|
Name |
Accession |
Description |
Interval |
E-value |
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-254 |
9.56e-169 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 465.71 E-value: 9.56e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 1 MPQQIELQNIVLQADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGAILADGQPISPCKLRGIK 80
Cdd:PRK10418 1 MPQQIELRNIALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 81 VATIMQNPRSAFNPLHTMAAHAKETCLASGKPADDATLIAALEAVGLENAARVLKLYPFEMSGGMLQRMMIAMALLCDAP 160
Cdd:PRK10418 81 IATIMQNPRSAFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 161 FIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNL 240
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSL 240
|
250
....*....|....
gi 501085142 241 VSAHLALYGMELAS 254
Cdd:PRK10418 241 VSAHLALYGMELAS 254
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
18-245 |
6.79e-124 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 351.29 E-value: 6.79e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 18 LVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGAILADGQPISPCKLRGIKVATIMQNPRSAFNPLHT 97
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPLSIRGRHIATIMQNPRTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 98 MAAHAKETCLASGKPADDATLIA--ALEAVGLENAARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVA 175
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALIleALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 176 QARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSAHL 245
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSAHL 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-243 |
3.62e-83 |
|
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: 251.51 E-value: 3.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGVRqTAGAILADGQPISPC------KLRGIKVATIMQNPRSAF 92
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGI-TSGEILFDGEDLLKLsekelrKIRGREIQMIFQDPMTSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 NPLHTMAAHAKET----CLASGKPADdATLIAALEAVGLENAARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPT 168
Cdd:COG0444 100 NPVMTVGDQIAEPlrihGGLSKAEAR-ERAIELLERVGLPDPERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPT 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 169 TDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSA 243
Cdd:COG0444 179 TALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENPRHPYTRALLSS 253
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-243 |
2.03e-81 |
|
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: 253.45 E-value: 2.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGAILADGQPI---SP---CKLRGIKVATIMQNPR 89
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLlglSErelRRIRGNRIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 90 SAFNPLHT--------MAAHAKetclASGKPADDATlIAALEAVGLENAARVLKLYPFEMSGGMLQRMMIAMALLCDAPF 161
Cdd:COG4172 103 TSLNPLHTigkqiaevLRLHRG----LSGAAARARA-LELLERVGIPDPERRLDAYPHQLSGGQRQRVMIAMALANEPDL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 162 IIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLV 241
Cdd:COG4172 178 LIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTRKLL 257
|
..
gi 501085142 242 SA 243
Cdd:COG4172 258 AA 259
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
16-223 |
1.17e-73 |
|
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: 223.92 E-value: 1.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGAILADGQPISP-----CKLRGIKVATIMQNPRS 90
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL----KPTSGSIIFDGKDLLKlsrrlRKIRRKEIQMVFQDPMS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 91 AFNPLHTMAAHAKETCLASGKPADDATL--IAALEAVGLENAARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPT 168
Cdd:cd03257 94 SLNPRMTIGEQIAEPLRIHGKLSKKEARkeAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 169 TDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELG 223
Cdd:cd03257 174 SALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-247 |
6.95e-69 |
|
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: 212.36 E-value: 6.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVL-----QADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGAILADGQPISPCKLRGI 79
Cdd:COG1124 2 LEVRNLSVsygqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGL----ERPWSGEVTFDGRPVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 --KVATIMQNPRSAFNPLHTMAAHAKETCLASGKPADDATLIAALEAVGLenAARVLKLYPFEMSGGMLQRMMIAMALLC 157
Cdd:COG1124 78 rrRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGL--PPSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 158 DAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVT 237
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYT 235
|
250
....*....|
gi 501085142 238 RNLVSAHLAL 247
Cdd:COG1124 236 RELLAASLAF 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
5.70e-68 |
|
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: 218.23 E-value: 5.70e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 1 MPQQIELQNIVLQ---ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGVRqTAGAILADGQPI--SPCK 75
Cdd:COG1123 1 MTPLLEVRDLSVRypgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGR-ISGEVLLDGRDLleLSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 76 LRGIKVATIMQNPRSAFNPLhTMAAHAKETCLASGKPADDAT--LIAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIAM 153
Cdd:COG1123 80 LRGRRIGMVFQDPMTQLNPV-TVGDQIAEALENLGLSRAEARarVLELLEAVGLE---RRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 154 ALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQ 233
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
15-243 |
6.39e-66 |
|
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: 212.84 E-value: 6.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPCKLRGIK-----VATIMQNPR 89
Cdd:COG1123 277 GVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP----TSGSILFDGKDLTKLSRRSLRelrrrVQMVFQDPY 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 90 SAFNPLHTMAAHAKETCLASG---KPADDATLIAALEAVGLEnaARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADE 166
Cdd:COG1123 353 SSLNPRMTVGDIIAEPLRLHGllsRAERRERVAELLERVGLP--PDLADRYPHELSGGQRQRVAIARALALEPKLLILDE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501085142 167 PTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSA 243
Cdd:COG1123 431 PTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAA 507
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-243 |
6.35e-59 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 194.92 E-value: 6.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 13 QADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPA-GVRQTAGAILADGQPI---SPCKLRGI---KVATIM 85
Cdd:PRK15134 19 QTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSpPVVYPSGDIRFHGESLlhaSEQTLRGVrgnKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 86 QNPRSAFNPLHTMAAHAKET-CLASG--KPADDATLIAALEAVGLENAARVLKLYPFEMSGGMLQRMMIAMALLCDAPFI 162
Cdd:PRK15134 99 QEPMVSLNPLHTLEKQLYEVlSLHRGmrREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 163 IADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVS 242
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLN 258
|
.
gi 501085142 243 A 243
Cdd:PRK15134 259 S 259
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-243 |
9.39e-51 |
|
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: 173.33 E-value: 9.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtaGAILADGQPI---SPCKLRGI--KVATIMQNPRSAFN 93
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-----GEIRFDGQDLdglSRRALRPLrrRMQVVFQDPFGSLS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 PLHT--------MAAHAKETclasGKPADDATLIAALEAVGLENAARvlKLYPFEMSGGMLQRMMIAMALLCDAPFIIAD 165
Cdd:COG4172 377 PRMTvgqiiaegLRVHGPGL----SAAERRARVAEALEEVGLDPAAR--HRYPHEFSGGQRQRIAIARALILEPKLLVLD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501085142 166 EPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSA 243
Cdd:COG4172 451 EPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAA 528
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-243 |
5.21e-49 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 164.13 E-value: 5.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPI---SPCKLRGI--KVATIMQNPRSAFN 93
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEP----TSGEILFDGQDItglSGRELRPLrrRMQMVFQDPYASLN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 PLHT--------MAAHAketcLASGKPADDATLiAALEAVGL--ENAARvlklYPFEMSGGMLQRMMIAMALLCDAPFII 163
Cdd:COG4608 110 PRMTvgdiiaepLRIHG----LASKAERRERVA-ELLELVGLrpEHADR----YPHEFSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 164 ADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSA 243
Cdd:COG4608 181 CDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQALLSA 260
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-243 |
4.81e-48 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 161.82 E-value: 4.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGVRqTAGAILADGQPI------SPCKLRGIKVATIMQNPRSAF 92
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGR-IGGSATFNGREIlnlpekELNKLRAEQISMIFQDPMTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 NPLHTMAAHAKETCL----ASGKPADDATlIAALEAVGLENAARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPT 168
Cdd:PRK09473 111 NPYMRVGEQLMEVLMlhkgMSKAEAFEES-VRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 169 TDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSA 243
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNA 264
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-243 |
4.51e-47 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 165.03 E-value: 4.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 1 MPQQIELQ----------NIVLQADR---PLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGAILAD 67
Cdd:PRK10261 1 MPHSDELDardvlavenlNIAFMQEQqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLL----EQAGGLVQCD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 68 G--------QPISPC--------KLRGIKVATIMQNPRSAFNPLHTMAAHAKETC-LASGKPADDATLIAA--LEAVGLE 128
Cdd:PRK10261 77 KmllrrrsrQVIELSeqsaaqmrHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIrLHQGASREEAMVEAKrmLDQVRIP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 129 NAARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLA 208
Cdd:PRK10261 157 EAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIA 236
|
250 260 270
....*....|....*....|....*....|....*
gi 501085142 209 DDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSA 243
Cdd:PRK10261 237 DRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAA 271
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-243 |
1.00e-43 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 150.28 E-value: 1.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGAILADG---QPISPC---KLRGIKVATIMQNPRSAF 92
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGqdlQRISEKerrNLVGAEVAMIFQDPMTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 NPLHTMA---AHAKETCLASGKPADDATLIAALEAVGLENAARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTT 169
Cdd:PRK11022 103 NPCYTVGfqiMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501085142 170 DLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSA 243
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRA 256
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-230 |
2.14e-38 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 133.61 E-value: 2.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVL--QADRPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAAL-GILPAgvrqTAGAILADGQPISPCKLRGI-- 79
Cdd:COG1122 1 IELENLSFsyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKS-TLLRLLnGLLKP----TSGEVLVDGKDITKKNLRELrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 KVATIMQNPRS-----------AFNPLHtmaahaketclaSGKPADDATLIA--ALEAVGLENaarVLKLYPFEMSGGML 146
Cdd:COG1122 76 KVGLVFQNPDDqlfaptveedvAFGPEN------------LGLPREEIRERVeeALELVGLEH---LADRPPHELSGGQK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 147 QRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESImRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVE 226
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
....
gi 501085142 227 TLFR 230
Cdd:COG1122 220 EVFS 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-228 |
3.71e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 133.27 E-value: 3.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPIS--PCKLRGiKV 81
Cdd:COG1131 1 IEVRGLTKRyGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRP----TSGEVRVLGEDVArdPAEVRR-RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 82 ATIMQNPrsAFNPLHTMAAHAKETCLASGKPADDATLIAA--LEAVGLENAARVLklyPFEMSGGMLQRMMIAMALLCDA 159
Cdd:COG1131 76 GYVPQEP--ALYPDLTVRENLRFFARLYGLPRKEARERIDelLELFGLTDAADRK---VGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501085142 160 PFIIADEPTTDLDVVAQARILDLLESImrsRAPGM--LLVTHDMGVVARLADDVAVMDNGKIVELGDVETL 228
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLREL---AAEGKtvLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-242 |
3.75e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 135.98 E-value: 3.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIV---LQADRPL--VHGVSLALRRGRVLALVGGSGSGKS--LTCAAALgilpagVRQTAGAILADGQPI---SPC 74
Cdd:COG1135 2 IELENLSktfPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKStlIRCINLL------ERPTSGSVLVDGVDLtalSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 75 KLRGI--KVATIMQNprsaFNPLH--TMA---AHAKEtclASGKPADDatlIAA-----LEAVGLENAARVlklYPFEMS 142
Cdd:COG1135 76 ELRAArrKIGMIFQH----FNLLSsrTVAenvALPLE---IAGVPKAE---IRKrvaelLELVGLSDKADA---YPSQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 143 GGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVEL 222
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
|
250 260
....*....|....*....|
gi 501085142 223 GDVETLFRTPQHSVTRNLVS 242
Cdd:COG1135 223 GPVLDVFANPQSELTRRFLP 242
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-243 |
4.49e-38 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 135.48 E-value: 4.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGAILADGQ-----PISPCKLRGIKVATIMQNPRSAFN 93
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKS-TLARLLTMIET---PTGGELYYQGQdllkaDPEAQKLLRQKIQIVFQNPYGSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 PLHTMAAHAKE-----TCLasGKPADDATLIAALEAVGL--ENAARvlklYPFEMSGGMLQRMMIAMALLCDAPFIIADE 166
Cdd:PRK11308 107 PRKKVGQILEEpllinTSL--SAAERREKALAMMAKVGLrpEHYDR----YPHMFSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501085142 167 PTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSA 243
Cdd:PRK11308 181 PVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSA 257
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-251 |
9.17e-38 |
|
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: 132.86 E-value: 9.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKS--LTCAAalGILPAgvrqTAGAILADGQPISPCKLRGI-- 79
Cdd:COG1120 2 LEAENLSVGyGGRPVLDDVSLSLPPGEVTALLGPNGSGKStlLRALA--GLLKP----SSGEVLLDGRDLASLSRRELar 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 KVATIMQNPRSAFnPLH-----TMAAHAKETCLASGKPADDATLIAALEAVGLEN-AARvlklyPF-EMSGGMLQRMMIA 152
Cdd:COG1120 76 RIAYVPQEPPAPF-GLTvrelvALGRYPHLGLFGRPSAEDREAVEEALERTGLEHlADR-----PVdELSGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 153 MALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGdvetlfrTP 232
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQG-------PP 222
|
250
....*....|....*....
gi 501085142 233 QHSVTRNLVSahlALYGME 251
Cdd:COG1120 223 EEVLTPELLE---EVYGVE 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-242 |
1.27e-37 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 138.30 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqtAGAILADGQPISPCKLRGI-----KVATIMQNPRSAFN 93
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-----QGEIWFDGQPLHNLNRRQLlpvrhRIQVVFQDPNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 PLHTMAAHAKETcLASGKP-----ADDATLIAALEAVGLENAARvlKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPT 168
Cdd:PRK15134 377 PRLNVLQIIEEG-LRVHQPtlsaaQREQQVIAVMEEVGLDPETR--HRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501085142 169 TDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVS 242
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-243 |
5.10e-37 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 132.72 E-value: 5.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGAILADGQ---PISPCKLRGI---KVATIMQNPRSAF 92
Cdd:COG4170 23 VDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIdllKLSPRERRKIigrEIAMIFQEPSSCL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 NPLHTMAAHAKETCLASG--------KPADDATLIAALEAVGLENAARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIA 164
Cdd:COG4170 103 DPSAKIGDQLIEAIPSWTfkgkwwqrFKWRKKRAIELLHRVGIKDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501085142 165 DEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSA 243
Cdd:COG4170 183 DEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKALLRS 261
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-233 |
1.31e-36 |
|
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: 129.24 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNI--VLQADRPLVH---GVSLALRRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGAILADGQPI---SPC 74
Cdd:cd03258 2 IELKNVskVFGDTGGKVTalkDVSLSVPKGEIFGIIGRSGAGKStlIRCINGLE------RPTSGSVLVDGTDLtllSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 75 KLRGI--KVATIMQNprsaFNPL--HTMA---AHAKEtcLASGKPADDATLIAA-LEAVGLENAArvlKLYPFEMSGGML 146
Cdd:cd03258 76 ELRKArrRIGMIFQH----FNLLssRTVFenvALPLE--IAGVPKAEIEERVLElLELVGLEDKA---DAYPAQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 147 QRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVE 226
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVE 226
|
....*..
gi 501085142 227 TLFRTPQ 233
Cdd:cd03258 227 EVFANPQ 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-218 |
8.30e-35 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 123.73 E-value: 8.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 6 ELQNIVLQ---ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPCKLRGI--K 80
Cdd:cd03225 1 ELKNLSFSypdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP----TSGEVLVDGKDLTKLSLKELrrK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 81 VATIMQNPRS-----------AFNPLHTMAAHAKetclasgkpaDDATLIAALEAVGLENaarVLKLYPFEMSGGMLQRM 149
Cdd:cd03225 77 VGLVFQNPDDqffgptveeevAFGLENLGLPEEE----------IEERVEEALELVGLEG---LRDRSPFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501085142 150 MIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESImRSRAPGMLLVTHDMGVVARLADDVAVMDNGK 218
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-233 |
8.57e-35 |
|
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: 124.54 E-value: 8.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKS--LTCAAALgilpagVRQTAGAILADGQPISPCKLRGIKV 81
Cdd:cd03261 1 IELRGLTKSfGGRTVLKGVDLDVRRGEILAIIGPSGSGKStlLRLIVGL------LRPDSGEVLIDGEDISGLSEAELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 82 A-----------------TIMQNprSAFnPLHTMAAHAKETClasgkpadDATLIAALEAVGLENAArvlKLYPFEMSGG 144
Cdd:cd03261 75 LrrrmgmlfqsgalfdslTVFEN--VAF-PLREHTRLSEEEI--------REIVLEKLEAVGLRGAE---DLYPAELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 145 MLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGD 224
Cdd:cd03261 141 MKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
....*....
gi 501085142 225 VETLFRTPQ 233
Cdd:cd03261 221 PEELRASDD 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-243 |
5.85e-34 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 124.82 E-value: 5.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPI---SPCKLRGIK--VATIMQNPRSAFN 93
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKA----TDGEVAWLGKDLlgmKDDEWRAVRsdIQMIFQDPLASLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 PLHTMAAHAKETcLASGKPADDATLI-----AALEAVGL-ENaarVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEP 167
Cdd:PRK15079 113 PRMTIGEIIAEP-LRTYHPKLSRQEVkdrvkAMMLKVGLlPN---LINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501085142 168 TTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSA 243
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSA 264
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-230 |
6.43e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.51 E-value: 6.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPCKLRgikVAT 83
Cdd:COG1121 7 IELENLTVSyGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP----TSGTVRLFGKPPRRARRR---IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 84 IMQnpRSAFNPlhTMAAHAKEtCLASG-----------KPADDATLIAALEAVGLENAARVlklyPF-EMSGGMLQRMMI 151
Cdd:COG1121 80 VPQ--RAEVDW--DFPITVRD-VVLMGrygrrglfrrpSRADREAVDEALERVGLEDLADR----PIgELSGGQQQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501085142 152 AMALLCDAPFIIADEPTTDLDVVAQARILDLLESiMRSRAPGMLLVTHDMGVVARLADDVAVMdNGKIVELGDVETLFR 230
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRE-LRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLT 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-232 |
1.04e-33 |
|
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: 122.01 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPCKLRGIKVA- 82
Cdd:COG1127 6 IEVRNLTKSfGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRP----DSGEILVDGQDITGLSEKELYELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 83 ----------------TIMQNprSAFnPL--HTmaahaketclasGKPADDATLIAA--LEAVGLENAArvlKLYPFEMS 142
Cdd:COG1127 82 rrigmlfqggalfdslTVFEN--VAF-PLreHT------------DLSEAEIRELVLekLELVGLPGAA---DKMPSELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 143 GGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVEL 222
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
250
....*....|
gi 501085142 223 GDVETLFRTP 232
Cdd:COG1127 224 GTPEELLASD 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-243 |
1.08e-33 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 128.05 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGAILADGQPI---SPCKLRGIK--VATIMQNPRSAFN 93
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRL----VESQGGEIIFNGQRIdtlSPGKLQALRrdIQFIFQDPYASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 PLHTMAAHAKETCLASG-KPADDATLIAA--LEAVGL--ENAARvlklYPFEMSGGMLQRMMIAMALLCDAPFIIADEPT 168
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGlLPGKAAAARVAwlLERVGLlpEHAWR----YPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 169 TDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSA 243
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAA 566
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
17-245 |
1.55e-33 |
|
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: 122.22 E-value: 1.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 17 PLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGAILADGQPISPCKLRGIK-----VATIMQNPRSA 91
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGL----EKPAQGTVSFRGQDLYQLDRKQRRafrrdVQLVFQDSPSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 92 FNPLHTMAAHAKETC---LASGKPADDATLIAALEAVGLEnaARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPT 168
Cdd:TIGR02769 101 VNPRMTVRQIIGEPLrhlTSLDESEQKARIAELLDMVGLR--SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501085142 169 TDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFrTPQHSVTRNLVSAHL 245
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL-SFKHPAGRNLQSAVL 254
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-228 |
1.68e-33 |
|
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: 127.18 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 2 PQQIELQNIVLQAD--RPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAAL-GILPAgvrqTAGAILADGQP---ISPCK 75
Cdd:COG4988 334 PPSIELEDVSFSYPggRPALDGLSLTIPPGERVALVGPSGAGKS-TLLNLLlGFLPP----YSGSILINGVDlsdLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 76 LRGiKVATIMQNPrsafnplHTMAAHAKETcLASGKP-ADDATLIAALEAVGL----------------ENAARVlklyp 138
Cdd:COG4988 409 WRR-QIAWVPQNP-------YLFAGTIREN-LRLGRPdASDEELEAALEAAGLdefvaalpdgldtplgEGGRGL----- 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 139 femSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARlADDVAVMDNGK 218
Cdd:COG4988 475 ---SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT--VILITHRLALLAQ-ADRILVLDDGR 548
|
250
....*....|
gi 501085142 219 IVELGDVETL 228
Cdd:COG4988 549 IVEQGTHEEL 558
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-169 |
2.24e-33 |
|
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: 118.13 E-value: 2.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPIS--PCKLRGIKVATIMQNPRsaFNPLH 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP----TEGTILLDGQDLTddERKSLRKEIGYVFQDPQ--LFPRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501085142 97 TMAAHAKE--TCLASGKPADDATLIAALEAVGLEN-AARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTT 169
Cdd:pfam00005 75 TVRENLRLglLLKGLSKREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-223 |
2.25e-33 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 119.08 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 6 ELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISpcKLRGIKVATI 84
Cdd:cd03214 1 EVENLSVGyGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKP----SSGEILLDGKDLA--SLSPKELARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 85 MqnprsafnplhtmaahaketclasgkpaddATLIAALEAVGLEN-AARVLKlypfEMSGGMLQRMMIAMALLCDAPFII 163
Cdd:cd03214 75 I------------------------------AYVPQALELLGLAHlADRPFN----ELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 164 ADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELG 223
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-219 |
2.92e-33 |
|
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: 118.65 E-value: 2.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGAILADGQPIS--PCKLRGiKV 81
Cdd:cd03230 1 IEVRNLSKRyGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLL----KPDSGEIKVLGKDIKkePEEVKR-RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 82 ATIMQNPRsafnplhtmaahaketclasgkPADDATliaaleavGLENaarvlklypFEMSGGMLQRMMIAMALLCDAPF 161
Cdd:cd03230 76 GYLPEEPS----------------------LYENLT--------VREN---------LKLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501085142 162 IIADEPTTDLDVVAQARILDLLESImRSRAPGMLLVTHDMGVVARLADDVAVMDNGKI 219
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-219 |
3.15e-33 |
|
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: 119.90 E-value: 3.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-----ADRPLVHGVSLALRRGRVLALVGGSGSGKSlTCaaaLGILpAGVRQ-TAGAILADGQPISPC---- 74
Cdd:cd03255 1 IELKNLSKTyggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TL---LNIL-GGLDRpTSGEVRVDGTDISKLseke 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 75 --KLRGIKVATIMQNprsaFNPLHTMAAhaKE----TCLASGKPADDATLIA--ALEAVGLENAarvLKLYPFEMSGGML 146
Cdd:cd03255 76 laAFRRRHIGFVFQS----FNLLPDLTA--LEnvelPLLLAGVPKKERRERAeeLLERVGLGDR---LNHYPSELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501085142 147 QRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMgVVARLADDVAVMDNGKI 219
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-245 |
1.35e-32 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 119.79 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGAILADGQPISPCKLRGIK-----VATIMQNPRSAF 92
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKS-----TLARLLVGLESpSQGNVSWRGEPLAKLNRAQRKafrrdIQMVFQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 NPLHTMAAHAKETC--LASGKPADDATLIAA-LEAVGLenAARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTT 169
Cdd:PRK10419 103 NPRKTVREIIREPLrhLLSLDKAERLARASEmLRAVDL--DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501085142 170 DLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVeTLFRTPQHSVTRNLVSAHL 245
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPV-GDKLTFSSPAGRVLQNAVL 255
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-221 |
9.14e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 116.30 E-value: 9.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 1 MPQQIELQNIVL-----QADRPLVHGVSLALRRGRVLALVGGSGSGKS--LTCAAALgilpagVRQTAGAILADGQPISP 73
Cdd:COG1136 1 MSPLLELRNLTKsygtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKStlLNILGGL------DRPTSGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 74 C------KLRGIKVATIMQNprsaFNPLHTMAAhaKE----TCLASGKPADDATLIA--ALEAVGLENaarVLKLYPFEM 141
Cdd:COG1136 75 LserelaRLRRRHIGFVFQF----FNLLPELTA--LEnvalPLLLAGVSRKERRERAreLLERVGLGD---RLDHRPSQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 142 SGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMgVVARLADDVAVMDNGKIVE 221
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-247 |
1.13e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 119.14 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVL---QADRPL--VHGVSLALRRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGAILADGQPI---SPC 74
Cdd:PRK11153 2 IELKNISKvfpQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKStlIRCINLLE------RPTSGRVLVDGQDLtalSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 75 KLRGI--KVATIMQNprsaFNPL--HTMA---AHAKEtclASGKPADDatlIAA-----LEAVGLENAARVlklYPFEMS 142
Cdd:PRK11153 76 ELRKArrQIGMIFQH----FNLLssRTVFdnvALPLE---LAGTPKAE---IKArvtelLELVGLSDKADR---YPAQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 143 GGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVEL 222
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQ 222
|
250 260
....*....|....*....|....*
gi 501085142 223 GDVETLFRTPQHSVTRNLVSAHLAL 247
Cdd:PRK11153 223 GTVSEVFSHPKHPLTREFIQSTLHL 247
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-247 |
7.10e-30 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 112.93 E-value: 7.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNI--VLQADRPL----VHGVSLALRRGRVLALVGGSGSGKSlTCAAALG--ILPagvrqTAGAILADGQPISPCK- 75
Cdd:TIGR04521 1 IKLKNVsyIYQPGTPFekkaLDDVSLTIEDGEFVAIIGHTGSGKS-TLIQHLNglLKP-----TSGTVTIDGRDITAKKk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 76 --LRGI--KVATIMQNPRS-----------AFNPLHTmaahaketclasGKPADDATLIA--ALEAVGLENAarVLKLYP 138
Cdd:TIGR04521 75 kkLKDLrkKVGLVFQFPEHqlfeetvykdiAFGPKNL------------GLSEEEAEERVkeALELVGLDEE--YLERSP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 139 FEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGK 218
Cdd:TIGR04521 141 FELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGK 220
|
250 260
....*....|....*....|....*....
gi 501085142 219 IVELGDVETLFRTPQHsvtrnLVSAHLAL 247
Cdd:TIGR04521 221 IVLDGTPREVFSDVDE-----LEKIGLDV 244
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-228 |
1.29e-29 |
|
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: 110.73 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKS--LTCAAALGILPAGVRqTAGAILADGQPI-----SPCKL 76
Cdd:cd03260 1 IELRDLNVYyGDKHALKDISLDIPKGEITALIGPSGCGKStlLRLLNRLNDLIPGAP-DEGEVLLDGKDIydldvDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 77 RgIKVATIMQNPrsafNPLHTMA----AHAKETCLASGKPADDATLIAALEAVGL-ENAARvlKLYPFEMSGGMLQRMMI 151
Cdd:cd03260 80 R-RRVGMVFQKP----NPFPGSIydnvAYGLRLHGIKLKEELDERVEEALRKAALwDEVKD--RLHALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501085142 152 AMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETL 228
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYT--IVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-228 |
4.78e-29 |
|
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: 114.93 E-value: 4.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ---ADRPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAALgilpAGVRQ-TAGAILADGQP---ISPCKLR 77
Cdd:COG2274 474 IELENVSFRypgDSPPVLDNISLTIKPGERVAIVGRSGSGKS-TLLKLL----LGLYEpTSGRILIDGIDlrqIDPASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 78 GiKVATIMQNPR----S-AFNplhtmaahaketcLASGKP-ADDATLIAALEAVGLENAARVLklyP--FEM-------- 141
Cdd:COG2274 549 R-QIGVVLQDVFlfsgTiREN-------------ITLGDPdATDEEIIEAARLAGLHDFIEAL---PmgYDTvvgeggsn 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 142 -SGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVaRLADDVAVMDNGKIV 220
Cdd:COG2274 612 lSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRT--VIIIAHRLSTI-RLADRIIVLDKGRIV 688
|
....*...
gi 501085142 221 ELGDVETL 228
Cdd:COG2274 689 EDGTHEEL 696
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
22-245 |
6.31e-29 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 109.92 E-value: 6.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 22 VSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGvRQTAGAILADGQPISPCKLRGIKVATIM--------QNPRSAFN 93
Cdd:TIGR02323 22 VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPD-HGTATYIMRSGAELELYQLSEAERRRLMrtewgfvhQNPRDGLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 PLHTMAAHAKETCLASGKPADD---ATLIAALEAVGLEnAARVLKLyPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTD 170
Cdd:TIGR02323 101 MRVSAGANIGERLMAIGARHYGnirATAQDWLEEVEID-PTRIDDL-PRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 171 LDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSAHL 245
Cdd:TIGR02323 179 LDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSSIL 253
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-219 |
1.15e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 107.98 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQAD-RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGAILADGQPIS---PCKLRGiK 80
Cdd:COG4619 1 LELEGLSFRVGgKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDP----PTSGEIYLDGKPLSampPPEWRR-Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 81 VATIMQNPRSAFNplhTMAAHAKETCLASGKPADDATLIAALEAVGLENAA---RVLKLypfemSGGMLQRMMIAMALLC 157
Cdd:COG4619 76 VAYVPQEPALWGG---TVRDNLPFPFQLRERKFDRERALELLERLGLPPDIldkPVERL-----SGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501085142 158 DAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKI 219
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-226 |
2.03e-28 |
|
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: 107.56 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVL-----QADRPLVHGVSLALRRGRVLALVGGSGSGKSlTcaaALGILpAG-VRQTAGAILADGQPISPcklRG 78
Cdd:cd03293 1 LEVRNVSKtygggGGAVTALEDISLSVEEGEFVALVGPSGCGKS-T---LLRII-AGlERPTSGEVLVDGEPVTG---PG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 79 IKVATIMQNP-----RSAFN----PLhtmaahaketcLASGKPADDATLIA--ALEAVGLENAArvlKLYPFEMSGGMLQ 147
Cdd:cd03293 73 PDRGYVFQQDallpwLTVLDnvalGL-----------ELQGVPKAEARERAeeLLELVGLSGFE---NAYPHQLSGGMRQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 148 RMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDN--GKIVELGDV 225
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVEV 218
|
.
gi 501085142 226 E 226
Cdd:cd03293 219 D 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-219 |
3.07e-28 |
|
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: 106.85 E-value: 3.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGAILADGQPISPCKLRgikVATIMQN------- 87
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK----PTSGSIRVFGKPLEKERKR---IGYVPQRrsidrdf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 88 PRSAFNpLHTMAAHAKETCLASGKPADDATLIAALEAVGLENaarvLKLYPF-EMSGGMLQRMMIAMALLCDAPFIIADE 166
Cdd:cd03235 84 PISVRD-VVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSE----LADRQIgELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501085142 167 PTTDLDVVAQARILDLLESiMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKI 219
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRE-LRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-243 |
3.75e-28 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 109.51 E-value: 3.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGAILADG------QPISPCKLRGIKVATIMQNPRSAF 92
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDidllrlSPRERRKLVGHNVSMIFQEPQSCL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 NPLHTMAAHaketcLASGKPA-------------DDATLIAALEAVGLENAARVLKLYPFEMSGGMLQRMMIAMALLCDA 159
Cdd:PRK15093 103 DPSERVGRQ-----LMQNIPGwtykgrwwqrfgwRKRRAIELLHRVGIKDHKDAMRSFPYELTEGECQKVMIAIALANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 160 PFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRN 239
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQA 257
|
....
gi 501085142 240 LVSA 243
Cdd:PRK15093 258 LIRA 261
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-221 |
4.02e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 107.87 E-value: 4.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 1 MPQQIELQNIVL-----QADRPLVHGVSLALRRGRVLALVGGSGSGKS--LTCAAalGILPAgvrqTAGAILADGQPISP 73
Cdd:COG1116 4 AAPALELRGVSKrfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKStlLRLIA--GLEKP----TSGEVLVDGKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 74 cklRGIKVATIMQNP-----RSAF-N---PLHtmaahaketclASGKPADDATLIA--ALEAVGLENAArvlKLYPFEMS 142
Cdd:COG1116 78 ---PGPDRGVVFQEPallpwLTVLdNvalGLE-----------LRGVPKAERRERAreLLELVGLAGFE---DAYPHQLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 143 GGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDN--GKIV 220
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
.
gi 501085142 221 E 221
Cdd:COG1116 221 E 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-232 |
1.22e-27 |
|
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: 106.23 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNI--VLQADRPLVHGVSLALRRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGAILADGQPIS---PCKLR-G 78
Cdd:cd03295 1 IEFENVtkRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTT----MKMINRLIEPTSGEIFIDGEDIReqdPVELRrK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 79 IKVA----------TIMQN----PRSAFNPLHTMAAHAKEtclasgkpaddatliaALEAVGLEnAARVLKLYPFEMSGG 144
Cdd:cd03295 77 IGYViqqiglfphmTVEENialvPKLLKWPKEKIRERADE----------------LLALVGLD-PAEFADRYPHELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 145 MLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGD 224
Cdd:cd03295 140 QQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
....*...
gi 501085142 225 VETLFRTP 232
Cdd:cd03295 220 PDEILRSP 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-221 |
1.68e-27 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 105.21 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ---ADRPLV--HGVSLALRRGRVLALVGGSGSGKS-LtcaaaLGILpAGV-RQTAGAILADGQPISP---- 73
Cdd:COG4181 9 IELRGLTKTvgtGAGELTilKGISLEVEAGESVAIVGASGSGKStL-----LGLL-AGLdRPTSGTVRLAGQDLFAlded 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 74 --CKLRGIKVATIMQNprsaFNPLHTMAAHakETC-----LASGKPADDATLiAALEAVGLenAARvLKLYPFEMSGGML 146
Cdd:COG4181 83 arARLRARHVGFVFQS----FQLLPTLTAL--ENVmlpleLAGRRDARARAR-ALLERVGL--GHR-LDHYPAQLSGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 147 QRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARlADDVAVMDNGKIVE 221
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
20-246 |
1.97e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 105.78 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 20 HGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQPISPCKLRGIKVAT-----------IMQNP 88
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKT----TLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAErrrllrtewgfVHQHP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 89 RSAFNPLHTMAAHAKETCLASGK---PADDATLIAALEAVGLEnAARVLKLyPFEMSGGMLQRMMIAMALLCDAPFIIAD 165
Cdd:PRK11701 99 RDGLRMQVSAGGNIGERLMAVGArhyGDIRATAGDWLERVEID-AARIDDL-PTTFSGGMQQRLQIARNLVTHPRLVFMD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 166 EPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSAHL 245
Cdd:PRK11701 177 EPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLLVSSVL 256
|
.
gi 501085142 246 A 246
Cdd:PRK11701 257 Q 257
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
20-221 |
2.10e-27 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 104.74 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 20 HGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQPISP------CKLRGIKVATIMQ--NPRSA 91
Cdd:TIGR02211 22 KGVSLSIGKGEIVAIVGSSGSGKS----TLLHLLGGLDNPTSGEVLFNGQSLSKlssnerAKLRNKKLGFIYQfhHLLPD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 92 FNPLHTMAAHAketcLASGKPADDATLIAA--LEAVGLENAarvLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTT 169
Cdd:TIGR02211 98 FTALENVAMPL----LIGKKSVKEAKERAYemLEKVGLEHR---INHRPSELSGGERQRVAIARALVNQPSLVLADEPTG 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501085142 170 DLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLaDDVAVMDNGKIVE 221
Cdd:TIGR02211 171 NLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
15-234 |
2.51e-27 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 104.51 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGAILADGQPI-SPCKLRGIKVATIMQNprSAFN 93
Cdd:cd03263 14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTT----LKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYCPQF--DALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 PLHTMAAHAKETCLASGKPADDATLIAaleavglENAARVLKLYPF------EMSGGMLQRMMIAMALLCDAPFIIADEP 167
Cdd:cd03263 88 DELTVREHLRFYARLKGLPKSEIKEEV-------ELLLRVLGLTDKankrarTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501085142 168 TTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARLADDVAVMDNGKIVELGdvetlfrTPQH 234
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRS--IILTTHSMDEAEALCDRIAIMSDGKLRCIG-------SPQE 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-234 |
2.90e-27 |
|
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: 109.47 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVL---QADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPI---SPCKLRG 78
Cdd:COG4987 334 LELEDVSFrypGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP----QSGSITLGGVDLrdlDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 79 iKVATIMQNPrsafnplHTMAAHAKETcLASGKP-ADDATLIAALEAVGL----------------ENAARVlklypfem 141
Cdd:COG4987 410 -RIAVVPQRP-------HLFDTTLREN-LRLARPdATDEELWAALERVGLgdwlaalpdgldtwlgEGGRRL-------- 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 142 SGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMgVVARLADDVAVMDNGKIVE 221
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRT--VLLITHRL-AGLERMDRILVLEDGRIVE 549
|
250
....*....|...
gi 501085142 222 LGDVETLFRTPQH 234
Cdd:COG4987 550 QGTHEELLAQNGR 562
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-218 |
1.09e-26 |
|
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: 101.17 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPCKLRGIK--VATIMQnprsaf 92
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP----TSGEILIDGKDIAKLPLEELRrrIGYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 nplhtmaahaketclasgkpaddatliaaleavglenaarvlklypfeMSGGMLQRMMIAMALLCDAPFIIADEPTTDLD 172
Cdd:cd00267 81 ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501085142 173 VVAQARILDLLESIMRSRAPgMLLVTHDMGVVARLADDVAVMDNGK 218
Cdd:cd00267 113 PASRERLLELLRELAEEGRT-VIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-218 |
1.50e-26 |
|
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: 101.49 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIV-LQADRPLVHGVSLALRRGRVLALVGGSGSGKS--LTCAAALgilpagVRQTAGAILADGQPISP----CKLR 77
Cdd:cd03229 1 LELKNVSkRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKStlLRCIAGL------EEPDSGSILIDGEDLTDledeLPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 78 GIKVATIMQnprsafnplhtmaahaketclasgkpadDATLIAALEAvgLENAARVLklypfemSGGMLQRMMIAMALLC 157
Cdd:cd03229 75 RRRIGMVFQ----------------------------DFALFPHLTV--LENIALGL-------SGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501085142 158 DAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGK 218
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-223 |
1.72e-26 |
|
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: 102.21 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNI-VLQADRPLVHGVSLALRRGRVLALVGGSGSGKS--LTCAAALgilpagVRQTAGAILADGQPIS--PCKLRGI 79
Cdd:cd03259 1 LELKGLsKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTtlLRLIAGL------ERPDSGEILIDGRDVTgvPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 kvATIMQNPRSafnpLHTMAAhAKETCLA---SGKPADDAT--LIAALEAVGLENaarVLKLYPFEMSGGMLQRMMIAMA 154
Cdd:cd03259 75 --GMVFQDYAL----FPHLTV-AENIAFGlklRGVPKAEIRarVRELLELVGLEG---LLNRYPHELSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501085142 155 LLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELG 223
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-218 |
2.23e-26 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 100.54 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ---ADRPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAAL-GILPAgvrqTAGAILADGQPISPCKLRGI- 79
Cdd:cd03228 1 IEFKNVSFSypgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKS-TLLKLLlRLYDP----TSGEILIDGVDLRDLDLESLr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 -KVATIMQNPRsafnplhtmaahaketcLASGkpaddaTLiaaleavgLENaarVLklypfemSGGMLQRMMIAMALLCD 158
Cdd:cd03228 76 kNIAYVPQDPF-----------------LFSG------TI--------REN---IL-------SGGQRQRIAIARALLRD 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 159 APFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVaRLADDVAVMDNGK 218
Cdd:cd03228 115 PPILILDEATSALDPETEALILEALRALAKGKT--VIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-245 |
3.26e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.52 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAALGIL--PAGVRQTAGAILADG-QPISPCK----- 75
Cdd:PRK11264 4 IEVKNLVKKfHGQTVLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLeqPEAGTIRVGDITIDTaRSLSQQKglirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 76 LRGiKVATIMQNprsaFN--PLHTMAAHAKE-TCLASGKPADDAT-----LIAALEAVGLENAarvlklYPFEMSGGMLQ 147
Cdd:PRK11264 83 LRQ-HVGFVFQN----FNlfPHRTVLENIIEgPVIVKGEPKEEATarareLLAKVGLAGKETS------YPRRLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 148 RMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPgMLLVTHDMGVVARLADDVAVMDNGKIVELGDVET 227
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
250
....*....|....*...
gi 501085142 228 LFRTPQHSVTRNLVSAHL 245
Cdd:PRK11264 231 LFADPQQPRTRQFLEKFL 248
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-220 |
5.50e-25 |
|
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: 98.79 E-value: 5.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ--ADRPLVHGVSLALRRGRVLALVGGSGSGKS--LTCAAALgilpagVRQTAGAILADGQPI---SPCKLR 77
Cdd:cd03256 1 IEVENLSKTypNGKKALKDVSLSINPGEFVALIGPSGAGKStlLRCLNGL------VEPTSGSVLIDGTDInklKGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 78 GI--KVATIMQNPR-----SAF-NPLHTMAA--HAKETCLASGKPADDATLIAALEAVGLENAA--RVLKLypfemSGGM 145
Cdd:cd03256 75 QLrrQIGMIFQQFNlierlSVLeNVLSGRLGrrSTWRSLFGLFPKEEKQRALAALERVGLLDKAyqRADQL-----SGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 146 LQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIV 220
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-228 |
5.63e-25 |
|
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: 99.16 E-value: 5.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTcaaaLGILpAGV-RQTAGAILADGQPI--SPCKLRGiK 80
Cdd:COG4555 2 IEVENLSKKyGKVPALKDVSFTAKDGEITGLLGPNGAGKTTL----LRML-AGLlKPDSGSILIDGEDVrkEPREARR-Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 81 VATIMQNprsafNPLH---TMAAHAKETCLASGKPADDATLIAA--LEAVGLENaarVLKLYPFEMSGGMLQRMMIAMAL 155
Cdd:COG4555 76 IGVLPDE-----RGLYdrlTVRENIRYFAELYGLFDEELKKRIEelIELLGLEE---FLDRRVGELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501085142 156 LCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETL 228
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-221 |
9.66e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 97.82 E-value: 9.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVL--QADRPLVHGVSLALRRGRVLALVGGSGSGKSlTCaaaLGILPAGVRQTAGAILADGQPISPCKLRGI--- 79
Cdd:COG2884 2 IRFENVSKryPGGREALSDVSLEIEKGEFVFLTGPSGAGKS-TL---LKLLYGEERPTSGQVLVNGQDLSRLKRREIpyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 --KVATIMQ-----NPRSAF-N---PLHtmaahaketclASGKPADDA--TLIAALEAVGLENAArvlKLYPFEMSGGML 146
Cdd:COG2884 78 rrRIGVVFQdfrllPDRTVYeNvalPLR-----------VTGKSRKEIrrRVREVLDLVGLSDKA---KALPHELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501085142 147 QRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSrapGM--LLVTHDMGVVARLADDVAVMDNGKIVE 221
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR---GTtvLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-219 |
1.24e-24 |
|
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: 97.22 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKS--LTCAAALgilpagVRQTAGAILADGQPISPCK-----L 76
Cdd:cd03262 1 IEIKNLHKSfGDFHVLKGIDLTVKKGEVVVIIGPSGSGKStlLRCINLL------EEPDSGTIIIDGLKLTDDKknineL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 77 RgIKVATIMQNprsaFNplhtMAAH--AKETCL-----ASGKPADDATLIA--ALEAVGLENAARVlklYPFEMSGGMLQ 147
Cdd:cd03262 75 R-QKVGMVFQQ----FN----LFPHltVLENITlapikVKGMSKAEAEERAleLLEKVGLADKADA---YPAQLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501085142 148 RMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSrapG--MLLVTHDMGVVARLADDVAVMDNGKI 219
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE---GmtMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-244 |
1.51e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 98.32 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSlTCAAalgILPAGVRQTAGAILADGQPIS--PCKLRGIKVATIMQNPRSAFNPLH 96
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKS-TLAK---MLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDPSTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 97 TMAAHAK-----ETCLASgkPADDATLIAALEAVGL--ENAArvlkLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTT 169
Cdd:PRK15112 105 RISQILDfplrlNTDLEP--EQREKQIIETLRQVGLlpDHAS----YYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 170 DLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSAH 244
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAGH 253
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-233 |
2.05e-24 |
|
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: 97.41 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPCKLRGIKVATI 84
Cdd:cd03299 1 LKVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKP----DSGKILLNGKDITNLPPEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 85 MQNprsafnplHTMAAHAK-ETCLASG-------KPADDATLIAALEAVGLENaarVLKLYPFEMSGGMLQRMMIAMALL 156
Cdd:cd03299 77 PQN--------YALFPHMTvYKNIAYGlkkrkvdKKEIERKVLEIAEMLGIDH---LLNRKPETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501085142 157 CDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQ 233
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-228 |
5.30e-24 |
|
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: 96.15 E-value: 5.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ---ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAaalgILPAGVRQTAGAILADGQPISPCKLRGI-- 79
Cdd:cd03251 1 VEFKNVTFRypgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVN----LIPRFYDVDSGRILIDGHDVRDYTLASLrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 KVATIMQNPrSAFNplHTMAAHaketcLASGKP-ADDATLIAALEAVGLEN-------------AARVLKLypfemSGGM 145
Cdd:cd03251 77 QIGLVSQDV-FLFN--DTVAEN-----IAYGRPgATREEVEEAARAANAHEfimelpegydtviGERGVKL-----SGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 146 LQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARlADDVAVMDNGKIVELGDV 225
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRT--TFVIAHRLSTIEN-ADRIVVLEDGKIVERGTH 220
|
...
gi 501085142 226 ETL 228
Cdd:cd03251 221 EEL 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-228 |
7.73e-24 |
|
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: 95.51 E-value: 7.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPIS--PCKLRgiKV 81
Cdd:cd03265 1 IEVENLVKKyGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKP----TSGRATVAGHDVVrePREVR--RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 82 ATIMQNPRSAFNPL---HTMAAHAKetclASGKPADDATLIAA--LEAVGLENAA-RVLKLYpfemSGGMLQRMMIAMAL 155
Cdd:cd03265 75 IGIVFQDLSVDDELtgwENLYIHAR----LYGVPGAERRERIDelLDFVGLLEAAdRLVKTY----SGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501085142 156 LCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETL 228
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-233 |
1.53e-23 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 95.79 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKS--LTCAAALgILPagvrqTAGAILADGQPISPC------KLRGIKVATIMQNprS 90
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKStlLRCINRL-IEP-----TSGKVLIDGQDIAAMsrkelrELRRKKISMVFQS--F 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 91 AFNPLHTM---AAHAKETclaSGKPADD--ATLIAALEAVGLENAARVlklYPFEMSGGMLQRMMIAMALLCDAPFIIAD 165
Cdd:cd03294 112 ALLPHRTVlenVAFGLEV---QGVPRAEreERAAEALELVGLEGWEHK---YPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501085142 166 EPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQ 233
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPA 253
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-219 |
2.20e-23 |
|
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: 94.01 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ--ADRPLVHGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQPIspCKLRGIKVA 82
Cdd:cd03292 1 IEFINVTKTypNGTAALDGINISISAGEFVFLVGPSGAGKS----TLLKLIYKEELPTSGTIRVNGQDV--SDLRGRAIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 83 TIMQNPRSAFN-----PLHTMAAHAKETCLASGKPADDAT--LIAALEAVGLENAARVlklYPFEMSGGMLQRMMIAMAL 155
Cdd:cd03292 75 YLRRKIGVVFQdfrllPDRNVYENVAFALEVTGVPPREIRkrVPAALELVGLSHKHRA---LPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501085142 156 LCDAPFIIADEPTTDLDVVAQARILDLLESImRSRAPGMLLVTHDMGVVARLADDVAVMDNGKI 219
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-233 |
3.07e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.47 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 22 VSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQPISPCK-------LRGiKVATIMQNPRS---- 90
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKS----TLLQHLNGLLQPTSGTVTIGERVITAGKknkklkpLRK-KVGIVFQFPEHqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 91 -------AFNPLHTmaahaketclasGKPADDATLIA--ALEAVGLENAarVLKLYPFEMSGGMLQRMMIAMALLCDAPF 161
Cdd:PRK13634 101 etvekdiCFGPMNF------------GVSEEDAKQKAreMIELVGLPEE--LLARSPFELSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501085142 162 IIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQ 233
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-223 |
4.58e-23 |
|
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: 97.48 E-value: 4.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ---ADRPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAalgILPAGVRQTAGAILADGQPISPCKLRGIK- 80
Cdd:TIGR02203 331 VEFRNVTFRypgRDRPALDSISLVIEPGETVALVGRSGSGKS-TLVN---LIPRFYEPDSGQILLDGHDLADYTLASLRr 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 81 -VATIMQNPrSAFNplHTMAAHaketcLASGKP--ADDATLIAALEAVGL----------------ENAARvlklypfeM 141
Cdd:TIGR02203 407 qVALVSQDV-VLFN--DTIANN-----IAYGRTeqADRAEIERALAAAYAqdfvdklplgldtpigENGVL--------L 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 142 SGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARlADDVAVMDNGKIVE 221
Cdd:TIGR02203 471 SGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRT--TLVIAHRLSTIEK-ADRIVVMDDGRIVE 547
|
..
gi 501085142 222 LG 223
Cdd:TIGR02203 548 RG 549
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-228 |
6.90e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 97.16 E-value: 6.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPI---SPCKLRGiKVATIMQNP--- 88
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDP----TSGRILIDGVDIrdlTLESLRR-QIGVVPQDTflf 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 89 -RS-AFNplhtmaahaketcLASGKP-ADDATLIAALEAVGL----------------ENAARVlklypfemSGGMLQRM 149
Cdd:COG1132 427 sGTiREN-------------IRYGRPdATDEEVEEAAKAAQAhefiealpdgydtvvgERGVNL--------SGGQRQRI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 150 MIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHdmgvvaRL-----ADDVAVMDNGKIVELGD 224
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRT--TIVIAH------RLstirnADRILVLDDGRIVEQGT 557
|
....
gi 501085142 225 VETL 228
Cdd:COG1132 558 HEEL 561
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-220 |
3.51e-22 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 90.78 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 18 LVHGVSLALRRGRVLALVGGSGSGKSlTCAAAL-GILpagvRQTAGAILADGQPISPCKLRGiKVATIMQNPRSAFnplh 96
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKT-TLAKILaGLI----KESSGSILLNGKPIKAKERRK-SIGYVMQDVDYQL---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 97 tMAAHAKETCLASGKPADDatliaaleavGLENAARVLKLY---------PFEMSGGMLQRMMIAMALLCDAPFIIADEP 167
Cdd:cd03226 85 -FTDSVREELLLGLKELDA----------GNEQAETVLKDLdlyalkerhPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501085142 168 TTDLDVVAQARILDLLESImRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIV 220
Cdd:cd03226 154 TSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
21-223 |
3.65e-22 |
|
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: 90.72 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 21 GVSLALRRGrVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPI--SPCKLRGIkVATIMQNPRsaFNPLHTM 98
Cdd:cd03264 18 GVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPP----SSGTIRIDGQDVlkQPQKLRRR-IGYLPQEFG--VYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 99 AAHAKETCLASGKPAD--DATLIAALEAVGLENAArvlKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQ 176
Cdd:cd03264 90 REFLDYIAWLKGIPSKevKARVDEVLELVNLGDRA---KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEER 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 501085142 177 ARILDLLESIMRSRApgMLLVTHDMGVVARLADDVAVMDNGKIVELG 223
Cdd:cd03264 167 IRFRNLLSELGEDRI--VILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-226 |
5.15e-22 |
|
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: 90.96 E-value: 5.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSlTCAAAL-GILPAgvrqTAGAILADGQPI---SPCKLRGIKVATIMQNPRsafnP 94
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKT-TLFNLIsGFLRP----TSGSVLFDGEDItglPPHEIARLGIGRTFQIPR----L 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 95 LHTM--------AAHA--KETCLASGKPADDATLIA----ALEAVGLENAARVLklyPFEMSGGMLQRMMIAMALLCDAP 160
Cdd:cd03219 87 FPELtvlenvmvAAQArtGSGLLLARARREEREAREraeeLLERVGLADLADRP---AGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501085142 161 FIIADEPTTDLDVVAQARILDLLESImRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVE 226
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-247 |
6.73e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.76 E-value: 6.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGAILADGQPI-SPCK---LRGI--KVATIMQNPRSA- 91
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALL----KPTTGTVTVDDITItHKTKdkyIRPVrkRIGMVFQFPESQl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 92 ---------------FN-PLHTMAAHAKETCLASGKPADdatliaaleavglenaarVLKLYPFEMSGGMLQRMMIAMAL 155
Cdd:PRK13646 99 fedtvereiifgpknFKmNLDEVKNYAHRLLMDLGFSRD------------------VMSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 156 LCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTpqhs 235
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD---- 236
|
250
....*....|..
gi 501085142 236 vTRNLVSAHLAL 247
Cdd:PRK13646 237 -KKKLADWHIGL 247
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-245 |
7.77e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 90.74 E-value: 7.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 4 QIELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKS--LTCAAALGILPAGVRqTAGAILADGQPI--SPCKLRG 78
Cdd:PRK14247 3 KIEIRDLKVSfGQVEVLDGVNLEIPDNTITALMGPSGSGKStlLRVFNRLIELYPEAR-VSGEVYLDGQDIfkMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 79 IKVATIMQ--NPRSAFNPLHTMAAHAKETCLASGKPADDATLIAALEAVGL-ENAARVLKLYPFEMSGGMLQRMMIAMAL 155
Cdd:PRK14247 82 RRVQMVFQipNPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLwDEVKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 156 LCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHS 235
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMT--IVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHE 239
|
250
....*....|
gi 501085142 236 VTRNLVSAHL 245
Cdd:PRK14247 240 LTEKYVTGRL 249
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
19-226 |
8.59e-22 |
|
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: 90.87 E-value: 8.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSlTCAAAL-GILPAgvrqTAGAILADGQPISPCK-----LRGIkvATIMQNPRsaf 92
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKT-TLFNLItGFYRP----TSGRILFDGRDITGLPphriaRLGI--ARTFQNPR--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 nPLHTM--------AAHAK------ETCLASGKPADDATLI-----AALEAVGLENAARVLklyPFEMSGGMLQRMMIAM 153
Cdd:COG0411 90 -LFPELtvlenvlvAAHARlgrgllAALLRLPRARREEREAreraeELLERVGLADRADEP---AGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501085142 154 ALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVE 226
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-228 |
1.07e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.74 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVL---QADRPLVHGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQPI---SPCKLR- 77
Cdd:PRK11160 339 LTLNNVSFtypDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAWDPQQGEILLNGQPIadySEAALRq 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 78 GIKVATimQNPrsafnplHTMAAHAKETCLASGKPADDATLIAALEAVGLEN---AARVLKLYPFE----MSGGMLQRMM 150
Cdd:PRK11160 415 AISVVS--QRV-------HLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKlleDDKGLNAWLGEggrqLSGGEQRRLG 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501085142 151 IAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARLaDDVAVMDNGKIVELGDVETL 228
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKT--VLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQEL 560
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-224 |
1.15e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 90.82 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVL---QADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPCKLRGI-- 79
Cdd:PRK13632 8 IKVENVSFsypNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKP----QSGEIKIDGITISKENLKEIrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 KVATIMQNPRSAFnplhtMAAHAKETcLASG------KPADDATLIAAL-EAVGLENAarvLKLYPFEMSGGMLQRMMIA 152
Cdd:PRK13632 84 KIGIIFQNPDNQF-----IGATVEDD-IAFGlenkkvPPKKMKDIIDDLaKKVGMEDY---LDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501085142 153 MALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVArLADDVAVMDNGKIVELGD 224
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGK 225
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-228 |
1.41e-21 |
|
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: 89.98 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQAD--RPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAALgilpagVR---QTAGAILADGQPISPCKL--- 76
Cdd:cd03253 1 IEFENVTFAYDpgRPVLKDVSFTIPAGKKVAIVGPSGSGKS-TILRLL------FRfydVSSGSILIDGQDIREVTLdsl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 77 -RGIKV---------ATIMQNPRSAfNPLHTmaahaKETCLASGKPADDATLIAALE-----AVGlenaARVLKLypfem 141
Cdd:cd03253 74 rRAIGVvpqdtvlfnDTIGYNIRYG-RPDAT-----DEEVIEAAKAAQIHDKIMRFPdgydtIVG----ERGLKL----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 142 SGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARlADDVAVMDNGKIVE 221
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRT--TIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
....*..
gi 501085142 222 LGDVETL 228
Cdd:cd03253 216 RGTHEEL 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-230 |
1.42e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 90.84 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 1 MPQQIELQNIVLQ---ADRPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAAL-GILpagvRQTAGAILADGQPISPCKL 76
Cdd:PRK13635 2 KEEIIRVEHISFRypdAATYALKDVSFSVYEGEWVAIVGHNGSGKS-TLAKLLnGLL----LPEAGTITVGGMVLSEETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 77 RGI--KVATIMQNPRSAF--NPLHTMAAHAKETClasGKPADDAT--LIAALEAVGLENaarVLKLYPFEMSGGMLQRMM 150
Cdd:PRK13635 77 WDVrrQVGMVFQNPDNQFvgATVQDDVAFGLENI---GVPREEMVerVDQALRQVGMED---FLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 151 IAMALLCDAPFIIADEPTTDLDvvAQARIlDLLESIMRSRAPGMLLV---THDMGVVARlADDVAVMDNGKIVELGDVET 227
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLD--PRGRR-EVLETVRQLKEQKGITVlsiTHDLDEAAQ-ADRVIVMNKGEILEEGTPEE 226
|
...
gi 501085142 228 LFR 230
Cdd:PRK13635 227 IFK 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-232 |
1.98e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 89.38 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKS--LTCAAALGILpagvrqTAGAILADGQPI--SPCKLRGI 79
Cdd:PRK09493 2 IEFKNVSKHfGPTQVLHNIDLNIDQGEVVVIIGPSGSGKStlLRCINKLEEI------TSGDLIVDGLKVndPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 KVA--------------TIMQNprSAFNPLHTMAAhaketclasGKPADDATLIAALEAVGLENAArvlKLYPFEMSGGM 145
Cdd:PRK09493 76 RQEagmvfqqfylfphlTALEN--VMFGPLRVRGA---------SKEEAEKQARELLAKVGLAERA---HHYPSELSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 146 LQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILdlleSIMRSRAP---GMLLVTHDMGVVARLADDVAVMDNGKIVEL 222
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPELRHEVL----KVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
|
250
....*....|
gi 501085142 223 GDVETLFRTP 232
Cdd:PRK09493 218 GDPQVLIKNP 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-223 |
3.66e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.06 E-value: 3.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPI---SPCKLRGIK 80
Cdd:PRK13548 3 LEARNLSVRlGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSP----DSGEVRLNGRPLadwSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 81 vATIMQNPRSAFnPLH-----TMAAHAketcLASGKPADDATLIAALEAVGLENAARvlKLYPfEMSGGMLQRMMIAMAL 155
Cdd:PRK13548 79 -AVLPQHSSLSF-PFTveevvAMGRAP----HGLSRAEDDALVAAALAQVDLAHLAG--RDYP-QLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501085142 156 L---CDAPF---IIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELG 223
Cdd:PRK13548 150 AqlwEPDGPprwLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-223 |
5.15e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.56 E-value: 5.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQPISPCKLRGIK--VATIMQNPrSAFN 93
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKS----TLINLLQRVFDPQSGRILIDGTDIRTVTRASLRrnIAVVFQDA-GLFN 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 plhtmaaHAKETCLASGKP-ADDATLIAALE-AVGLENAARVLKLYPF-------EMSGGMLQRMMIAMALLCDAPFIIA 164
Cdd:PRK13657 423 -------RSIEDNIRVGRPdATDEEMRAAAErAQAHDFIERKPDGYDTvvgergrQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501085142 165 DEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVaRLADDVAVMDNGKIVELG 223
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELMKGRT--TFIIAHRLSTV-RNADRILVFDNGRVVESG 551
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-245 |
1.19e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.59 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 1 MPQQIELQNI-VLQADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAG-VRQTAGAILADGQPISPCKLRG 78
Cdd:PRK14267 1 MKFAIETVNLrVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeEARVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 79 I----KVATIMQ--NPRSAFNPLHTMAAHAKETCLASGKPADDATLIAALEAVGL-ENAARVLKLYPFEMSGGMLQRMMI 151
Cdd:PRK14267 81 IevrrEVGMVFQypNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALwDEVKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 152 AMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRT 231
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYT--IVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
250
....*....|....
gi 501085142 232 PQHSVTRNLVSAHL 245
Cdd:PRK14267 239 PEHELTEKYVTGAL 252
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-232 |
1.22e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.90 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPCKLRGI--KV 81
Cdd:PRK09536 4 IDVSDLSVEfGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTP----TAGTVLVAGDDVEALSARAAsrRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 82 ATIMQNPRSAFN----PLHTMAAHAKETCLASGKPADDATLIAALEAVGLEN-AARVLKlypfEMSGGMLQRMMIAMALL 156
Cdd:PRK09536 80 ASVPQDTSLSFEfdvrQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQfADRPVT----SLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501085142 157 CDAPFIIADEPTTDLDVVAQARILDLLESIMRSrAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTP 232
Cdd:PRK09536 156 QATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-232 |
1.42e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.12 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 23 SLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPIS--PCKLRgiKVATIMQNprsafnplHTMAA 100
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPP----DSGRILWNGQDLTalPPAER--PVSMLFQE--------NNLFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 101 H---AKETCLA---SGK--PADDATLIAALEAVGLENaarVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLD 172
Cdd:COG3840 85 HltvAQNIGLGlrpGLKltAEQRAQVEQALERVGLAG---LLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 173 VVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTP 232
Cdd:COG3840 162 PALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-241 |
2.29e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.99 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 4 QIELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKS--LTCAAALgilpagVRQTAGAILADGQPI---SPCKL- 76
Cdd:PRK11231 2 TLRTENLTVGyGTKRILNDLSLSLPTGKITALIGPNGCGKStlLKCFARL------LTPQSGTVFLGDKPIsmlSSRQLa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 77 -------------RGIKVATIMQNPRSAFNPLHtmaahaketclasGK--PADDATLIAALEAVGLEN-AARVLKlypfE 140
Cdd:PRK11231 76 rrlallpqhhltpEGITVRELVAYGRSPWLSLW-------------GRlsAEDNARVNQAMEQTRINHlADRRLT----D 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 141 MSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLEsIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIV 220
Cdd:PRK11231 139 LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR-ELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
250 260
....*....|....*....|.
gi 501085142 221 ELGdvetlfrTPQHSVTRNLV 241
Cdd:PRK11231 218 AQG-------TPEEVMTPGLL 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-214 |
3.37e-20 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 89.27 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPC--KLRGIKVATIMQNPrsafn 93
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDP----TEGSIAVNGVPLADAdaDSWRDQIAWVPQHP----- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 plHTMAAHAKETCLASGKPADDATLIAALEAVGLENAARVLKLY--------PFEMSGGMLQRMMIAMALLCDAPFIIAD 165
Cdd:TIGR02857 406 --FLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGldtpigegGAGLSGGQAQRLALARAFLRDAPLLLLD 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 501085142 166 EPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMgVVARLADDVAVM 214
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRALAQGRT--VLLVTHRL-ALAALADRIVVL 529
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-214 |
7.59e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.21 E-value: 7.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 14 ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGAILADGqpispcklrGIKVATIMQnpRSAFN 93
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL----RPTSGTVRRAG---------GARVAYVPQ--RSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 P--------LHTMAAHAKETCLASGKPADDATLIAALEAVGLEN-AARVLKlypfEMSGGMLQRMMIAMALLCDAPFIIA 164
Cdd:NF040873 68 DslpltvrdLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADlAGRQLG----ELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501085142 165 DEPTTDLDVVAQARILDLLESImRSRAPGMLLVTHDMGVVARlADDVAVM 214
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-235 |
8.86e-20 |
|
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: 84.98 E-value: 8.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTcaaaLGILpAGVRQ-TAGAILADGQPISPCKLRGIKVA 82
Cdd:cd03300 1 IELENVSKFyGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLI-AGFETpTSGEILLDGKDITNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 83 TIMQNprSAFNPLHTMAAHAKETCLASGKPADD--ATLIAALEAVGLENAARvlkLYPFEMSGGMLQRMMIAMALLCDAP 160
Cdd:cd03300 76 TVFQN--YALFPHLTVFENIAFGLRLKKLPKAEikERVAEALDLVQLEGYAN---RKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 161 FIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHS 235
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANR 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-233 |
1.01e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.51 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 21 GVSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGAILADGQPI-----SPCKLRGiKVATIMQNPRS----- 90
Cdd:PRK13639 20 GINFKAEKGEMVALLGPNGAGKSTLFLHFNGIL----KPTSGEVLIKGEPIkydkkSLLEVRK-TVGIVFQNPDDqlfap 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 91 ------AFNPLHTmaahaketclasGKPADDAT--LIAALEAVGLENAArvlKLYPFEMSGGMLQRMMIAMALLCDAPFI 162
Cdd:PRK13639 95 tveedvAFGPLNL------------GLSKEEVEkrVKEALKAVGMEGFE---NKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501085142 163 IADEPTTDLDVVAQARILDLLESIMRSrapGMLLV--THDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQ 233
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKE---GITIIisTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-215 |
1.18e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.48 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 18 LVHGVSLALRRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGAILADGQPISP------CKLRGIKVATIMQ--NPR 89
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKS-TLLHLLGGLDT---PTSGDVIFNGQPMSKlssaakAELRNQKLGFIYQfhHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 90 SAFNPLHTMAAhakeTCLASGKPADDATLIA--ALEAVGLENAArvlKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEP 167
Cdd:PRK11629 100 PDFTALENVAM----PLLIGKKKPAEINSRAleMLAAVGLEHRA---NHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 501085142 168 TTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMD 215
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRD 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-220 |
1.18e-19 |
|
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: 84.18 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ---ADRPLVHGVSLALRRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGAILADGQPIS---PCKLR 77
Cdd:cd03245 3 IEFRNVSFSypnQEIPALDNVSLTIRAGEKVAIIGRVGSGKS-----TLLKLLAGLYKpTSGSVLLDGTDIRqldPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 78 GiKVATIMQNPRSAFNPLhtmaahaKETcLASGKP-ADDATLIAALEAVGLENAARvlkLYP-----------FEMSGGM 145
Cdd:cd03245 78 R-NIGYVPQDVTLFYGTL-------RDN-ITLGAPlADDERILRAAELAGVTDFVN---KHPngldlqigergRGLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 146 LQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVArLADDVAVMDNGKIV 220
Cdd:cd03245 146 RQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKT--LIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-220 |
2.18e-19 |
|
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: 82.09 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 21 GVSLALRRGRVLALVGGSGSGKSLTCaaalGILpAGVRQ-TAGAILADGQPISPcklrgikvatimQNPRSAfnplhtma 99
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLM----KIL-SGLYKpDSGEILVDGKEVSF------------ASPRDA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 100 ahaketcLASGkpaddatlIAALeavglenaarvlklypFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARI 179
Cdd:cd03216 73 -------RRAG--------IAMV----------------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 501085142 180 LDLLESiMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIV 220
Cdd:cd03216 122 FKVIRR-LRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-219 |
3.75e-19 |
|
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: 81.88 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ---ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPCKLR--GI 79
Cdd:cd03246 1 LEVENVSFRypgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRP----TSGRVRLDGADISQWDPNelGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 KVATIMQNPRsafnplhtmaahaketcLASGKPADDAtliaaleavglenaarvlklypfeMSGGMLQRMMIAMALLCDA 159
Cdd:cd03246 77 HVGYLPQDDE-----------------LFSGSIAENI------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 160 PFIIADEPTTDLDVVAQARILDLLESiMRSRAPGMLLVTHDMGVVARlADDVAVMDNGKI 219
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAA-LKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-223 |
3.92e-19 |
|
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: 81.98 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQPIS--PCKLRGiKVATIMQNPrsaf 92
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKS----TLLQLLTGDLKPQQGEITLDGVPVSdlEKALSS-LISVLNQRP---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 nplHTMaahaketclasgkpadDATLiaaleavgLENAARVLklypfemSGGMLQRMMIAMALLCDAPFIIADEPTTDLD 172
Cdd:cd03247 85 ---YLF----------------DTTL--------RNNLGRRF-------SGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 501085142 173 VVAQARILDLLESIMRSRApgMLLVTHDMGVVARlADDVAVMDNGKIVELG 223
Cdd:cd03247 131 PITERQLLSLIFEVLKDKT--LIWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-246 |
5.22e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 83.55 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQAD-RPLVHGVSLALRRGRVLALVGGSGSGKS--LTCAAALGILPAGVRqTAGAILADGQPISP--CKLRGI 79
Cdd:PRK14258 8 IKVNNLSFYYDtQKILEGVSMEIYQSKVTAIIGPSGCGKStfLKCLNRMNELESEVR-VEGRVEFFNQNIYErrVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 KVATIMQNPRSAFNPLHTMAAHAKETCLASGKPA--DDATLIAALEAVGL-ENAARVLKLYPFEMSGGMLQRMMIAMALL 156
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKleIDDIVESALKDADLwDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 157 CDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDN-----GKIVELGDVETLFRT 231
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNS 246
|
250
....*....|....*
gi 501085142 232 PQHSVTRNLVSAHLA 246
Cdd:PRK14258 247 PHDSRTREYVLSRLG 261
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-240 |
5.39e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 85.08 E-value: 5.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADG---QPISPCKLRGI---KVATIMQNprSAF 92
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKS----TMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVrrkKIAMVFQS--FAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 NPLHTMAAHAKETCLASGKPADD--ATLIAALEAVGLENAARVlklYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTD 170
Cdd:PRK10070 118 MPHMTVLDNTAFGMELAGINAEErrEKALDALRQVGLENYAHS---YPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 171 LDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNL 240
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-243 |
6.57e-19 |
|
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: 82.59 E-value: 6.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVL----QADRPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAALgilpagvrQ-----TAGAILADGQPIS--- 72
Cdd:cd03249 1 IEFKNVSFrypsRPDVPILKGLSLTIPPGKTVALVGSSGCGKS-TVVSLL--------ErfydpTSGEILLDGVDIRdln 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 73 PCKLRGiKVATIMQNPrsafnplHTMAAHAKETcLASGKPadDATLIAALEAVGLENAARVLKLYP-----------FEM 141
Cdd:cd03249 72 LRWLRS-QIGLVSQEP-------VLFDGTIAEN-IRYGKP--DATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 142 SGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVaRLADDVAVMDNGKIVE 221
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRT--TIVIAHRLSTI-RNADLIAVLQNGQVVE 217
|
250 260
....*....|....*....|..
gi 501085142 222 LGDVETLFRtpQHSVTRNLVSA 243
Cdd:cd03249 218 QGTHDELMA--QKGVYAKLVKA 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-219 |
1.07e-18 |
|
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: 81.75 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAalgILPAGVRQTAGAILADGQPISPCKLRGI--KVATIMQNP---- 88
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKS-TVVA---LLENFYQPQGGQVLLDGKPISQYEHKYLhsKVSLVGQEPvlfa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 89 RS-AFNPLHTMAAHAKETCLASGKPADDATLIAALEA-----VGLENAarvlklypfEMSGGMLQRMMIAMALLCDAPFI 162
Cdd:cd03248 102 RSlQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASgydteVGEKGS---------QLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501085142 163 IADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARlADDVAVMDNGKI 219
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALYDWPERRT--VLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
19-232 |
2.53e-18 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 82.82 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPIS--PCKLRGIkvATIMQNprSAFNPLH 96
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPP----DSGKIYLDGKDITnlPPEKRGI--AYVYQN--YMLFPHK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 97 TMAAHaketcLASG----KPADDATLIAALEAVGLENAARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLD 172
Cdd:NF040840 88 TVFEN-----IAFGlklrKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 173 VVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTP 232
Cdd:NF040840 163 VQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRP 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-223 |
3.07e-18 |
|
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: 80.40 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPCKL------- 76
Cdd:cd03269 1 LEVENVTKRfGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILP----DSGEVLFDGKPLDIAARnrigylp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 77 --RGI----KVATIMQnprsAFNPLHTMaahaketclasgKPADDATLIAA-LEAVGLEN-AARVLKlypfEMSGGMLQR 148
Cdd:cd03269 77 eeRGLypkmKVIDQLV----YLAQLKGL------------KKEEARRRIDEwLERLELSEyANKRVE----ELSKGNQQK 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501085142 149 MMIAMALLCDAPFIIADEPTTDLDVVAQarilDLLESIMRS-RAPG--MLLVTHDMGVVARLADDVAVMDNGKIVELG 223
Cdd:cd03269 137 VQFIAAVIHDPELLILDEPFSGLDPVNV----ELLKDVIRElARAGktVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-230 |
3.44e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.70 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 4 QIELQNIVLQADRPL----VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGAI-LADGQPISPCKLRG 78
Cdd:PRK13643 3 KFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLL----QPTEGKVtVGDIVVSSTSKQKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 79 IK-----VATIMQNPRSAFnplhtmaahAKETCLAS--------GKPADDATLIAA--LEAVGLenAARVLKLYPFEMSG 143
Cdd:PRK13643 79 IKpvrkkVGVVFQFPESQL---------FEETVLKDvafgpqnfGIPKEKAEKIAAekLEMVGL--ADEFWEKSPFELSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 144 GMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSrAPGMLLVTHDMGVVARLADDVAVMDNGKIVELG 223
Cdd:PRK13643 148 GQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
....*..
gi 501085142 224 DVETLFR 230
Cdd:PRK13643 227 TPSDVFQ 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-229 |
4.05e-18 |
|
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: 80.35 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQAD--RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPCK---LRGi 79
Cdd:cd03254 3 IEFENVNFSYDekKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDP----QKGQILIDGIDIRDISrksLRS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 KVATIMQNPrsafnplHTMAAHAKETCLASGKPADDATLIAALEAVGLENAARVL-KLYPFEM-------SGGMLQRMMI 151
Cdd:cd03254 78 MIGVVLQDT-------FLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLpNGYDTVLgenggnlSQGERQLLAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501085142 152 AMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVaRLADDVAVMDNGKIVELGDVETLF 229
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRT--SIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDELL 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-232 |
4.66e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 80.51 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKS--LTCAAALgilpagVRQTAGAILADGQPISPCKLRGI-- 79
Cdd:COG4604 2 IEIKNVSKRyGGKVVLDDVSLTIPKGGITALIGPNGAGKStlLSMISRL------LPPDSGEVLVDGLDVATTPSRELak 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 KVATIMQNPrsAFNPLHTMA--------AHAKetclasGKP-ADDATLIA-ALEAVGLEN-AARVLKlypfEMSGGMLQR 148
Cdd:COG4604 76 RLAILRQEN--HINSRLTVRelvafgrfPYSK------GRLtAEDREIIDeAIAYLDLEDlADRYLD----ELSGGQRQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 149 MMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETL 228
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
....
gi 501085142 229 FRTP 232
Cdd:COG4604 224 ITPE 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-229 |
6.53e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.82 E-value: 6.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 23 SLALRRGRVLALVGGSGSGKSLTCAAALGILpagVRQTAGAILADGQ-PISPCKLRGIK-----VATIMQNPRS------ 90
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI---ISETGQTIVGDYAiPANLKKIKEVKrlrkeIGLVFQFPEYqlfqet 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 91 -----AFNPLHtmaahaketcLASGKPADDATLIAALEAVGLENaaRVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIAD 165
Cdd:PRK13645 108 iekdiAFGPVN----------LGENKQEAYKKVPELLKLVQLPE--DYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501085142 166 EPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLF 229
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-251 |
7.16e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.70 E-value: 7.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGAILADGQPISPCkLRGIKVATIMQNPRSAFN----- 93
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGF----VRLASGKISILGQPTRQA-LQKNLVAYVPQSEEVDWSfpvlv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 -PLHTMAAHAKETCLASGKPADDATLIAALEAVG-LENAARVLKlypfEMSGGMLQRMMIAMALLCDAPFIIADEPTTDL 171
Cdd:PRK15056 98 eDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDmVEFRHRQIG----ELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 172 DVVAQARILDLLESiMRSRAPGMLLVTHDMGVVARLAdDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSAHLALYGME 251
Cdd:PRK15056 174 DVKTEARIISLLRE-LRDEGKTMLVSTHNLGSVTEFC-DYTVMVKGTVLASGPTETTFTAENLELAFSGVLRHVALNGSE 251
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-228 |
7.67e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.20 E-value: 7.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 2 PQQIELQN-IVLQAD-RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPagvrqTAGAILADGQP---ISPCKL 76
Cdd:PRK11174 347 PVTIEAEDlEILSPDgKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-----YQGSLKINGIElreLDPESW 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 77 RGiKVATIMQNPrsafnplHTMAAHAKETCLASGKPADDATLIAALE-----------AVGL-----ENAARVlklypfe 140
Cdd:PRK11174 422 RK-HLSWVGQNP-------QLPHGTLRDNVLLGNPDASDEQLQQALEnawvseflpllPQGLdtpigDQAAGL------- 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 141 mSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHdmgvvaRLA-----DDVAVMD 215
Cdd:PRK11174 487 -SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQT--TLMVTH------QLEdlaqwDQIWVMQ 557
|
250
....*....|...
gi 501085142 216 NGKIVELGDVETL 228
Cdd:PRK11174 558 DGQIVQQGDYAEL 570
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
19-228 |
9.47e-18 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 80.51 E-value: 9.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGAILADGQPI--SPCKLR-GIKVATIMQNPRSAFNPL 95
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTT----IRMLTTLLRPTSGTARVAGYDVvrEPRKVRrSIGIVPQYASVDEDLTGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 96 HTMAAHAKetclASGKPADDATLIAA--LEAVGLENAARVLKLYpfeMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDV 173
Cdd:TIGR01188 85 ENLEMMGR----LYGLPKDEAEERAEelLELFELGEAADRPVGT---YSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 174 VAQARILDLLESiMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETL 228
Cdd:TIGR01188 158 RTRRAIWDYIRA-LKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-230 |
1.18e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 80.09 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 22 VSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPIS--PCKLRGI--KVATIMQNPRS------- 90
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKP----TSGKIIIDGVDITdkKVKLSDIrkKVGLVFQYPEYqlfeeti 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 91 ----AFNPLHtmaahaketcLASGKPADDATLIAALEAVGLENAARVLKlYPFEMSGGMLQRMMIAMALLCDAPFIIADE 166
Cdd:PRK13637 102 ekdiAFGPIN----------LGLSEEEIENRVKRAMNIVGLDYEDYKDK-SPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501085142 167 PTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFR 230
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-219 |
1.57e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 77.47 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPI---SPCKLRGIKVATIMQNPrsafnpl 95
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPP----ASGEITLDGKPVtrrSPRDAIRAGIAYVPEDR------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 96 htmaahaKETCLASGKPADDATLIAALeavglenaarvlklypfeMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVA 175
Cdd:cd03215 85 -------KREGLVLDLSVAENIALSSL------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 501085142 176 QARILDLLESiMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKI 219
Cdd:cd03215 140 KAEIYRLIRE-LADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-228 |
2.60e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.92 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVL----QADRPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGAILADGQPISP--CKLRG 78
Cdd:TIGR00958 479 IEFQDVSFsypnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKS-TVAALLQNL---YQPTGGQVLLDGVPLVQydHHYLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 79 IKVATIMQNPRsafnplhTMAAHAKETCLASGKPADDATLIAALEAVGLENAARVL-KLYPFE-------MSGGMLQRMM 150
Cdd:TIGR00958 555 RQVALVGQEPV-------LFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFpNGYDTEvgekgsqLSGGQKQRIA 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501085142 151 IAMALLCDAPFIIADEPTTDLDvvaqARILDLLESIMRSRAPGMLLVTHDMGVVARlADDVAVMDNGKIVELGDVETL 228
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-233 |
3.37e-17 |
|
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: 78.15 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQADR-PLVHGVSLALRRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGAILADGQPISPCKLRGIKVA 82
Cdd:cd03296 3 IEVRNVSKRFGDfVALDDVSLDIPSGELVALLGPSGSGKT-----TLLRLIAGLERpDSGTILFGGEDATDVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 83 TIMQNpRSAFNPL---HTMAAHAKETCLASGKPAD--DATLIAALEAVGLENAArvlKLYPFEMSGGMLQRMMIAMALLC 157
Cdd:cd03296 78 FVFQH-YALFRHMtvfDNVAFGLRVKPRSERPPEAeiRAKVHELLKLVQLDWLA---DRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 158 DAPFIIADEPTTDLDvvaqARILDLLESIMRSRAPGM----LLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQ 233
Cdd:cd03296 154 EPKVLLLDEPFGALD----AKVRKELRRWLRRLHDELhvttVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-233 |
3.87e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 78.69 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKSlTCAaalgilpagvRQTAGAILADGQPISPCKLRGI------------KVAT 83
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKS-TIS----------KLINGLLLPDDNPNSKITVDGItltaktvwdireKVGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 84 IMQNPRSAFnplhtmaahaketclASGKPADDAtliaaleAVGLENAA-----------RVL---------KLYPFEMSG 143
Cdd:PRK13640 89 VFQNPDNQF---------------VGATVGDDV-------AFGLENRAvprpemikivrDVLadvgmldyiDSEPANLSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 144 GMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGvVARLADDVAVMDNGKIVELG 223
Cdd:PRK13640 147 GQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQG 225
|
250
....*....|
gi 501085142 224 DVETLFRTPQ 233
Cdd:PRK13640 226 SPVEIFSKVE 235
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-247 |
4.79e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.31 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ--ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGAILADGQPISPCKLRGIK-- 80
Cdd:PRK13652 4 IETRDLCYSysGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL----KPTSGSVLIRGEPITKENIREVRkf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 81 VATIMQNPRSA-FNPLHTMAAHAKETCLASGKPADDATLIAALEAVGLENaarVLKLYPFEMSGGMLQRMMIAMALLCDA 159
Cdd:PRK13652 80 VGLVFQNPDDQiFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEE---LRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 160 PFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHsvtrn 239
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL----- 231
|
....*...
gi 501085142 240 LVSAHLAL 247
Cdd:PRK13652 232 LARVHLDL 239
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-231 |
4.84e-17 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 77.82 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKS-LtcaaaLGILPAGVRQTAGA---ILadGQPISPCKLRGI 79
Cdd:COG1119 4 LELRNVTVRrGGKTILDDISWTVKPGEHWAILGPNGAGKStL-----LSLITGDLPPTYGNdvrLF--GERRGGEDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 K-----VATIMQNprsAFNPLHTmaahAKETcLASGK-----------PADDATLIAALEAVGLEN-AARvlklyPF-EM 141
Cdd:COG1119 77 RkriglVSPALQL---RFPRDET----VLDV-VLSGFfdsiglyreptDEQRERARELLELLGLAHlADR-----PFgTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 142 SGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVE 221
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
250
....*....|
gi 501085142 222 LGDVETLFRT 231
Cdd:COG1119 224 AGPKEEVLTS 233
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-223 |
5.96e-17 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 77.02 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGAILADG-----QPISPCKLRGIKVATIMQNPR-SA- 91
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAGLLEPDAGFATVDGfdvvkEPAEARRRLGFVSDSTGLYDRlTAr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 92 -----FNPLHTMAAHAketclasgkpaddatLIAALEAVglenaARVLKLYPF------EMSGGMLQRMMIAMALLCDAP 160
Cdd:cd03266 97 enleyFAGLYGLKGDE---------------LTARLEEL-----ADRLGMEELldrrvgGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501085142 161 FIIADEPTTDLDVVAQARILDLLESiMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELG 223
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
16-220 |
8.28e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.84 E-value: 8.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGAILADGQPISPCKLRGI-----KVATIMQNPRS 90
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI----ERPSAGKIWFSGHDITRLKNREVpflrrQIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 91 AFNplHTMAAHAKETCLASGKPADDAT--LIAALEAVGLENAArvlKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPT 168
Cdd:PRK10908 91 LMD--RTVYDNVAIPLIIAGASGDDIRrrVSAALDKVGLLDKA---KNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501085142 169 TDLDVVAQARILDLLESIMRSRAPgMLLVTHDMGVVARLADDVAVMDNGKIV 220
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFNRVGVT-VLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-250 |
1.24e-16 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 78.23 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 31 VLALVGGSGSGKS--LTCAAALGILPAGVRQTAGAILADGQP---ISPCKLRgikVATIMQNPRsaFNPLHTMAA---HA 102
Cdd:TIGR02142 25 VTAIFGRSGSGKTtlIRLIAGLTRPDEGEIVLNGRTLFDSRKgifLPPEKRR---IGYVFQEAR--LFPHLSVRGnlrYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 103 KETCLASGKPADDATLIAALeavGLENaarVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDL 182
Cdd:TIGR02142 100 MKRARPSERRISFERVIELL---GIGH---LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501085142 183 LESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELG---------DVETLFRTPQHSVTRNLVSAHLALYGM 250
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGpiaevwaspDLPWLAREDQGSLIEGVVAEHDQHYGL 250
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-245 |
1.33e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.93 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 18 LVHGVSLALRRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGAILADGQPISPCKLRG--IKVA---------TI 84
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKStfLRCINFLE------KPSEGSIVVNGQTINLVRDKDgqLKVAdknqlrllrTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 85 MQNPRSAFNPLHTMAA-----HAKETCLASGKPADDATLIAALEAVGLENAARvlKLYPFEMSGGMLQRMMIAMALLCDA 159
Cdd:PRK10619 94 LTMVFQHFNLWSHMTVlenvmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ--GKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 160 PFIIADEPTTDLDVVAQARILDLLESIMRsRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRN 239
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQ 250
|
....*.
gi 501085142 240 LVSAHL 245
Cdd:PRK10619 251 FLKGSL 256
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-230 |
1.38e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.09 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNI--VLQADRPL----VHGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQPI-SPCKLR 77
Cdd:PRK13649 3 INLQNVsyTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKS----TIMQLLNGLHVPTQGSVRVDDTLItSTSKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 78 GIK-----VATIMQNPRS-----------AFNPLHTMAAHAKETCLASGKpaddatliaaLEAVGLenAARVLKLYPFEM 141
Cdd:PRK13649 79 DIKqirkkVGLVFQFPESqlfeetvlkdvAFGPQNFGVSQEEAEALAREK----------LALVGI--SESLFEKNPFEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 142 SGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSrapGM--LLVTHDMGVVARLADDVAVMDNGKI 219
Cdd:PRK13649 147 SGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS---GMtiVLVTHLMDDVANYADFVYVLEKGKL 223
|
250
....*....|.
gi 501085142 220 VELGDVETLFR 230
Cdd:PRK13649 224 VLSGKPKDIFQ 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-223 |
1.75e-16 |
|
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: 75.61 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 4 QIELQNIVL---QADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPIS---PCKLR 77
Cdd:cd03244 2 DIEFKNVSLryrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL----SSGSILIDGVDISkigLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 78 GiKVATIMQNP-------RSAFNPLHTmaahaketclasgkpADDATLIAALEAVGLEN--AARVLKL-YPFEMSGGML- 146
Cdd:cd03244 78 S-RISIIPQDPvlfsgtiRSNLDPFGE---------------YSDEELWQALERVGLKEfvESLPGGLdTVVEEGGENLs 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 147 --QR--MMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHdmgvvaRL-----ADDVAVMDNG 217
Cdd:cd03244 142 vgQRqlLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCT--VLTIAH------RLdtiidSDRILVLDKG 213
|
....*.
gi 501085142 218 KIVELG 223
Cdd:cd03244 214 RVVEFD 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-242 |
1.90e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 76.35 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTaGAILADGQPI-SP----CKLRGiKVATIMQNPrsa 91
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKStlLRSINRMNDLNPEVTIT-GSIVYNGHNIySPrtdtVDLRK-EIGMVFQQP--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 92 fNPLHTMAAHAKETCLASGKPADDATLIAALEAvGLENAA------RVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIAD 165
Cdd:PRK14239 96 -NPFPMSIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGASiwdevkDRLHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501085142 166 EPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVS 242
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYT--MLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYIS 248
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-232 |
2.25e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.36 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 14 ADRPLVHGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQPISP--CKLRGIKVATIMQNPRSA 91
Cdd:PRK10575 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKS----TLLKMLGRHQPPSEGEILLDAQPLESwsSKAFARKVAYLPQQLPAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 92 ----FNPLHTMAAHAKETCLASGKPADDATLIAALEAVGLENAARVLKlypFEMSGGMLQRMMIAMALLCDAPFIIADEP 167
Cdd:PRK10575 98 egmtVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLV---DSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 168 TTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTP 232
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-233 |
2.40e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.41 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 22 VSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGAILADGQPISPC-------KLRGiKVATIMQNPRSA--- 91
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALL----KPSSGTITIAGYHITPEtgnknlkKLRK-KVSLVFQFPEAQlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 92 --------FNPLHTMAAhaketclasgkpaDDATLIAALE---AVGLENaaRVLKLYPFEMSGGMLQRMMIAmALLCDAP 160
Cdd:PRK13641 101 ntvlkdveFGPKNFGFS-------------EDEAKEKALKwlkKVGLSE--DLISKSPFELSGGQMRRVAIA-GVMAYEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501085142 161 FIIA-DEPTTDLDVVAQARILDLLESIMRSrAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQ 233
Cdd:PRK13641 165 EILClDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-200 |
2.83e-16 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 77.79 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGqpISPCKLRGIKVATIM----QNPrs 90
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP----LQGEVTLDG--VPVSSLDQDEVRRRVsvcaQDA-- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 91 afnplHTMAAHAKETCLASGKPADDATLIAALEAVGLENAAR--------VLKLYPFEMSGGMLQRMMIAMALLCDAPFI 162
Cdd:TIGR02868 419 -----HLFDTTVRENLRLARPDATDEELWAALERVGLADWLRalpdgldtVLGEGGARLSGGERQRLALARALLADAPIL 493
|
170 180 190
....*....|....*....|....*....|....*...
gi 501085142 163 IADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHD 200
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLEDLLAALSGRT--VVLITHH 529
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
16-220 |
3.62e-16 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 74.67 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGAILADGQPISPCKLRG-----------IKVA 82
Cdd:TIGR02982 18 KQVLFDINLEINPGEIVILTGPSGSGKTtlLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLRRrigyifqahnlLGFL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 83 TIMQNPRSAFNpLHTMAAHAKETCLAsgkpaddatlIAALEAVGLENAarvLKLYPFEMSGGMLQRMMIAMALLCDAPFI 162
Cdd:TIGR02982 98 TARQNVQMALE-LQPNLSYQEARERA----------RAMLEAVGLGDH---LNYYPHNLSGGQKQRVAIARALVHHPKLV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501085142 163 IADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVArLADDVAVMDNGKIV 220
Cdd:TIGR02982 164 LADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILD-VADRILQMEDGKLL 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-229 |
3.66e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 75.92 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 1 MPQQIELQNIVLQAD----RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPCKL 76
Cdd:PRK13650 1 MSNIIEVKNLTFKYKedqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEA----ESGQIIIDGDLLTEENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 77 RGI--KVATIMQNPRSAF--------------N---PLHTMAAHAKEtclasgkpaddatliaALEAVGLENAArvlKLY 137
Cdd:PRK13650 77 WDIrhKIGMVFQNPDNQFvgatveddvafgleNkgiPHEEMKERVNE----------------ALELVGMQDFK---ERE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 138 PFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDvvAQARiLDLLESIMRSRAPGMLLV---THDMGVVArLADDVAVM 214
Cdd:PRK13650 138 PARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD--PEGR-LELIKTIKGIRDDYQMTVisiTHDLDEVA-LSDRVLVM 213
|
250
....*....|....*
gi 501085142 215 DNGKIVELGDVETLF 229
Cdd:PRK13650 214 KNGQVESTSTPRELF 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-250 |
3.80e-16 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 75.19 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 21 GVSLALRRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGAILADGQPISPcklRGIKVATIMQNprSAFNPLHT-- 97
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKS-----TLLNLISGLAQpTSGGVILEGKQITE---PGPDRMVVFQN--YSLLPWLTvr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 98 --MAAHAKETCLASGKPADDATLIAALEAVGLENAArvlKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVA 175
Cdd:TIGR01184 73 enIALAVDRVLPDLSKSERRAIVEEHIALVGLTEAA---DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501085142 176 QARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDV-ETLFRTPQHsvtRNLVSAHLALYGM 250
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQIlEVPFPRPRD---RLEVVEDPSYYDL 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
15-221 |
4.35e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.41 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGAILADGQPIsPCKLR----GIKVATIMQNPRS 90
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD----AGKITVLGVPV-PARARlaraRIGVVPQFDNLDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 91 AFNplhtmaahAKETCLASGK------PADDATLIAALEAVGLENAA--RVLklypfEMSGGMLQRMMIAMALLCDAPFI 162
Cdd:PRK13536 128 EFT--------VRENLLVFGRyfgmstREIEAVIPSLLEFARLESKAdaRVS-----DLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 163 IADEPTTDLDVVAQARILDLLESIMrSRAPGMLLVTHDMGVVARLADDVAVMDNG-KIVE 221
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGrKIAE 253
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-206 |
5.27e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.43 E-value: 5.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 21 GVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQPISP------CKLRGIKVATIMQN----Prs 90
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKS----TLLAILAGLDDGSSGEVSLVGQPLHQmdeearAKLRAKHVGFVFQSfmliP-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 91 AFNPLHTMAAHAKETCLASGKPADDAtlIAALEAVGLenaARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTD 170
Cdd:PRK10584 102 TLNALENVELPALLRGESSRQSRNGA--KALLEQLGL---GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 501085142 171 LDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVAR 206
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-232 |
6.07e-16 |
|
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: 75.91 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 22 VSLALRRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGAILADGQpispcklRGIKVAT-------IMQNPRsaf 92
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTtlLRAIAGLERPDSGRIRLGGEVLQDSA-------RGIFLPPhrrrigyVFQEAR--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 npLHtmaAH--AKETCL----ASGKPADDATLIAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADE 166
Cdd:COG4148 88 --LF---PHlsVRGNLLygrkRAPRAERRISFDEVVELLGIG---HLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501085142 167 PTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTP 232
Cdd:COG4148 160 PLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-220 |
6.93e-16 |
|
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: 74.29 E-value: 6.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 17 PLVHGVSLALRRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGAILADGqpISPCK-----LRGIKVATIMQN---- 87
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTT----LKILSGLLQPTSGEVRVAG--LVPWKrrkkfLRRIGVVFGQKTqlww 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 88 ---PRSAFNPLHTM----AAHAKETClasgkpaddATLIAALEAvglenaARVLKLYPFEMSGGMLQRMMIAMALLCDAP 160
Cdd:cd03267 109 dlpVIDSFYLLAAIydlpPARFKKRL---------DELSELLDL------EELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 161 FIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIV 220
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-221 |
7.61e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 74.51 E-value: 7.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 14 ADRPLVHGVSLALRRGRVLALVGGSGSGKS--LTCAAalGILPAgvrqTAGAILADGQPIS-PCKLRGI---KVA----- 82
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTtlLNLIA--GFLAP----SSGEITLDGVPVTgPGADRGVvfqKDAllpwl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 83 TIMQNprSAFnPLHtmaahaketcLAsGKPADDATLIAA--LEAVGLENAARVlklYPFEMSGGMLQRMMIAMALLCDAP 160
Cdd:COG4525 92 NVLDN--VAF-GLR----------LR-GVPKAERRARAEelLALVGLADFARR---RIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501085142 161 FIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDN--GKIVE 221
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVE 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
5-229 |
8.74e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.79 E-value: 8.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ--ADRPL-VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPCKLRGIK- 80
Cdd:PRK13648 8 IVFKNVSFQyqSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKV----KSGEIFYNNQAITDDNFEKLRk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 81 -VATIMQNPRSAF--NPLHTMAAHAKETCLAsgkPADDATLIA--ALEAVGLENAArvlKLYPFEMSGGMLQRMMIAMAL 155
Cdd:PRK13648 84 hIGIVFQNPDNQFvgSIVKYDVAFGLENHAV---PYDEMHRRVseALKQVDMLERA---DYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501085142 156 LCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMgVVARLADDVAVMDNGKIVELGDVETLF 229
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDL-SEAMEADHVIVMNKGTVYKEGTPTEIF 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-231 |
9.12e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.12 E-value: 9.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKS-----LTcaaalGILpagvRQTAGAILADGqpISPCKLRgikvatimqnprsafn 93
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSttikmLT-----GIL----VPTSGEVRVLG--YVPFKRR---------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 plhtmAAHAKETCLASGK--------PADDA-TLIAALEAVG-------LENAARVLKLYPF------EMSGGmlQRMM- 150
Cdd:COG4586 91 -----KEFARRIGVVFGQrsqlwwdlPAIDSfRLLKAIYRIPdaeykkrLDELVELLDLGELldtpvrQLSLG--QRMRc 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 151 -IAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLF 229
Cdd:COG4586 164 eLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELK 243
|
..
gi 501085142 230 RT 231
Cdd:COG4586 244 ER 245
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-228 |
1.20e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.83 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ---ADRPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAALgilpagVR---QTAGAILADGQPISPCKLRG 78
Cdd:PRK11176 342 IEFRNVTFTypgKEVPALRNINFKIPAGKTVALVGRSGSGKS-TIANLL------TRfydIDEGEILLDGHDLRDYTLAS 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 79 IK--VATIMQNPRsAFNplHTMA---AHAKETCLASGKPADDATLIAALEAV-----GL-----ENAArvlklypfEMSG 143
Cdd:PRK11176 415 LRnqVALVSQNVH-LFN--DTIAnniAYARTEQYSREQIEEAARMAYAMDFInkmdnGLdtvigENGV--------LLSG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 144 GMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARlADDVAVMDNGKIVELG 223
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRT--SLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
....*
gi 501085142 224 DVETL 228
Cdd:PRK11176 561 THAEL 565
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-221 |
1.32e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.84 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGAILADGQPI---SPCKLRGIK 80
Cdd:PRK13537 8 IDFRNVEKRyGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL----THPDAGSISLCGEPVpsrARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 81 VATIMQNPRSAFNPLHTMAAHAKETCLASGKPAddATLIAALEAVGLENAA--RVLklypfEMSGGMLQRMMIAMALLCD 158
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENLLVFGRYFGLSAAAAR--ALVPPLLEFAKLENKAdaKVG-----ELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501085142 159 APFIIADEPTTDLDVVAQARILDLLESIMrSRAPGMLLVTHDMGVVARLADDVAVMDNG-KIVE 221
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGrKIAE 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-228 |
1.39e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 6 ELQNIVLQADRPL--VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPI---SPCKLRGIK 80
Cdd:COG3845 259 EVENLSVRDDRGVpaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPP----ASGSIRLDGEDItglSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 81 VA---------------TIMQN------PRSAFNP-----LHTMAAHAKEtclasgkpaddatLIAALE--AVGLENAAR 132
Cdd:COG3845 335 VAyipedrlgrglvpdmSVAENlilgryRRPPFSRggfldRKAIRAFAEE-------------LIEEFDvrTPGPDTPAR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 133 VLklypfemSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLesiMRSRAPGM--LLVTHDMGVVARLADD 210
Cdd:COG3845 402 SL-------SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRL---LELRDAGAavLLISEDLDEILALSDR 471
|
250
....*....|....*...
gi 501085142 211 VAVMDNGKIVELGDVETL 228
Cdd:COG3845 472 IAVMYEGRIVGEVPAAEA 489
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-223 |
1.94e-15 |
|
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: 72.53 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 23 SLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPCKLRGIKVATIMQNprsafnplHTMAAHA 102
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETP----QSGRVLINGVDVTAAPPADRPVSMLFQE--------NNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 103 K-ETCLASG-------KPADDATLIAALEAVGLENaarVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVV 174
Cdd:cd03298 86 TvEQNVGLGlspglklTAEDRQAIEVALARVGLAG---LEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 501085142 175 AQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELG 223
Cdd:cd03298 163 LRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
21-229 |
1.99e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 73.73 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 21 GVSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGAILADGQPISPCKlRGI-----KVATIMQNPRsafNPL 95
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLFQNLNGIL----KPSSGRILFDGKPIDYSR-KGLmklreSVGMVFQDPD---NQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 96 HTMAAHAKET--CLASGKPADDA--TLIAALEAVGLENaarvLKLYPFE-MSGGMLQRMMIAMALLCDAPFIIADEPTTD 170
Cdd:PRK13636 96 FSASVYQDVSfgAVNLKLPEDEVrkRVDNALKRTGIEH----LKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501085142 171 LDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLF 229
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-230 |
2.20e-15 |
|
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: 75.22 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAI---LAD-----GQPISPCKLRGIKVATIMQNPRS 90
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEP----TSGEVnvrVGDewvdmTKPGPDGRGRAKRYIGILHQEYD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 91 AFnPLHTMAAHAKETcLASGKPADDATLIA--ALEAVGL--ENAARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADE 166
Cdd:TIGR03269 376 LY-PHRTVLDNLTEA-IGLELPDELARMKAviTLKMVGFdeEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501085142 167 PTTDLDVVAQariLDLLESIMRSRAP---GMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFR 230
Cdd:TIGR03269 454 PTGTMDPITK---VDVTHSILKAREEmeqTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-226 |
2.50e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 72.51 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 6 ELQNIVL-QADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGVRqTAGAILADGQPIS--PCKLRGIKVa 82
Cdd:COG4136 3 SLENLTItLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFS-ASGEVLLNGRRLTalPAEQRRIGI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 83 tIMQNPrsAFNPLHTMAAHaketcLASGKPAD------DATLIAALEAVGLEN-AARvlklYPFEMSGGMLQRMMIAMAL 155
Cdd:COG4136 81 -LFQDD--LLFPHLSVGEN-----LAFALPPTigraqrRARVEQALEEAGLAGfADR----DPATLSGGQRARVALLRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501085142 156 LCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDmgvvarlADDVAvmDNGKIVELGDVE 226
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD-------EEDAP--AAGRVLDLGNWQ 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-228 |
3.26e-15 |
|
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: 72.08 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPIS--PCKLR---GIkvATIMQNpRSAFn 93
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPP----RSGSIRFDGRDITglPPHERaraGI--GYVPEG-RRIF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 PLHT------MAAHAKetclasGKPADDATLiaaleavglenaARVLKLYP----------FEMSGGmlQRMM--IAMAL 155
Cdd:cd03224 88 PELTveenllLGAYAR------RRAKRKARL------------ERVYELFPrlkerrkqlaGTLSGG--EQQMlaIARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 156 LCDAPFIIADEPTTDLDVVAQARILDLLESImrsRAPGM--LLVTHDMGVVARLADDVAVMDNGKIVELGDVETL 228
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIREL---RDEGVtiLLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-233 |
3.63e-15 |
|
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: 72.32 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPI---SPCKL--RGIkvATIMQNpRSAFN 93
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPP----RSGSIRFDGEDItglPPHRIarLGI--GYVPEG-RRIFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 PLhT------MAAHAketclASGKPADDATLiaaleavglenaARVLKLYP----------FEMSGGmlQRMM--IAMAL 155
Cdd:COG0410 92 SL-TveenllLGAYA-----RRDRAEVRADL------------ERVYELFPrlkerrrqraGTLSGG--EQQMlaIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 156 LCDAPFIIADEPTTDLdvvAQARILDLLESIMRSRAPGM--LLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQ 233
Cdd:COG0410 152 MSRPKLLLLDEPSLGL---APLIVEEIFEIIRRLNREGVtiLLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-228 |
4.21e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.28 E-value: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 20 HGVSLALRRGRVLALVGGSGSGKS-LtcaaaLGILpAGV-RQTAGAILADGQPISPcklRGIKVA--------------- 82
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKStL-----MKIL-SGVyQPDSGEILLDGEPVRF---RSPRDAqaagiaiihqelnlv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 83 ---TIMQN------PRSA-FNPLHTMAAHAKEtclasgkpaddatliaALEAVGLE-NAARVLKlypfEMSGGmlQRMM- 150
Cdd:COG1129 92 pnlSVAENiflgrePRRGgLIDWRAMRRRARE----------------LLARLGLDiDPDTPVG----DLSVA--QQQLv 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501085142 151 -IAMALLCDAPFIIADEPTTDLDVVAQARILDLLESImRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETL 228
Cdd:COG1129 150 eIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-232 |
5.21e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 73.72 E-value: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQAD-RPLVHGVSLALRRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGAILADGQPIS--PCKLRGIK 80
Cdd:PRK11607 20 LEIRNLTKSFDgQHAVDDVSLTIYKGEIFALLGASGCGKS-----TLLRMLAGFEQpTAGQIMLDGVDLShvPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 81 vatiMQNPRSAFNPLHT----MAAHAKETCLASGKPADDATliaalEAVGLENAARVLKLYPFEMSGGMLQRMMIAMALL 156
Cdd:PRK11607 95 ----MMFQSYALFPHMTveqnIAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 157 CDAPFIIADEPTTDLDVVAQAR----ILDLLESImrsrAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTP 232
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDRmqleVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-229 |
5.58e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.35 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGAILADGQPISPCKlRGI-----KVATIMQNPR 89
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLL----RPQKGAVLWQGKPLDYSK-RGLlalrqQVATVFQDPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 90 SAFnpLHTMAAHAKETCLASGKPADDATLIAALEAVGLENAARvLKLYPFE-MSGGMLQRMMIAMALLCDAPFIIADEPT 168
Cdd:PRK13638 88 QQI--FYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQH-FRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501085142 169 TDLDVVAQARILDLLESIMrSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLF 229
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIV-AQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-241 |
5.93e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.39 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQ---------PISPCKLRGiKVATIM 85
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKS----TLLKVLNRLIEIYDSKIKVDGKvlyfgkdifQIDAIKLRK-EVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 86 QNPrsafNPLHTMA-----AHAKETCLASGKPADDATLIAALEAVGL-ENAARVLKLYPFEMSGGMLQRMMIAMALLCDA 159
Cdd:PRK14246 97 QQP----NPFPHLSiydniAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 160 PFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRN 239
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITELKNEIA--IVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
..
gi 501085142 240 LV 241
Cdd:PRK14246 251 YV 252
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-230 |
6.26e-15 |
|
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: 71.75 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ--ADRPLV-HGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPIS---PCKLRG 78
Cdd:cd03252 1 ITFEHVRFRykPDGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVP----ENGRVLVDGHDLAladPAWLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 79 iKVATIMQ-----NPRSAFNPLHTMAAHAKETCLASGKPADDATLIAAL----EAVGLENAArvlklypfEMSGGMLQRM 149
Cdd:cd03252 77 -QVGVVLQenvlfNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELpegyDTIVGEQGA--------GLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 150 MIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVaRLADDVAVMDNGKIVELGDVETLF 229
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRT--VIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDELL 224
|
.
gi 501085142 230 R 230
Cdd:cd03252 225 A 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-223 |
7.79e-15 |
|
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: 71.17 E-value: 7.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 29 GRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGAILADGQP---ISPCKLRgikVATIMQNprsafNPLHTMAAHAK 103
Cdd:cd03297 23 EEVTGIFGASGAGKStlLRCIAGLEKPDGGTIVLNGTVLFDSRKkinLPPQQRK---IGLVFQQ-----YALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 104 ETCLASGKPADDATLIAALEAVGLENAARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLL 183
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501085142 184 ESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELG 223
Cdd:cd03297 175 KQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-219 |
9.59e-15 |
|
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: 73.51 E-value: 9.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISpCKLRGIKVATIMQNPRSAFNPL 95
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP----TSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 96 HTMAAHAKETCLASGKPADDATLI--AALEAVGLENA----ARvlklypfEMSGGMLQRMMIAMALLCDAPFIIADEPTT 169
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGRSWEEAQLEmeAMLEDTGLHHKrneeAQ-------DLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501085142 170 DLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARLADDVAVMDNGKI 219
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYRSGRT--IIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-242 |
1.41e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.35 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGAILAD----GQPISPCKLRGiKVATIMQNPrsaf 92
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKStiLRCFNRLNDLIPGFRVEGKVTFHGknlyAPDVDPVEVRR-RIGMVFQKP---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 NPL-----HTMAAHAKetclASGKPADDATLI--AALEAVGLENAARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIAD 165
Cdd:PRK14243 101 NPFpksiyDNIAYGAR----INGYKGDMDELVerSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 166 EPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARLADDVAVMD---------NGKIVELGDVETLFRTPQHSV 236
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYT--IIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQQQA 254
|
....*.
gi 501085142 237 TRNLVS 242
Cdd:PRK14243 255 TRDYVS 260
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-234 |
1.55e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 72.03 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 4 QIELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTcaaaLGILpAGV-RQTAGAILADGQPIS--PCKLRGI 79
Cdd:COG3839 3 SLELENVSKSyGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRMI-AGLeDPTSGEILIGGRDVTdlPPKDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 KVA----------TIMQNprSAFnPLHtmaahaketclASGKPAD--DATLIAALEAVGLENaarVLKLYPFEMSGGMLQ 147
Cdd:COG3839 78 AMVfqsyalyphmTVYEN--IAF-PLK-----------LRKVPKAeiDRRVREAAELLGLED---LLDRKPKQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 148 RMMIAMALLCDAPFIIADEPTTDLD----VVAQARILDLLEsimRSRAPgMLLVTHD----MgvvaRLADDVAVMDNGKI 219
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHR---RLGTT-TIYVTHDqveaM----TLADRIAVMNDGRI 212
|
250
....*....|....*
gi 501085142 220 VELGDVETLFRTPQH 234
Cdd:COG3839 213 QQVGTPEELYDRPAN 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
120-243 |
1.57e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.28 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 120 AALEAVGLENAAR-VLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARIldllESIMRSRAPGM--LL 196
Cdd:PRK14271 142 ARLTEVGLWDAVKdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI----EEFIRSLADRLtvII 217
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 501085142 197 VTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSVTRNLVSA 243
Cdd:PRK14271 218 VTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAG 264
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-226 |
2.38e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 70.10 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 6 ELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAAL-GIlpAGVRQTAGAILADGQPI---SPCK--LRG 78
Cdd:COG0396 2 EIKNLHVSvEGKEILKGVNLTIKPGEVHAIMGPNGSGKS-TLAKVLmGH--PKYEVTSGSILLDGEDIlelSPDEraRAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 79 IKVAtiMQNP------------RSAFNplhtmaAHAKEtclASGKPADDATLIAALEAVGLENAArvLKLYPFE-MSGGM 145
Cdd:COG0396 79 IFLA--FQYPveipgvsvsnflRTALN------ARRGE---ELSAREFLKLLKEKMKELGLDEDF--LDRYVNEgFSGGE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 146 LQRMMIA-MALLcdAP-FIIADEPTTDLDVVAqARIL-DLLESiMRSRAPGMLLVTHdmgvVARL-----ADDVAVMDNG 217
Cdd:COG0396 146 KKRNEILqMLLL--EPkLAILDETDSGLDIDA-LRIVaEGVNK-LRSPDRGILIITH----YQRIldyikPDFVHVLVDG 217
|
....*....
gi 501085142 218 KIVELGDVE 226
Cdd:COG0396 218 RIVKSGGKE 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-217 |
3.22e-14 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 69.77 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 17 PLVHGVSLALRRGRVLALVGGSGSGKS--LTCaaalgiLPAGVRQTAGAIL--ADGQPISPCKLRGIKVATIMQN----- 87
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKStlLKC------IYGNYLPDSGSILvrHDGGWVDLAQASPREILALRRRtigyv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 88 -------PR-SAfnpLHTMAahakETCLASGKPADDATLIAA--LEAVGLEnaARVLKLYPFEMSGGMLQRMMIAMALLC 157
Cdd:COG4778 99 sqflrviPRvSA---LDVVA----EPLLERGVDREEARARARelLARLNLP--ERLWDLPPATFSGGEQQRVNIARGFIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 158 DAPFIIADEPTTDLDVVAQARILDLLESIMRSRApGMLLVTHDMGVVARLADDVAVMDNG 217
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIEEAKARGT-AIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-223 |
3.64e-14 |
|
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: 69.61 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGVRqTAGAILADGQPISPCKLRGIkVATIMQNPRsaFNP 94
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGT-TSGQILFNGQPRKPDQFQKC-VAYVRQDDI--LLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 95 LHTMAAHAKETC-LASGKPADDATLIAALEAVGLENAA--RVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDL 171
Cdd:cd03234 95 GLTVRETLTYTAiLRLPRKSSDAIRKKRVEDVLLRDLAltRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501085142 172 DVVAQARILDLLESIMRsRAPGMLLVTHDMGV-VARLADDVAVMDNGKIVELG 223
Cdd:cd03234 175 DSFTALNLVSTLSQLAR-RNRIVILTIHQPRSdLFRLFDRILLLSSGEIVYSG 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-236 |
3.77e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.62 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 18 LVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGVrQTAGAILADGQPISPCKLRGIKvATIMQNprSAFNPLHT 97
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGV-KGSGSVLLNGMPIDAKEMRAIS-AYVQQD--DLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 98 MAAH--------AKETCLASGKpadDATLIAALEAVGLENAARVLKLYPFEM---SGGMLQRMMIAMALLCDAPFIIADE 166
Cdd:TIGR00955 116 VREHlmfqahlrMPRRVTKKEK---RERVDEVLQALGLRKCANTRIGVPGRVkglSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 167 PTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGdvetlfrTPQHSV 236
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG-------SPDQAV 255
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-218 |
4.82e-14 |
|
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: 67.09 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSltcaaalgilpagvrqtagailadgqpispcklrgikvaT 83
Cdd:cd03221 1 IELENLSKTyGGKLLLKDISLTINPGDRIGLVGRNGAGKS---------------------------------------T 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 84 ImqnprsafnpLHTMAAHAKETclaSGKPADDATL-IAALEavglenaarvlklypfEMSGGMLQRMMIAMALLCDAPFI 162
Cdd:cd03221 42 L----------LKLIAGELEPD---EGIVTWGSTVkIGYFE----------------QLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501085142 163 IADEPTTDLDVVAQarilDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGK 218
Cdd:cd03221 93 LLDEPTNHLDLESI----EALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
107-232 |
1.16e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.11 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 107 LASGKPADDATLIAA--LEAVGLENAarVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLle 184
Cdd:PRK13631 143 VALGVKKSEAKKLAKfyLNKMGLDDS--YLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQL-- 218
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 501085142 185 sIMRSRAPG--MLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTP 232
Cdd:PRK13631 219 -ILDAKANNktVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-234 |
1.44e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.70 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGVR----QTAGAILADGQP---ISPCKLRGIKvATIMQNP 88
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAprgaRVTGDVTLNGEPlaaIDAPRLARLR-AVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 89 RSAFnplhtmAAHAKETCLASGKP---ADDATLIA----ALEAVGLENAARVLKLYPFEMSGGMLQRMMIAMAL------ 155
Cdd:PRK13547 93 QPAF------AFSAREIVLLGRYPharRAGALTHRdgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 156 ---LCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFrTP 232
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL-TP 245
|
..
gi 501085142 233 QH 234
Cdd:PRK13547 246 AH 247
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
110-224 |
4.15e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.42 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 110 GKPADDATLIAA--LEAVGLENAarVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIM 187
Cdd:PRK13651 135 GVSKEEAKKRAAkyIELVGLDES--YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN 212
|
90 100 110
....*....|....*....|....*....|....*..
gi 501085142 188 RSrAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGD 224
Cdd:PRK13651 213 KQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGD 248
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-232 |
5.65e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.93 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 17 PLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGAILADG-QPISPCKLRGIK--VATIMQNPRSAF- 92
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLL----RPQKGKVLVSGiDTGDFSKLQGIRklVGIVFQNPETQFv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 --NPLHTMAAHAKETCLAsgkPADDATLI-AALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTT 169
Cdd:PRK13644 92 grTVEEDLAFGPENLCLP---PIEIRKRVdRALAEIGLE---KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501085142 170 DLDVVAQARILDLLESIMRsRAPGMLLVTHDMGVVaRLADDVAVMDNGKIVELGDVETLFRTP 232
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-236 |
5.78e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.04 E-value: 5.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 1 MPQQIELQNIVL----QADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGAILADGQPISPCKL 76
Cdd:PRK13642 1 MNKILEVENLVFkyekESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLF----EEFEGKVKIDGELLTAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 77 RGI--KVATIMQNPRSAF--NPLHTMAAHAKETclaSGKPADDaTLIAALEAVGLENAARVLKLYPFEMSGGMLQRMMIA 152
Cdd:PRK13642 77 WNLrrKIGMVFQNPDNQFvgATVEDDVAFGMEN---QGIPREE-MIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 153 MALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARlADDVAVMDNGKIVELGDVETLFRTP 232
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATS 231
|
....
gi 501085142 233 QHSV 236
Cdd:PRK13642 232 EDMV 235
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-211 |
6.66e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 6.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 1 MPQQIELQNI-VLQADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGAILADGQpispcklrgI 79
Cdd:PRK09544 1 MTSLVSLENVsVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGL----VAPDEGVIKRNGK---------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 KVATIMQNprsafnpLH---TMAAHAKE-TCLASGKPADDatLIAALEAVgleNAARVLKLYPFEMSGGMLQRMMIAMAL 155
Cdd:PRK09544 68 RIGYVPQK-------LYldtTLPLTVNRfLRLRPGTKKED--ILPALKRV---QAGHLIDAPMQKLSGGETQRVLLARAL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501085142 156 LCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDV 211
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-222 |
8.03e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 8.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 6 ELQNIVlQADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGAILADGQPISP-CKLRGIK--VA 82
Cdd:PRK09700 267 EVRNVT-SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK----RAGGEIRLNGKDISPrSPLDAVKkgMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 83 TIMQNPR-SAFNPLHTMAAH-AKETCLASGKPADDATLIAALEAVGLENAAR---VLKLYPF-----EMSGGMLQRMMIA 152
Cdd:PRK09700 342 YITESRRdNGFFPNFSIAQNmAISRSLKDGGYKGAMGLFHEVDEQRTAENQRellALKCHSVnqnitELSGGNQQKVLIS 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501085142 153 MALLCDAPFIIADEPTTDLDVVAQARILdlleSIMRSRA---PGMLLVTHDMGVVARLADDVAVMDNGKIVEL 222
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIY----KVMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-223 |
8.22e-13 |
|
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: 65.26 E-value: 8.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 6 ELQNIVLQADRPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAALgilpAGVRQTA---GAILADGQPISPCKLRGIkVA 82
Cdd:cd03213 12 TVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKS-TLLNAL----AGRRTGLgvsGEVLINGRPLDKRSFRKI-IG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 83 TIMQnprsafnplhtmaahaketclasgkpaDDaTLIAAL---EAvgLENAARVLKLypfemSGGMLQRMMIAMALLCDA 159
Cdd:cd03213 86 YVPQ---------------------------DD-ILHPTLtvrET--LMFAAKLRGL-----SGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 160 PFIIADEPTTDLDVVAQARILDLLeSIMRSRAPGMLLVTHD-MGVVARLADDVAVMDNGKIVELG 223
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLL-RRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-223 |
8.38e-13 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 65.35 E-value: 8.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTcaaaLGILpAGVRQ-TAGAILADGQPIS--PCKLRGIk 80
Cdd:cd03301 1 VELENVTKRfGNVTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMI-AGLEEpTSGRIYIGGRDVTdlPPKDRDI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 81 vATIMQNprSAFNPLHT----MAAHAKetcLASGKPAD-DATLIAALEAVGLENaarVLKLYPFEMSGGMLQRMMIAMAL 155
Cdd:cd03301 75 -AMVFQN--YALYPHMTvydnIAFGLK---LRKVPKDEiDERVREVAELLQIEH---LLDRKPKQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501085142 156 LCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELG 223
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-226 |
9.44e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.40 E-value: 9.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 2 PQQIELQNIVLQA--------DRPLVHGVSLALRRGRVLALVGGSGSGKS-LtcaaaLGILpAGVRQ-TAGAIladgqpi 71
Cdd:COG0488 306 PPPERLGKKVLELeglsksygDKTLLDDLSLRIDRGDRIGLIGPNGAGKStL-----LKLL-AGELEpDSGTV------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 72 spcKL-RGIKVATIMQNpRSAFNPLHTMAAHaketcLASGKP-ADDATLIAALEAVG-----LENAARVLklypfemSGG 144
Cdd:COG0488 373 ---KLgETVKIGYFDQH-QEELDPDKTVLDE-----LRDGAPgGTEQEVRGYLGRFLfsgddAFKPVGVL-------SGG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 145 MLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESImrsraPG-MLLVTHDMGVVARLADDVAVMDNGKIVE-L 222
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-----PGtVLLVSHDRYFLDRVATRILEFEDGGVREyP 511
|
....
gi 501085142 223 GDVE 226
Cdd:COG0488 512 GGYD 515
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-226 |
9.79e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 64.86 E-value: 9.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 14 ADRPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAALGILPaGVRQTAGAILADGQ-----PISPCKLRGIKVAtiMQNP 88
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKS-TLAKTIMGHP-KYEVTEGEILFKGEditdlPPEERARLGIFLA--FQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 89 rsafnplhtmaahaketclasgkpaddatliAALEAVGLENAARVLKlYPFemSGGMLQRMMIAMALLCDAPFIIADEPT 168
Cdd:cd03217 87 -------------------------------PEIPGVKNADFLRYVN-EGF--SGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501085142 169 TDLDVVAQARILDLLESiMRSRAPGMLLVTHdmgvVARLADD-----VAVMDNGKIVELGDVE 226
Cdd:cd03217 133 SGLDIDALRLVAEVINK-LREEGKSVLIITH----YQRLLDYikpdrVHVLYDGRIVKSGDKE 190
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-224 |
1.11e-12 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 65.27 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 23 SLALRRGRVLALVGGSGSGKSLTCAAALGIL-PAgvrqtAGAILADGQPI--SPCKLRGIKVA----------TIMQNPR 89
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIePA-----SGSIKVNDQSHtgLAPYQRPVSMLfqennlfahlTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 90 SAFNPLHTMAAHAKETclasgkpaddatLIAALEAVGLENaarVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTT 169
Cdd:TIGR01277 93 LGLHPGLKLNAEQQEK------------VVDAAQQVGIAD---YLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 170 DLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGD 224
Cdd:TIGR01277 158 ALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-224 |
1.38e-12 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 66.70 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 4 QIELQNIVLQA---DRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISpcklrgik 80
Cdd:COG4618 330 RLSVENLTVVPpgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP----TAGSVRLDGADLS-------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 81 vatimQNPRSAFNPlhtmaaH----AKETCLASG---------KPADDATLIAALEAVGLENAarVLKL---YPFE---- 140
Cdd:COG4618 398 -----QWDREELGR------HigylPQDVELFDGtiaeniarfGDADPEKVVAAAKLAGVHEM--ILRLpdgYDTRigeg 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 141 ---MSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARildLLESIMRSRAPGM--LLVTHDMGVVArLADDVAVMD 215
Cdd:COG4618 465 garLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAA---LAAAIRALKARGAtvVVITHRPSLLA-AVDKLLVLR 540
|
....*....
gi 501085142 216 NGKIVELGD 224
Cdd:COG4618 541 DGRVQAFGP 549
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-219 |
1.51e-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: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 7 LQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKS-LtcaaaLGILpagvrqtAGAILADGQPISpcKLRGIKVATI 84
Cdd:COG0488 1 LENLSKSfGGRPLLDDVSLSINPGDRIGLVGRNGAGKStL-----LKIL-------AGELEPDSGEVS--IPKGLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 85 MQNPR------------SAFNPLHTMAAHAKETCLASGKPADD----ATLIAALEAVG---LEN-AARVL-----KLYPF 139
Cdd:COG0488 67 PQEPPldddltvldtvlDGDAELRALEAELEELEAKLAEPDEDlerlAELQEEFEALGgweAEArAEEILsglgfPEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 140 -----EMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAqariLDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVM 214
Cdd:COG0488 147 drpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILEL 222
|
....*
gi 501085142 215 DNGKI 219
Cdd:COG0488 223 DRGKL 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-228 |
1.71e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.53 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 21 GVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPCKLRGI--KVATIMQNPRS-------- 90
Cdd:PRK13647 23 GLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLP----QRGRVKVMGREVNAENEKWVrsKVGLVFQDPDDqvfsstvw 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 91 ---AFNPLHtMAAHAKETclasgkpadDATLIAALEAVGLENAArvlKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEP 167
Cdd:PRK13647 99 ddvAFGPVN-MGLDKDEV---------ERRVEEALKAVRMWDFR---DKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501085142 168 TTDLDVVAQARILDLLESIMRsRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETL 228
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-232 |
1.71e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 66.26 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQADRPLV-HGVSLALRRGRVLALVGGSGSGKSltcaAALGILpAGV-RQTAGAILADGQPISPCKLRGIKVA 82
Cdd:PRK10851 3 IEIANIKKSFGRTQVlNDISLDIPSGQMVALLGPSGSGKT----TLLRII-AGLeHQTSGHIRFHGTDVSRLHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 83 TIMQN----------PRSAFN----PLH----TMAAHAKETCLasgkpaddatliaaLEAVGLENAArvlKLYPFEMSGG 144
Cdd:PRK10851 78 FVFQHyalfrhmtvfDNIAFGltvlPRRerpnAAAIKAKVTQL--------------LEMVQLAHLA---DRYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 145 MLQRMMIAMALLCDAPFIIADEPTTDLDvvAQAR------ILDLLESIMRSRapgmLLVTHDMGVVARLADDVAVMDNGK 218
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALD--AQVRkelrrwLRQLHEELKFTS----VFVTHDQEEAMEVADRVVVMSQGN 214
|
250
....*....|....
gi 501085142 219 IVELGDVETLFRTP 232
Cdd:PRK10851 215 IEQAGTPDQVWREP 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
16-221 |
1.82e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.11 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGAILADGQPIS-PCKLRGIkvatIMQNprSAFNP 94
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ----HGSITLDGKPVEgPGAERGV----VFQN--EGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 95 LHTMAAH-AKETCLAS-GKPADDATLIAALEAVGLENAArvlKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLD 172
Cdd:PRK11248 84 WRNVQDNvAFGLQLAGvEKMQRLEIAHQMLKKVGLEGAE---KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 501085142 173 VVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVM--DNGKIVE 221
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVE 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-220 |
2.08e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 66.29 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 21 GVSLALRRGRVLALVGGSGSGKSlTCAAALGIL---PAGVRQTAGAILADGQPISPCKLRGIKVATIMQnpRSAFNPlHT 97
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKS-TLMNILGCLdkpTSGTYRVAGQDVATLDADALAQLRREHFGFIFQ--RYHLLS-HL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 98 MAAHAKE---TCLASGKPADDATLIAALEAVGLENaaRVlKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVV 174
Cdd:PRK10535 102 TAAQNVEvpaVYAGLERKQRLLRAQELLQRLGLED--RV-EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501085142 175 AQARILDLLESiMRSRAPGMLLVTHDMGVVARlADDVAVMDNGKIV 220
Cdd:PRK10535 179 SGEEVMAILHQ-LRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-233 |
2.92e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 64.26 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNI-----VLQAdrplVHGVSLALRRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGAILADGQPISPCKLR 77
Cdd:COG4161 3 IQLKNIncfygSHQA----LFDINLECPSGETLVLLGPSGAGKSslLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 78 GI--KVA------------TIMQNPRSAfnplhtmaahakeTCLASGKPADDATLIAA--LEAVGLENAARVlklYPFEM 141
Cdd:COG4161 79 LLrqKVGmvfqqynlwphlTVMENLIEA-------------PCKVLGLSKEQAREKAMklLARLRLTDKADR---FPLHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 142 SGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESImrsRAPGM--LLVTHDMGVVARLADDVAVMDNGKI 219
Cdd:COG4161 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL---SQTGItqVIVTHEVEFARKVASQVVYMEKGRI 219
|
250
....*....|....
gi 501085142 220 VELGDVEtLFRTPQ 233
Cdd:COG4161 220 IEQGDAS-HFTQPQ 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-236 |
2.96e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.79 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQPI---SPCKLRGIKVATIMQNPRSA 91
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKT----TLLRLIGGQIAPDHGEILFDGENIpamSRSRLYTVRKRMSMLFQSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 92 F----NPLHTMAAHAKE-TCLAsgKPADDATLIAALEAVGLENAArvlKLYPFEMSGGMLQRMMIAMALLCDAPFIIADE 166
Cdd:PRK11831 95 LftdmNVFDNVAYPLREhTQLP--APLLHSTVMMKLEAVGLRGAA---KLMPSELSGGMARRAALARAIALEPDLIMFDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 167 PTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQHSV 236
Cdd:PRK11831 170 PFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRV 239
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-250 |
5.21e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.85 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 18 LVHGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQPIS--PCKLRGIKVATIMQNPRS----A 91
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKS----TLLRTLSRLMTPAHGHVWLDGEHIQhyASKEVARRIGLLAQNATTpgdiT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 92 FNPLHTMAAHAKETCLASGKPADDATLIAALEAVGLENAARvlkLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDL 171
Cdd:PRK10253 98 VQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLAD---QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501085142 172 DVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGdvetlfrTPQHSVTRNLVSahlALYGM 250
Cdd:PRK10253 175 DISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELIE---RIYGL 243
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-223 |
6.77e-12 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 62.81 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 4 QIELQNIVLQ--ADRPLV-HGVSLALRRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGAILADGQPISPCKLRGI- 79
Cdd:cd03369 6 EIEVENLSVRyaPDLPPVlKNVSFKVKAGEKIGIVGRTGAGKS-TLILALFRF---LEAEEGKIEIDGIDISTIPLEDLr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 -KVATIMQNPrsafnplhTMAAHAKETCLASGKPADDATLIAALE-AVGLENaarvlklypfeMSGGMLQRMMIAMALLC 157
Cdd:cd03369 82 sSLTIIPQDP--------TLFSGTIRSNLDPFDEYSDEEIYGALRvSEGGLN-----------LSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501085142 158 DAPFIIADEPTTDLDVVAQArildLLESIMRSRAPG--MLLVTHDMGVVARLaDDVAVMDNGKIVELG 223
Cdd:cd03369 143 RPRVLVLDEATASIDYATDA----LIQKTIREEFTNstILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-228 |
8.37e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.06 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 23 SLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQP---ISPCKlRGIKVA----------TIMQNPR 89
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTP----ASGSLTLNGQDhttTPPSR-RPVSMLfqennlfshlTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 90 SAFNPLHTMAAHAKETclasgkpaddatLIAALEAVGLENaarVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTT 169
Cdd:PRK10771 94 LGLNPGLKLNAAQREK------------LHAIARQMGIED---LLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501085142 170 DLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETL 228
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
14-219 |
1.03e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.16 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 14 ADRPLVHGVSLALRRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGAILADGQPIspcklrgikvATIMQNPRSAF 92
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKS-----TLLRLLAGLETpSAGELLAGTAPL----------AEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 N-----PLHTMAAHAKetcLA-SGKPADDAtlIAALEAVGLENAArvlKLYPFEMSGGMLQRMMIAMALLCDAPFIIADE 166
Cdd:PRK11247 88 QdarllPWKKVIDNVG---LGlKGQWRDAA--LQALAAVGLADRA---NEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501085142 167 PTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKI 219
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
137-233 |
1.03e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 62.72 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 137 YPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSrapGM--LLVTHDMGVVARLADDVAVM 214
Cdd:PRK11124 138 FPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET---GItqVIVTHEVEVARKTASRVVYM 214
|
90
....*....|....*....
gi 501085142 215 DNGKIVELGDvETLFRTPQ 233
Cdd:PRK11124 215 ENGHIVEQGD-ASCFTQPQ 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-220 |
1.08e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.59 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQPISPCKLRGI--KVATIMQNPRSAFNPLH 96
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRATSGRIVFDGKDITDWQTAKImrEAVAIVPEGRRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 97 TmaahakETCLASGKPADDATLIaaleavgLENAARVLKLYP--FE--------MSGGMLQRMMIAMALLCDAPFIIADE 166
Cdd:PRK11614 97 V------EENLAMGGFFAERDQF-------QERIKWVYELFPrlHErriqragtMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501085142 167 PTTDLdvvAQARILDLLESIMRSRAPGM--LLVTHDMGVVARLADDVAVMDNGKIV 220
Cdd:PRK11614 164 PSLGL---APIIIQQIFDTIEQLREQGMtiFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-198 |
1.09e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.06 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 4 QIELQNIVLQ--ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtagailaDGQPISPCKlrgikv 81
Cdd:COG4178 362 ALALEDLTLRtpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG----------SGRIARPAG------ 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 82 ATIMQNPRSAFNPLHTMAAhaketCLA---SGKPADDATLIAALEAVGLENAA----------RVLklypfemSGGMLQR 148
Cdd:COG4178 426 ARVLFLPQRPYLPLGTLRE-----ALLypaTAEAFSDAELREALEAVGLGHLAerldeeadwdQVL-------SLGEQQR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501085142 149 MMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLesimRSRAPGMLLVT 198
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLL----REELPGTTVIS 539
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-228 |
1.26e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.05 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGIlpAGVRQTAGAIL----------------AD 67
Cdd:TIGR03269 1 IEVKNLTKKfDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGM--DQYEPTSGRIIyhvalcekcgyverpsKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 68 GQPISPC--KLRGIKV----------ATIMQnpRSAFNPLHTMAAHAKETCLAS--------GKPADDATLIAA--LEAV 125
Cdd:TIGR03269 79 GEPCPVCggTLEPEEVdfwnlsdklrRRIRK--RIAIMLQRTFALYGDDTVLDNvlealeeiGYEGKEAVGRAVdlIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 126 GLENaaRVLKLyPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVA 205
Cdd:TIGR03269 157 QLSH--RITHI-ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|...
gi 501085142 206 RLADDVAVMDNGKIVELGDVETL 228
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
15-205 |
1.70e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.74 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGK-SLtcaaaLGILPAGVRQTAGAILADGQPISPCK------------LRGIKV 81
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKtSL-----LRILAGLARPDAGEVLWQGEPIRRQRdeyhqdllylghQPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 82 ATimqnprSAFNPLHTMAAHAKetclasgkPADDATLIAALEAVGLEN----AARVLklypfemSGGmlQRMMIAMA--L 155
Cdd:PRK13538 88 EL------TALENLRFYQRLHG--------PGDDEALWEALAQVGLAGfedvPVRQL-------SAG--QQRRVALArlW 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501085142 156 LCDAPFIIADEPTTDLDVVAQARILDLLESimRSRAPGMLLVT--HDMGVVA 205
Cdd:PRK13538 145 LTRAPLWILDEPFTAIDKQGVARLEALLAQ--HAEQGGMVILTthQDLPVAS 194
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-229 |
1.81e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.80 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 1 MPQQIELQNIVLQ-------ADRPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGAILADGqpISP 73
Cdd:PRK13633 1 MNEMIKCKNVSYKyesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKS-TIAKHMNAL---LIPSEGKVYVDG--LDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 74 CKLRGI-----KVATIMQNPRS-----------AFNPlHTMAAHAKETclasGKPADDAtliaaLEAVGLENAARvlkLY 137
Cdd:PRK13633 75 SDEENLwdirnKAGMVFQNPDNqivativeedvAFGP-ENLGIPPEEI----RERVDES-----LKKVGMYEYRR---HA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 138 PFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARlADDVAVMDNG 217
Cdd:PRK13633 142 PHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSG 220
|
250
....*....|..
gi 501085142 218 KIVELGDVETLF 229
Cdd:PRK13633 221 KVVMEGTPKEIF 232
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
134-226 |
2.97e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.58 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 134 LKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAV 213
Cdd:PRK11144 122 LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVV 201
|
90
....*....|...
gi 501085142 214 MDNGKIVELGDVE 226
Cdd:PRK11144 202 LEQGKVKAFGPLE 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-223 |
3.51e-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: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKS-LtcaaaLGILpAGV-RQTAGAILADGQPISPCKLRGikvatimqnprsAFNPLH 96
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKStL-----LRLL-AGIyPPDSGTVTVRGRVSSLLGLGG------------GFNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 97 TMAAHAKETCLASG-KPADDATLIAA-LEAVGLENAA-RVLKLYpfemSGGMLQRMMIAMALLCDAPFIIADEPTTDLDV 173
Cdd:cd03220 100 TGRENIYLNGRLLGlSRKEIDEKIDEiIEFSELGDFIdLPVKTY----SSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501085142 174 VAQARILDLLESiMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELG 223
Cdd:cd03220 176 AFQEKCQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-220 |
4.73e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 62.34 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPIspcKLRGIKVA------------- 82
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPA----DSGEIRLDGKPV---RIRSPRDAiragiayvpedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 83 --------TIMQNprsafnplHTMAAHAKetcLASGKPADDATLIAALEAV---------GLENAARVLklypfemSGGM 145
Cdd:COG1129 338 geglvldlSIREN--------ITLASLDR---LSRGGLLDRRRERALAEEYikrlriktpSPEQPVGNL-------SGGN 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501085142 146 LQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLlesIMRSRAPGM--LLVTHDMGVVARLADDVAVMDNGKIV 220
Cdd:COG1129 400 QQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRL---IRELAAEGKavIVISSELPELLGLSDRILVMREGRIV 473
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-219 |
7.08e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 61.76 E-value: 7.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrQTAGAILADGQPI---SPCKLRGIKVATIMQNpRSAF 92
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPG---KFEGNVFINGKPVdirNPAQAIRAGIAMVPED-RKRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 NPLHTMAAHAKETCLASGKPADDATLIAALEAVGLENAARVLKL---YPF----EMSGGMLQRMMIAMALLCDAPFIIAD 165
Cdd:TIGR02633 349 GIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVktaSPFlpigRLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 501085142 166 EPTTDLDVVAQARILDLLESIMRsRAPGMLLVTHDMGVVARLADDVAVMDNGKI 219
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-219 |
1.28e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.03 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTcaaalgilpagVRQTAGAILADGQPISPCKLRGIKV------ATIMQNPRS-- 90
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTL-----------LRHLSGLITGDKSAGSHIELLGRTVqregrlARDIRKSRAnt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 91 -----AFNPLHTMAAHAK------------ETCLASGKPADDATLIAALEAVGLENAA--RVLKLypfemSGGMLQRMMI 151
Cdd:PRK09984 89 gyifqQFNLVNRLSVLENvligalgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAhqRVSTL-----SGGQQQRVAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501085142 152 AMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKI 219
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-223 |
1.44e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 22 VSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqtAGAILADGQPISPCKLRGIKV--ATIMQNPRSAFN-PL-HT 97
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-----SGSIQFAGQPLEAWSAAELARhrAYLSQQQTPPFAmPVfQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 98 MAAHAKetclASGKPADDATLIAAL-EAVGLENA-ARVLKlypfEMSGGMLQRMMIAMALLCDAPFI-------IADEPT 168
Cdd:PRK03695 90 LTLHQP----DKTRTEAVASALNEVaEALGLDDKlGRSVN----QLSGGEWQRVRLAAVVLQVWPDInpagqllLLDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 169 TDLDvVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELG 223
Cdd:PRK03695 162 NSLD-VAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASG 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
140-214 |
2.03e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 2.03e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 140 EMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARLADDVAVM 214
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKY--VLVVEHDLAVLDYLADNVHIA 284
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-227 |
2.40e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.04 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 1 MPQQIELQNIV-----LQAdrplVHGVSLALRRGRVLALVGGSGSGKS-LtcaaaLGILpAG-VRQTAGAILADGQPISP 73
Cdd:COG3845 2 MPPALELRGITkrfggVVA----NDDVSLTVRPGEIHALLGENGAGKStL-----MKIL-YGlYQPDSGEILIDGKPVRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 74 cklrgikvatimQNPRSAfnplhtMAA-------HAKetclasgkpaddatLIAAL---E--AVGLEN-----------A 130
Cdd:COG3845 72 ------------RSPRDA------IALgigmvhqHFM--------------LVPNLtvaEniVLGLEPtkggrldrkaaR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 131 ARVLKL---YPFE---------MSGGMLQRMMIAMALLCDAPFIIADEPTTdldVVAQARILDLLESIMRSRAPGM--LL 196
Cdd:COG3845 120 ARIRELserYGLDvdpdakvedLSVGEQQRVEILKALYRGARILILDEPTA---VLTPQEADELFEILRRLAAEGKsiIF 196
|
250 260 270
....*....|....*....|....*....|.
gi 501085142 197 VTHDMGVVARLADDVAVMDNGKIVelGDVET 227
Cdd:COG3845 197 ITHKLREVMAIADRVTVLRRGKVV--GTVDT 225
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-226 |
3.79e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.50 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNivLQA---DRPLVHGVSLALRRGRVLALVGGSGSGKSlTCAAALGILPAgVRQTAGAILADGQPIspCKL----- 76
Cdd:CHL00131 8 LEIKN--LHAsvnENEILKGLNLSINKGEIHAIMGPNGSGKS-TLSKVIAGHPA-YKILEGDILFKGESI--LDLepeer 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 77 --RGIKVAtiMQNP------------RSAFNPLHTmaahaketclASGKPADDA----TLIAA-LEAVGLEnaARVLKLY 137
Cdd:CHL00131 82 ahLGIFLA--FQYPieipgvsnadflRLAYNSKRK----------FQGLPELDPleflEIINEkLKLVGMD--PSFLSRN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 138 PFE-MSGGMLQRMMI-AMALLcDAPFIIADEPTTDLDVVAQARILDLLESIMRSrAPGMLLVTHdmgvVARL-----ADD 210
Cdd:CHL00131 148 VNEgFSGGEKKRNEIlQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITH----YQRLldyikPDY 221
|
250
....*....|....*.
gi 501085142 211 VAVMDNGKIVELGDVE 226
Cdd:CHL00131 222 VHVMQNGKIIKTGDAE 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
16-232 |
7.02e-10 |
|
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: 57.55 E-value: 7.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGAILADGQPIS--PCKLR---GIkvATIMQNPrS 90
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGL----VKPDSGKILLDGQDITklPMHKRarlGI--GYLPQEA-S 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 91 AFNPLhTMAAHAKetCLASGKPADDATLIAALEAVgLE--NAARVLKLYPFEMSGGMLQRMMIAMALLCDAPFIIADEPT 168
Cdd:cd03218 86 IFRKL-TVEENIL--AVLEIRGLSKKEREEKLEEL-LEefHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501085142 169 TDLDVVAQARILDLLEsIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTP 232
Cdd:cd03218 162 AGVDPIAVQDIQKIIK-ILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-222 |
9.83e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.44 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 3 QQIELQNIVLQADRP--LVHGVSLALRRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGAILADGQPISpcklrgi 79
Cdd:PRK10522 321 QTLELRNVTFAYQDNgfSVGPINLTIKRGELLFLIGGNGSGKS-----TLAMLLTGLYQpQSGEILLDGKPVT------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 kvATIMQNPRSAFNPLHTmAAHAKETCLAS-GKPADDATLIAALEAVGLENAARV--LKLYPFEMSGGMLQRMMIAMALL 156
Cdd:PRK10522 389 --AEQPEDYRKLFSAVFT-DFHLFDQLLGPeGKPANPALVEKWLERLKMAHKLELedGRISNLKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501085142 157 CDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARlADDVAVMDNGKIVEL 222
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSEL 530
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-234 |
1.14e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 57.16 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 21 GVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqtAGAILADGQPISPCKLRGIKV--ATIMQNPRSAFN-PL-H 96
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-----QGEILLNGRPLSDWSAAELARhrAYLSQQQSPPFAmPVfQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 97 TMAAHAKetclASGKPADDATLIAAL-EAVGLENaarvlKL-YPFE-MSGGMLQRMMIAMALL-------CDAPFIIADE 166
Cdd:COG4138 89 YLALHQP----AGASSEAVEQLLAQLaEALGLED-----KLsRPLTqLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501085142 167 PTTDLDVVAQARILDLLESImrSRAPGMLLV-THDMGVVARLADDVAVMDNGKIVELGDVETLFrTPQH 234
Cdd:COG4138 160 PMNSLDVAQQAALDRLLREL--CQQGITVVMsSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPEN 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-228 |
1.28e-09 |
|
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: 58.49 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 6 ELQNIVLQADRPLVHGVSLALRRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGAILADGQPISpcklrgIKVATIM 85
Cdd:TIGR01257 1942 ELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTT----FKMLTGDTTVTSGDATVAGKSIL------TNISDVH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 86 QN----PR-SAFNPLHTMAAHAKETCLASGKPADDATLIA--ALEAVGLE-NAARVLKLYpfemSGGMLQRMMIAMALLC 157
Cdd:TIGR01257 2012 QNmgycPQfDAIDDLLTGREHLYLYARLRGVPAEEIEKVAnwSIQSLGLSlYADRLAGTY----SGGNKRKLSTAIALIG 2087
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501085142 158 DAPFIIADEPTTDLDVVAQARILDLLESIMRS-RApgMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETL 228
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREgRA--VVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-232 |
1.76e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.04 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAaalgiLPAGVRQ-TAGAILADGQPISPCKLRGIKVA 82
Cdd:PRK11432 7 VVLKNITKRfGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLR-----LVAGLEKpTEGQIFIDGEDVTHRSIQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 83 TIMQNprSAFNPLHTMAAHAKETCLASGKPADD--ATLIAALEAVGLENAArvlKLYPFEMSGGMLQRMMIAMALLCDAP 160
Cdd:PRK11432 82 MVFQS--YALFPHMSLGENVGYGLKMLGVPKEErkQRVKEALELVDLAGFE---DRYVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501085142 161 FIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTP 232
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-199 |
1.86e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.04 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPIspcklRGIKVATIMQ--NPRSAF 92
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP----AAGTIKLDGGDI-----DDPDVAEACHylGHRNAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 NPLHTMA------AHAKETclasgkpaDDATLIAALEAVGLENAARVlklyPF-EMSGGMLQRMMIAMALLCDAPFIIAD 165
Cdd:PRK13539 85 KPALTVAenlefwAAFLGG--------EELDIAAALEAVGLAPLAHL----PFgYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|....*
gi 501085142 166 EPTTDLDVVAQARILDLLESimRSRAPGM-LLVTH 199
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRA--HLAQGGIvIAATH 185
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
140-214 |
2.03e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.49 E-value: 2.03e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501085142 140 EMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDV---VAQARILDLLESIMRSrapgMLLVTHDMGVVARLADDVAVM 214
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIyqrLNVARLIRELAEEGKY----VLVVEHDLAILDYLADYVHIL 285
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-232 |
7.49e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.87 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 13 QADRPLVHGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQPISPCKL---RGiKVATIMQNPr 89
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSEGDIRFHDIPLTKLQLdswRS-RLAVVSQTP- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 90 saFNPLHTMAAHaketcLASGKPadDATliaaleAVGLENAAR-------VLKL---YPFE-------MSGGMLQRMMIA 152
Cdd:PRK10789 399 --FLFSDTVANN-----IALGRP--DAT------QQEIEHVARlasvhddILRLpqgYDTEvgergvmLSGGQKQRISIA 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 153 MALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRApgMLLVTHDMGVVARlADDVAVMDNGKIVELGDVETLFRTP 232
Cdd:PRK10789 464 RALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRT--VIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
16-233 |
7.96e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.51 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGAILADGQPISPCKL-----RGI----KVATIMQ 86
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP----RDAGNIIIDDEDISLLPLhararRGIgylpQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 87 NpRSAFNPLhtMAAHAKETCLASGKPADDAT-LIAALEAVGLENAARVlklypfEMSGGMLQRMMIAMALLCDAPFIIAD 165
Cdd:PRK10895 92 R-LSVYDNL--MAVLQIRDDLSAEQREDRANeLMEEFHIEHLRDSMGQ------SLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501085142 166 EPTTDLDVVAQARILDLLESiMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQ 233
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-219 |
1.02e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.06 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 22 VSLALRRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGAILADGQPISPCKLRGIKVATIMQNP--RSAFNpLHTMA 99
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRP----ARGGRIMLNGKEINALSTAQRLARGLVYLPedRQSSG-LYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 100 AHAKETC-LASGKP-------ADDATLIAALEAVGL-----ENAARVLklypfemSGGMLQRMMIAMALLCDAPFIIADE 166
Cdd:PRK15439 357 PLAWNVCaLTHNRRgfwikpaRENAVLERYRRALNIkfnhaEQAARTL-------SGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501085142 167 PTTDLDVVAQARILDLLESIMRSRApGMLLVTHDMGVVARLADDVAVMDNGKI 219
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQNV-AVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-218 |
1.91e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.55 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 1 MPQQIELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGVRQtaGAILADGQPispcklrgI 79
Cdd:PRK13549 2 MEYLLEMKNITKTfGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYE--GEIIFEGEE--------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 KVATIMQNPRSAFNPLHTMAAHAKETCLA-----------SGKPADDATLIAA---LEAVGLE--NAARVLKLypfemSG 143
Cdd:PRK13549 72 QASNIRDTERAGIAIIHQELALVKELSVLeniflgneitpGGIMDYDAMYLRAqklLAQLKLDinPATPVGNL-----GL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 144 GMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESiMRSRAPGMLLVTHDMGVVARLADDVAVMDNGK 218
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRD-LKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-228 |
3.17e-08 |
|
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: 53.68 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGVRQtaGAILADGQPISPCKLRGIKVATI-MQNPRSAFNPLHT 97
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWD--GEIYWSGSPLKASNIRDTERAGIvIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 98 MAAH---AKETCLASGKPADDATLIAALE-----AVGLENAARVLKlypfEMSGGMLQRMMIAMALLCDAPFIIADEPTT 169
Cdd:TIGR02633 95 VAENiflGNEITLPGGRMAYNAMYLRAKNllrelQLDADNVTRPVG----DYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501085142 170 DLDVVAQARILDLLESiMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETL 228
Cdd:TIGR02633 171 SLTEKETEILLDIIRD-LKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
140-214 |
4.35e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.37 E-value: 4.35e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501085142 140 EMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDV---VAQARILDLLESIMRSrapgMLLVTHDMGVVARLADDVAVM 214
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrLNAARLIRELAEDDNY----VLVVEHDLAVLDYLSDYIHCL 212
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
19-246 |
5.48e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.82 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSgksltcAAALGILPAGVRQTAGAILADGQPISPCKLRGIKVATIMQNP-----RSAFN 93
Cdd:NF000106 29 VDGVDLDVREGTVLGVLGP*GA------A**RGALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPvr*grRESFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 plhtmaahAKETCLASGKPAD----DATLIA--ALEAVGL-ENAARVLKLYpfemSGGMLQRMMIAMALLCDAPFIIADE 166
Cdd:NF000106 103 --------GRENLYMIGR*LDlsrkDARARAdeLLERFSLtEAAGRAAAKY----SGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 167 PTTDLDVVAQARILDLLESIMRSRAPgMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETLfRTPQHSVTRNLVSAHLA 246
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDGAT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL-KTKVGGRTLQIRPAHAA 248
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-219 |
5.53e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 17 PLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGAILADGQPISPcklrgikvatimQNPRSAF-NPL 95
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP----RTSGYVTLDGHEVVT------------RSPQDGLaNGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 96 HTMAAHAKETCLASGKPADDATLIAALE-----AVGLENAARVLKLYPF----------------EMSGGMLQRMMIAMA 154
Cdd:PRK10762 330 VYISEDRKRDGLVLGMSVKENMSLTALRyfsraGGSLKHADEQQAVSDFirlfniktpsmeqaigLLSGGNQQKVAIARG 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501085142 155 LLCDAPFIIADEPTTDLDVVAQARILDLlesIMRSRAPGM--LLVTHDMGVVARLADDVAVMDNGKI 219
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIYQL---INQFKAEGLsiILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-221 |
5.68e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 21 GVSLALRRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGAILADGQPISpcklrgikvatiMQNPRSAFNP----- 94
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKS----TLLKIL-SGNYQpDAGSILIDGQEMR------------FASTTAALAAgvaii 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 95 ---LHT---MAAhAKETCL----ASGKPADDATLIA----ALEAVGLE-NAARVLKlypfEMSGGMLQRMMIAMALLCDA 159
Cdd:PRK11288 85 yqeLHLvpeMTV-AENLYLgqlpHKGGIVNRRLLNYeareQLEHLGVDiDPDTPLK----YLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 160 PFIIADEPTTDLdvvaQARILDLLESIMRS-RAPG--MLLVTHDMGVVARLADDVAVMDNGKIVE 221
Cdd:PRK11288 160 RVIAFDEPTSSL----SAREIEQLFRVIRElRAEGrvILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-228 |
8.45e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 8.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 1 MPQQIELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGAILADGQP---ISPCKL 76
Cdd:PRK15439 8 APPLLCARSISKQySGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVP----PDSGTLEIGGNPcarLTPAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 77 RGIKVATIMQNPRSAFNplhtmaAHAKET-CLASGKPADDATLIAALeavgLENAARVLKLypfEMSGGML-----QRMM 150
Cdd:PRK15439 84 HQLGIYLVPQEPLLFPN------LSVKENiLFGLPKRQASMQKMKQL----LAALGCQLDL---DSSAGSLevadrQIVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501085142 151 IAMALLCDAPFIIADEPTTDLDVVAQARILDLLESiMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETL 228
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASLTPAETERLFSRIRE-LLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-227 |
1.84e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 22 VSLALRRGRVLALVGGSGSGKSlTCAAAL-GILPAGvrQTAGAILADGQpisPCKLRGIK------VATIMQnpRSAFNP 94
Cdd:NF040905 20 VNLSVREGEIHALCGENGAGKS-TLMKVLsGVYPHG--SYEGEILFDGE---VCRFKDIRdsealgIVIIHQ--ELALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 95 LHTMAahakETCLASGKPAD------DATLIAA---LEAVGL-EN-AARVLKLypfemsG-GMLQRMMIAMALLCDAPFI 162
Cdd:NF040905 92 YLSIA----ENIFLGNERAKrgvidwNETNRRArelLAKVGLdESpDTLVTDI------GvGKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501085142 163 IADEPTTDLDVVAQARILDLLesiMRSRAPGM--LLVTHDMGVVARLADDVAVMDNGKIVELGDVET 227
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLL---LELKAQGItsIIISHKLNEIRRVADSITVLRDGRTIETLDCRA 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-239 |
1.85e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 17 PLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGAILADGQPISPCKLRGIK--VATIMQNP-----R 89
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRI----VELEKGRIMIDDCDVAKFGLTDLRrvLSIIPQSPvlfsgT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 90 SAFNpLHTMAAHaketclasgkpaDDATLIAALEAVGLENAARV----LKLYPFE----MSGGMLQRMMIAMALLCDAPF 161
Cdd:PLN03232 1326 VRFN-IDPFSEH------------NDADLWEALERAHIKDVIDRnpfgLDAEVSEggenFSVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 162 IIADEPTTDLDVvaqaRILDLLESIMRS--RAPGMLLVTHDMGVVARlADDVAVMDNGKIVElgdvetlFRTPQHSVTRN 239
Cdd:PLN03232 1393 LVLDEATASVDV----RTDSLIQRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLE-------YDSPQELLSRD 1460
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
140-215 |
1.86e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.86e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501085142 140 EMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDV---VAQARIldlLESIMRSRAPGMLLVTHDMGVVARLADDVAVMD 215
Cdd:PRK13409 453 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrLAVAKA---IRRIAEEREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
140-215 |
2.91e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.94 E-value: 2.91e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501085142 140 EMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDV---VAQARIldlLESIMRSRAPGMLLVTHDMGVVARLADDVAVMD 215
Cdd:COG1245 455 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrLAVAKA---IRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-214 |
3.94e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.57 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvRQTAGAILADGQPISPcklrgikVATIMQnprsafnpl 95
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG--TPVAGCVDVPDNQFGR-------EASLID--------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 96 htmaahaketCLASGKPADDAtlIAALEAVGLENAARVLKLYPfEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVa 175
Cdd:COG2401 105 ----------AIGRKGDFKDA--VELLNAVGLSDAVLWLRRFK-ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501085142 176 QARILDL-LESIMRSRAPGMLLVTHDMGVVARLADDVAVM 214
Cdd:COG2401 171 TAKRVARnLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-228 |
4.01e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.89 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQADR---PLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGAILADGQPISPCKLRGIK- 80
Cdd:PLN03130 1238 IKFEDVVLRYRPelpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRI----VELERGRILIDGCDISKFGLMDLRk 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 81 -VATIMQNP-----RSAFNpLHTMAAHaketclasgkpaDDATLIAALEAVGLENAARV----LKLYPFE----MSGGML 146
Cdd:PLN03130 1314 vLGIIPQAPvlfsgTVRFN-LDPFNEH------------NDADLWESLERAHLKDVIRRnslgLDAEVSEagenFSVGQR 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 147 QRMMIAMALLCDAPFIIADEPTTDLDVVAQArildLLESIMRS--RAPGMLLVTHDMGVVARlADDVAVMDNGKIVELGD 224
Cdd:PLN03130 1381 QLLSLARALLRRSKILVLDEATAAVDVRTDA----LIQKTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDT 1455
|
....
gi 501085142 225 VETL 228
Cdd:PLN03130 1456 PENL 1459
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-200 |
6.92e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 6 ELQNIVLQ-ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvrqtagailadgQPISPCKLRGIK--VA 82
Cdd:PRK11147 321 EMENVNYQiDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQL---------------QADSGRIHCGTKleVA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 83 TIMQNpRSAFNPLHTM---AAHAKETCLASGK--------------PADDATLIAALeavglenaarvlklypfemSGGM 145
Cdd:PRK11147 386 YFDQH-RAELDPEKTVmdnLAEGKQEVMVNGRprhvlgylqdflfhPKRAMTPVKAL-------------------SGGE 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 146 LQRMMIAMALLCDAPFIIADEPTTDLDVvaqaRILDLLESIMRSRAPGMLLVTHD 200
Cdd:PRK11147 446 RNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-204 |
1.26e-06 |
|
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: 47.87 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQPISPCK------LRGIKVATIMQNPR 89
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKT----TLLRILAGLSPPLAGRVLLNGGPLDFQRdsiargLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 90 SAFNPLHTMAA-HAKETCLasgkpaddatliAALEAVGLenaaRVLKLYPF-EMSGGMLQRMMIAMALLCDAPFIIADEP 167
Cdd:cd03231 89 SVLENLRFWHAdHSDEQVE------------EALARVGL----NGFEDRPVaQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 501085142 168 TTDLDVVAQARILDLLESimRSRAPGMLLVT--HDMGVV 204
Cdd:cd03231 153 TTALDKAGVARFAEAMAG--HCARGGMVVLTthQDLGLS 189
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-189 |
1.39e-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: 47.62 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAgvRQTAGAI----LADGQPISPCKLRGIkvATIMQNPrs 90
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKT----TLLDVLAG--RKTAGVItgeiLINGRPLDKNFQRST--GYVEQQD-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 91 AFNPLHTMaahaKETCLASgkpaddatliAALEAVGLENAARVlklypfemsggmlqrmMIAMALLCDAPFIIADEPTTD 170
Cdd:cd03232 89 VHSPNLTV----REALRFS----------ALLRGLSVEQRKRL----------------TIGVELAAKPSILFLDEPTSG 138
|
170
....*....|....*....
gi 501085142 171 LDVVAQARILDLLESIMRS 189
Cdd:cd03232 139 LDSQAAYNIVRFLKKLADS 157
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-243 |
1.82e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 17 PLV-HGVSLALRRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGAILADGQPISPCKLRGIK--VATIMQNP----- 88
Cdd:PTZ00243 1323 PLVlRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRM----VEVCGGEIRVNGREIGAYGLRELRrqFSMIPQDPvlfdg 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 89 --RSAFNPLhtmaahaketclasgKPADDATLIAALEAVGL-ENAA--------RVLKlYPFEMSGGMLQRMMIAMALLC 157
Cdd:PTZ00243 1399 tvRQNVDPF---------------LEASSAEVWAALELVGLrERVAsesegidsRVLE-GGSNYSVGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 158 -DAPFIIADEPTTDLDVVAQARILDLLESIMRsrAPGMLLVTHDMGVVARLaDDVAVMDNGKIVELGDVETLFRTPQhSV 236
Cdd:PTZ00243 1463 kGSGFILMDEATANIDPALDRQIQATVMSAFS--AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQ-SI 1538
|
....*..
gi 501085142 237 TRNLVSA 243
Cdd:PTZ00243 1539 FHSMVEA 1545
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-219 |
1.84e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 16 RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPaGVRQtaGAILADGQPISpcklrgikvatiMQNPRSAFNpl 95
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP-GRWE--GEIFIDGKPVK------------IRNPQQAIA-- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 96 HTMA---------------AHAKETCLASGKPADDATLI-AALEAVGLENAARVLKL---YPF----EMSGGMLQRMMIA 152
Cdd:PRK13549 338 QGIAmvpedrkrdgivpvmGVGKNITLAALDRFTGGSRIdDAAELKTILESIQRLKVktaSPElaiaRLSGGNQQKAVLA 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501085142 153 MALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRsRAPGMLLVTHDMGVVARLADDVAVMDNGKI 219
Cdd:PRK13549 418 KCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-229 |
2.14e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.18 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 4 QIELQNIVL--QADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGAILADGQPISPCKLRGIK- 80
Cdd:PRK10790 340 RIDIDNVSFayRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL----TEGEIRLDGRPLSSLSHSVLRq 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 81 -VATIMQNPRsafnplhTMAahakETCLAS---GKPADDATLIAALEAVGLENAARVLK--LY-PFEMSGGML---QRMM 150
Cdd:PRK10790 416 gVAMVQQDPV-------VLA----DTFLANvtlGRDISEEQVWQALETVQLAELARSLPdgLYtPLGEQGNNLsvgQKQL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 151 IAMA-LLCDAPFI-IADEPTTDLDVVAQARILDLLESImRSRAPgMLLVTHDMGVVARlADDVAVMDNGKIVELGDVETL 228
Cdd:PRK10790 485 LALArVLVQTPQIlILDEATANIDSGTEQAIQQALAAV-REHTT-LVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
.
gi 501085142 229 F 229
Cdd:PRK10790 562 L 562
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
13-229 |
2.22e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.40 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 13 QADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGAILADGQpispcklrgikVATImqnPRSAF 92
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEM----DKVEGHVHMKGS-----------VAYV---PQQAW 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 NPLHTMaahaKETCLAsGKPADDATLIAALEAVGLENAarvLKLYP-----------FEMSGGMLQRMMIAMALLCDAPF 161
Cdd:TIGR00957 710 IQNDSL----RENILF-GKALNEKYYQQVLEACALLPD---LEILPsgdrteigekgVNLSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501085142 162 IIADEPTTDLDVVAQARILDLL---ESIMRSRApgMLLVTHDMGVVARLaDDVAVMDNGKIVELGDVETLF 229
Cdd:TIGR00957 782 YLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKT--RILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 849
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-218 |
3.05e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.91 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 19 VHGVSLALRRGRVLALVGGSGSGKS--LTCaaalgiLPAGVRQTAGAILADGQPISpcKLRGIKVATI-----MQNPRsA 91
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTtvFNC------LTGFYKPTGGTILLRGQHIE--GLPGHQIARMgvvrtFQHVR-L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 92 FNPLHTMaahakETCLASGKPADDATLIAAL---------EAVGLENAARVLK---LYPF------EMSGGMLQRMMIAM 153
Cdd:PRK11300 92 FREMTVI-----ENLLVAQHQQLKTGLFSGLlktpafrraESEALDRAATWLErvgLLEHanrqagNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 154 ALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGK 218
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
128-233 |
3.16e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.33 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 128 ENAARVLKL------YPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLD----VVAQARILDLLESIMRSrapgMLLV 197
Cdd:PRK11000 115 NQVAEVLQLahlldrKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRLGRT----MIYV 190
|
90 100 110
....*....|....*....|....*....|....*.
gi 501085142 198 THDMGVVARLADDVAVMDNGKIVELGDVETLFRTPQ 233
Cdd:PRK11000 191 THDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
140-250 |
3.33e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 140 EMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNgki 219
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG--- 147
|
90 100 110
....*....|....*....|....*....|.
gi 501085142 220 vELGdVETLFRTPQHsvTRNLVSAHLALYGM 250
Cdd:cd03222 148 -EPG-VYGIASQPKG--TREGINRFLRGYLI 174
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
140-215 |
4.71e-06 |
|
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: 46.63 E-value: 4.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501085142 140 EMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMD 215
Cdd:cd03237 115 ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-232 |
6.82e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 46.48 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQAD-RPLVHGVSLALRRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGAILADGQPIS--PCKLRgiK 80
Cdd:PRK09452 15 VELRGISKSFDgKEVISNLDLTINNGEFLTLLGPSGCGKT----TVLRLI-AGFETpDSGRIMLDGQDIThvPAENR--H 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 81 VATIMQNprSAFNPLHTMAAHaketcLASG-----KPADDAT--LIAALEAVGLENAARvlkLYPFEMSGGMLQRMMIAM 153
Cdd:PRK09452 88 VNTVFQS--YALFPHMTVFEN-----VAFGlrmqkTPAAEITprVMEALRMVQLEEFAQ---RKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 154 ALLCDAPFIIADEPTTDLDvvAQARILDLLESIMRSRAPGM--LLVTHDMGVVARLADDVAVMDNGKIVELGDVETLFRT 231
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALD--YKLRKQMQNELKALQRKLGItfVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 235
|
.
gi 501085142 232 P 232
Cdd:PRK09452 236 P 236
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
136-219 |
7.29e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.66 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 136 LYPFE------MSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESImRSRAPGM-LLV-THDMGVVARL 207
Cdd:NF033858 126 LAPFAdrpagkLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRI-RAERPGMsVLVaTAYMEEAERF 204
|
90
....*....|..
gi 501085142 208 aDDVAVMDNGKI 219
Cdd:NF033858 205 -DWLVAMDAGRV 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
13-218 |
7.83e-06 |
|
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: 45.54 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 13 QADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGAI-LADGQPIspcklrgIKVATIMQNpr 89
Cdd:cd03250 15 QETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKlsGSVSVPGSIaYVSQEPW-------IQNGTIREN-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 90 safnplhtmaahaketcLASGKPADDATLIAALEAVGLEnaaRVLKLYPF-------E----MSGGMLQRMMIAMALLCD 158
Cdd:cd03250 86 -----------------ILFGKPFDEERYEKVIKACALE---PDLEILPDgdlteigEkginLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501085142 159 APFIIADEPTTDLDVVAQARILD--LLESIMRSRApgMLLVTHDMGVVARlADDVAVMDNGK 218
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKT--RILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
140-220 |
8.13e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 140 EMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAqariLDLLESIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKI 219
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
.
gi 501085142 220 V 220
Cdd:PRK11147 232 V 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-220 |
8.78e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.44 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 18 LVHGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADGQPISPCKLRGIKVATIMQNP--RSA--FN 93
Cdd:PRK11288 268 LREPISFSVRAGEIVGLFGLVGAGRS----ELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPedRKAegII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 PLHTMA---------AHAKETCLASGK-PADDA-TLIAALeAVGLENAARVLKLypfeMSGGMLQRMMIAMALLCDAPFI 162
Cdd:PRK11288 344 PVHSVAdninisarrHHLRAGCLINNRwEAENAdRFIRSL-NIKTPSREQLIMN----LSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501085142 163 IADEPTTDLDVVAQARILDLL-ESIMRSRApgMLLVTHDMGVVARLADDVAVMDNGKIV 220
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIyELAAQGVA--VLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-228 |
1.46e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 13 QADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvrqtagaiLADGQPIspckLRGiKVATIMQnPRSAF 92
Cdd:PLN03130 627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP---------RSDASVV----IRG-TVAYVPQ-VSWIF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 93 NplhtmaAHAKETCLAsGKPADDATLIAALEAVGLEnaaRVLKLYP-----------FEMSGGMLQRMMIAMALLCDAPF 161
Cdd:PLN03130 692 N------ATVRDNILF-GSPFDPERYERAIDVTALQ---HDLDLLPggdlteigergVNISGGQKQRVSMARAVYSNSDV 761
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501085142 162 IIADEPTTDLDV-VAQARILDLLESIMRSRApgMLLVTHDMGVVARLaDDVAVMDNGKIVELGDVETL 228
Cdd:PLN03130 762 YIFDDPLSALDAhVGRQVFDKCIKDELRGKT--RVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEEL 826
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
147-225 |
2.10e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 147 QRMMIAMALLCDAPFIIADEPTTDLdvvAQARIlDLLESIM---RSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELG 223
Cdd:PRK09700 152 QMLEIAKTLMLDAKVIIMDEPTSSL---TNKEV-DYLFLIMnqlRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
..
gi 501085142 224 DV 225
Cdd:PRK09700 228 MV 229
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-184 |
2.29e-05 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 43.68 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 5 IELQNIVLQ--ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtagailaDGQPISPCKlrgikva 82
Cdd:cd03223 1 IELENLSLAtpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG----------SGRIGMPEG------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 83 timqnPRSAFNPLHTMaahaketcLASGkpaddaTLIAALeavglenaarvlkLYPFEM--SGGMLQRMMIAMALLCDAP 160
Cdd:cd03223 64 -----EDLLFLPQRPY--------LPLG------TLREQL-------------IYPWDDvlSGGEQQRLAFARLLLHKPK 111
|
170 180
....*....|....*....|....
gi 501085142 161 FIIADEPTTDLDVVAQARILDLLE 184
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLK 135
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-217 |
2.78e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 43.86 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 14 ADRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALG---ILPAGVRQTAGAILADGQPISPCKLRGiKVATIMQNPrs 90
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGemqTLEGKVHWSNKNESEPSFEATRSRNRY-SVAYAAQKP-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 91 afnplHTMAAHAKETcLASGKPADDATLIAALEAVGLENAarvLKLYPF-----------EMSGGMLQRMMIAMALLCDA 159
Cdd:cd03290 89 -----WLLNATVEEN-ITFGSPFNKQRYKAVTDACSLQPD---IDLLPFgdqteigergiNLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501085142 160 PFIIADEPTTDLDV-----VAQARILDLLESIMRSrapgMLLVTHDMGVVARlADDVAVMDNG 217
Cdd:cd03290 160 NIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKRT----LVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
141-245 |
3.03e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 141 MSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRsRAPGMLLVTHDMGVVARLADDVAVMDNGKIV 220
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
90 100
....*....|....*....|....*
gi 501085142 221 elGDVETLfRTPQHSVTRnLVSAHL 245
Cdd:PRK10982 471 --GIVDTK-TTTQNEILR-LASLHL 491
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
148-211 |
5.14e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.98 E-value: 5.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501085142 148 RMMIAMALLCDAPFIIADEPTTDLDV--VAQArILDLLESIMRSRAPGMLLVTHDMGVVaRLADDV 211
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLDEenIEES-LAEIIEERKSQKNFQLIVITHDEELV-DAADHI 192
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-223 |
8.14e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 43.33 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILPAgvRQTAGAILADGQPISPCKLRGIKVAT----------- 83
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQG--NNFTGTILANNRKPTKQILKRTGFVTqddilyphltv 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 84 --------IMQNPRSAFNPLHTMAAHaketclasgkpaddaTLIAALEAVGLENAArVLKLYPFEMSGGMLQRMMIAMAL 155
Cdd:PLN03211 158 retlvfcsLLRLPKSLTKQEKILVAE---------------SVISELGLTKCENTI-IGNSFIRGISGGERKRVSIAHEM 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501085142 156 LCDAPFIIADEPTTDLDVVAQARILDLLESIMRSrapGMLLVT---HDMGVVARLADDVAVMDNGKIVELG 223
Cdd:PLN03211 222 LINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK---GKTIVTsmhQPSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-228 |
1.54e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 22 VSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGAILADGQPIS---------------PCKLRGIKVATIMQ 86
Cdd:PRK10982 17 VNLKVRPHSIHALMGENGAGKSTLLKCLFGIY----QKDSGSILFQGKEIDfksskealengismvHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 87 NPRSAFNPLhtmaahaKETCLASGKPADDATLIAALEAVGLENAARVLKLYPFEMsggmlQRMMIAMALLCDAPFIIADE 166
Cdd:PRK10982 93 NMWLGRYPT-------KGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQM-----QMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501085142 167 PTTDL---DVVAQARILDLLesimRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELGDVETL 228
Cdd:PRK10982 161 PTSSLtekEVNHLFTIIRKL----KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-73 |
2.70e-04 |
|
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: 41.71 E-value: 2.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501085142 2 PQQIELQNIV-----LQADRPLVHG-VSLALRRGRVLALVGGSGSGKSlTCAAAL-GILPAgvrqTAGAILADGQPISP 73
Cdd:COG4615 325 FQTLELRGVTyrypgEDGDEGFTLGpIDLTIRRGELVFIVGGNGSGKS-TLAKLLtGLYRP----ESGEILLDGQPVTA 398
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-232 |
2.88e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 41.37 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 4 QIELQNIVLQ--ADRPLVHGVSLALRRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGAILADGQPIS---PcKLR 77
Cdd:PRK11650 3 GLKLQAVRKSydGKTQVIKGIDLDVADGEFIVLVGPSGCGKS-----TLLRMVAGLERiTSGEIWIGGRVVNeleP-ADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 78 GIkvATIMQNprSAFNPLHT----MAAHAKetclASGKPADDatlIAALeavgLENAARVLKLYPF------EMSGGmlQ 147
Cdd:PRK11650 77 DI--AMVFQN--YALYPHMSvrenMAYGLK----IRGMPKAE---IEER----VAEAARILELEPLldrkprELSGG--Q 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 148 RMMIAM--ALLCDAPFIIADEPTTDLDvvAQARILDLLE--SIMRSRAPGMLLVTHDMGVVARLADDVAVMDNGKIVELG 223
Cdd:PRK11650 140 RQRVAMgrAIVREPAVFLFDEPLSNLD--AKLRVQMRLEiqRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIG 217
|
....*....
gi 501085142 224 DVETLFRTP 232
Cdd:PRK11650 218 TPVEVYEKP 226
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
15-199 |
3.30e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 40.70 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 15 DRPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGAILADGQPISPcKLRGIKVATIMQNPRSAFNP 94
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLL----NPEKGEILFERQSIKK-DLCTYQKQLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 95 LHTMaahaKETCLASgkpaddatLIAALEAVGLENAARVLKL-----YPFE-MSGGMLQRMMIAMALLCDAPFIIADEPT 168
Cdd:PRK13540 88 YLTL----RENCLYD--------IHFSPGAVGITELCRLFSLehlidYPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|...
gi 501085142 169 TDLDVVAqarILDLLESIMRSRAPG--MLLVTH 199
Cdd:PRK13540 156 VALDELS---LLTIITKIQEHRAKGgaVLLTSH 185
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
218-243 |
4.81e-04 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 38.11 E-value: 4.81e-04
10 20
....*....|....*....|....*.
gi 501085142 218 KIVELGDVETLFRTPQHSVTRNLVSA 243
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSA 26
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-232 |
1.32e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.76 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 18 LVHGVSLALRRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGAILADgqpispcklRGI----KVATIMqNPRSAFN 93
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKS----TLLQSLLSQFEISEGRVWAE---------RSIayvpQQAWIM-NATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 94 PL---HTMAAHAKETCLASGKPADDATLIAALEAVGLENAArvlklypfEMSGGMLQRMMIAMALLCDAPFIIADEPTTD 170
Cdd:PTZ00243 741 ILffdEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGV--------NLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501085142 171 LDVVAQARIldlLESIMRSRAPGM--LLVTHDMGVVARlADDVAVMDNGKIVELGDVETLFRTP 232
Cdd:PTZ00243 813 LDAHVGERV---VEECFLGALAGKtrVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-244 |
1.36e-03 |
|
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: 39.12 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 4 QIELQNIVLQAD---RPLVHGVSLALRRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGAILADGQPISPCKLRGI- 79
Cdd:cd03288 19 EIKIHDLCVRYEnnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRM----VDIFDGKIVIDGIDISKLPLHTLr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 80 -KVATIMQNPrsafnplhTMAAHAKETCLASGKPADDATLIAALEAVGLENaarVLKLYPFEM-----------SGGMLQ 147
Cdd:cd03288 95 sRLSIILQDP--------ILFSGSIRFNLDPECKCTDDRLWEALEIAQLKN---MVKSLPGGLdavvteggenfSVGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 148 RMMIAMALLCDAPFIIADEPTTDLDVVAQarilDLLESIMRSRAPGMLLVTHDMGVVARL-ADDVAVMDNGKIVELGDVE 226
Cdd:cd03288 164 LFCLARAFVRKSSILIMDEATASIDMATE----NILQKVVMTAFADRTVVTIAHRVSTILdADLVLVLSRGILVECDTPE 239
|
250
....*....|....*...
gi 501085142 227 TLFrTPQHSVTRNLVSAH 244
Cdd:cd03288 240 NLL-AQEDGVFASLVRTD 256
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-222 |
2.64e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 38.76 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 11 VLQADRPLVHGVSLALRRGRVLALVGGSGSGKSltcaAALGILpAGVRQ--TAGAILADGqpispcklrgIKVATIMQNP 88
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKS----TLLRIM-AGVDKdfNGEARPQPG----------IKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 89 RsaFNPLHTMAAHAKETC--------------LASGKPADD--------ATLIAALEAVG-------LENAARVLKLYPF 139
Cdd:TIGR03719 78 Q--LDPTKTVRENVEEGVaeikdaldrfneisAKYAEPDADfdklaaeqAELQEIIDAADawdldsqLEIAMDALRCPPW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 140 E-----MSGGMLQRMMIAmALLCDAP-FIIADEPTTDLDvvaqARILDLLESIMRSRAPGMLLVTHDmgvvaR-LADDVA 212
Cdd:TIGR03719 156 DadvtkLSGGERRRVALC-RLLLSKPdMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD-----RyFLDNVA 225
|
250
....*....|
gi 501085142 213 vmdnGKIVEL 222
Cdd:TIGR03719 226 ----GWILEL 231
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
142-200 |
3.04e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 38.61 E-value: 3.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 501085142 142 SGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAqariLDLLESIMRSRAPGMLLVTHD 200
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA----VIWLEKWLKSYQGTLILISHD 205
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
136-211 |
3.66e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.48 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 136 LYPFEMSGGmlQRMMIAMALLC------------DAPF--IIADEPTTDLDVVAQARILDLLESiMRSRAPG-MLLVTHD 200
Cdd:PRK02224 777 LEPEQLSGG--ERALFNLSLRCaiyrllaegiegDAPLppLILDEPTVFLDSGHVSQLVDLVES-MRRLGVEqIVVVSHD 853
|
90
....*....|.
gi 501085142 201 MGVVARlADDV 211
Cdd:PRK02224 854 DELVGA-ADDL 863
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
137-216 |
3.91e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.47 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085142 137 YPFEMSGGMLQRMMIAMALLCDAPFIIADEPTTDLDVVAQARILDLLESIMRSRAPGMLLVTHDMGVVARlADDVAVMDN 216
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNN 1433
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
141-208 |
4.12e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 36.95 E-value: 4.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501085142 141 MSGGMLQRMMIAMAL----LCDAPFIIADEPTTDLDVVAQARILDLlesIMRSRAPG--MLLVTHDMGVVARLA 208
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEA---ILEHLVKGaqVIVITHLPELAELAD 148
|
|
| |
