PGVSMSN---FLRSAATAIRG--EPPKLRHWVKEVKAAMAALDIDpafaersVNEGFSGGEKkrheilQL-----ELL-K 168
Cdd:cd03244 91 SGTIRSNldpFGEYSDEELWQalERVGLKEFVESLPGGLDTVVEE-------GGENLSVGQR------QLlclarALLrK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 950436399 169 PKIAILDETDSGLDVDALRVVSEGV-NRYAESQhggILLITH-------YTRILryihpeyvhVFVGGRIVESG 234
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIrEAFKDCT---VLTIAHrldtiidSDRIL---------VLDKGRVVEFD 219
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-74 |
1.14e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 1.14e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG-HPkyHVT-SGTITLDGA 74
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvYP--HGSyEGEILFDGE 65
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
25-237 |
1.61e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 48.25 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDERARAGLFLAMQYPvEVPGVSM 104
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQP--PSEGEILLDAQPLESWSSKAFARKVAYLPQQLP-AAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 105 SNFLRSAATAIRGEPPKLRHWVKE-VKAAMAALDIDPaFAERSVnEGFSGGEKKRHEILQLELLKPKIAILDETDSGLD- 182
Cdd:PRK10575 103 RELVAIGRYPWHGALGRFGAADREkVEEAISLVGLKP-LAHRLV-DSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDi 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 950436399 183 ---VDALRVVSEgvnryaESQHGGILLITHYTRI---LRYIhpEYVHVFVGGRIVESGGSE 237
Cdd:PRK10575 181 ahqVDVLALVHR------LSQERGLTVIAVLHDInmaARYC--DYLVALRGGEMIAQGTPA 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
26-234 |
1.82e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 47.82 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYhvTSGTITLDGADVLAMSIDErARAGLFLAMQYPVEVPGVSMS 105
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKV--KSGEIFYNNQAITDDNFEK-LRKHIGIVFQNPDNQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 106 NFlrSAATAIRGEPPKLRHWVKEVKAAMAALD-IDPAFAErsvNEGFSGGEKKRHEILQLELLKPKIAILDETDSGLDVD 184
Cdd:PRK13648 102 KY--DVAFGLENHAVPYDEMHRRVSEALKQVDmLERADYE---PNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 950436399 185 ALRVVSEGVNRYAESQHGGILLITHytRILRYIHPEYVHVFVGGRIVESG 234
Cdd:PRK13648 177 ARQNLLDLVRKVKSEHNITIISITH--DLSEAMEADHVIVMNKGTVYKEG 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
25-195 |
1.84e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 48.06 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMSIDERARAGLFLAMQypVEVPG- 101
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRlmTP----AHGHVWLDGEHIQHYASKEVARRIGLLAQN--ATTPGd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 102 VSMSNFLrsaATAIRGEPPKLRHWVKE----VKAAMAALDIDpAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDET 177
Cdd:PRK10253 96 ITVQELV---ARGRYPHQPLFTRWRKEdeeaVTKAMQATGIT-HLADQSVDT-LSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180
....*....|....*....|..
gi 950436399 178 DSGLD----VDALRVVSEgVNR 195
Cdd:PRK10253 171 TTWLDishqIDLLELLSE-LNR 191
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-181 |
1.92e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSIDERARAGLFLAMQYPVEVPGVS-M 104
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG--IYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSvM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 105 SNFLrsaataiRGEPPKLRHWV------KEVKAAMAALDIDPAFAERSVNegFSGGEKKRHEILQLELLKPKIAILDETD 178
Cdd:PRK10982 92 DNMW-------LGRYPTKGMFVdqdkmyRDTKAIFDELDIDIDPRAKVAT--LSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
...
gi 950436399 179 SGL 181
Cdd:PRK10982 163 SSL 165
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
29-76 |
2.01e-06 |
|
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: 48.64 E-value: 2.01e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 950436399 29 VDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADV 76
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGL--YRPESGEILLDGQPV 396
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-91 |
2.60e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.09 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 2 TILEIKDLHVSvenpaeadheiPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMSI 81
Cdd:COG1129 255 VVLEVEGLSVG-----------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFG--ADPADSGEIRLDGKPVRIRSP 321
|
90
....*....|
gi 950436399 82 DERARAGLFL 91
Cdd:COG1129 322 RDAIRAGIAY 331
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-259 |
3.87e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIagHPKYHVTSGTITLDGADVLAMSIDERARAgLFLAMQYPVEVPGVS 103
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNAL--FRIVELEKGRIMIDDCDVAKFGLTDLRRV-LSIIPQSPVLFSGTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 104 MSNFlrsaatairgePPKLRH-----WVKEVKAAMA-ALDIDPAFAERSVNEG---FSGGEKKRHEILQLELLKPKIAIL 174
Cdd:PLN03232 1327 RFNI-----------DPFSEHndadlWEALERAHIKdVIDRNPFGLDAEVSEGgenFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 175 DETDSGLDV--DAL--RVVSEgvnryaESQHGGILLITHytRILRYIHPEYVHVFVGGRIVESGGSEladELDQNGYVGF 250
Cdd:PLN03232 1396 DEATASVDVrtDSLiqRTIRE------EFKSCTMLVIAH--RLNTIIDCDKILVLSSGQVLEYDSPQ---ELLSRDTSAF 1464
|
250
....*....|....*.
gi 950436399 251 S-------PASGRYPH 259
Cdd:PLN03232 1465 FrmvhstgPANAQYLS 1480
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-188 |
4.23e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.33 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 11 VSVENPAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGAdvlAMSIDERARAGLF 90
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGDLFIGEK---RMNDVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 91 LAMQ----YPVEVPGVSMSNFLRSAATAiRGEPPKLRHWVKEVKAAMAALDIDPafaersvnEGFSGGEKKRHEILQLEL 166
Cdd:PRK11000 79 MVFQsyalYPHLSVAENMSFGLKLAGAK-KEEINQRVNQVAEVLQLAHLLDRKP--------KALSGGQRQRVAIGRTLV 149
|
170 180
....*....|....*....|..
gi 950436399 167 LKPKIAILDETDSGLDVdALRV 188
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDA-ALRV 170
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
40-209 |
4.37e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 40 ALMGPNGSGKSTLSYAIAGhpKYHVTSGTItLDGADVLAMSIDERARAGLFLAmqypvevpgvsmSNFLRSAATAIRGEP 119
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISG--ELQPSSGTV-FRSAKVRMAVFSQHHVDGLDLS------------SNPLLYMMRCFPGVP 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 120 PKlrhwvkEVKAAMAALDIDPAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYaes 199
Cdd:PLN03073 604 EQ------KLRAHLGSFGVTGNLALQPMYT-LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLF--- 673
|
170
....*....|
gi 950436399 200 qHGGILLITH 209
Cdd:PLN03073 674 -QGGVLMVSH 682
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-234 |
4.39e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 47.10 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 5 EIKDLHVSVENPAeadHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMSid 82
Cdd:PRK11153 3 ELKNISKVFPQGG---RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLleRP----TSGRVLVDGQDLTALS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 83 eraRAGLFLAMQypvevpGVSMS----NFL--RSAATAIrGEPPKLRHWVK-EVKAAMAAL----------DIDPAfaer 145
Cdd:PRK11153 74 ---EKELRKARR------QIGMIfqhfNLLssRTVFDNV-ALPLELAGTPKaEIKARVTELlelvglsdkaDRYPA---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 146 svneGFSGGEKKRHEILQLELLKPKIAILDETDSGLD-------VDALRvvseGVNRyaesQHG-GILLITHYTRILRYI 217
Cdd:PRK11153 140 ----QLSGGQKQRVAIARALASNPKVLLCDEATSALDpattrsiLELLK----DINR----ELGlTIVLITHEMDVVKRI 207
|
250
....*....|....*..
gi 950436399 218 HPEyVHVFVGGRIVESG 234
Cdd:PRK11153 208 CDR-VAVIDAGRLVEQG 223
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-182 |
4.70e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVenPAEADHEIpILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpkyHVTSGTITLDGADVLAMSID 82
Cdd:TIGR00956 759 IFHWRNLTYEV--KIKKEKRV-ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE----RVTTGVITGGDRLVNGRPLD 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 83 ERARAGLFLAMQYPVEVPGVSM------SNFLRSAATAIRGEppKLRhWVKEVkaaMAALDIDpAFAERSV---NEGFSG 153
Cdd:TIGR00956 832 SSFQRSIGYVQQQDLHLPTSTVreslrfSAYLRQPKSVSKSE--KME-YVEEV---IKLLEME-SYADAVVgvpGEGLNV 904
|
170 180 190
....*....|....*....|....*....|.
gi 950436399 154 GEKKRHEIlQLELL-KPKIAI-LDETDSGLD 182
Cdd:TIGR00956 905 EQRKRLTI-GVELVaKPKLLLfLDEPTSGLD 934
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-237 |
6.74e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.24 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 17 AEADHEIPILRGVDLTVK-SGET--------------HALMGPNGSGKST-------LSYAIAGHpKYhvtSGTITLDGA 74
Cdd:PRK14271 13 ADVDAAAPAMAAVNLTLGfAGKTvldqvsmgfparavTSLMGPTGSGKTTflrtlnrMNDKVSGY-RY---SGDVLLGGR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 75 DVLAMS--IDERARAGLFLamQYPVEVPGVSMSNFLrsaaTAIRGEPPKLRHWVKEV-KAAMAALDIDPAFAERSVNEGF 151
Cdd:PRK14271 89 SIFNYRdvLEFRRRVGMLF--QRPNPFPMSIMDNVL----AGVRAHKLVPRKEFRGVaQARLTEVGLWDAVKDRLSDSPF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 152 --SGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQhgGILLITHYTRILRYIhPEYVHVFVGGR 229
Cdd:PRK14271 163 rlSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARI-SDRAALFFDGR 239
|
....*...
gi 950436399 230 IVESGGSE 237
Cdd:PRK14271 240 LVEEGPTE 247
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
24-237 |
1.07e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 46.25 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHpkYHVTSGTITLDGADVLAMSiDERARAGLFLAMQYPVevpgVS 103
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGY--YPLTEGEIRLDGRPLSSLS-HSVLRQGVAMVQQDPV----VL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 104 MSNFLrsaATAIRGeppklRHWVKE-VKAAMAALDIdpAFAERSVNEG-----------FSGGEKKRHEILQLELLKPKI 171
Cdd:PRK10790 428 ADTFL---ANVTLG-----RDISEEqVWQALETVQL--AELARSLPDGlytplgeqgnnLSVGQKQLLALARVLVQTPQI 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 950436399 172 AILDET----DSGLD---VDALRVVSEgvnryaesqHGGILLITHytRILRYIHPEYVHVFVGGRIVESGGSE 237
Cdd:PRK10790 498 LILDEAtaniDSGTEqaiQQALAAVRE---------HTTLVVIAH--RLSTIVEADTILVLHRGQAVEQGTHQ 559
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-86 |
2.20e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.49 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MT-ILEIKDLHVSVENpaeADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAM 79
Cdd:PRK10535 1 MTaLLELKDIRRSYPS---GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDK--PTSGTYRVAGQDVATL 75
|
....*..
gi 950436399 80 SIDERAR 86
Cdd:PRK10535 76 DADALAQ 82
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-209 |
2.57e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 31 LTVKSGETHA-----LMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDgadvlamsideraragLFLAM--QYPVEVPGVS 103
Cdd:PRK13409 355 LEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLK--PDEGEVDPE----------------LKISYkpQYIKPDYDGT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 104 MSNFLRSAATAIRGeppklrHWVK-EVkaaMAALDIDPAFaERSVNEgFSGGEKKRHEILQLELLKPKIAILDETDSGLD 182
Cdd:PRK13409 417 VEDLLRSITDDLGS------SYYKsEI---IKPLQLERLL-DKNVKD-LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
170 180
....*....|....*....|....*..
gi 950436399 183 VDALRVVSEGVNRYAESQHGGILLITH 209
Cdd:PRK13409 486 VEQRLAVAKAIRRIAEEREATALVVDH 512
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-234 |
2.69e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.84 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 3 ILEIKDLHVSVENPAEadHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPKYhvtsGTITLD----GADV 76
Cdd:PRK13631 21 ILRVKNLYCVFDEKQE--NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGliKSKY----GTIQVGdiyiGDKK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 77 LAMSID-----------ERARAGLFLAMQYPvevpgvSMSNFLRSAATAIRGEPPKLRhwVKEVKAAMAA------LDID 139
Cdd:PRK13631 95 NNHELItnpyskkiknfKELRRRVSMVFQFP------EYQLFKDTIEKDIMFGPVALG--VKKSEAKKLAkfylnkMGLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 140 PAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVnRYAESQHGGILLITHYTRILRYIhP 219
Cdd:PRK13631 167 DSYLERSPFG-LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTMEHVLEV-A 243
|
250
....*....|....*
gi 950436399 220 EYVHVFVGGRIVESG 234
Cdd:PRK13631 244 DEVIVMDKGKILKTG 258
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-237 |
4.69e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.02 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 1 MTILEIKDLHVSVENPaeaDHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPK--YHVTSGTITLDGADVLA 78
Cdd:PRK15093 1 MPLLDIRNLTIEFKTS---DGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnWRVTADRMRFDDIDLLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 79 MSIDERAR-AGLFLAM--QYPVEV--PGVSMSnflRSAATAIRGEPPKLRHWVKEVKAAMAALDI-------DPAFAERS 146
Cdd:PRK15093 78 LSPRERRKlVGHNVSMifQEPQSCldPSERVG---RQLMQNIPGWTYKGRWWQRFGWRKRRAIELlhrvgikDHKDAMRS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 147 VNEGFSGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHYTRILRYIhPEYVHVFV 226
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQW-ADKINVLY 233
|
250
....*....|.
gi 950436399 227 GGRIVESGGSE 237
Cdd:PRK15093 234 CGQTVETAPSK 244
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-232 |
5.60e-05 |
|
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: 43.36 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVENPAEadheiPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIagHPKYHVTSGTITLDGADVLAMSIdE 83
Cdd:cd03288 20 IKIHDLCVRYENNLK-----PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAF--FRMVDIFDGKIVIDGIDISKLPL-H 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 84 RARAGLFLAMQYPVevpgvsmsnfLRSAATAIRGEPPKL----RHW----VKEVKAAMAALdidPAFAERSVNEG---FS 152
Cdd:cd03288 92 TLRSRLSIILQDPI----------LFSGSIRFNLDPECKctddRLWealeIAQLKNMVKSL---PGGLDAVVTEGgenFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 153 GGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGV-NRYAESQhggILLITHytRILRYIHPEYVHVFVGGRIV 231
Cdd:cd03288 159 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVmTAFADRT---VVTIAH--RVSTILDADLVLVLSRGILV 233
|
.
gi 950436399 232 E 232
Cdd:cd03288 234 E 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-209 |
8.92e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 42.79 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 11 VSVENPAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLdgadvlamsiDERARAG 88
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGlvAP----DEGVIKR----------NGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 89 -----LFLAMQYPVEVpgvsmSNFLRsaatairgeppkLRHWVKEVkaamaalDIDPAFAErsVNEG---------FSGG 154
Cdd:PRK09544 71 yvpqkLYLDTTLPLTV-----NRFLR------------LRPGTKKE-------DILPALKR--VQAGhlidapmqkLSGG 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 950436399 155 EKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITH 209
Cdd:PRK09544 125 ETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSH 179
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
36-234 |
1.07e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.31 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 36 GETHALMGPNGSGKSTLSYAIAghPKYHVTSGTITLDGA--DVLAMSIDERARAGLFLAMQYPV------EVPGVSMSNF 107
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALL--RLVESQGGEIIFNGQriDTLSPGKLQALRRDIQFIFQDPYasldprQTVGDSIMEP 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 108 LRSAATaIRGEPPKLRhwvkeVKAAMAALDIDPAFAERSVNEgFSGGEKKRHEILQLELLKPKIAILDETDSGLDVDalr 187
Cdd:PRK10261 428 LRVHGL-LPGKAAAAR-----VAWLLERVGLLPEHAWRYPHE-FSGGQRQRICIARALALNPKVIIADEAVSALDVS--- 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 950436399 188 VVSEGVNRYAESQHG-GI--LLITHYTRILRYIhPEYVHVFVGGRIVESG 234
Cdd:PRK10261 498 IRGQIINLLLDLQRDfGIayLFISHDMAVVERI-SHRVAVMYLGQIVEIG 546
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-61 |
1.08e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 1.08e-04
10 20 30
....*....|....*....|....*....|....*....
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG-HPK 61
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQ 312
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
151-222 |
1.17e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 1.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 950436399 151 FSGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAESQHGGILLITHYTRILRYIHPEYV 222
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFV 651
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
25-237 |
1.37e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 42.31 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTL-------------SYAIAGHpKYHVTSGTitlDGADVLAMsideRARAGLFL 91
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLlrvlnllemprsgTLNIAGN-HFDFSKTP---SDKAIREL----RRNVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 92 aMQY---------------PVEVPGVSmsnflRSAAtairgeppklrhwVKEVKAAMAALDIDPaFAERsvnegF----S 152
Cdd:PRK11124 89 -QQYnlwphltvqqnlieaPCRVLGLS-----KDQA-------------LARAEKLLERLRLKP-YADR-----FplhlS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 153 GGEKKRHEILQLELLKPKIAILDETDSGLDVDalrVVSEGVNRYAESQHGGI--LLITHYTRILRYIHPEYVHVfVGGRI 230
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPE---ITAQIVSIIRELAETGItqVIVTHEVEVARKTASRVVYM-ENGHI 219
|
....*..
gi 950436399 231 VESGGSE 237
Cdd:PRK11124 220 VEQGDAS 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-80 |
1.45e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.06 E-value: 1.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADVLAMS 80
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGG--QIAPDHGEILFDGENIPAMS 75
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-209 |
1.57e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 41.71 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVSVEnpaeadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMSi 81
Cdd:PRK13538 2 LEARNLACERD-------ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlaRP----DAGEVLWQGEPIRRQR- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 82 DERARAGLFLAMQypvevPGVS--MSNF--LRSAAtAIRGEPPKLRHWvkevkAAMAALDIdpafaersvnEGF------ 151
Cdd:PRK13538 70 DEYHQDLLYLGHQ-----PGIKteLTALenLRFYQ-RLHGPGDDEALW-----EALAQVGL----------AGFedvpvr 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 950436399 152 --SGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAEsqHGGI-LLITH 209
Cdd:PRK13538 129 qlSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAE--QGGMvILTTH 187
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
25-209 |
2.98e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 40.95 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 25 ILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDGADVLAMSidERARAGL------FLaMQYP 96
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGldTP----TSGDVIFNGQPMSKLS--SAAKAELrnqklgFI-YQFH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 97 VEVPGVsmsNFLRSAATA--IRGEPPKLRHwvKEVKAAMAALDIDPAFAERSVNegFSGGEKKRHEILQLELLKPKIAIL 174
Cdd:PRK11629 97 HLLPDF---TALENVAMPllIGKKKPAEIN--SRALEMLAAVGLEHRANHRPSE--LSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190
....*....|....*....|....*....|....*
gi 950436399 175 DETDSGLDVDALRVVSEGVNRYAESQHGGILLITH 209
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTH 204
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-73 |
3.10e-04 |
|
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: 41.62 E-value: 3.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 950436399 29 VDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDG 73
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGleRP----DSGRIRLGG 60
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-185 |
3.57e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.45 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 2 TILEIKDLHV-SVENPaeadhEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPKYhvtSGTITLDGADV-- 76
Cdd:PRK13549 258 VILEVRNLTAwDPVNP-----HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGayPGRW---EGEIFIDGKPVki 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 77 ----------LAMSIDERARAGLFLAMQYPVEVPGVSMSNF-----LRSAA--TAIRGEPPKLRhwvkeVKAAMAALDId 139
Cdd:PRK13549 330 rnpqqaiaqgIAMVPEDRKRDGIVPVMGVGKNITLAALDRFtggsrIDDAAelKTILESIQRLK-----VKTASPELAI- 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 950436399 140 pafaersvnEGFSGGEKKRHEILQLELLKPKIAILDETDSGLDVDA 185
Cdd:PRK13549 404 ---------ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGA 440
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-89 |
3.99e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 2 TILEIKDLhvSVENPAEADHEIpiLRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKYHVTSGTITLDGADVLAMSI 81
Cdd:NF040905 256 VVFEVKNW--TVYHPLHPERKV--VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNISGTVFKDGKEVDVSTV 331
|
....*...
gi 950436399 82 DERARAGL 89
Cdd:NF040905 332 SDAIDAGL 339
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-69 |
4.29e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 4.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 950436399 7 KDLH---VSVENPAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTI 69
Cdd:PRK15064 313 KKLHrnaLEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG--ELEPDSGTV 376
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
26-80 |
1.28e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.87 E-value: 1.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpkyhVT---SGTITLDG-ADVLAMS 80
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAG-----VTmpnKGTVDIKGsAALIAIS 93
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
6-89 |
1.35e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 6 IKDLHVsvenPAEADHEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGaDVLAMSIDera 85
Cdd:PRK13546 24 MKDALI----PKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGG--SLSPTVGKVDRNG-EVSVIAIS--- 93
|
....
gi 950436399 86 rAGL 89
Cdd:PRK13546 94 -AGL 96
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-210 |
1.44e-03 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 40.00 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 24 PILRGVDLTVKSGETHALMGPNGSGK-STLSYAIAGHPKyhvTSGTITLDGADVlAMSIDErARAGLFLAMQYPVEVPGV 102
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKtTTLSILTGLLPP---TSGTVLVGGKDI-ETNLDA-VRQSLGMCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 103 SMSNFLRSAATAirgeppKLRHWvKEVKAAMAALDIDPAFAERSVNEG--FSGGEKKRHEILQLELLKPKIAILDETDSG 180
Cdd:TIGR01257 1019 TVAEHILFYAQL------KGRSW-EEAQLEMEAMLEDTGLHHKRNEEAqdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190
....*....|....*....|....*....|
gi 950436399 181 LDVDALRVVSEGVNRYAESQhgGILLITHY 210
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGR--TIIMSTHH 1119
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-76 |
1.58e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.60 E-value: 1.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGhpKYHVTSGTITLDGADV 76
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTG--IYTRDAGSILYLGKEV 68
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-208 |
1.82e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 39.26 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 21 HEIPILRGVDLT----------VKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADVLAMSIDERARAGLf 90
Cdd:PRK15439 264 AGAPVLTVEDLTgegfrnisleVRAGEILGLAGVVGAGRTELAETLYGLRP--ARGGRIMLNGKEINALSTAQRLARGL- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 91 lamqypVEVP------GVSMSNFLR-SAATAIRGEPPklrHWVKEVKAAM------AALDIDPAFAERSVnEGFSGGEKK 157
Cdd:PRK15439 341 ------VYLPedrqssGLYLDAPLAwNVCALTHNRRG---FWIKPARENAvleryrRALNIKFNHAEQAA-RTLSGGNQQ 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 950436399 158 RHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRYAEsQHGGILLIT 208
Cdd:PRK15439 411 KVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAA-QNVAVLFIS 460
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-87 |
1.90e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.34 E-value: 1.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 950436399 26 LRGVDLTVKSGETHALMGPNGSGKSTLSYAIAGHPKyhVTSGTITLDGADvlaMSiDERARA 87
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARK--IQQGRVEVLGGD---MA-DARHRR 72
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-185 |
1.93e-03 |
|
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: 39.42 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 5 EIKDLHVSVENPAEADHEIPILRGVD---LTVKSGETHALMGPNGSGKSTLSYAIAG-HPKYHvtSGTITLDGADV---- 76
Cdd:TIGR02633 252 EIGDVILEARNLTCWDVINPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKF--EGNVFINGKPVdirn 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 77 --------LAMSIDERARAGLFLAMQYPVEVPGVSMSNFLRSAATAIRGEPPKLRHWVKEVKAAMAALDIDPAfaersvn 148
Cdd:TIGR02633 330 paqairagIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIG------- 402
|
170 180 190
....*....|....*....|....*....|....*..
gi 950436399 149 eGFSGGEKKRHEILQLELLKPKIAILDETDSGLDVDA 185
Cdd:TIGR02633 403 -RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-242 |
2.22e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.24 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 4 LEIKDLHVS-VENPaeadhEIPILRGVDLTVKSGETHALMGPNGSGKST-----LSYAIAGHPKYHVTSGTITLDGADVL 77
Cdd:PTZ00265 1166 IEIMDVNFRyISRP-----NVPIYKDLTFSCDSKKTTAIVGETGSGKSTvmsllMRFYDLKNDHHIVFKNEHTNDMTNEQ 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 78 AMSIDERARAGLFLAMQYPVEVPGVSMSNF-----------------------LRSAATAIRGEPPKLRHWVKE------ 128
Cdd:PTZ00265 1241 DYQGDEEQNVGMKNVNEFSLTKEGGSGEDStvfknsgkilldgvdicdynlkdLRNLFSIVSQEPMLFNMSIYEnikfgk 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950436399 129 -------VKAA--MAALD--IDPAFAERSVNEG-----FSGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEG 192
Cdd:PTZ00265 1321 edatredVKRAckFAAIDefIESLPNKYDTNVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 950436399 193 VNRYAESQHGGILLITHytRILRYIHPEYVHVFVG----GRIVESGGSElaDEL 242
Cdd:PTZ00265 1401 IVDIKDKADKTIITIAH--RIASIKRSDKIVVFNNpdrtGSFVQAHGTH--EEL 1450
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-58 |
3.09e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.46 E-value: 3.09e-03
10 20
....*....|....*....|....*....
gi 950436399 30 DLTVKSGETHALMGPNGSGKSTLSYAIAG 58
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG 51
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
28-57 |
4.65e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.88 E-value: 4.65e-03
10 20 30
....*....|....*....|....*....|
gi 950436399 28 GVDLTVKSGETHALMGPNGSGKSTLSYAIA 57
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLLDAIQ 43
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-73 |
5.26e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 37.46 E-value: 5.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 950436399 21 HEIPILRGVDLTVKSGETHALMGPNGSGKSTLSYAIAG--HPkyhvTSGTITLDG 73
Cdd:PRK15112 24 QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGmiEP----TSGELLIDD 74
|
|
| |
