|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-326 |
5.82e-169 |
|
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: 472.23 E-value: 5.82e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhVHHGRVTLLGEDVLNASEK 84
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPG--ITSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQWRGARVAMIFQEPMTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAQVMDRYPFELSGGMRQR 164
Cdd:COG0444 79 ELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 165 VMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTL 244
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 245 IHHPVHPYSIGLLRCAPENGEPREILPAIPGTVPNLSHLPRGCAFRERCFAAGAKCSET-PRLISTGaEGQQAACWYPQQ 323
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEePPLREVG-PGHRVACHLYEE 317
|
...
gi 505383390 324 ETR 326
Cdd:COG0444 318 EAP 320
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-274 |
2.96e-133 |
|
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: 389.43 E-value: 2.96e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSYHVHhGRVTLLGEDVLN 80
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPS-GSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQLRQWRGARVAMIFQEPMTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAQVMDRYPFELSGG 160
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 161 MRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGI 240
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250 260 270
....*....|....*....|....*....|....
gi 505383390 241 TQTLIHHPVHPYSIGLLRCAPEnGEPREILPAIP 274
Cdd:COG4172 241 TAELFAAPQHPYTRKLLAAEPR-GDPRPVPPDAP 273
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-324 |
1.81e-118 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 344.79 E-value: 1.81e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLpeGSYHVHHGRVTLLGEDVLN 80
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL--AANGRIGGSATFNGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQLRQWRGARVAMIFQEPMTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAQVMDRYPFELSGG 160
Cdd:PRK09473 86 LPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 161 MRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGI 240
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 241 TQTLIHHPVHPYSIGLLRCAPENGEPREILPAIPGTVPNLSHLPRGCAFRERCFAAGAKCSETPRLISTGaEGQQAACWY 320
Cdd:PRK09473 246 ARDVFYQPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSSAPPLEEFG-PGRLRACFK 324
|
....
gi 505383390 321 PQQE 324
Cdd:PRK09473 325 PVEE 328
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-239 |
1.20e-111 |
|
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: 323.30 E-value: 1.20e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEK 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTS-----GSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRqWRGARVAMIFQEPMTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLgEMQIPDAAQVMDRYPFELSGGMRQR 164
Cdd:cd03257 76 LRK-IRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLL-LVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 165 VMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-262 |
1.81e-96 |
|
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: 294.89 E-value: 1.81e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFPIF-RGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPegsyhVHHGRVTLLGEDVL 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR-----PTSGSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 80 NASEKQLRQWRGaRVAMIFQEPMTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPdaAQVMDRYPFELSG 159
Cdd:COG1123 331 KLSRRSLRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP--PDLADRYPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 160 GMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
250 260
....*....|....*....|...
gi 505383390 240 ITQTLIHHPVHPYSIGLLRCAPE 262
Cdd:COG1123 488 PTEEVFANPQHPYTRALLAAVPS 510
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-327 |
4.01e-96 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 287.78 E-value: 4.01e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFPIFRG-------DVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTL 73
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGlfgrtvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTS-----GEILF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 74 LGEDVLNASEKQLRQWRgARVAMIFQEPMTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPdaAQVMDRY 153
Cdd:COG4608 78 DGQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR--PEHADRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 154 PFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAG 233
Cdd:COG4608 155 PHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 234 SVIESGITQTLIHHPVHPYSIGLLRCAP--ENGEPREILPaIPGTVPNLSHLPRGCAFRERCFAAGAKC-SETPRLISTG 310
Cdd:COG4608 235 KIVEIAPRDELYARPLHPYTQALLSAVPvpDPERRRERIV-LEGDVPSPLNPPSGCRFHTRCPYAQDRCaTEEPPLREVG 313
|
330
....*....|....*..
gi 505383390 311 AeGQQAACWYPQQETRH 327
Cdd:COG4608 314 P-GHQVACHLAEEGSGV 329
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
6-321 |
3.53e-94 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 282.95 E-value: 3.53e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEgSYHVHHGRVTLLGEDVLNASEKQ 85
Cdd:COG4170 4 LDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD-NWHVTADRFRWNGIDLLKLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQWRGARVAMIFQEPMTALNPTRRIGRQMVEVIRQHQ---SLSRRDAQQK--AIALLGEMQIPDAAQVMDRYPFELSGG 160
Cdd:COG4170 83 RRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTfkgKWWQRFKWRKkrAIELLHRVGIKDHKDIMNSYPHELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 161 MRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGI 240
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 241 TQTLIHHPVHPYSIGLLRCAPENGEP---REILPAIPGTVPNLSHLPRGCAFRERCFAAGAKCSETPRLisTGAEGQQAA 317
Cdd:COG4170 243 TEQILKSPHHPYTKALLRSMPDFRQPlphKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVETPRL--RKIKGHEFA 320
|
....
gi 505383390 318 CWYP 321
Cdd:COG4170 321 CHFP 324
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-280 |
1.08e-91 |
|
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: 282.56 E-value: 1.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 3 DSVLSIEDLHLSFPifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhVHHGRVTLLGEDVLNAS 82
Cdd:COG1123 2 TPLLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGG--RISGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 83 EkqlrQWRGARVAMIFQEPMTALNPTRrIGRQMVEVIRQhQSLSRRDAQQKAIALLGEMQIpdaAQVMDRYPFELSGGMR 162
Cdd:COG1123 78 E----ALRGRRIGMVFQDPMTQLNPVT-VGDQIAEALEN-LGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 163 QRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQ 242
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 505383390 243 TLIHHPvhpysiGLLRCAPENGEPREILPAIPGTVPNL 280
Cdd:COG1123 229 EILAAP------QALAAVPRLGAARGRAAPAAAAAEPL 260
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-321 |
4.92e-90 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 272.00 E-value: 4.92e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 4 SVLSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPegsyhvHHGRVT-----LLGEDV 78
Cdd:PRK11022 2 ALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID------YPGRVMaekleFNGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 79 LNASEKQLRQWRGARVAMIFQEPMTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAQVMDRYPFELS 158
Cdd:PRK11022 76 QRISEKERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 159 GGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIES 238
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 239 GITQTLIHHPVHPYSIGLLRCAPENGEPREILPAIPGTVPNLSHLPRGCAFRERCFAAGAKC-SETPRLISTGaeGQQAA 317
Cdd:PRK11022 236 GKAHDIFRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCrAEEPALNMLA--GRQSK 313
|
....
gi 505383390 318 CWYP 321
Cdd:PRK11022 314 CHYP 317
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-262 |
1.01e-80 |
|
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: 254.61 E-value: 1.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFPIFRG-------DVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPegsyhvHHGRVTLLGED 77
Cdd:COG4172 275 LLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP------SEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 78 VLNASEKQLRQWRgARVAMIFQEPMTALNPTRRIGRQMVEVIRQHQ-SLSRRDAQQKAIALLGEMQIPDAAqvMDRYPFE 156
Cdd:COG4172 349 LDGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDPAA--RHRYPHE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 LSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVI 236
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
250 260
....*....|....*....|....*.
gi 505383390 237 ESGITQTLIHHPVHPYSIGLLRCAPE 262
Cdd:COG4172 506 EQGPTEQVFDAPQHPYTRALLAAAPL 531
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-267 |
1.25e-79 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 254.39 E-value: 1.25e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 2 SDSVLSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSYHVHHGRVTLLGE----- 76
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRsrqvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 77 DVLNASEKQLRQWRGARVAMIFQEPMTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAQVMDRYPFE 156
Cdd:PRK10261 89 ELSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 LSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVI 236
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260 270
....*....|....*....|....*....|.
gi 505383390 237 ESGITQTLIHHPVHPYSIGLLRCAPENGEPR 267
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVPQLGAMK 279
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-280 |
1.65e-78 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 248.85 E-value: 1.65e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSYHVHHGRVTLLGEDVLN 80
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQLRQWRGARVAMIFQEPMTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAQVMDRYPFELSGG 160
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 161 MRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGI 240
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 505383390 241 TQTLIHHPVHPYSIGLLRCAPEnGEPreiLPAIPGTVPNL 280
Cdd:PRK15134 241 AATLFSAPTHPYTQKLLNSEPS-GDP---VPLPEPASPLL 276
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-321 |
2.67e-77 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 239.70 E-value: 2.67e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMlAMRLLPEGSYHVHHGRVTLLGEDVLNASEK 84
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAK-AICGVTKDNWRVTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQWRGARVAMIFQEPMTALNPTRRIGRQMVEVI-------RQHQSLSRRdaQQKAIALLGEMQIPDAAQVMDRYPFEL 157
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgwtykgRWWQRFGWR--KRRAIELLHRVGIKDHKDAMRSFPYEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 158 SGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIE 237
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 238 SGITQTLIHHPVHPYSIGLLRCAPENGEP---REILPAIPGTVPNLSHLPRGCAFRERCFAAGAKCSETPRLisTGAEGQ 314
Cdd:PRK15093 240 TAPSKELVTTPHHPYTQALIRAIPDFGSAmphKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIETPRL--TGAKNH 317
|
....*..
gi 505383390 315 QAACWYP 321
Cdd:PRK15093 318 LYACHFP 324
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-261 |
5.85e-77 |
|
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: 235.85 E-value: 5.85e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEgsyhvHHGRVTLLGEDVLNASEKQ 85
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP-----WSGEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRqwrgARVAMIFQEPMTALNPTRRIGRQMVEVIRQHqslSRRDAQQKAIALLGEMQIPDAaqVMDRYPFELSGGMRQRV 165
Cdd:COG1124 77 FR----RRVQMVFQDPYASLHPRHTVDRILAEPLRIH---GLPDREERIAELLEQVGLPPS--FLDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 166 MIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLI 245
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|....*.
gi 505383390 246 HHPVHPYSIGLLRCAP 261
Cdd:COG1124 228 AGPKHPYTRELLAASL 243
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-318 |
5.40e-73 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 228.82 E-value: 5.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFPIFRGD---------VHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLG 75
Cdd:PRK15079 8 LLEVADLKVHFDIKDGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATD-----GEVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 76 EDVLNASEKQlrqWRGAR--VAMIFQEPMTALNPTRRIGRQMVEVIRQHQ-SLSRRDAQQKAIALLgeMQIPDAAQVMDR 152
Cdd:PRK15079 83 KDLLGMKDDE---WRAVRsdIQMIFQDPLASLNPRMTIGEIIAEPLRTYHpKLSRQEVKDRVKAMM--LKVGLLPNLINR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 153 YPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYA 232
Cdd:PRK15079 158 YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 233 GSVIESGITQTLIHHPVHPYSIGLLRCAP------ENGEPREILpaiPGTVPNLSHLPRGCAFRERCFAAGAKCSETPRL 306
Cdd:PRK15079 238 GHAVELGTYDEVYHNPLHPYTKALMSAVPipdpdlERNKTIQLL---EGELPSPINPPSGCVFRTRCPIAGPECAKTRPV 314
|
330
....*....|..
gi 505383390 307 IsTGAEGQQAAC 318
Cdd:PRK15079 315 L-EGSFRHAVSC 325
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
27-257 |
7.98e-73 |
|
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: 224.56 E-value: 7.98e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 27 HVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSYHVHhGRVTLLGEDVLNASekqlrqWRGARVAMIFQEPMTALN 106
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTS-GEILLDGRPLLPLS------IRGRHIATIMQNPRTAFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 107 PTRRIGRQMVEVIRQHQSLSRrDAQQKAIALLGEMQIPDAAQVMDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTA 186
Cdd:TIGR02770 77 PLFTMGNHAIETLRSLGKLSK-QARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505383390 187 LDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPVHPYSIGLL 257
Cdd:TIGR02770 156 LDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLL 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-323 |
8.79e-72 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 225.23 E-value: 8.79e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFPIFRG------DVHALNHVSLEIGRGEIVGVVGESGSGKSVTA-MLAMRLLPEgsyhvhHGRVTL 73
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGlfkperLVKALDGVSFTLERGKTLAVVGESGCGKSTLArLLTMIETPT------GGELYY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 74 LGEDVLNAS---EKQLRQwrgaRVAMIFQEPMTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLgemqipdaAQV- 149
Cdd:PRK11308 75 QGQDLLKADpeaQKLLRQ----KIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMM--------AKVg 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 150 -----MDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLC 224
Cdd:PRK11308 143 lrpehYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 225 DRMYVMYAGSVIESGITQTLIHHPVHPYSIGLLRCAPE-NGEPREILPAIPGTVPNLSHLPRGCAFRERCFAAGAKCS-E 302
Cdd:PRK11308 223 DEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSATPRlNPDDRRERIKLTGELPSPLNPPPGCAFNARCPRAFGRCRqE 302
|
330 340
....*....|....*....|.
gi 505383390 303 TPRLisTGAEGQQAACWYPQQ 323
Cdd:PRK11308 303 QPQL--RDYDGRLVACFAVEQ 321
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-257 |
6.19e-56 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 182.21 E-value: 6.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 4 SVLSIEDLHLSFPifRGDVHalnHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSYHVHhGRVTLLGEDVLNASe 83
Cdd:PRK10418 3 QQIELRNIALQAA--QPLVH---GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTA-GRVLLDGKPVAPCA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 84 kqlrqWRGARVAMIFQEPMTALNPTRRIGRQMVEVIRQhqsLSRRDAQQKAIALLGEMQIPDAAQVMDRYPFELSGGMRQ 163
Cdd:PRK10418 76 -----LRGRKIATIMQNPRSAFNPLHTMHTHARETCLA---LGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 164 RVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQT 243
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVET 227
|
250
....*....|....
gi 505383390 244 LIHHPVHPYSIGLL 257
Cdd:PRK10418 228 LFNAPKHAVTRSLV 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-246 |
2.55e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 179.87 E-value: 2.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLpEGSYHVHHGRVTLLGEDVlnasEKQ 85
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTT----IRML-LGLLRPTSGEVRVLGEDV----ARD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQWRgARVAMIFQEPmtALNPTRRiGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELSGGMRQRV 165
Cdd:COG1131 68 PAEVR-RRIGYVPQEP--ALYPDLT-VRENLRFFARLYGLPRKEARERIDELLELFGLTDAA---DRKVGTLSGGMKQRL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 166 MIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLI 245
Cdd:COG1131 141 GLALALLHDPELLILDEPTSGLDPEARRELWELLR-ELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
.
gi 505383390 246 H 246
Cdd:COG1131 220 A 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-237 |
2.94e-55 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 179.47 E-value: 2.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 3 DSVLSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAM--LAMRLLPEGsyhvhhGRVTLLGEDVLN 80
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLniLGGLDRPTS------GEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQLRQWRGARVAMIFQEP-----MTAL-NptrrigrqmVEVIRQHQSLSRRDAQQKAIALLGEMQIPDaaqVMDRYP 154
Cdd:COG1136 75 LSERELARLRRRHIGFVFQFFnllpeLTALeN---------VALPLLLAGVSRKERRERARELLERVGLGD---RLDHRP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 155 FELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQlCDRMYVMYAGS 234
Cdd:COG1136 143 SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGR 221
|
...
gi 505383390 235 VIE 237
Cdd:COG1136 222 IVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-230 |
1.89e-54 |
|
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: 177.30 E-value: 1.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSvT--AMLAMRLLPEgsyhvhHGRVTLLGEDVLNASE 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TllNILGGLDRPT------SGEVRVDGTDISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 84 KQLRQWRGARVAMIFQEP-----MTALnptrrigrQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAaqvMDRYPFELS 158
Cdd:cd03255 74 KELAAFRRRHIGFVFQSFnllpdLTAL--------ENVELPLLLAGVPKKERRERAEELLERVGLGDR---LNHYPSELS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505383390 159 GGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSqLCDRMYVM 230
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIEL 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-252 |
1.04e-53 |
|
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: 175.94 E-value: 1.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLL-PEgsyhvhHGRVTLLGEDVL 79
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLrPD------SGEILVDGQDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 80 NASEKQLRQWRgARVAMIFQEP-----MTAL-NptrrigrqmVEV-IRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDR 152
Cdd:COG1127 71 GLSEKELYELR-RRIGMLFQGGalfdsLTVFeN---------VAFpLREHTDLSEAEIRELVLEKLELVGLPGAA---DK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 153 YPFELSGGMRQRVMIALAFSCEPELIIADEPTTALD-VTVqRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMY 231
Cdd:COG1127 138 MPSELSGGMRKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLA 216
|
250 260
....*....|....*....|.
gi 505383390 232 AGSVIESGITQTLIHHPvHPY 252
Cdd:COG1127 217 DGKIIAEGTPEELLASD-DPW 236
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-248 |
2.10e-52 |
|
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: 172.13 E-value: 2.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQ 85
Cdd:COG1122 1 IELENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTS-----GEVLVDGKDITKKNLRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQwrgaRVAMIFQEPMTAL-NPT---------RRIGrqmvevirqhqsLSRRDAQQKAIALLGEMQIPDAAqvmDRYPF 155
Cdd:COG1122 73 LRR----KVGLVFQNPDDQLfAPTveedvafgpENLG------------LPREEIRERVEEALELVGLEHLA---DRPPH 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 156 ELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSV 235
Cdd:COG1122 134 ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLK-RLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
250
....*....|...
gi 505383390 236 IESGITQTLIHHP 248
Cdd:COG1122 213 VADGTPREVFSDY 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-260 |
2.19e-51 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 177.59 E-value: 2.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFPIFRG-------DVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEgsyhvhHGRVTLLGED 77
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS------QGEIWFDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 78 VLNASEKQLRQWRgARVAMIFQEPMTALNPTRRIGRQMVEVIRQHQ-SLSRRDAQQKAIALLGEMQI-PDAAQvmdRYPF 155
Cdd:PRK15134 349 LHNLNRRQLLPVR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMEEVGLdPETRH---RYPA 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 156 ELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSV 235
Cdd:PRK15134 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
250 260
....*....|....*....|....*
gi 505383390 236 IESGITQTLIHHPVHPYSIGLLRCA 260
Cdd:PRK15134 505 VEQGDCERVFAAPQQEYTRQLLALS 529
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-251 |
5.30e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 172.18 E-value: 5.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTamLAmRLL-----PEGsyhvhhGRVTLLGEDVLN 80
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS-T--LI-RCInllerPTS------GSVLVDGVDLTA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQLRQWRgARVAMIFQE---------------PMtalnptrrigrqmvevirQHQSLSRRDAQQKAIALLGEMQIPD 145
Cdd:COG1135 72 LSERELRAAR-RKIGMIFQHfnllssrtvaenvalPL------------------EIAGVPKAEIRKRVAELLELVGLSD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 146 AAqvmDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARAS-GTSVLFISHDMAVVSQLC 224
Cdd:COG1135 133 KA---DAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLK-DINRElGLTIVLITHEMDVVRRIC 208
|
250 260
....*....|....*....|....*..
gi 505383390 225 DRMYVMYAGSVIESGITQTLIHHPVHP 251
Cdd:COG1135 209 DRVAVLENGRIVEQGPVLDVFANPQSE 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-248 |
1.46e-49 |
|
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: 165.06 E-value: 1.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMRLLPEGSyhvhHGRVTLLGEDVLNASEK 84
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLERPT----SGSVLVDGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQWRgARVAMIFQEpMTALNptRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELSGGMRQR 164
Cdd:cd03258 76 ELRKAR-RRIGMIFQH-FNLLS--SRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKA---DAYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 165 VMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTL 244
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
....
gi 505383390 245 IHHP 248
Cdd:cd03258 229 FANP 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-252 |
2.31e-47 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 159.59 E-value: 2.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQ 85
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDS-----GEVLIDGEDISGLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQWRgARVAMIFQEP-----MTAlnptrrigRQMVEV-IRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELSG 159
Cdd:cd03261 72 LYRLR-RRMGMLFQSGalfdsLTV--------FENVAFpLREHTRLSEEEIREIVLEKLEAVGLRGAE---DLYPAELSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 160 GMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:cd03261 140 GMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
250
....*....|...
gi 505383390 240 ITQTLIHHPvHPY 252
Cdd:cd03261 220 TPEELRASD-DPL 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-233 |
3.02e-46 |
|
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: 155.70 E-value: 3.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 7 SIEDLHLSFPifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQL 86
Cdd:cd03225 1 ELKNLSFSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTS-----GEVLVDGKDLTKLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 87 RQwrgaRVAMIFQepmtalNPTRRIGRQMV--EVI--RQHQSLSRRDAQQKAIALLGEMQIPDaaqVMDRYPFELSGGMR 162
Cdd:cd03225 74 RR----KVGLVFQ------NPDDQFFGPTVeeEVAfgLENLGLPEEEIEERVEEALELVGLEG---LRDRSPFTLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505383390 163 QRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAG 233
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLK-KLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-230 |
4.06e-46 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 157.17 E-value: 4.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAM-LAMRLLPEGSyhvhhGRVTLLGEDVL 79
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS-TLLrLIAGLEKPTS-----GEVLVDGKPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 80 NAsekqlrqwrGARVAMIFQEPmtALNPTRRIgRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELSG 159
Cdd:COG1116 77 GP---------GPDRGVVFQEP--ALLPWLTV-LDNVALGLELRGVPKAERRERARELLELVGLAGFE---DAYPHQLSG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383390 160 GMRQRVMIALAFSCEPELIIADEPTTALDV----TVQRQVLRLLkhkaRASGTSVLFISHDM--AVVsqLCDRMYVM 230
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLRLW----QETGKTVLFVTHDVdeAVF--LADRVVVL 212
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-236 |
2.60e-45 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 154.44 E-value: 2.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 4 SVLSIEDLHLSFPifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASE 83
Cdd:COG3638 1 PMLELRNLSKRYP---GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTS-----GEILVDGQDVTALRG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 84 KQLRQWRgARVAMIFQEP-----MTALNP--TRRIGRqmvevIRQHQSLSR---RDAQQKAIALLGEMQIPDAAQVM-Dr 152
Cdd:COG3638 73 RALRRLR-RRIGMIFQQFnlvprLSVLTNvlAGRLGR-----TSTWRSLLGlfpPEDRERALEALERVGLADKAYQRaD- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 153 ypfELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYA 232
Cdd:COG3638 146 ---QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD 222
|
....
gi 505383390 233 GSVI 236
Cdd:COG3638 223 GRVV 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-239 |
8.43e-45 |
|
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: 153.09 E-value: 8.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLpEGSYHVHHGRVTLLGEDVlnasEK 84
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTL----LRML-AGLLKPDSGSILIDGEDV----RK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQWRgARVAMIFQEPMTalnPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDaaqVMDRYPFELSGGMRQR 164
Cdd:COG4555 68 EPREAR-RQIGVLPDERGL---YDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEE---FLDRRVGELSTGMKKK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 165 VMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDVMARRLLREILR-ALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-251 |
2.01e-44 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 154.96 E-value: 2.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 8 IEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMRLLPEGSyhvhHGRVTLLGEDVLNASEKQLR 87
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLLERPT----SGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 88 QWRgARVAMIFQE---------------PMTALNptrrigrqmvevirqhqsLSRRDAQQKAIALLGEMQIPDAAqvmDR 152
Cdd:PRK11153 79 KAR-RQIGMIFQHfnllssrtvfdnvalPLELAG------------------TPKAEIKARVTELLELVGLSDKA---DR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 153 YPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYA 232
Cdd:PRK11153 137 YPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDA 216
|
250
....*....|....*....
gi 505383390 233 GSVIESGITQTLIHHPVHP 251
Cdd:PRK11153 217 GRLVEQGTVSEVFSHPKHP 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-274 |
2.34e-44 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 152.92 E-value: 2.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKSVTAmlamRLLPeGSYHVHHGRVTLLGEDVLNASEKQLRQWRGArVAMIFQEPMTA 104
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLA----RLLV-GLESPSQGNVSWRGEPLAKLNRAQRKAFRRD-IQMVFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 105 LNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAaqVMDRYPFELSGGMRQRVMIALAFSCEPELIIADEPT 184
Cdd:PRK10419 102 VNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDS--VLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 185 TALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPvHPYSIGLLRCapeng 264
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFS-SPAGRVLQNA----- 253
|
250
....*....|
gi 505383390 265 epreILPAIP 274
Cdd:PRK10419 254 ----VLPAFP 259
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-261 |
4.70e-44 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 159.64 E-value: 4.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 2 SDSVLSIEDLHLSFPIFRG-------DVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLpegsyHVHHGRVTLL 74
Cdd:PRK10261 310 GEPILQVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV-----ESQGGEIIFN 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 75 GEDVLNASEKQLRQWRgARVAMIFQEPMTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQI-PDAAQvmdRY 153
Cdd:PRK10261 385 GQRIDTLSPGKLQALR-RDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAW---RY 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 154 PFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAG 233
Cdd:PRK10261 461 PHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLG 540
|
250 260
....*....|....*....|....*...
gi 505383390 234 SVIESGITQTLIHHPVHPYSIGLLRCAP 261
Cdd:PRK10261 541 QIVEIGPRRAVFENPQHPYTRKLMAAVP 568
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
6-257 |
5.03e-44 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 151.91 E-value: 5.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPI-----FRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTA-MLAMRLLPEGsyhvhhgrvtllGEDVL 79
Cdd:COG4167 5 LEVRNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAkMLAGIIEPTS------------GEILI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 80 NASEKQLR--QWRGARVAMIFQEPMTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQI-PDAAQVmdrYPFE 156
Cdd:COG4167 73 NGHKLEYGdyKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPEHANF---YPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 LSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVI 236
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
250 260
....*....|....*....|.
gi 505383390 237 ESGITQTLIHHPVHPYSIGLL 257
Cdd:COG4167 230 EYGKTAEVFANPQHEVTKRLI 250
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-251 |
6.59e-44 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 150.53 E-value: 6.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMRLL--PEGsyhvhhGRVTLLGEDVlNAS 82
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKS-TLLRCINLLeePDS------GTITVDGEDL-TDS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 83 EKQLRQWRgARVAMIFQE----P-MTAL-NPTrrigrqmvEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFE 156
Cdd:COG1126 69 KKDINKLR-RKVGMVFQQfnlfPhLTVLeNVT--------LAPIKVKKMSKAEAEERAMELLERVGLADKA---DAYPAQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 LSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARaSGTSVLFISHDMAVVSQLCDRMYVMYAGSVI 236
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAK-EGMTMVVVTHEMGFAREVADRVVFMDGGRIV 215
|
250
....*....|....*
gi 505383390 237 ESGITQTLIHHPVHP 251
Cdd:COG1126 216 EEGPPEEFFENPQHE 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-235 |
1.50e-43 |
|
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: 147.54 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVT-AMLAMRLLPEGsyhvhhGRVTLLGEDVLNASEK 84
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLiKIILGLLKPDS------GEIKVLGKDIKKEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRqwrgaRVAMIFQEPMtalnptrrigrqmvevirqhqslsrrdaqqkaiaLLGEMQipdaaqVMDrYpFELSGGMRQR 164
Cdd:cd03230 71 VKR-----RIGYLPEEPS----------------------------------LYENLT------VRE-N-LKLSGGMKQR 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505383390 165 VMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSV 235
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESRREFWELLR-ELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-245 |
4.32e-43 |
|
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: 149.04 E-value: 4.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSfpifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAM-RLLPegsyhVHHGRVTLLGEDVLNASE 83
Cdd:COG1120 1 MLEAENLSVG----YGGRPVLDDVSLSLPPGEVTALLGPNGSGKS-TLLRALaGLLK-----PSSGEVLLDGRDLASLSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 84 KQLRQwrgaRVAMIFQEPMTALNPTrriGRQMVEVIRQ-HQS----LSRRDAQ--QKAIALLGemqipdAAQVMDRYPFE 156
Cdd:COG1120 71 RELAR----RIAYVPQEPPAPFGLT---VRELVALGRYpHLGlfgrPSAEDREavEEALERTG------LEHLADRPVDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 LSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVI 236
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
....*....
gi 505383390 237 ESGITQTLI 245
Cdd:COG1120 218 AQGPPEEVL 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-237 |
9.36e-43 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 147.58 E-value: 9.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRL-LPEGsyhvhhGRVTLLGEDVL 79
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPTS------GTVRLAGQDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 80 NASEKQLRQWRGARVAMIFQE----P-MTAL-N---PTRRIGrqmvevirqhqslsRRDAQQKAIALLGEMQIpdaAQVM 150
Cdd:COG4181 78 ALDEDARARLRARHVGFVFQSfqllPtLTALeNvmlPLELAG--------------RRDARARARALLERVGL---GHRL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 151 DRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQlCDRMYVM 230
Cdd:COG4181 141 DHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRL 219
|
....*..
gi 505383390 231 YAGSVIE 237
Cdd:COG4181 220 RAGRLVE 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-230 |
1.57e-42 |
|
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: 146.46 E-value: 1.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAmRLLPEGSyhvhhGRVTLLGEDVlnasek 84
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKStLLRIIA-GLERPTS-----GEVLVDGEPV------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 qlrQWRGARVAMIFQEPmtALNPTRRIgRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELSGGMRQR 164
Cdd:cd03293 69 ---TGPGPDRGYVFQQD--ALLPWLTV-LDNVALGLELQGVPKAEARERAEELLELVGLSGFE---NAYPHQLSGGMRQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 165 VMIALAFSCEPELIIADEPTTALDV----TVQRQVLRLLKHkaraSGTSVLFISHDMAVVSQLCDRMYVM 230
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRE----TGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
23-256 |
7.78e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 143.75 E-value: 7.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 23 HALNHVSLEIGRGEIVGVVGESGSGKSvTAM--LAMRLLPEgsyhvhHGRVTLLGEDVLNASEKQLRQWRgARVAMIFQE 100
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKS-TLIqhLNGLLKPT------SGTVTIDGRDITAKKKKKLKDLR-KKVGLVFQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 101 PmtalnptrrigrqmvevirQHQ-----------------SLSRRDAQQKAIALLGEMQIPDaaQVMDRYPFELSGGMRQ 163
Cdd:TIGR04521 91 P-------------------EHQlfeetvykdiafgpknlGLSEEEAEERVKEALELVGLDE--EYLERSPFELSGGQMR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 164 RVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQT 243
Cdd:TIGR04521 150 RVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPRE 229
|
250
....*....|...
gi 505383390 244 LIHHPVHPYSIGL 256
Cdd:TIGR04521 230 VFSDVDELEKIGL 242
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-244 |
1.81e-40 |
|
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: 141.55 E-value: 1.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQ 85
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTS-----GSVLIDGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQWRgARVAMIFQ-----EPMTALN-------PTRRIGRQMVevirqhQSLSRRDaQQKAIALLGEMQIPD-AAQVMDr 152
Cdd:cd03256 73 LRQLR-RQIGMIFQqfnliERLSVLEnvlsgrlGRRSTWRSLF------GLFPKEE-KQRALAALERVGLLDkAYQRAD- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 153 ypfELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYA 232
Cdd:cd03256 144 ---QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD 220
|
250
....*....|..
gi 505383390 233 GSVIESGITQTL 244
Cdd:cd03256 221 GRIVFDGPPAEL 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-253 |
6.98e-40 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 140.83 E-value: 6.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAMRLLPEG---SYHVHHGRVTllge 76
Cdd:PRK11701 2 MDQPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTtLLNALSARLAPDAgevHYRMRDGQLR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 77 DVLNASEKQLRQWRGARVAMIFQEPMTALNPTRRIG-----RQMVEVIRQHQSLsrrdaQQKAIALLGEMQIPdaAQVMD 151
Cdd:PRK11701 74 DLYALSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGgnigeRLMAVGARHYGDI-----RATAGDWLERVEID--AARID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 152 RYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMY 231
Cdd:PRK11701 147 DLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMK 226
|
250 260
....*....|....*....|..
gi 505383390 232 AGSVIESGITQTLIHHPVHPYS 253
Cdd:PRK11701 227 QGRVVESGLTDQVLDDPQHPYT 248
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-239 |
5.30e-39 |
|
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: 138.25 E-value: 5.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 2 SDSVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAmrllpeGSYHVHHGRVTLLGEDVLN 80
Cdd:COG0411 1 SDPLLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTtLFNLIT------GFYRPTSGRILFDGRDITG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 asekqLRQWRGAR--VAMIFQEP-----MTAL-N----PTRRIGRQMVEVIRQHQSLSR--RDAQQKAIALLGEMQIpda 146
Cdd:COG0411 71 -----LPPHRIARlgIARTFQNPrlfpeLTVLeNvlvaAHARLGRGLLAALLRLPRARReeREARERAEELLERVGL--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 147 AQVMDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDR 226
Cdd:COG0411 143 ADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADR 222
|
250
....*....|...
gi 505383390 227 MYVMYAGSVIESG 239
Cdd:COG0411 223 IVVLDFGRVIAEG 235
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-244 |
1.02e-38 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 137.43 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFPifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMRLLPEGSyhvhHGRVTLLGEDVLNASEK 84
Cdd:TIGR02315 1 MLEVENLSKVYP---NGKQALKNINLNINPGEFVAIIGPSGAGKS-TLLRCINRLVEPS----SGSILLEGTDITKLRGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQWRgARVAMIFQE-----PMTALNP--TRRIGRQmvEVIRQHQSLSRRDAQQKAIALLGEMQIPD-AAQVMDrypfE 156
Cdd:TIGR02315 73 KLRKLR-RRIGMIFQHynlieRLTVLENvlHGRLGYK--PTWRSLLGRFSEEDKERALSALERVGLADkAYQRAD----Q 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 LSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVI 236
Cdd:TIGR02315 146 LSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
....*...
gi 505383390 237 ESGITQTL 244
Cdd:TIGR02315 226 FDGAPSEL 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-252 |
5.12e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 138.31 E-value: 5.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTA-MLAmrllpeGSYHVHHGRVTLLGEDVL 79
Cdd:COG3842 1 MAMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLrMIA------GFETPDSGRILLDGRDVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 80 N-ASEKqlrqwRGarVAMIFQEP-----MTALnptrrigrqmvEVIR---QHQSLSRRDAQQKAIALLGEMQIPDAAqvm 150
Cdd:COG3842 71 GlPPEK-----RN--VGMVFQDYalfphLTVA-----------ENVAfglRMRGVPKAEIRARVAELLELVGLEGLA--- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 151 DRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHD----MAvvsqLCDR 226
Cdd:COG3842 130 DRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADR 205
|
250 260
....*....|....*....|....*.
gi 505383390 227 MYVMYAGSVIESGITQTLIHHPVHPY 252
Cdd:COG3842 206 IAVMNDGRIEQVGTPEEIYERPATRF 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-233 |
2.93e-37 |
|
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: 132.65 E-value: 2.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMRLL--PEGsyhvhhGRVTLLGEDVlNASE 83
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKS-TLLRCINLLeePDS------GTIIIDGLKL-TDDK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 84 KQLRQWRgARVAMIFQ-----EPMTALNptrrigrQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELS 158
Cdd:cd03262 69 KNINELR-QKVGMVFQqfnlfPHLTVLE-------NITLAPIKVKGMSKAEAEERALELLEKVGLADKA---DAYPAQLS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 159 GGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARaSGTSVLFISHDMAVVSQLCDRMYVMYAG 233
Cdd:cd03262 138 GGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-185 |
4.98e-37 |
|
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: 129.69 E-value: 4.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKSVTA-MLAMRLLPEGsyhvhhGRVTLLGEDVLNASEKQLRQwrgaRVAMIFQEPmt 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLkLIAGLLSPTE------GTILLDGQDLTDDERKSLRK----EIGYVFQDP-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 104 ALNPTRRIGRQMVEVIRqHQSLSRRDAQQKAIALLGEMQIPD-AAQVMDRYPFELSGGMRQRVMIALAFSCEPELIIADE 182
Cdd:pfam00005 69 QLFPRLTVRENLRLGLL-LKGLSKREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
...
gi 505383390 183 PTT 185
Cdd:pfam00005 148 PTA 150
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
18-252 |
5.23e-37 |
|
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: 132.81 E-value: 5.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 18 FRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQLRQwrgaRVAMI 97
Cdd:cd03295 10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTS-----GEIFIDGEDIREQDPVELRR----KIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 98 FQEpmTALNPTRRIgRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAaQVMDRYPFELSGGMRQRVMIALAFSCEPEL 177
Cdd:cd03295 81 IQQ--IGLFPHMTV-EENIALVPKLLKWPKEKIRERADELLALVGLDPA-EFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 178 IIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPVHPY 252
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-233 |
6.20e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 129.67 E-value: 6.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 7 SIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPegsyhVHHGRVTLLGEDVLNASEKQL 86
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-----PTSGEILIDGKDIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 87 RQwrgaRVAMIFQepmtalnptrrigrqmvevirqhqslsrrdaqqkaiallgemqipdaaqvmdrypfeLSGGMRQRVM 166
Cdd:cd00267 72 RR----RIGYVPQ---------------------------------------------------------LSGGQRQRVA 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383390 167 IALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAG 233
Cdd:cd00267 91 LARALLLNPDLLLLDEPTSGLDPASRERLLELLR-ELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-245 |
1.39e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.75 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKS--VTAMLamRLLPegsyhVHHGRVTLLGEDV 78
Cdd:COG1121 2 MMMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKStlLKAIL--GLLP-----PTSGTVRLFGKPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 79 LNASEK-----QlrqwrgaRVAMIFQEPMTAlnptrrigRQMVEVIRQHQS-----LSRRDaQQKAIALLGEMQIPDAAq 148
Cdd:COG1121 71 RRARRRigyvpQ-------RAEVDWDFPITV--------RDVVLMGRYGRRglfrrPSRAD-REAVDEALERVGLEDLA- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 149 vmDRyPF-ELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkHKARASGTSVLFISHDMAVVSQLCDRM 227
Cdd:COG1121 134 --DR-PIgELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELL-RELRREGKTILVVTHDLGAVREYFDRV 209
|
250
....*....|....*...
gi 505383390 228 YVMyAGSVIESGITQTLI 245
Cdd:COG1121 210 LLL-NRGLVAHGPPEEVL 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-239 |
1.59e-36 |
|
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: 129.48 E-value: 1.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 7 SIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAM-RLLPEGSyhvhhGRVTLLGEDVLNASEKQ 85
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKS-TLLKTLaGLLKPSS-----GEILLDGKDLASLSPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQWRGarvamifqepmtalnptrrigrqmveVIRQhqslsrrdaqqkAIALLGemqipdAAQVMDRYPFELSGGMRQRV 165
Cdd:cd03214 71 LARKIA--------------------------YVPQ------------ALELLG------LAHLADRPFNELSGGERQRV 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383390 166 MIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:cd03214 107 LLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-239 |
1.87e-36 |
|
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: 131.02 E-value: 1.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAM-LAMRLLPEGSyhvhhGRVTLLGEDVLNASEK 84
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKT-TLFnLISGFLRPTS-----GSVLFDGEDITGLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQwRGarVAMIFQEP-----MTALNPTR--RIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDaaqVMDRYPFEL 157
Cdd:cd03219 71 EIAR-LG--IGRTFQIPrlfpeLTVLENVMvaAQARTGSGLLLARARREEREARERAEELLERVGLAD---LADRPAGEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 158 SGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIE 237
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIR-ELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIA 223
|
..
gi 505383390 238 SG 239
Cdd:cd03219 224 EG 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-239 |
4.31e-36 |
|
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: 129.56 E-value: 4.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLpEGSYHVHHGRVTLLGEDVLNASEKQ 85
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLI-AGLERPDSGEILIDGRDVTGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 lrqwRgaRVAMIFQEPmtALNPTRRIGRQMVEVIRqHQSLSRRDAQQKAIALLGEMQIPDaaqVMDRYPFELSGGMRQRV 165
Cdd:cd03259 72 ----R--NIGMVFQDY--ALFPHLTVAENIAFGLK-LRGVPKAEIRARVRELLELVGLEG---LLNRYPHELSGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383390 166 MIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-252 |
6.56e-36 |
|
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: 130.46 E-value: 6.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQLRQWRGARVAMIFQ 99
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTS-----GKVLIDGQDIAAMSRKELRELRRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 100 EpmTALNPTRRIGRQMV---EVirqhQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELSGGMRQRVMIALAFSCEPE 176
Cdd:cd03294 110 S--FALLPHRTVLENVAfglEV----QGVPRAEREERAAEALELVGLEGWE---HKYPDELSGGMQQRVGLARALAVDPD 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 177 LIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPVHPY 252
Cdd:cd03294 181 ILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-239 |
8.19e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.02 E-value: 8.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFPifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVtamLaMRLLPeGSYHVHHGRVTLLGEDVLNASEK 84
Cdd:COG2884 1 MIRFENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKST---L-LKLLY-GEERPTSGQVLVNGQDLSRLKRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQWRgARVAMIFQEP-----MTAL-N---PTRRIGRqmvevirqhqslSRRDAQQKAIALLGEMQIPDAAqvmDRYPF 155
Cdd:COG2884 73 EIPYLR-RRIGVVFQDFrllpdRTVYeNvalPLRVTGK------------SRKEIRRRVREVLDLVGLSDKA---KALPH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 156 ELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSV 235
Cdd:COG2884 137 ELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLE-EINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
....
gi 505383390 236 IESG 239
Cdd:COG2884 216 VRDE 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-244 |
1.59e-35 |
|
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: 128.45 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSYHVHHGRVTLLGEDVLNASEKQ 85
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LrqWRGARVAMIFQEPmtalNPTRR-IGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDaaQVMDR-YPFELSGGMRQ 163
Cdd:cd03260 77 L--ELRRRVGMVFQKP----NPFPGsIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWD--EVKDRlHALGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 164 RVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARAsgTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQT 243
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 505383390 244 L 244
Cdd:cd03260 227 I 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-244 |
1.89e-35 |
|
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: 128.01 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVT-AMLAMRLLPEGsyhvhhGRVTLLGEDVLnASEK 84
Cdd:cd03263 1 LQIRNLTKTYK--KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTlKMLTGELRPTS------GTAYINGYSIR-TDRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQwrgaRVAMIFQ-----EPMTalnptrriGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDaaqVMDRYPFELSG 159
Cdd:cd03263 72 AARQ----SLGYCPQfdalfDELT--------VREHLRFYARLKGLPKSEIKEEVELLLRVLGLTD---KANKRARTLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 160 GMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARasGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:cd03263 137 GMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
....*
gi 505383390 240 ITQTL 244
Cdd:cd03263 215 SPQEL 219
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
18-253 |
4.61e-35 |
|
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: 128.02 E-value: 4.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 18 FRGDVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAMRLLPEgsyhvhHGRVTLLGED-----VLNASEKQLRQWRG 91
Cdd:TIGR02323 12 SYGGGKGCRDVSFDLYPGEVLGIVGESGSGKStLLGCLAGRLAPD------HGTATYIMRSgaeleLYQLSEAERRRLMR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 92 ARVAMIFQEPMTALNPT----RRIGRQMVEVIRQHQSLSRRDAQQkaiaLLGEMQIPDAAqvMDRYPFELSGGMRQRVMI 167
Cdd:TIGR02323 86 TEWGFVHQNPRDGLRMRvsagANIGERLMAIGARHYGNIRATAQD----WLEEVEIDPTR--IDDLPRAFSGGMQQRLQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 168 ALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHH 247
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDD 239
|
....*.
gi 505383390 248 PVHPYS 253
Cdd:TIGR02323 240 PQHPYT 245
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-233 |
7.38e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.08 E-value: 7.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPegsyhVHHGRVTLLGEDVlnaSEKQ 85
Cdd:COG4619 1 LELEGLSFRV----GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDP-----PTSGEIYLDGKPL---SAMP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQWRgARVAMIFQEPmtalnptrRIGRQMVE--VIRQHQSLSRRDAQQKAIALLGEMQIPDAaqVMDRYPFELSGGMRQ 163
Cdd:COG4619 69 PPEWR-RQVAYVPQEP--------ALWGGTVRdnLPFPFQLRERKFDRERALELLERLGLPPD--ILDKPVERLSGGERQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 164 RVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAG 233
Cdd:COG4619 138 RLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
19-233 |
5.82e-34 |
|
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: 122.68 E-value: 5.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 19 RGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVlNASEKQLRQWRgARVAMIF 98
Cdd:cd03229 10 YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDS-----GSILIDGEDL-TDLEDELPPLR-RRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 99 QEPmtALNPTrrigrqmvevirqhqsLSRRDAqqkaIALLgemqipdaaqvmdrypfeLSGGMRQRVMIALAFSCEPELI 178
Cdd:cd03229 83 QDF--ALFPH----------------LTVLEN----IALG------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 179 IADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAG 233
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-244 |
7.19e-34 |
|
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: 125.97 E-value: 7.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKSVTA-MLAMRLLPEGsyhvhhGRVTLLGEDVLNASEKqLRQwrgaRVAMIF 98
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIrMLTTLLRPTS------GTARVAGYDVVREPRK-VRR----SIGIVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 99 QEPMTALNPTrriGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELSGGMRQRVMIALAFSCEPELI 178
Cdd:TIGR01188 73 QYASVDEDLT---GRENLEMMGRLYGLPKDEAEERAEELLELFELGEAA---DRPVGTYSGGMRRRLDIAASLIHQPDVL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 179 IADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTL 244
Cdd:TIGR01188 147 FLDEPTTGLDPRTRRAIWDYIR-ALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-260 |
7.45e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 127.19 E-value: 7.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSdsvLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVT-AMLAmrllpeGSYHVHHGRVTLLGEDVL 79
Cdd:COG1118 1 MS---IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLlRIIA------GLETPDSGRIVLNGRDLF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 80 NASEKQLRqwrgaRVAMIFQEP-----MTalnptrrigrqmvevIRQ-------HQSLSRRDAQQKAIALLGEMQIPDAA 147
Cdd:COG1118 68 TNLPPRER-----RVGFVFQHYalfphMT---------------VAEniafglrVRPPSKAEIRARVEELLELVQLEGLA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 148 qvmDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRM 227
Cdd:COG1118 128 ---DRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRV 204
|
250 260 270
....*....|....*....|....*....|...
gi 505383390 228 YVMYAGSVIESGITQTLIHHPVHPYSIGLLRCA 260
Cdd:COG1118 205 VVMNQGRIEQVGTPDEVYDRPATPFVARFLGCV 237
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-236 |
1.60e-33 |
|
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: 121.00 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLpEGSYHVHHGRVTLLGEDVLNASEKQ 85
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTL----MKIL-SGLYKPDSGEILVDGKEVSFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQwrgARVAMIFQepmtalnptrrigrqmvevirqhqslsrrdaqqkaiallgemqipdaaqvmdrypfeLSGGMRQRV 165
Cdd:cd03216 72 ARR---AGIAMVYQ---------------------------------------------------------LSVGERQMV 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505383390 166 MIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVI 236
Cdd:cd03216 92 EIARALARNARLLILDEPTAALTPAEVERLFKVIR-RLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-239 |
3.79e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 124.07 E-value: 3.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVlnaSEK 84
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDS-----GEVLWDGEPL---DPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQW------RGarvamifqepmtaLNPTRRIGRQMVEVIRQHQsLSRRDAQQKAIALLGEMQIPDAA----Qvmdryp 154
Cdd:COG4152 69 DRRRIgylpeeRG-------------LYPKMKVGEQLVYLARLKG-LSKAEAKRRADEWLERLGLGDRAnkkvE------ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 155 fELSGGMRQRVMIALAFSCEPELIIADEPTTALD-VTVQ--RQVLRLLKhkarASGTSVLFISHDMAVVSQLCDRMYVMY 231
Cdd:COG4152 129 -ELSKGNQQKVQLIAALLHDPELLILDEPFSGLDpVNVEllKDVIRELA----AKGTTVIFSSHQMELVEELCDRIVIIN 203
|
....*...
gi 505383390 232 AGSVIESG 239
Cdd:COG4152 204 KGRKVLSG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-239 |
2.27e-32 |
|
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: 119.78 E-value: 2.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVT-AMLAMRLLPEGsyhvhhGRVTLLGEDVLnasek 84
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTlRMLAGLLEPDA------GFATVDGFDVV----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 qlRQWRGARVAMIFQEPMTALNPtRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIpdaAQVMDRYPFELSGGMRQR 164
Cdd:cd03266 71 --KEPAEARRRLGFVSDSTGLYD-RLTARENLEYFAGLYGLKGDELTARLEELADRLGM---EELLDRRVGGFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 165 VMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKaRASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-244 |
2.83e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.13 E-value: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 2 SDSVLSIEDLHLSFPifrgDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAM--LAmrllpeGSYHVHHGRVTLLGEDVL 79
Cdd:COG1129 1 AEPLLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKS-TLMkiLS------GVYQPDSGEILLDGEPVR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 80 NASEKQLRQwrgARVAMIFQEPmtALNPTR------RIGRQmvevIRQHQSLSRRDAQQKAIALLGEMQI---PDaAQVM 150
Cdd:COG1129 70 FRSPRDAQA---AGIAIIHQEL--NLVPNLsvaeniFLGRE----PRRGGLIDWRAMRRRARELLARLGLdidPD-TPVG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 151 DrypfeLSGGMRQRVMIALAFSCEPELIIADEPTTALDvtvQRQVLRLLK--HKARASGTSVLFISHDMAVVSQLCDRMY 228
Cdd:COG1129 140 D-----LSVAQQQLVEIARALSRDARVLILDEPTASLT---EREVERLFRiiRRLKAQGVAIIYISHRLDEVFEIADRVT 211
|
250
....*....|....*.
gi 505383390 229 VMYAGSVIESGITQTL 244
Cdd:COG1129 212 VLRDGRLVGTGPVAEL 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-248 |
3.03e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.20 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMRLLPEgsyhVHHGRVTLLGEDVL--NASEKQLRQWRGarvaMI 97
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKS-TLLRCINKLEE----ITSGDLIVDGLKVNdpKVDERLIRQEAG----MV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 98 FQE----P-MTALN-----PTRRIGrqmvevirqhqsLSRRDAQQKAIALLGEMQIpdaAQVMDRYPFELSGGMRQRVMI 167
Cdd:PRK09493 83 FQQfylfPhLTALEnvmfgPLRVRG------------ASKEEAEKQARELLAKVGL---AERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 168 ALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLfISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHH 247
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
.
gi 505383390 248 P 248
Cdd:PRK09493 227 P 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-244 |
3.27e-32 |
|
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: 119.40 E-value: 3.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKSVT-AMLAMRLLPEGsyhvhhGRVTLLGEDVLnaseKQLRQWRgARVAMIF 98
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTiKMLTTLLKPTS------GRATVAGHDVV----REPREVR-RRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 99 QEPMTALNPTrriGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELSGGMRQRVMIALAFSCEPELI 178
Cdd:cd03265 80 QDLSVDDELT---GWENLYIHARLYGVPGAERRERIDELLDFVGLLEAA---DRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 179 IADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTL 244
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-230 |
1.30e-31 |
|
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: 116.33 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLlpegsYHVHHGRVTLLGEDVLNASEKQ 85
Cdd:cd03228 1 IEFKNVSFSYP--GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRL-----YDPTSGEILIDGVDLRDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQwrgaRVAMIFQEP----MTalnptrrigrqmvevIRqhqslsrrdaqqkaiallgemqipdaaqvmdrypfE--LSG 159
Cdd:cd03228 74 LRK----NIAYVPQDPflfsGT---------------IR-----------------------------------EniLSG 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505383390 160 GMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkhKARASGTSVLFISHDMAVVsQLCDRMYVM 230
Cdd:cd03228 100 GQRQRIAIARALLRDPPILILDEATSALDPETEALILEAL--RALAKGKTVIVIAHRLSTI-RDADRIIVL 167
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-237 |
1.40e-31 |
|
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: 117.84 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEK 84
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTS-----GEVLFNGQSLSKLSSN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQWRGARVAMIFQ-----EPMTALNPTrrigrqMVEVIRQHQSlsRRDAQQKAIALLGEMQIPDAaqvMDRYPFELSG 159
Cdd:TIGR02211 76 ERAKLRNKKLGFIYQfhhllPDFTALENV------AMPLLIGKKS--VKEAKERAYEMLEKVGLEHR---INHRPSELSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505383390 160 GMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLcDRMYVMYAGSVIE 237
Cdd:TIGR02211 145 GERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-247 |
2.77e-31 |
|
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: 123.33 E-value: 2.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 2 SDSVLSIEDLHLSFPifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPegsyhVHHGRVTLLGEDVLNA 81
Cdd:COG4988 333 GPPSIELEDVSFSYP---GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP-----PYSGSILINGVDLSDL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 82 SEKQLRQwrgaRVAMIFQEPMTaLNPTRRigrqmvEVIRqhqsLSRRDAQ----QKAIALLGemqipdAAQVMDRYP--- 154
Cdd:COG4988 405 DPASWRR----QIAWVPQNPYL-FAGTIR------ENLR----LGRPDASdeelEAALEAAG------LDEFVAALPdgl 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 155 --------FELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkhKARASGTSVLFISHDMAVVSQlCDR 226
Cdd:COG4988 464 dtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL--RRLAKGRTVILITHRLALLAQ-ADR 540
|
250 260
....*....|....*....|.
gi 505383390 227 MYVMYAGSVIESGITQTLIHH 247
Cdd:COG4988 541 ILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-239 |
2.86e-31 |
|
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: 116.86 E-value: 2.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 7 SIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEgsyhvHHGRVTLLGEDVLNASEkql 86
Cdd:cd03235 1 EVEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP-----TSGSIRVFGKPLEKERK--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 87 rqwrgaRVAMIFQE-------PMTALN--PTRRIGRqmvevIRQHQSLSRRDAQqKAIALLGEMQIPDAAqvmDRYPFEL 157
Cdd:cd03235 69 ------RIGYVPQRrsidrdfPISVRDvvLMGLYGH-----KGLFRRLSKADKA-KVDEALERVGLSELA---DRQIGEL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 158 SGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRmYVMYAGSVIE 237
Cdd:cd03235 134 SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR-ELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVA 211
|
..
gi 505383390 238 SG 239
Cdd:cd03235 212 SG 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-251 |
4.14e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 117.76 E-value: 4.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMRLLP---EGSYHVHHGRVTLLGE- 76
Cdd:PRK10619 1 MSENKLNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEkpsEGSIVVNGQTINLVRDk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 77 --DVLNASEKQLRQWRgARVAMIFQE-----PMTALnptrrigRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAQv 149
Cdd:PRK10619 76 dgQLKVADKNQLRLLR-TRLTMVFQHfnlwsHMTVL-------ENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 150 mDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARaSGTSVLFISHDMAVVSQLCDRMYV 229
Cdd:PRK10619 147 -GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIF 224
|
250 260
....*....|....*....|..
gi 505383390 230 MYAGSVIESGITQTLIHHPVHP 251
Cdd:PRK10619 225 LHQGKIEEEGAPEQLFGNPQSP 246
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
20-257 |
1.35e-30 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 115.67 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLPeGSYHVHHGRVTLLGEDVLNASEkqlrqwRGARVAMIFQ 99
Cdd:TIGR00968 11 GSFQALDDVNLEVPTGSLVALLGPSGSGKSTL----LRIIA-GLEQPDSGRIRLNGQDATRVHA------RDRKIGFVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 100 EpmTALNPTRRIgRQMVEV---IRQHQSLSRRdaqQKAIALLGEMQIpdaAQVMDRYPFELSGGMRQRVMIALAFSCEPE 176
Cdd:TIGR00968 80 H--YALFKHLTV-RDNIAFgleIRKHPKAKIK---ARVEELLELVQL---EGLGDRYPNQLSGGQRQRVALARALAVEPQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 177 LIIADEPTTALDVTVQRQV---LRLLKHKARAsgTSVlFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPVHPYS 253
Cdd:TIGR00968 151 VLLLDEPFGALDAKVRKELrswLRKLHDEVHV--TTV-FVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFV 227
|
....
gi 505383390 254 IGLL 257
Cdd:TIGR00968 228 MSFL 231
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-239 |
3.18e-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 upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 115.61 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLL-PEGsyhvhhGRVTLLGEDVLNASE- 83
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLlPTS------GKVTVDGLDTLDEENl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 84 KQLRQwrgaRVAMIFQepmtalNPTRRIGRQMVE--VirqhqslsrrdaqqkAIAL--LG----EMQ--IPDAAQVM--- 150
Cdd:TIGR04520 73 WEIRK----KVGMVFQ------NPDNQFVGATVEddV---------------AFGLenLGvpreEMRkrVDEALKLVgme 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 151 ---DRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDM--AVvsqLCD 225
Cdd:TIGR04520 128 dfrDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMeeAV---LAD 204
|
250
....*....|....
gi 505383390 226 RMYVMYAGSVIESG 239
Cdd:TIGR04520 205 RVIVMNKGKIVAEG 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
20-257 |
9.67e-30 |
|
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: 113.59 E-value: 9.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLPeGSYHVHHGRVTLLGEDvlnASEKQLRQwRGarVAMIFQ 99
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTL----LRLIA-GLERPDSGTILFGGED---ATDVPVQE-RN--VGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 100 EpmTALNPTRRIGRQM---VEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELSGGMRQRVMIALAFSCEPE 176
Cdd:cd03296 82 H--YALFRHMTVFDNVafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLA---DRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 177 LIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPVHPYSIGL 256
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSF 236
|
.
gi 505383390 257 L 257
Cdd:cd03296 237 L 237
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-216 |
1.05e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 113.80 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 4 SVLSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGK-SVTAMLAMRLLPEGsyhvhhGRVTLLGEDVlnas 82
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKtTLLNLIAGFLAPSS------GEITLDGVPV---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 83 ekqlrQWRGARVAMIFQEpmTALNPTRRIgRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAQvmdRYPFELSGGMR 162
Cdd:COG4525 72 -----TGPGADRGVVFQK--DALLPWLNV-LDNVAFGLRLRGVPKAERRARAEELLALVGLADFAR---RRIWQLSGGMR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505383390 163 QRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHD 216
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-249 |
1.93e-29 |
|
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: 112.43 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPIFRgdvhaLNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNAS-EK 84
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDS-----GKILLNGKDITNLPpEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QlrqwrgaRVAMIFQEpmTALNPTRRIGRQMVEVIRqHQSLSRRDAQQKAIALLGEMQIpdaAQVMDRYPFELSGGMRQR 164
Cdd:cd03299 71 R-------DISYVPQN--YALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGI---DHLLNRKPETLSGGEQQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 165 VMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTL 244
Cdd:cd03299 138 VAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
....*
gi 505383390 245 IHHPV 249
Cdd:cd03299 218 FKKPK 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-245 |
2.20e-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: 118.40 E-value: 2.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLlpegsYHVHHGRVTLLGEDVLNASEKQ 85
Cdd:COG2274 474 IELENVSFRYP--GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL-----YEPTSGRILIDGIDLRQIDPAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQWrgarVAMIFQEP------------MTALNPTRRigrQMVEVIRQ---HQSLSRR----DAQqkaialLGEMQIPda 146
Cdd:COG2274 547 LRRQ----IGVVLQDVflfsgtirenitLGDPDATDE---EIIEAARLaglHDFIEALpmgyDTV------VGEGGSN-- 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 147 aqvmdrypfeLSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkhKARASGTSVLFISHDMAVVsQLCDR 226
Cdd:COG2274 612 ----------LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL--RRLLKGRTVIIIAHRLSTI-RLADR 678
|
250
....*....|....*....
gi 505383390 227 MYVMYAGSVIESGITQTLI 245
Cdd:COG2274 679 IIVLDKGRIVEDGTHEELL 697
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
17-252 |
5.65e-29 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 112.88 E-value: 5.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 17 IFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamLAM--RLLPEGSyhvhhGRVTLLGEDVLNASEKQLRqwrgarv 94
Cdd:COG1125 10 RYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTT--LRMinRLIEPTS-----GRILIDGEDIRDLDPVELR------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 95 amifqepmtalnptRRIGRqmveVIRQ-----HQSL-------------SRRDAQQKAIALLGEMQIpDAAQVMDRYPFE 156
Cdd:COG1125 76 --------------RRIGY----VIQQiglfpHMTVaeniatvprllgwDKERIRARVDELLELVGL-DPEEYRDRYPHE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 LSGGMRQRVMIALAFSCEPELIIADEPTTALD-VT---VQRQVLRLLkhkaRASGTSVLFISHDM--AVvsQLCDRMYVM 230
Cdd:COG1125 137 LSGGQQQRVGVARALAADPPILLMDEPFGALDpITreqLQDELLRLQ----RELGKTIVFVTHDIdeAL--KLGDRIAVM 210
|
250 260
....*....|....*....|..
gi 505383390 231 YAGSVIESGITQTLIHHPVHPY 252
Cdd:COG1125 211 REGRIVQYDTPEEILANPANDF 232
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-250 |
1.27e-28 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 111.42 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 19 RGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTA-MLAMRLLPEGSYHVHHGRVTLLGEdvlnasekqlRQWRGARVAMI 97
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAkMLAGMIEPTSGELLIDDHPLHFGD----------YSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 98 FQEPMTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQI-PDAAQVmdrYPFELSGGMRQRVMIALAFSCEPE 176
Cdd:PRK15112 93 FQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASY---YPHMLAPGQKQRLGLARALILRPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383390 177 LIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPVH 250
Cdd:PRK15112 170 VIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLH 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-245 |
1.59e-28 |
|
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: 115.28 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 19 RGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLP--EGSYHVhhgrvtLLGEDVLNASEKQ-LRQWRGAR-V 94
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEptSGEVNV------RVGDEWVDMTKPGpDGRGRAKRyI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 95 AMIFQEpmTALNPTRRIGRQMVEVIrqhqSLSRRD--AQQKAIALLGEMQIPD--AAQVMDRYPFELSGGMRQRVMIALA 170
Cdd:TIGR03269 368 GILHQE--YDLYPHRTVLDNLTEAI----GLELPDelARMKAVITLKMVGFDEekAEEILDKYPDELSEGERHRVALAQV 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 171 FSCEPELIIADEPTTALDVTVQRQVLRLLkHKARAS-GTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLI 245
Cdd:TIGR03269 442 LIKEPRIVILDEPTGTMDPITKVDVTHSI-LKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-248 |
2.69e-28 |
|
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: 114.86 E-value: 2.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPegsyhVHHGRVTLLGEDVLNASEKQ 85
Cdd:COG4987 334 LELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD-----PQSGSITLGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQwrgaRVAMIFQEP----MTALNpTRRIGR------QMVEVIRQHQsLSR--RDAQQKAIALLGEmqipDAAQvmdry 153
Cdd:COG4987 407 LRR----RIAVVPQRPhlfdTTLRE-NLRLARpdatdeELWAALERVG-LGDwlAALPDGLDTWLGE----GGRR----- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 154 pfeLSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkhKARASGTSVLFISHDMAVVSQlCDRMYVMYAG 233
Cdd:COG4987 472 ---LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL--LEALAGRTVLLITHRLAGLER-MDRILVLEDG 545
|
250
....*....|....*
gi 505383390 234 SVIESGITQTLIHHP 248
Cdd:COG4987 546 RIVEQGTHEELLAQN 560
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-239 |
1.02e-27 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 107.30 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLpEGSYHVHHGRVTLLGEDVLNASEKQ 85
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTT----MKII-LGLIKPDSGEITFDGKSYQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 lrqwrgARVAMIFQEP-----MTALNPTRRIGRQMvevirqhqsLSRRDAQQKAIALLGEMQIPDaaqvmdRYPFELSGG 160
Cdd:cd03268 72 ------RRIGALIEAPgfypnLTARENLRLLARLL---------GIRKKRIDEVLDVVGLKDSAK------KKVKGFSLG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 161 MRQRVMIALAFSCEPELIIADEPTTALD---VTVQRQVLRLLkhkaRASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIE 237
Cdd:cd03268 131 MKQRLGIALALLGNPDLLILDEPTNGLDpdgIKELRELILSL----RDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
..
gi 505383390 238 SG 239
Cdd:cd03268 207 EG 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-239 |
1.09e-27 |
|
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: 107.37 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQ 85
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS-----GEVLFDGKPLDIAARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 ---LRQWRGarvamifqepmtaLNPTRRIGRQMVeVIRQHQSLSRRDAQQKAIALLGEMQIPDAAQVMDRypfELSGGMR 162
Cdd:cd03269 72 igyLPEERG-------------LYPKMKVIDQLV-YLAQLKGLKKEEARRRIDEWLERLELSEYANKRVE---ELSKGNQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383390 163 QRVMIALAFSCEPELIIADEPTTALDVtVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:cd03269 135 QKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-233 |
1.24e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.43 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLsfpifRGD--VHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPegsyhVHHGRVTLLGEDVLNAS 82
Cdd:COG3845 257 VLEVENLSV-----RDDrgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP-----PASGSIRLDGEDITGLS 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 83 EKQLRQwrgARVAMIFQEPM-TALNPTRRI------GRQMVEVIRQHQSLSRRDAQQKAIALLGEMQI--PDAAQVMDRy 153
Cdd:COG3845 327 PRERRR---LGVAYIPEDRLgRGLVPDMSVaenlilGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDVrtPGPDTPARS- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 154 pfeLSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAG 233
Cdd:COG3845 403 ---LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLL-ELRDAGAAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
18-251 |
1.25e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 108.30 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 18 FRGDVhALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMRLL--PEGSyHVHHGRVTLLGEDVLNASEKQLRQWRgARVA 95
Cdd:PRK11264 13 FHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLeqPEAG-TIRVGDITIDTARSLSQQKGLIRQLR-QHVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 96 MIFQEpmTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIpdaAQVMDRYPFELSGGMRQRVMIALAFSCEP 175
Cdd:PRK11264 89 FVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL---AGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 176 ELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLfISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPVHP 251
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQP 238
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-239 |
1.96e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 110.70 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMRllpeGSYHVHHGRVTLLGEDVLNASEKQ 85
Cdd:PRK09536 4 IDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKT-TLLRAIN----GTLTPTAGTVLVAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LrqwrGARVAMIFQEPMTALNPTrriGRQMVEVIRqHQSLSRRDAQQKA--IALLGEMQIPDAAQVMDRYPFELSGGMRQ 163
Cdd:PRK09536 75 A----SRRVASVPQDTSLSFEFD---VRQVVEMGR-TPHRSRFDTWTETdrAAVERAMERTGVAQFADRPVTSLSGGERQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 164 RVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFIsHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAG 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-236 |
3.50e-27 |
|
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: 105.80 E-value: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 7 SIEDLHLSFpifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEgsyhvHHGRVtLLGEDVLNASEkql 86
Cdd:cd03226 1 RIENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE-----SSGSI-LLNGKPIKAKE--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 87 rqwRGARVAMIFQepmtalNPTRRIGRQMV--EVIRQHQSLSrrDAQQKAIALLGEMQIpdaAQVMDRYPFELSGGMRQR 164
Cdd:cd03226 69 ---RRKSIGYVMQ------DVDYQLFTDSVreELLLGLKELD--AGNEQAETVLKDLDL---YALKERHPLSLSGGQKQR 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505383390 165 VMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARAsGTSVLFISHDMAVVSQLCDRMYVMYAGSVI 236
Cdd:cd03226 135 LAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-252 |
3.60e-27 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 109.81 E-value: 3.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKSvTaMLAM--RLLPegsyhVHHGRVTLLGEDVLNASEKQLRQWRGARVAMI 97
Cdd:COG4175 38 GQTVGVNDASFDVEEGEIFVIMGLSGSGKS-T-LVRClnRLIE-----PTAGEVLIDGEDITKLSKKELRELRRKKMSMV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 98 FQEpmTALNPTRRIgRQMV----EVirqhQSLSRRDAQQKAIALLgemqipdaAQV-----MDRYPFELSGGMRQRVMIA 168
Cdd:COG4175 111 FQH--FALLPHRTV-LENVafglEI----QGVPKAERRERAREAL--------ELVglagwEDSYPDELSGGMQQRVGLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 169 LAFSCEPELIIADEPTTALD----VTVQRQVLRLLK--HKarasgtSVLFISHDM--AVvsQLCDRMYVMYAGSVIESGI 240
Cdd:COG4175 176 RALATDPDILLMDEAFSALDplirREMQDELLELQAklKK------TIVFITHDLdeAL--RLGDRIAIMKDGRIVQIGT 247
|
250
....*....|..
gi 505383390 241 TQTLIHHPVHPY 252
Cdd:COG4175 248 PEEILTNPANDY 259
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-241 |
4.30e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.89 E-value: 4.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAM--LAmrllpeGSYHVHHGRVTLLGEDV 78
Cdd:COG3845 1 MMPPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKS-TLMkiLY------GLYQPDSGEILIDGKPV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 79 LNASEKQLRQwrgARVAMIFQ-----EPMTAL------NPTRRIGRqmvevirqhqsLSRRDAQQKAIALlgemqipdaa 147
Cdd:COG3845 70 RIRSPRDAIA---LGIGMVHQhfmlvPNLTVAenivlgLEPTKGGR-----------LDRKAARARIREL---------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 148 qvMDRYPFE---------LSGGMRQRVMIALAFSCEPELIIADEPTTALdvTVQ--RQVLRLLKhKARASGTSVLFISHD 216
Cdd:COG3845 126 --SERYGLDvdpdakvedLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILR-RLAAEGKSIIFITHK 200
|
250 260
....*....|....*....|....*
gi 505383390 217 MAVVSQLCDRMYVMYAGSVIESGIT 241
Cdd:COG3845 201 LREVMAIADRVTVLRRGKVVGTVDT 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-251 |
1.28e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.62 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSfpifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLpEGSYHVHHGRVTLLGedvlnaseK 84
Cdd:PRK13548 2 MLEARNLSVR----LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTL----LRAL-SGELSPDSGEVRLNG--------R 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQWRGARVAmifqepmtalnptRRIGrqmveVIRQHQSLS----------------RRDAQQKAIALLGEMQIPDAAQ 148
Cdd:PRK13548 65 PLADWSPAELA-------------RRRA-----VLPQHSSLSfpftveevvamgraphGLSRAEDDALVAAALAQVDLAH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 149 VMDRYPFELSGGMRQRVMIA--LA----FSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQ 222
Cdd:PRK13548 127 LAGRDYPQLSGGEQQRVQLArvLAqlwePDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAAR 206
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 505383390 223 LCDRMYVMYAGSVIESG-----ITQTLI----HHPV----HP 251
Cdd:PRK13548 207 YADRIVLLHQGRLVADGtpaevLTPETLrrvyGADVlvqpHP 248
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-237 |
1.36e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.45 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMR--LLPEGsyhvhhGRVTLLGEDV-LNASEKQLRQWRgARVAMIFQEP 101
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKS-TLMQHFNalLKPSS------GTITIAGYHItPETGNKNLKKLR-KKVSLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 102 MTALNPTRRIgrQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDaaQVMDRYPFELSGGMRQRVMIALAFSCEPELIIAD 181
Cdd:PRK13641 95 EAQLFENTVL--KDVEFGPKNFGFSEDEAKEKALKWLKKVGLSE--DLISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 182 EPTTALDVTVQRQVLRLLKHKARAsGTSVLFISHDMAVVSQLCDRMYVMYAGSVIE 237
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
20-226 |
2.53e-26 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 103.46 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAMrLLPEGSyhvhhGRVTLLGEDVLNASEKQLRQWRGARVAMIF 98
Cdd:TIGR03608 9 GDKVILDDLNLTIEKGKMYAIIGESGSGKStLLNIIGL-LEKFDS-----GQVYLNGQETPPLNSKKASKFRREKLGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 99 QEpmTALNPTRRIgRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIpdaAQVMDRYPFELSGGMRQRVMIALAFSCEPELI 178
Cdd:TIGR03608 83 QN--FALIENETV-EENLDLGLKYKKLSKKEKREKKKEALEKVGL---NLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505383390 179 IADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQlCDR 226
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLL-ELNDEGKTIIIVTHDPEVAKQ-ADR 202
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
24-256 |
2.61e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.49 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 24 ALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAMRLLPEgsyhvhHGRVTLlGEDVLNA--SEKQLRQWRgARVAMIFQE 100
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKStLLQHLNGLLQPT------SGTVTI-GERVITAgkKNKKLKPLR-KKVGIVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 101 PMtalnptrrigRQMVE--VIR------QHQSLSRRDAQQKAIALLGEMQIPDAaqVMDRYPFELSGGMRQRVMIALAFS 172
Cdd:PRK13634 94 PE----------HQLFEetVEKdicfgpMNFGVSEEDAKQKAREMIELVGLPEE--LLARSPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 173 CEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPVHPY 252
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELE 241
|
....
gi 505383390 253 SIGL 256
Cdd:PRK13634 242 AIGL 245
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-235 |
2.65e-26 |
|
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: 102.51 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSfpifrgdvHALNHVSLEIGRGEIVGVVGESGSGKS--VTAMLAMRllpegsyHVHHGRVTLLGEDVLNAS 82
Cdd:cd03215 4 VLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTelAEALFGLR-------PPASGEITLDGKPVTRRS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 83 ekqLRQWRGARVAMIFQEpmtalnptrrigrqmveviRQHQslsrrdaqqkaiALLGEMQIPDAAQVmdryPFELSGGMR 162
Cdd:cd03215 69 ---PRDAIRAGIAYVPED-------------------RKRE------------GLVLDLSVAENIAL----SSLLSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505383390 163 QRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSV 235
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLI-RELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-248 |
2.96e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 104.32 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpiFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMRLL--PEGsyhvhhGRVTLLGEDV---LN 80
Cdd:COG4161 1 MSIQLKNINC--FYGSHQALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLetPDS------GQLNIAGHQFdfsQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQLRQWRGaRVAMIFQEpmTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELSGG 160
Cdd:COG4161 72 PSEKAIRLLRQ-KVGMVFQQ--YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKA---DRFPLHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 161 MRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLfISHDMAVVSQLCDRMYVMYAGSVIESGi 240
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVI-VTHEVEFARKVASQVVYMEKGRIIEQG- 223
|
....*...
gi 505383390 241 TQTLIHHP 248
Cdd:COG4161 224 DASHFTQP 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
35-239 |
3.67e-26 |
|
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: 103.14 E-value: 3.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 35 GEIVGVVGESGSGKSVtamlAMRLLpEGSYHVHHGRVTLLGEdVLNASEKQLR---QWRgaRVAMIFQEpmTALNPTRRI 111
Cdd:cd03297 23 EEVTGIFGASGAGKST----LLRCI-AGLEKPDGGTIVLNGT-VLFDSRKKINlppQQR--KIGLVFQQ--YALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 112 GRQMVEVIRQHQSLSRRDAQQKAIALLGemqipdAAQVMDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTV 191
Cdd:cd03297 93 RENLAFGLKRKRNREDRISVDELLDLLG------LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505383390 192 QRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-247 |
5.41e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 103.62 E-value: 5.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDsVLSIEDLHLSFPIF------------------RGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTamLaMRLLpEG 62
Cdd:COG1134 1 MSS-MIEVENVSKSYRLYhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKS-T--L-LKLI-AG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 63 SYHVHHGRVTLLGedvlnasekqlrqwrgaRVAMIFqEPMTALNP--TrriGRQMVEVIRQHQSLSRRDAQQK-----AI 135
Cdd:COG1134 75 ILEPTSGRVEVNG-----------------RVSALL-ELGAGFHPelT---GRENIYLNGRLLGLSRKEIDEKfdeivEF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 136 ALLGE-MQIPdaaqvMDRYpfelSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKaRASGTSVLFIS 214
Cdd:COG1134 134 AELGDfIDQP-----VKTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVS 203
|
250 260 270
....*....|....*....|....*....|...
gi 505383390 215 HDMAVVSQLCDRMYVMYAGSVIESGITQTLIHH 247
Cdd:COG1134 204 HSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-222 |
5.80e-26 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 102.71 E-value: 5.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFPifrGDVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAMRLLPEgsyhvhHGRVTLLGEDVLNASE 83
Cdd:TIGR02673 1 MIEFHNVSKAYP---GGVAALHDVSLHIRKGEFLFLTGPSGAGKTtLLKLLYGALTPS------RGQVRIAGEDVNRLRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 84 KQLRQWRgARVAMIFQEpmTALNPTRRIGRQmVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAaqvMDRYPFELSGGMRQ 163
Cdd:TIGR02673 72 RQLPLLR-RRIGVVFQD--FRLLPDRTVYEN-VALPLEVRGKKEREIQRRVGAALRQVGLEHK---ADAFPEQLSGGEQQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505383390 164 RVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkHKARASGTSVLFISHDMAVVSQ 222
Cdd:TIGR02673 145 RVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLL-KRLNKRGTTVIVATHDLSLVDR 202
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-250 |
7.98e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 105.54 E-value: 7.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDsvLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTA-MLAmrllpeGSYHVHHGRVTLLGEDVL 79
Cdd:COG3839 1 MAS--LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLrMIA------GLEDPTSGEILIGGRDVT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 80 NASEKQlrqwRGarVAMIFQEPmtALNPtrrigrqmvevirqHQS-------------LSRRDAQQKAIALLGEMQIpda 146
Cdd:COG3839 69 DLPPKD----RN--IAMVFQSY--ALYP--------------HMTvyeniafplklrkVPKAEIDRRVREAAELLGL--- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 147 AQVMDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALD----VTVQRQVLRLLkhkaRASGTSVLFISHD----MA 218
Cdd:COG3839 124 EDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLH----RRLGTTTIYVTHDqveaMT 199
|
250 260 270
....*....|....*....|....*....|..
gi 505383390 219 vvsqLCDRMYVMYAGSVIESGITQTLIHHPVH 250
Cdd:COG3839 200 ----LADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
5-234 |
8.41e-26 |
|
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: 102.51 E-value: 8.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFPIF-RGDV--HALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAMRLLP-EGSYHVHH--GRVtllgeD 77
Cdd:COG4778 4 LLEVENLSKTFTLHlQGGKrlPVLDGVSFSVAAGECVALTGPSGAGKStLLKCIYGNYLPdSGSILVRHdgGWV-----D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 78 VLNASEKQlrqwrgarvamifqepMTALnptRR--IG------RQM-----VEVIRQ---HQSLSRRDAQQKAIALLGEM 141
Cdd:COG4778 79 LAQASPRE----------------ILAL---RRrtIGyvsqflRVIprvsaLDVVAEpllERGVDREEARARARELLARL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 142 QIPDAaqVMDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkHKARASGTSVLFISHDMAVVS 221
Cdd:COG4778 140 NLPER--LWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELI-EEAKARGTAIIGIFHDEEVRE 216
|
250
....*....|...
gi 505383390 222 QLCDRMYVMYAGS 234
Cdd:COG4778 217 AVADRVVDVTPFS 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-239 |
2.13e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.82 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 24 ALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVL--NASEKQLRQwrgaRVAMIFQEP 101
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTS-----GKIIIDGVDITdkKVKLSDIRK----KVGLVFQYP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 102 M-----------TALNPtRRIGRQMVEVirqhqslSRRdaQQKAIALLGemqiPDAAQVMDRYPFELSGGMRQRVMIALA 170
Cdd:PRK13637 93 EyqlfeetiekdIAFGP-INLGLSEEEI-------ENR--VKRAMNIVG----LDYEDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383390 171 FSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-251 |
2.30e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 102.04 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 2 SDSVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAM-R---LLPEGSYhvhHGRVTLLGED 77
Cdd:COG1117 8 LEPKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKS-TLLRCLnRmndLIPGARV---EGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 78 VLNASEK--QLRqwrgARVAMIFQEPmtalNP-------------------TRRIGRQMVEvirqhQSLsrRDAqqkaiA 136
Cdd:COG1117 80 IYDPDVDvvELR----RRVGMVFQKP----NPfpksiydnvayglrlhgikSKSELDEIVE-----ESL--RKA-----A 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 137 LLGEmqipdaaqVMDR---YPFELSGGMRQRVMIALAFSCEPELIIADEPTTALD-VTVQR--QVLRLLKHKarasgTSV 210
Cdd:COG1117 140 LWDE--------VKDRlkkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAKieELILELKKD-----YTI 206
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 505383390 211 LFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPVHP 251
Cdd:COG1117 207 VIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDK 247
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
10-248 |
3.27e-25 |
|
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: 103.64 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 10 DLHLSFPIFRGDVhalnhvSLEIGRGEIVGVVGESGSGK-SVTAMLAmrllpeGSYHVHHGRVTLLGEdVLNASEKqlRQ 88
Cdd:COG4148 6 DFRLRRGGFTLDV------DFTLPGRGVTALFGPSGSGKtTLLRAIA------GLERPDSGRIRLGGE-VLQDSAR--GI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 89 WRGA---RVAMIFQEPmtALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGemqIpdaAQVMDRYPFELSGGMRQRV 165
Cdd:COG4148 71 FLPPhrrRIGYVFQEA--RLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLG---I---GHLLDRRPATLSGGERQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 166 MIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLI 245
Cdd:COG4148 143 AIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVL 222
|
...
gi 505383390 246 HHP 248
Cdd:COG4148 223 SRP 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-239 |
4.49e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 105.63 E-value: 4.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLlpegsYHVHHGRVTLLGEDVLNASEKQ 85
Cdd:COG1132 340 IEFENVSFSYP---GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF-----YDPTSGRILIDGVDIRDLTLES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQwrgaRVAMIFQEP----MTALnptrrigrqmvEVIRqhqsLSRRDAQQKAI--ALlgemqipDAAQVMD---RYPF- 155
Cdd:COG1132 412 LRR----QIGVVPQDTflfsGTIR-----------ENIR----YGRPDATDEEVeeAA-------KAAQAHEfieALPDg 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 156 ----------ELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARasGTSVLFISHDMAVVsQLCD 225
Cdd:COG1132 466 ydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTI-RNAD 542
|
250
....*....|....
gi 505383390 226 RMYVMYAGSVIESG 239
Cdd:COG1132 543 RILVLDDGRIVEQG 556
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-248 |
4.56e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.87 E-value: 4.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 4 SVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPegsyhVHHGRVTLLGEDVLNase 83
Cdd:COG1137 2 MTLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK-----PDSGRIFLDGEDITH--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 84 kqLRQWRGARVAMIF--QEPmtalnptrRIGRQM-VE----VIRQHQSLSRRDAQQKAIALLGEMQIpdaAQVMDRYPFE 156
Cdd:COG1137 70 --LPMHKRARLGIGYlpQEA--------SIFRKLtVEdnilAVLELRKLSKKEREERLEELLEEFGI---THLRKSKAYS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 LSGGMRQRVMIALAFSCEPELIIADEPTTALD-VTVQ--RQVLRLLKHKarasGTSVLFISHDmavVS---QLCDRMYVM 230
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDpIAVAdiQKIIRHLKER----GIGVLITDHN---VRetlGICDRAYII 209
|
250
....*....|....*...
gi 505383390 231 YAGSVIESGITQTLIHHP 248
Cdd:COG1137 210 SEGKVLAEGTPEEILNNP 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-249 |
5.15e-25 |
|
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: 100.77 E-value: 5.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLPeGSYHVHHGRVTLLGEDVLN--ASEKQlrqwrgarVAMI 97
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIA-GFETPTSGEILLDGKDITNlpPHKRP--------VNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 98 FQEpmTALNPTRRIGRQMVEVIRQhQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELSGGMRQRVMIALAFSCEPEL 177
Cdd:cd03300 78 FQN--YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYA---NRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505383390 178 IIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPV 249
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
29-252 |
5.22e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 103.96 E-value: 5.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 29 SLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGsyhvhHGRVTLLGEDVLNASEKQLRQWRGARVAMIFQE-----PMT 103
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT-----RGQVLIDGVDIAKISDAELREVRRKKIAMVFQSfalmpHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 104 ALNPTRrIGRQMVEVIRQHQslsrrdaQQKAIALLGEMQIPDAAQvmdRYPFELSGGMRQRVMIALAFSCEPELIIADEP 183
Cdd:PRK10070 123 VLDNTA-FGMELAGINAEER-------REKALDALRQVGLENYAH---SYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 184 TTALDVTVQRQVL-RLLKHKARASGTsVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPVHPY 252
Cdd:PRK10070 192 FSALDPLIRTEMQdELVKLQAKHQRT-IVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-239 |
8.13e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 100.47 E-value: 8.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpiFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMRLL--PE-GSYHVHHGRVTLLGedvlNAS 82
Cdd:PRK11124 1 MSIQLNGINC--FYGAHQALFDITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLemPRsGTLNIAGNHFDFSK----TPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 83 EKQLRQWRgARVAMIFQE----P-MTALN-----PTRRIGrqmvevirqhqsLSRRDAQQKAIALLGEMQIPDAAqvmDR 152
Cdd:PRK11124 74 DKAIRELR-RNVGMVFQQynlwPhLTVQQnlieaPCRVLG------------LSKDQALARAEKLLERLRLKPYA---DR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 153 YPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLfISHDMAVVSQLCDRMYVMYA 232
Cdd:PRK11124 138 FPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMEN 216
|
....*..
gi 505383390 233 GSVIESG 239
Cdd:PRK11124 217 GHIVEQG 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-239 |
1.10e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.86 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFPifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTA-MLAMRLLPEGsyhvhhGRVTLLGedvL 79
Cdd:PRK13635 1 MKEEIIRVEHISFRYP--DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAkLLNGLLLPEA------GTITVGG---M 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 80 NASEKQLRQWRgARVAMIFQEPMTALNPT------------RRIGR-QMVEVIRQhqslsrrdaqqkAIALLGeMQipda 146
Cdd:PRK13635 70 VLSEETVWDVR-RQVGMVFQNPDNQFVGAtvqddvafglenIGVPReEMVERVDQ------------ALRQVG-ME---- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 147 aQVMDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQlCDR 226
Cdd:PRK13635 132 -DFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADR 209
|
250
....*....|...
gi 505383390 227 MYVMYAGSVIESG 239
Cdd:PRK13635 210 VIVMNKGEILEEG 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
24-244 |
1.16e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.01 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 24 ALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSYHVHHGRVTLLGEdvlnASEKQLRQWRgARVAMIFQEPMT 103
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHK----TKDKYIRPVR-KRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 104 AL---NPTRRIgrqmvEVIRQHQSLSRRDAQQKAIALLgeMQIPDAAQVMDRYPFELSGGMRQRVMIALAFSCEPELIIA 180
Cdd:PRK13646 97 QLfedTVEREI-----IFGPKNFKMNLDEVKNYAHRLL--MDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383390 181 DEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTL 244
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-244 |
1.19e-24 |
|
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: 99.43 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLA-MRLLPegsyhVHHGRVTLLGEDVLN-ASE 83
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKT-TLLKTiMGLLP-----PRSGSIRFDGRDITGlPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 84 KQLRqwRGarVAMIFQEpmtalnptRRIGRQM--VEVIRQHQSLSRRDAQQKAIALLGEMqIPDAAQVMDRYPFELSGGM 161
Cdd:cd03224 71 ERAR--AG--IGYVPEG--------RRIFPELtvEENLLLGAYARRRAKRKARLERVYEL-FPRLKERRKQLAGTLSGGE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 162 RQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGIT 241
Cdd:cd03224 138 QQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIR-ELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTA 216
|
...
gi 505383390 242 QTL 244
Cdd:cd03224 217 AEL 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-239 |
1.65e-24 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 98.80 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGeIVGVVGESGSGKSvTAMLAMRLLPEGSYhvhhGRVTLLGEDVLNASEKq 85
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKT-TLMRILATLTPPSS----GTIRIDGQDVLKQPQK- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQwrgaRVAMIFQEPMTALNPTrriGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELSGGMRQRV 165
Cdd:cd03264 70 LRR----RIGYLPQEFGVYPNFT---VREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRA---KKKIGSLSGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383390 166 MIALAFSCEPELIIADEPTTALDVtVQRQVLRLLKHKArASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDP-EERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-248 |
3.83e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.93 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSfpIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKsvTAMLamRLLPeGSYHVHHGRVTLLGEDV--LNASE 83
Cdd:PRK10851 1 MSIEIANIK--KSFGRTQVLNDISLDIPSGQMVALLGPSGSGK--TTLL--RIIA-GLEHQTSGHIRFHGTDVsrLHARD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 84 KQlrqwrgarVAMIFQEpmTALNptrrigRQM---------VEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYP 154
Cdd:PRK10851 74 RK--------VGFVFQH--YALF------RHMtvfdniafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLA---DRYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 155 FELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLK--HKaRASGTSVlFISHDMAVVSQLCDRMYVMYA 232
Cdd:PRK10851 135 AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRqlHE-ELKFTSV-FVTHDQEEAMEVADRVVVMSQ 212
|
250
....*....|....*.
gi 505383390 233 GSVIESGITQTLIHHP 248
Cdd:PRK10851 213 GNIEQAGTPDQVWREP 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-256 |
3.97e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.40 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 3 DSVLSIEDLHLSFPIfRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAmrllpEGSYHVHHGRVTLLGEDVLNAS 82
Cdd:PRK13642 2 NKILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLI-----DGLFEEFEGKVKIDGELLTAEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 83 EKQLRQwrgaRVAMIFQEPmtalnPTRRIGRQMVEVI---RQHQSLSRRDAQQKAIALLGEMQIPDaaqVMDRYPFELSG 159
Cdd:PRK13642 76 VWNLRR----KIGMVFQNP-----DNQFVGATVEDDVafgMENQGIPREEMIKRVDEALLAVNMLD---FKTREPARLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 160 GMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQlCDRMYVMYAGSVIESG 239
Cdd:PRK13642 144 GQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEA 222
|
250
....*....|....*..
gi 505383390 240 ITQTLIHHPVHPYSIGL 256
Cdd:PRK13642 223 APSELFATSEDMVEIGL 239
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
8-245 |
6.52e-24 |
|
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: 97.61 E-value: 6.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 8 IEDLHLSFPIfRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLlpegsYHVHHGRVTLLGEDV--LNasekq 85
Cdd:cd03249 3 FKNVSFRYPS-RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERF-----YDPTSGEILLDGVDIrdLN----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQWRgARVAMIFQEPMTaLNPTrrigrqmvevIRQHQSLSRRDAQQK---AIALLGE-----MQIPDA--AQVMDRYpF 155
Cdd:cd03249 72 LRWLR-SQIGLVSQEPVL-FDGT----------IAENIRYGKPDATDEeveEAAKKANihdfiMSLPDGydTLVGERG-S 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 156 ELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARAsGTSVLFISHDMAVVsQLCDRMYVMYAGSV 235
Cdd:cd03249 139 QLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALD-RAMK-GRTTIVIAHRLSTI-RNADLIAVLQNGQV 215
|
250
....*....|
gi 505383390 236 IESGITQTLI 245
Cdd:cd03249 216 VEQGTHDELM 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-247 |
8.74e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 97.88 E-value: 8.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSfpifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLpEGSYHVHHGRVTLLGedvlnaseKQ 85
Cdd:COG4559 2 LEAENLSVR----LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTL----LKLL-TGELTPSSGEVRLNG--------RP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQWRGARVAmifqepmtalnptRRIGrqmveVIRQHQSLS-----------------RRDAQQKAIAllgemqipdaAQ 148
Cdd:COG4559 65 LAAWSPWELA-------------RRRA-----VLPQHSSLAfpftveevvalgraphgSSAAQDRQIV----------RE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 149 VMDR----------YPfELSGGMRQRVMIA--LA-----FSCEPELIIADEPTTALDVTVQRQVLRLLKHKARAsGTSVL 211
Cdd:COG4559 117 ALALvglahlagrsYQ-TLSGGEQQRVQLArvLAqlwepVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVV 194
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 505383390 212 FISHDMAVVSQLCDRMYVMYAGSVIESG-----ITQTLIHH 247
Cdd:COG4559 195 AVLHDLNLAAQYADRILLLHQGRLVAQGtpeevLTDELLER 235
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-250 |
8.86e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 98.24 E-value: 8.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSYHVHHGRVTLLGEDVLNAseKQLRQWRgARVAMIFQEPmta 104
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNY--RDVLEFR-RRVGMLFQRP--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 105 lNP-TRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAaqVMDRY---PFELSGGMRQRVMIALAFSCEPELIIA 180
Cdd:PRK14271 111 -NPfPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDA--VKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 181 DEPTTALDVTVQRQVLRLLkhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPVH 250
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFI--RSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKH 255
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-239 |
1.00e-23 |
|
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: 96.55 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLPeGSYHVHHGRVTLLGEDVLNASEKQ 85
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIA-GLEEPTSGRIYIGGRDVTDLPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 lrqwRGarVAMIFQEpmTALNPTRRIGRQMVevirqhQSLSRRDAQQKAIallgEMQIPDAA------QVMDRYPFELSG 159
Cdd:cd03301 72 ----RD--IAMVFQN--YALYPHMTVYDNIA------FGLKLRKVPKDEI----DERVREVAellqieHLLDRKPKQLSG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 160 GMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:cd03301 134 GQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-216 |
1.08e-23 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 96.39 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSfpifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSvtaMLaMRLLpEGSYHVHHGRVTLLGEDVlnasEK 84
Cdd:COG4133 2 MLEAENLSCR----RGERLLFSGLSFTLAAGEALALTGPNGSGKT---TL-LRIL-AGLLPPSAGEVLWNGEPI----RD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQWRgARVAMIFQEP-----MTALnptrrigrqmvEVIRQHQSLSRRDAQQKAI-ALLGEMQIPDAAqvmDRYPFELS 158
Cdd:COG4133 69 AREDYR-RRLAYLGHADglkpeLTVR-----------ENLRFWAALYGLRADREAIdEALEAVGLAGLA---DLPVRQLS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505383390 159 GGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHkARASGTSVLFISHD 216
Cdd:COG4133 134 AGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-226 |
1.15e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 96.77 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 8 IEDLHLSFPIFRGD--VHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMRLLPEGSyhvhHGRVTLLGEDVLNASEKQ 85
Cdd:PRK10584 7 VEVHHLKKSVGQGEheLSILTGVELVVKRGETIALIGESGSGKS-TLLAILAGLDDGS----SGEVSLVGQPLHQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQWRGARVAMIFQEPMtaLNPTRRiGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIpdaAQVMDRYPFELSGGMRQRV 165
Cdd:PRK10584 82 RAKLRAKHVGFVFQSFM--LIPTLN-ALENVELPALLRGESSRQSRNGAKALLEQLGL---GKRLDHLPAQLSGGEQQRV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505383390 166 MIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQlCDR 226
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDR 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
24-239 |
1.21e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 98.24 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 24 ALNHVSLEIGRGEIVGVVGESGSGKSVTA--MLAMrLLPEGsyhvhhGRVTLLGEDVLNasEKQLRQWRgARVAMIFQep 101
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAkhMNAL-LIPSE------GKVYVDGLDTSD--EENLWDIR-NKAGMVFQ-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 102 mtalNPTRRIGRQMVEV----------IRQHQSLSRRDAQQKAIAllgemqipdaaqvMDRY----PFELSGGMRQRVMI 167
Cdd:PRK13633 93 ----NPDNQIVATIVEEdvafgpenlgIPPEEIRERVDESLKKVG-------------MYEYrrhaPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505383390 168 ALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQlCDRMYVMYAGSVIESG 239
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
234-320 |
1.66e-23 |
|
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: 92.43 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 234 SVIESGITQTLIHHPVHPYSIGLLRCAPENGEPREILPAIPGTVPNLSHLPRGCAFRERCFAAGAKCSETPRLISTGAEG 313
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEIAEG 80
|
....*..
gi 505383390 314 QQAACWY 320
Cdd:TIGR01727 81 HRVACHL 87
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-239 |
1.79e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 97.37 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 2 SDSVLSIEDLHLSFPifRGDVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAmrllpeGSYHVHHGRVTLLGEDVLN 80
Cdd:PRK13632 4 KSVMIKVENVSFSYP--NSENNALKNVSFEINEGEYVAILGHNGSGKStISKILT------GLLKPQSGEIKIDGITISK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQLRQwrgaRVAMIFQepmtalNPTRR-IGRQMVEVIR---QHQSLSRRDAQQKaiallgemqIPDAAQV------M 150
Cdd:PRK13632 76 ENLKEIRK----KIGIIFQ------NPDNQfIGATVEDDIAfglENKKVPPKKMKDI---------IDDLAKKvgmedyL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 151 DRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSqLCDRMYVM 230
Cdd:PRK13632 137 DKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVF 215
|
....*....
gi 505383390 231 YAGSVIESG 239
Cdd:PRK13632 216 SEGKLIAQG 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-251 |
1.93e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 96.36 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 29 SLEIGRGEIVGVVGESGSGKSvT--AMLAmrllpeGSYHVHHGRVTLLGEDVLNASEkqlrqwrGAR-VAMIFQEP---- 101
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKS-TllNLIA------GFLPPDSGRILWNGQDLTALPP-------AERpVSMLFQENnlfp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 102 -MT-------ALNPTRRigrqmvevirqhqsLSRRDaQQKAIALLGEMQIpdaAQVMDRYPFELSGGMRQRVMIALAFSC 173
Cdd:COG3840 85 hLTvaqniglGLRPGLK--------------LTAEQ-RAQVEQALERVGL---AGLLDRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505383390 174 EPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPVHP 251
Cdd:COG3840 147 KRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-250 |
4.42e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 95.75 E-value: 4.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 4 SVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLL---PEGSYHvhhGRVTLLGEDVLN 80
Cdd:PRK14247 2 NKIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelyPEARVS---GEVYLDGQDIFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQLRQwrgaRVAMIFQEPmtalNPTRRI--------GRQMVEVIRqhqslSRRDAQQKAIALLGEMQIPDaaQVMDR 152
Cdd:PRK14247 75 MDVIELRR----RVQMVFQIP----NPIPNLsifenvalGLKLNRLVK-----SKKELQERVRWALEKAQLWD--EVKDR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 153 Y---PFELSGGMRQRVMIALAFSCEPELIIADEPTTALD----VTVQRQVLRLLKHKArasgtsVLFISHDMAVVSQLCD 225
Cdd:PRK14247 140 LdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDpentAKIESLFLELKKDMT------IVLVTHFPQQAARISD 213
|
250 260
....*....|....*....|....*
gi 505383390 226 RMYVMYAGSVIESGITQTLIHHPVH 250
Cdd:PRK14247 214 YVAFLYKGQIVEWGPTREVFTNPRH 238
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-239 |
5.35e-23 |
|
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: 95.48 E-value: 5.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 8 IEDLHLSFPIFRGD-----------------VHALNHVSLEIGRGEIVGVVGESGSGKSVT-AMLAMRLLPEGsyhvhhG 69
Cdd:cd03267 3 VSNLSKSYRVYSKEpgligslkslfkrkyreVEALKGISFTIEKGEIVGFIGPNGAGKTTTlKILSGLLQPTS------G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 70 RVTLLGEDVLNASEKQLRqwrgaRVAMIFQE---------PMTALNPTRRIGRqmvevirqhqsLSRRDAQQKaIALLGE 140
Cdd:cd03267 77 EVRVAGLVPWKRRKKFLR-----RIGVVFGQktqlwwdlpVIDSFYLLAAIYD-----------LPPARFKKR-LDELSE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 141 MQipDAAQVMDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVV 220
Cdd:cd03267 140 LL--DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDI 217
|
250
....*....|....*....
gi 505383390 221 SQLCDRMYVMYAGSVIESG 239
Cdd:cd03267 218 EALARRVLVIDKGRLLYDG 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-249 |
5.97e-23 |
|
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: 94.92 E-value: 5.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVT-AMLAmrllpeGSYHVHHGRVTLLGEDVlnaseK 84
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTfYMIV------GLVKPDSGKILLDGQDI-----T 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQWRGARVAMIF--QEP-----MTAlnptrrigRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIpdaAQVMDRYPFEL 157
Cdd:cd03218 66 KLPMHKRARLGIGYlpQEAsifrkLTV--------EENILAVLEIRGLSKKEREEKLEELLEEFHI---THLRKSKASSL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 158 SGGMRQRVMIALAFSCEPELIIADEPTTALD-VTVQ--RQVLRLLKhkarASGTSVLFISHDMAVVSQLCDRMYVMYAGS 234
Cdd:cd03218 135 SGGERRRVEIARALATNPKFLLLDEPFAGVDpIAVQdiQKIIKILK----DRGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
250
....*....|....*
gi 505383390 235 VIESGITQTLIHHPV 249
Cdd:cd03218 211 VLAEGTPEEIAANEL 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
24-239 |
7.41e-23 |
|
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: 94.99 E-value: 7.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 24 ALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLlpegsYHVHHGRVTLLGEDVLNASEKQLRqwrgARVAMIFQEPMT 103
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRF-----YDVDSGRILIDGHDVRDYTLASLR----RQIGLVSQDVFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 104 aLNPTrrigrqmvevIRQHQSLSRRDAQQKAI------ALLGE--MQIPDA--AQVMDRyPFELSGGMRQRVMIALAFSC 173
Cdd:cd03251 88 -FNDT----------VAENIAYGRPGATREEVeeaaraANAHEfiMELPEGydTVIGER-GVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 174 EPELIIADEPTTALDVTVQRQVLRLLKHKARasGTSVLFISHDMAVVSQlCDRMYVMYAGSVIESG 239
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-239 |
7.91e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 95.97 E-value: 7.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 24 ALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLpEGSYHVHHGRVTLLGEDVLNASE-KQLRQWRgARVAMIFQEPM 102
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTI----MQLL-NGLHVPTQGSVRVDDTLITSTSKnKDIKQIR-KKVGLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 103 TALNPTRRIgrQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDaaQVMDRYPFELSGGMRQRVMIALAFSCEPELIIADE 182
Cdd:PRK13649 96 SQLFEETVL--KDVAFGPQNFGVSQEEAEALAREKLALVGISE--SLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505383390 183 PTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFK-KLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-222 |
1.02e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 98.64 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 4 SVLSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMRLLPE---GSYHVhhgrvtlLGEDVLN 80
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLDKptsGTYRV-------AGQDVAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQLRQWRGARVAMIFQE-----PMTALnptrrigrQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAaqvMDRYPF 155
Cdd:PRK10535 75 LDADALAQLRREHFGFIFQRyhllsHLTAA--------QNVEVPAVYAGLERKQRLLRAQELLQRLGLEDR---VEYQPS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383390 156 ELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkHKARASGTSVLFISHDMAVVSQ 222
Cdd:PRK10535 144 QLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAIL-HQLRDRGHTVIIVTHDPQVAAQ 209
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
12-245 |
1.23e-22 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 94.48 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 12 HLSFPiFRGD-VHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQLRqwr 90
Cdd:cd03252 5 HVRFR-YKPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPEN-----GRVLVDGHDLALADPAWLR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 91 gARVAMIFQEPmTALNptrRIGRQMVEVIRQHQSLSR-RDAQQKAIALLGEMQIPDA-AQVMDRYPFELSGGMRQRVMIA 168
Cdd:cd03252 76 -RQVGVVLQEN-VLFN---RSIRDNIALADPGMSMERvIEAAKLAGAHDFISELPEGyDTIVGEQGAGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383390 169 LAFSCEPELIIADEPTTALDVTVQRQVLRLLkhKARASGTSVLFISHDMAVVSQlCDRMYVMYAGSVIESGITQTLI 245
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNM--HDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-239 |
1.26e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.19 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 3 DSVLSIEDLHLSFpifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMrllpEGSYHVHHGRVTLLGEDVLNAS 82
Cdd:PRK13647 2 DNIIEVEDLHFRY---KDGTKALKGLSLSIPEGSKTALLGPNGAGKS-TLLLHL----NGIYLPQRGRVKVMGREVNAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 83 EKQLRqwrgARVAMIFQEP------MTALNPtrrigrqmVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFE 156
Cdd:PRK13647 74 EKWVR----SKVGLVFQDPddqvfsSTVWDD--------VAFGPVNMGLDKDEVERRVEEALKAVRMWDFR---DKPPYH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 LSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVI 236
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILD-RLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
...
gi 505383390 237 ESG 239
Cdd:PRK13647 218 AEG 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-239 |
1.68e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.69 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 21 DVHALNHVSLEIGRGEIVGVVGESGSGKS--VTAMLAMRLLPEGSYHV------HHGRVTLLGEDVLNASEKQLRQWRgA 92
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKStlVTHFNGLIKSKYGTIQVgdiyigDKKNNHELITNPYSKKIKNFKELR-R 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 93 RVAMIFQEPMTALNPTRRIGRQMVEVIRQHQslSRRDAQQKAIALLGEMQIPDAaqVMDRYPFELSGGMRQRVMIALAFS 172
Cdd:PRK13631 117 RVSMVFQFPEYQLFKDTIEKDIMFGPVALGV--KKSEAKKLAKFYLNKMGLDDS--YLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383390 173 CEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLIL-DAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-235 |
2.35e-22 |
|
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: 92.86 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAMRLLPEGsyhvhhGRVTLLGEDVLNASEKQLRQWRgARVAMIF 98
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKStLLKLIYKEELPTS------GTIRVNGQDVSDLRGRAIPYLR-RKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 99 QEpmTALNPTRRIGRQM---VEVIRQhqslSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELSGGMRQRVMIALAFSCEP 175
Cdd:cd03292 85 QD--FRLLPDRNVYENVafaLEVTGV----PPREIRKRVPAALELVGLSHKH---RALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 176 ELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSV 235
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLK-KINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-239 |
2.80e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.93 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLL-PEgsyhvhHGRVTLLGEDVLNASEK 84
Cdd:PRK11231 3 LRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLtPQ------SGTVFLGDKPISMLSSR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQwrgaRVAMIFQEPMTalnPTRRIGRQMVEVIRQ-HQS----LSRRDAQQKAIAllgeMQIPDAAQVMDRYPFELSG 159
Cdd:PRK11231 73 QLAR----RLALLPQHHLT---PEGITVRELVAYGRSpWLSlwgrLSAEDNARVNQA----MEQTRINHLADRRLTDLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 160 GMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR-ELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-236 |
3.47e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.63 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLsfpifRGDVHalnHVSLEIGRGEIVGVVGESGSGKSVTAMLAMrllpeGSYHVHHGRVTLLGEDVLNASek 84
Cdd:COG1129 256 VLEVEGLSV-----GGVVR---DVSFSVRAGEILGIAGLVGAGRTELARALF-----GADPADSGEIRLDGKPVRIRS-- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 qLRQWRGARVAM---------IFQEpMT-----ALNPTRRIGRQMVevirqhqsLSRRDAQQKAIALLGEMQI--PDAAQ 148
Cdd:COG1129 321 -PRDAIRAGIAYvpedrkgegLVLD-LSireniTLASLDRLSRGGL--------LDRRRERALAEEYIKRLRIktPSPEQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 149 VMDrypfELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkHKARASGTSVLFISHDMAVVSQLCDRMY 228
Cdd:COG1129 391 PVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLI-RELAAEGKAVIVISSELPELLGLSDRIL 465
|
....*...
gi 505383390 229 VMYAGSVI 236
Cdd:COG1129 466 VMREGRIV 473
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-245 |
3.95e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.22 E-value: 3.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 7 SIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQL 86
Cdd:COG4604 3 EIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDS-----GEVLVDGLDVATTPSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 87 RQwrgaRVAMIFQEPMTALNPTRRigrQMVEVIR--QHQS-LSRRDAQ--QKAIALLG--EMQipdaaqvmDRYPFELSG 159
Cdd:COG4604 74 AK----RLAILRQENHINSRLTVR---ELVAFGRfpYSKGrLTAEDREiiDEAIAYLDleDLA--------DRYLDELSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 160 GMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
....*.
gi 505383390 240 ITQTLI 245
Cdd:COG4604 219 TPEEII 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
25-239 |
5.08e-22 |
|
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: 92.68 E-value: 5.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLlpegsYHVHHGRVTLLGEDVLNASEKQLRQwrgaRVAMIFQEpmTA 104
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRF-----YDVSSGSILIDGQDIREVTLDSLRR----AIGVVPQD--TV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 105 L-NPTR----RIGRqmvevirqhqsLSRRDAQQKAIALLGE-----MQIPDA--AQVMDRyPFELSGGMRQRVMIALAFS 172
Cdd:cd03253 86 LfNDTIgyniRYGR-----------PDATDEEVIEAAKAAQihdkiMRFPDGydTIVGER-GLKLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383390 173 CEPELIIADEPTTALDVTVQRQVLRLLkhKARASGTSVLFISHDMAVVSQlCDRMYVMYAGSVIESG 239
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAAL--RDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-215 |
6.00e-22 |
|
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: 92.84 E-value: 6.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 3 DSVLSIEDLHlsfpIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhHGRVTLLGEDVLNAS 82
Cdd:COG1119 1 DPLLELRNVT----VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTY----GNDVRLFGERRGGED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 83 EKQLRQ---WRGARVAMIFQEPMTALNptrrigrqMVE-----VIRQHQSLSRRDaQQKAIALLGEMQIpdaAQVMDRYP 154
Cdd:COG1119 73 VWELRKrigLVSPALQLRFPRDETVLD--------VVLsgffdSIGLYREPTDEQ-RERARELLELLGL---AHLADRPF 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505383390 155 FELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISH 215
Cdd:COG1119 141 GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-239 |
6.23e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.44 E-value: 6.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTamLAMRLLPEGSYHVHHGRVTLLGEDVLNAS--E 83
Cdd:COG0396 1 LEIKNLHVSV----EGKEILKGVNLTIKPGEVHAIMGPNGSGKS-T--LAKVLMGHPKYEVTSGSILLDGEDILELSpdE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 84 kqlRQWRGarVAMIFQEPM------------TALNPTRRigrqmvevirqhQSLSRRDAQQKAIALLGEMQIPDAAqvMD 151
Cdd:COG0396 74 ---RARAG--IFLAFQYPVeipgvsvsnflrTALNARRG------------EELSAREFLKLLKEKMKELGLDEDF--LD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 152 RYPFE-LSGGMRQRV----MIALafscEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISH-----DMAVVs 221
Cdd:COG0396 135 RYVNEgFSGGEKKRNeilqMLLL----EPKLAILDETDSGLDIDALRIVAEGVN-KLRSPDRGILIITHyqrilDYIKP- 208
|
250
....*....|....*...
gi 505383390 222 qlcDRMYVMYAGSVIESG 239
Cdd:COG0396 209 ---DFVHVLVDGRIVKSG 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-248 |
7.73e-22 |
|
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: 91.97 E-value: 7.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 3 DSVLSIEDLHlsfpIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPegsyhVHHGRVTLLGEDVLNAS 82
Cdd:COG0410 1 MPMLEVENLH----AGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP-----PRSGSIRFDGEDITGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 83 EKQLRQwRGarVAMIFQEpmtalnptRRIGRQM-VEvirqhQSL-----SRRDAQQKAiallgemqiPDAAQVMDRYP-- 154
Cdd:COG0410 72 PHRIAR-LG--IGYVPEG--------RRIFPSLtVE-----ENLllgayARRDRAEVR---------ADLERVYELFPrl 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 155 --------FELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDR 226
Cdd:COG0410 127 kerrrqraGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIR-RLNREGVTILLVEQNARFALEIADR 205
|
250 260
....*....|....*....|..
gi 505383390 227 MYVMYAGSVIESGITQTLIHHP 248
Cdd:COG0410 206 AYVLERGRIVLEGTAAELLADP 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-250 |
8.15e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.53 E-value: 8.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLsfpiFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMR----LLPEgsyhvhhgrVTLLGE 76
Cdd:PRK14239 1 MTEPILQVSDLSV----YYNKKKALNSVSLDFYPNEITALIGPSGSGKS-TLLRSINrmndLNPE---------VTITGS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 77 DVLN--------ASEKQLRQwrgaRVAMIFQEPmtalNP-TRRIGRQMVEVIRqhqslsrrdaqqkaIALLGEMQIPDAA 147
Cdd:PRK14239 67 IVYNghniysprTDTVDLRK----EIGMVFQQP----NPfPMSIYENVVYGLR--------------LKGIKDKQVLDEA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 148 ------------QVMDRY---PFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQV---LRLLKHKarasgTS 209
Cdd:PRK14239 125 vekslkgasiwdEVKDRLhdsALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIeetLLGLKDD-----YT 199
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 505383390 210 VLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPVH 250
Cdd:PRK14239 200 MLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-239 |
8.23e-22 |
|
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: 91.83 E-value: 8.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPIF------------------RGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLpEGSYHVH 67
Cdd:cd03220 1 IELENVSKSYPTYkggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTL----LRLL-AGIYPPD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 68 HGRVTLLGedvlnasekqlrqwrgaRVAMIFqEPMTALNP-------TRRIGRQMvevirqhqSLSRRDAQQK-----AI 135
Cdd:cd03220 76 SGTVTVRG-----------------RVSSLL-GLGGGFNPeltgrenIYLNGRLL--------GLSRKEIDEKideiiEF 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 136 ALLGEmqipdaaqVMDRyPF-ELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKaRASGTSVLFIS 214
Cdd:cd03220 130 SELGD--------FIDL-PVkTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVS 199
|
250 260
....*....|....*....|....*
gi 505383390 215 HDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:cd03220 200 HDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-247 |
1.60e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 92.84 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 22 VHALNHVSLEIGRGEIVGVVGESGSGKSVT-AMLAMRLLPEGsyhvhhGRVTLLGEDVLNASEKQLRQwrgarVAMIF-Q 99
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTiKMLTGILVPTS------GEVRVLGYVPFKRRKEFARR-----IGVVFgQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 100 epmtalnptrrigRQMVevirqHQSLSRRDAqqkaIALLGEM-QIPDAA--QVMDRY-------PF------ELSGGMRQ 163
Cdd:COG4586 104 -------------RSQL-----WWDLPAIDS----FRLLKAIyRIPDAEykKRLDELvelldlgELldtpvrQLSLGQRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 164 RVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQT 243
Cdd:COG4586 162 RCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEE 241
|
....
gi 505383390 244 LIHH 247
Cdd:COG4586 242 LKER 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-245 |
4.96e-21 |
|
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: 93.33 E-value: 4.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSV-TAML-AMRLLPEGS----YHVHH-------GRVT 72
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVlMHVLrGMDQYEPTSgriiYHVALcekcgyvERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 73 LLGE--------------DVLNASEKQLRQWRgARVAMIFQEPMtALNPTRRIgrqMVEVIRQHQSL--SRRDAQQKAIA 136
Cdd:TIGR03269 77 KVGEpcpvcggtlepeevDFWNLSDKLRRRIR-KRIAIMLQRTF-ALYGDDTV---LDNVLEALEEIgyEGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 137 LLGEMQIPDAAQVMDRypfELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHD 216
Cdd:TIGR03269 152 LIEMVQLSHRITHIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHW 228
|
250 260
....*....|....*....|....*....
gi 505383390 217 MAVVSQLCDRMYVMYAGSVIESGITQTLI 245
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEGTPDEVV 257
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-239 |
5.50e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 90.68 E-value: 5.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFPifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVtLLGEDVLN 80
Cdd:PRK13636 1 MEDYILKVEELNYNYS---DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSS-----GRI-LFDGKPID 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQLRQWRGArVAMIFQEPMTALNPTRRIgrQMVEVIRQHQSLSRRDAQQKAIALLGEMQIpdaAQVMDRYPFELSGG 160
Cdd:PRK13636 72 YSRKGLMKLRES-VGMVFQDPDNQLFSASVY--QDVSFGAVNLKLPEDEVRKRVDNALKRTGI---EHLKDKPTHCLSFG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383390 161 MRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-252 |
8.20e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 91.33 E-value: 8.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 28 VSLEIGRGEIVGVVGESGSGK-SVTAMLAMRLLPEGsyhvhhGRVTLLGEdVLNASEK--QLRQWRgARVAMIFQEpmTA 104
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKtTLIRLIAGLTRPDE------GEIVLNGR-TLFDSRKgiFLPPEK-RRIGYVFQE--AR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 105 LNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGemqipdAAQVMDRYPFELSGGMRQRVMIALAFSCEPELIIADEPT 184
Cdd:TIGR02142 86 LFPHLSVRGNLRYGMKRARPSERRISFERVIELLG------IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505383390 185 TALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPVHPY 252
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
24-239 |
8.82e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.45 E-value: 8.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 24 ALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLpegsyhVHHGRVTLLGEDVLNASEKQLRQWRGAR--VAMIFQEP 101
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI------ISETGQTIVGDYAIPANLKKIKEVKRLRkeIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 102 MTALnptrrigrqMVEVIRQ-------HQSLSRRDAQQKAIALLGEMQIPDaaQVMDRYPFELSGGMRQRVMIALAFSCE 174
Cdd:PRK13645 100 EYQL---------FQETIEKdiafgpvNLGENKQEAYKKVPELLKLVQLPE--DYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 175 PELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-239 |
8.90e-21 |
|
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: 87.75 E-value: 8.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAmrllpEGSYHVHHGRVTLLGEDVLNAsEKQ 85
Cdd:cd03247 1 LSINNVSFSYP--EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLL-----TGDLKPQQGEITLDGVPVSDL-EKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQwrgaRVAMIFQEPMTaLNPTRRigrqmvevirqhQSLSRRdaqqkaiallgemqipdaaqvmdrypfeLSGGMRQRV 165
Cdd:cd03247 73 LSS----LISVLNQRPYL-FDTTLR------------NNLGRR----------------------------FSGGERQRL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383390 166 MIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARasGTSVLFISHDMAVVSQLcDRMYVMYAGSVIESG 239
Cdd:cd03247 108 ALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-256 |
1.21e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.43 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFPiFRGDV-HALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMrllpeGSYHVHHGRVTLLGEDVL 79
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQ-YQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMI-----GIEKVKSGEIFYNNQAIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 80 NASEKQLRQwrgaRVAMIFQEPmtalnptrriGRQMVEVIRQH--------QSLSRRDAQQKAIALLGEMQIPDAAqvmD 151
Cdd:PRK13648 75 DDNFEKLRK----HIGIVFQNP----------DNQFVGSIVKYdvafglenHAVPYDEMHRRVSEALKQVDMLERA---D 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 152 RYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQlCDRMYVMY 231
Cdd:PRK13648 138 YEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMN 216
|
250 260
....*....|....*....|....*
gi 505383390 232 AGSVIESGITQTLIHHPVHPYSIGL 256
Cdd:PRK13648 217 KGTVYKEGTPTEIFDHAEELTRIGL 241
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-239 |
1.41e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 89.37 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFPifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMrllpEGSYHVHHGRVTLLGEDvLNASEK 84
Cdd:PRK13639 1 ILETRDLKYSYP---DGTEALKGINFKAEKGEMVALLGPNGAGKS-TLFLHF----NGILKPTSGEVLIKGEP-IKYDKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQWRgARVAMIFQEPMTAL-NPTRR---------IGRQMVEVIRqhqslsRRDAQQKAIALLGEMQIPdaaqvmdryP 154
Cdd:PRK13639 72 SLLEVR-KTVGIVFQNPDDQLfAPTVEedvafgplnLGLSKEEVEK------RVKEALKAVGMEGFENKP---------P 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 155 FELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGS 234
Cdd:PRK13639 136 HHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLL-YDLNKEGITIIISTHDVDLVPVYADKVYVMSDGK 214
|
....*
gi 505383390 235 VIESG 239
Cdd:PRK13639 215 IIKEG 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-256 |
1.73e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.47 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEdlHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAMRLLPEGSyhvHHGRVTLLGedvL 79
Cdd:PRK13640 1 MKDNIVEFK--HVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKStISKLINGLLLPDDN---PNSKITVDG---I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 80 NASEKQLRQWRgARVAMIFQEPMTALN------------PTRRIGR-QMVEVIRQhqslsrrdaqqkAIALLGEMQIPDA 146
Cdd:PRK13640 73 TLTAKTVWDIR-EKVGIVFQNPDNQFVgatvgddvafglENRAVPRpEMIKIVRD------------VLADVGMLDYIDS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 147 AqvmdryPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQlCDR 226
Cdd:PRK13640 140 E------PANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQ 212
|
250 260 270
....*....|....*....|....*....|
gi 505383390 227 MYVMYAGSVIESGITQTLIHHPVHPYSIGL 256
Cdd:PRK13640 213 VLVLDDGKLLAQGSPVEIFSKVEMLKEIGL 242
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-239 |
3.14e-20 |
|
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: 86.81 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSfpifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVtamLAMRLLPEGSYHVHHGRVTLLGEDVLNAsEKQ 85
Cdd:cd03217 1 LEIKDLHVS----VGGKEILKGVNLTIKKGEVHALMGPNGSGKST---LAKTIMGHPKYEVTEGEILFKGEDITDL-PPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQWRGarVAMIFQEPmtalnptrrigrqmvevirqhqslsrrdaqqkaiallgeMQIPdAAQVMD--RYPFE-LSGGMR 162
Cdd:cd03217 73 ERARLG--IFLAFQYP---------------------------------------PEIP-GVKNADflRYVNEgFSGGEK 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505383390 163 QRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQL-CDRMYVMYAGSVIESG 239
Cdd:cd03217 111 KRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVIN-KLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-250 |
3.44e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.98 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 7 SIEDLHLSfpIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSYHVHHGRVTLLGEDVLNASEKQL 86
Cdd:PRK14267 4 AIETVNLR--VYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 87 RQWRgaRVAMIFQEPmtalNP--------TRRIGRQMVEVIRQHQSLSRRD--AQQKAiALLGEmqipdaaqVMDR---Y 153
Cdd:PRK14267 82 EVRR--EVGMVFQYP----NPfphltiydNVAIGVKLNGLVKSKKELDERVewALKKA-ALWDE--------VKDRlndY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 154 PFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkHKARASGTSVLfISHDMAVVSQLCDRMYVMYAG 233
Cdd:PRK14267 147 PSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELL-FELKKEYTIVL-VTHSPAQAARVSDYVAFLYLG 224
|
250
....*....|....*..
gi 505383390 234 SVIESGITQTLIHHPVH 250
Cdd:PRK14267 225 KLIEVGPTRKVFENPEH 241
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-248 |
4.88e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.94 E-value: 4.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 8 IEDLHLSFpIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQLR 87
Cdd:PRK13652 4 IETRDLCY-SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTS-----GSVLIRGEPITKENIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 88 QWrgarVAMIFQEPMTAL-NPT--RRIGRQMVEVIRQHQSLSRRdaQQKAIALLGemqipdAAQVMDRYPFELSGGMRQR 164
Cdd:PRK13652 78 KF----VGLVFQNPDDQIfSPTveQDIAFGPINLGLDEETVAHR--VSSALHMLG------LEELRDRVPHHLSGGEKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 165 VMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTL 244
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
....
gi 505383390 245 IHHP 248
Cdd:PRK13652 226 FLQP 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-217 |
8.09e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.06 E-value: 8.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 24 ALNHVSLEIGRGEIVGVVGESGSGKsvTAMLAmrlLPEGSYHVHHGRVTLLGEDVlnasekqlrQWRGARVAMIFQEpmT 103
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGK--TTLLN---LIAGFVPYQHGSITLDGKPV---------EGPGAERGVVFQN--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 104 ALNPTRRIgRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAQvmdRYPFELSGGMRQRVMIALAFSCEPELIIADEP 183
Cdd:PRK11248 80 GLLPWRNV-QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEK---RYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190
....*....|....*....|....*....|....
gi 505383390 184 TTALDVTVQRQVLRLLKHKARASGTSVLFISHDM 217
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-221 |
1.35e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.98 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSYHVHHGRvtllgedvlnasekqlrqwrGARVAMIFQ 99
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG--------------------GARVAYVPQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 100 E-------PMTAlnptrrigRQMVEVIR-QHQSLSRR---DAQQKAIALLGEMQIPDAAqvmDRYPFELSGGMRQRVMIA 168
Cdd:NF040873 63 RsevpdslPLTV--------RDLVAMGRwARRGLWRRltrDDRAAVDDALERVGLADLA---GRQLGELSGGQRQRALLA 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505383390 169 LAFSCEPELIIADEPTTALDVTVQRQVLRLLKHkARASGTSVLFISHDMAVVS 221
Cdd:NF040873 132 QGLAQEADLLLLDEPTTGLDAESRERIIALLAE-EHARGATVVVVTHDLELVR 183
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
236-300 |
1.70e-19 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus 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.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 80.91 E-value: 1.70e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 236 IESGITQTLIHHPVHPYSIGLLRCAPENGEPREILPAIPGTVPNLSHLPRGCAFRERCFAAGAKC 300
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-239 |
2.48e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 86.33 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 24 ALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSYHVHHGRVTLLGedvlNASEKQLRQWRgARVAMIFQEPMT 103
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSS----TSKQKEIKPVR-KKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 104 ALNPTRRIgrQMVEVIRQHQSLSRRDAQQKAIALLgEMqIPDAAQVMDRYPFELSGGMRQRVMIALAFSCEPELIIADEP 183
Cdd:PRK13643 96 QLFEETVL--KDVAFGPQNFGIPKEKAEKIAAEKL-EM-VGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 184 TTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:PRK13643 172 TAGLDPKARIEMMQLFE-SIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-237 |
3.46e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 3.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvT--AMLAMRLLPEGsyhvhhGRVTlLGEDVlnas 82
Cdd:COG0488 315 VLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKS-TllKLLAGELEPDS------GTVK-LGETV---- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 83 ekqlrqwrgaRVAMIFQEpMTALNPTRRIgrqmVEVIRQhqsLSRRDAQQKAIALLGEMQIPDAAQvmDRYPFELSGGMR 162
Cdd:COG0488 379 ----------KIGYFDQH-QEELDPDKTV----LDELRD---GAPGGTEQEVRGYLGRFLFSGDDA--FKPVGVLSGGEK 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 163 QRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHkarASGTsVLFISHDMAVVSQLCDRMYVMYAGSVIE 237
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD---FPGT-VLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-239 |
4.23e-19 |
|
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: 84.08 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 27 HVSLEIGRGEIVGVVGESGSGKS-VTAMLAMRLLPEGsyhvhhGRVTLLGEDVlNASEKQLRQwrgarVAMIFQEP--MT 103
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKStLLNLIAGFETPQS------GRVLINGVDV-TAAPPADRP-----VSMLFQENnlFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 104 ALNPTRRIGRQMVEvirqhqSLSRRDAQQKAI-ALLGEMQIpdaAQVMDRYPFELSGGMRQRVMIALAFSCEPELIIADE 182
Cdd:cd03298 84 HLTVEQNVGLGLSP------GLKLTAEDRQAIeVALARVGL---AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505383390 183 PTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-236 |
5.72e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 84.75 E-value: 5.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpiFRG---DVHALNHVSLEIGRGEIVGVVGESGSGKSvT--AMLAmrllpeGSYHVHHGRVTLLGEDVLN 80
Cdd:COG1101 2 LELKNLSKTF--NPGtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKS-TllNAIA------GSLPPDSGSILIDGKDVTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQlrqwRGARVAMIFQEP-------MT-------ALNPTRRIGrqmvevIRQHQSLSRRDAQQKAIALLG---EMQI 143
Cdd:COG1101 73 LPEYK----RAKYIGRVFQDPmmgtapsMTieenlalAYRRGKRRG------LRRGLTKKRRELFRELLATLGlglENRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 144 PDAAQVmdrypfeLSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDM--AVvs 221
Cdd:COG1101 143 DTKVGL-------LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMeqAL-- 213
|
250
....*....|....*
gi 505383390 222 QLCDRMYVMYAGSVI 236
Cdd:COG1101 214 DYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
25-241 |
9.79e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.40 E-value: 9.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQLRQwrgaRVAMIFQepmta 104
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES-----GQIIIDGDLLTEENVWDIRH----KIGMVFQ----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 105 lNPTRRIGRQMVE----VIRQHQSLSRRDAQ---QKAIALLGeMQipdaaQVMDRYPFELSGGMRQRVMIALAFSCEPEL 177
Cdd:PRK13650 89 -NPDNQFVGATVEddvaFGLENKGIPHEEMKervNEALELVG-MQ-----DFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383390 178 IIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSqLCDRMYVMYAGSViESGIT 241
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV-ESTST 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-248 |
1.34e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.56 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 2 SDSVLSIEDLHLsfpiFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSYHVH-HGRVTLLGEDVLN 80
Cdd:PRK14246 7 AEDVFNISRLYL----YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKvDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQLRQwrgaRVAMIFQEPMTAlnPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIpdAAQVMDRY---PFEL 157
Cdd:PRK14246 83 IDAIKLRK----EVGMVFQQPNPF--PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGL--WKEVYDRLnspASQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 158 SGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARAsgTSVLFISHDMAVVSQLCDRMYVMYAGSVIE 237
Cdd:PRK14246 155 SGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
250
....*....|.
gi 505383390 238 SGITQTLIHHP 248
Cdd:PRK14246 233 WGSSNEIFTSP 243
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-218 |
1.41e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 82.53 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHlsfpIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAMRLLPEGSYhvhHGRVTLLGEDvLNASEK 84
Cdd:COG4136 2 LSLENLT----ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKStLLAAIAGTLSPAFSA---SGEVLLNGRR-LTALPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRqwrgaRVAMIFQEPMtaLNPTRRIGRQMVEVIRqhQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELSGGMRQR 164
Cdd:COG4136 74 EQR-----RIGILFQDDL--LFPHLSVGENLAFALP--PTIGRAQRRARVEQALEEAGLAGFA---DRDPATLSGGQRAR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505383390 165 VMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMA 218
Cdd:COG4136 142 VALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-249 |
2.01e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.09 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamLAMRLlpeGSYHVHHGRVTLLGEDVLN 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTT--LRMLL---GLTHPDAGSISLCGEPVPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASekqlRQWRgARVAMIFQepMTALNPTRRIgRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAQVMDRypfELSGG 160
Cdd:PRK13537 74 RA----RHAR-QRVGVVPQ--FDNLDPDFTV-RENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVG---ELSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 161 MRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGI 240
Cdd:PRK13537 143 MKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLR-SLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGA 221
|
....*....
gi 505383390 241 TQTLIHHPV 249
Cdd:PRK13537 222 PHALIESEI 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-216 |
2.60e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.50 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 8 IEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTamLaMRLLpEGSYHVHHGRVTLLgedvlnasekqlr 87
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKS-T--L-LKIL-AGELEPDSGEVSIP------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 88 qwRGARVAMIFQEP------------MTALNPTRRIGRQMVEV----------IRQHQSLSRR-------DAQQKAIALL 138
Cdd:COG0488 59 --KGLRIGYLPQEPpldddltvldtvLDGDAELRALEAELEELeaklaepdedLERLAELQEEfealggwEAEARAEEIL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383390 139 GEMQIPDAAQvmDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDV-TVQrqvlRLLKHKARASGTsVLFISHD 216
Cdd:COG0488 137 SGLGFPEEDL--DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIE----WLEEFLKNYPGT-VLVVSHD 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-245 |
2.71e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.26 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRllpegSYHVHHGRVTLLGEDVLNASEKQ 85
Cdd:PRK11160 339 LTLNNVSFTYP--DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTR-----AWDPQQGEILLNGQPIADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQwrgarvamifqePMTALNptrrigrQMVEVIrqhqSLSRRDAQQKAIALLGEMQIPDA-AQVMDRYPFE-------- 156
Cdd:PRK11160 412 LRQ------------AISVVS-------QRVHLF----SATLRDNLLLAAPNASDEALIEVlQQVGLEKLLEddkglnaw 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 -------LSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARasGTSVLFISHDMAVVSQLcDRMYV 229
Cdd:PRK11160 469 lgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICV 545
|
250
....*....|....*.
gi 505383390 230 MYAGSVIESGITQTLI 245
Cdd:PRK11160 546 MDNGQIIEQGTHQELL 561
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
25-227 |
2.76e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.17 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQLRQWRGARVAMIFQ----- 99
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTS-----GDVIFNGQPMSKLSSAAKAELRNQKLGFIYQfhhll 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 100 EPMTALNPTRR---IGRQmvevirqhqslSRRDAQQKAIALLGEMQIPDAAQvmdRYPFELSGGMRQRVMIALAFSCEPE 176
Cdd:PRK11629 100 PDFTALENVAMpllIGKK-----------KPAEINSRALEMLAAVGLEHRAN---HRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505383390 177 LIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMavvsQLCDRM 227
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL----QLAKRM 212
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
28-239 |
3.65e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 28 VSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDV--LNASEKQLRQwrgarVAMIFQEPmtal 105
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA-----GNIIIDDEDIslLPLHARARRG-----IGYLPQEA---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 106 NPTRRIG--RQMVEVIRQHQSLSRRDAQQKAIALLGEMQIpdaAQVMDRYPFELSGGMRQRVMIALAFSCEPELIIADEP 183
Cdd:PRK10895 88 SIFRRLSvyDNLMAVLQIRDDLSAEQREDRANELMEEFHI---EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 184 TTALDVTVQRQVLRLLKHkARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHG 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-248 |
4.21e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.73 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFPifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVtamLAMRLlpEGSYHVHHGRVTLLGEDVLNASEK 84
Cdd:PRK13644 1 MIRLENVSYSYP---DGTPALENINLVIKKGEYIGIIGKNGSGKST---LALHL--NGLLRPQKGKVLVSGIDTGDFSKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QlrqwrGAR--VAMIFQEPMTALnptrrIGRQMVEVIR---QHQSLSRRDAQQKAIALLGEMQIpdaAQVMDRYPFELSG 159
Cdd:PRK13644 73 Q-----GIRklVGIVFQNPETQF-----VGRTVEEDLAfgpENLCLPPIEIRKRVDRALAEIGL---EKYRHRSPKTLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 160 GMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVsQLCDRMYVMYAGSVIESG 239
Cdd:PRK13644 140 GQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIK-KLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEG 217
|
....*....
gi 505383390 240 ITQTLIHHP 248
Cdd:PRK13644 218 EPENVLSDV 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-230 |
5.05e-18 |
|
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: 84.65 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 2 SDSVLSIEDLHLSFPifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNA 81
Cdd:TIGR02857 318 PASSLEFSGVSVAYP---GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTE-----GSIAVNGVPLADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 82 SEKQLRQwrgaRVAMIFQEPmTALNPTrrigrqMVEVIRqhqsLSRRDAQ----QKAIALLGEMQIPDAA-----QVMDR 152
Cdd:TIGR02857 390 DADSWRD----QIAWVPQHP-FLFAGT------IAENIR----LARPDASdaeiREALERAGLDEFVAALpqgldTPIGE 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505383390 153 YPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkhKARASGTSVLFISHDMAVVsQLCDRMYVM 230
Cdd:TIGR02857 455 GGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEAL--RALAQGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-245 |
6.14e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.34 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLnasekqlRQWRGARVAMIFQ 99
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA-----GKITVLGVPVP-------ARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 100 EPMTALNPTRRIgRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELSGGMRQRVMIALAFSCEPELII 179
Cdd:PRK13536 120 PQFDNLDLEFTV-RENLLVFGRYFGMSTREIEAVIPSLLEFARLESKA---DARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 180 ADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLI 245
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLR-SLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-244 |
8.25e-18 |
|
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: 80.97 E-value: 8.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAMRLLPEgsyhvhHGRVTLLGEDVLNASEKQ--------LRQWRGAR-- 93
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKStLLNLISGLAQPT------SGGVILEGKQITEPGPDRmvvfqnysLLPWLTVRen 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 94 VAMIFQEPMTALNPTRRigrqmVEVIRQHqslsrrdaqqkaIALLGemqIPDAAqvmDRYPFELSGGMRQRVMIALAFSC 173
Cdd:TIGR01184 75 IALAVDRVLPDLSKSER-----RAIVEEH------------IALVG---LTEAA---DKRPGQLSGGMKQRVAIARALSI 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505383390 174 EPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSviESGITQTL 244
Cdd:TIGR01184 132 RPKVLLLDEPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGP--AANIGQIL 200
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-216 |
1.06e-17 |
|
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: 83.56 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEgsyhvHHGRVTLLGEDVLNASEKQ 85
Cdd:TIGR02868 335 LELRDLSAGYP---GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP-----LQGEVTLDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRqwrgARVAMIFQEPM---TALNPTRRIGR------QMVEVIRQhqslsrrdaqqkaiALLGEM--QIPDAAQ-VMDRY 153
Cdd:TIGR02868 407 VR----RRVSVCAQDAHlfdTTVRENLRLARpdatdeELWAALER--------------VGLADWlrALPDGLDtVLGEG 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505383390 154 PFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkhKARASGTSVLFISHD 216
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
10-244 |
1.59e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 83.23 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 10 DLHLSFPIfRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLlpegsYHVHHGRVTLLGEDVLNASEKQLRQw 89
Cdd:TIGR00958 483 DVSFSYPN-RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL-----YQPTGGQVLLDGVPLVQYDHHYLHR- 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 90 rgaRVAMIFQEPMTalnptrrIGRQMVEVI----RQHQSLSRRDAQQKAIALLGEMQIPDAAQ-VMDRYPFELSGGMRQR 164
Cdd:TIGR00958 556 ---QVALVGQEPVL-------FSGSVRENIayglTDTPDEEIMAAAKAANAHDFIMEFPNGYDtEVGEKGSQLSGGQKQR 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 165 VMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARasgtSVLFISHDMAVVSQlCDRMYVMYAGSVIESGITQTL 244
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASR----TVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
19-248 |
2.94e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.19 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 19 RGDVHALNHVSLEIGRGEIVGVVGESGSGKsvTAMLamRLLpEGSYHVHHGRVTLLGEDVLNASEKQLRQWRgARVAMIF 98
Cdd:PRK11831 17 RGNRCIFDNISLTVPRGKITAIMGPSGIGK--TTLL--RLI-GGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 99 QEP--MTALNPTRRIGRQMVEVIRQHQSLSRRDAQQK--AIALLGemqipdAAQVMdryPFELSGGMRQRVMIALAFSCE 174
Cdd:PRK11831 91 QSGalFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKleAVGLRG------AAKLM---PSELSGGMARRAALARAIALE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383390 175 PELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHP 248
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-253 |
3.17e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.42 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAmrllpeGSYHVHHGRVTLLGEDVLNASE 83
Cdd:PRK11607 19 LLEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKStLLRMLA------GFEQPTAGQIMLDGVDLSHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 84 KQlrqwrgARVAMIFQEpmTALNPTRRIGRQMVEVIRQHQsLSRRDAQQKAIALLGEMQIPDAAQvmdRYPFELSGGMRQ 163
Cdd:PRK11607 89 YQ------RPINMMFQS--YALFPHMTVEQNIAFGLKQDK-LPKAEIASRVNEMLGLVHMQEFAK---RKPHQLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 164 RVMIALAFSCEPELIIADEPTTALDVTV----QRQVLRLLKhkaRASGTSVLfISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILE---RVGVTCVM-VTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
250
....*....|....
gi 505383390 240 ITQTLIHHPVHPYS 253
Cdd:PRK11607 233 EPEEIYEHPTTRYS 246
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-257 |
3.84e-17 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 80.62 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 40 VVGESGSGKSVTAMLAmrllpEGSYHVHHGRVTLLGEDVLNASeKQLRQwrgarVAMIFQEpmTALNPTRRIGRQMVEVI 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLL-----AGFEQPDSGSIMLDGEDVTNVP-PHLRH-----INMVFQS--YALFPHMTVEENVAFGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 120 RQhQSLSRRDAQQKAIALLGEMQIPDAAQvmdRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLL 199
Cdd:TIGR01187 68 KM-RKVPRAEIKPRVLEALRLVQLEEFAD---RKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505383390 200 KHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHPVHPYSIGLL 257
Cdd:TIGR01187 144 KTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-236 |
5.11e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.59 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFPifrgDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLpEGSYHVHHGRVTLLGEDVLNASEK 84
Cdd:PRK10762 4 LLQLKGIDKAFP----GVKALSGAALNVYPGRVMALVGENGAGKSTM----MKVL-TGIYTRDAGSILYLGKEVTFNGPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQwrgARVAMIFQEpmtaLN--PTRRI------GRQMVEVIrqhQSLSRRDAQQKAIALLGEMQIPDAAQvmdRYPFE 156
Cdd:PRK10762 75 SSQE---AGIGIIHQE----LNliPQLTIaeniflGREFVNRF---GRIDWKKMYAEADKLLARLNLRFSSD---KLVGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 LSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVI 236
Cdd:PRK10762 142 LSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIR-ELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-239 |
7.27e-17 |
|
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: 80.95 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVtamLAmRLLPeGSYHVHHGRVTLLGEDvlnasekq 85
Cdd:COG4618 331 LSVENLTVVPP--GSKRPILRGVSFSLEPGEVLGVIGPSGSGKST---LA-RLLV-GVWPPTAGSVRLDGAD-------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRQWRGARVAmifqepmtalnptRRIGR--QMVEV----IRQHqslsrrdaqqkaIALLGEmqiPDAAQVMD-------- 151
Cdd:COG4618 396 LSQWDREELG-------------RHIGYlpQDVELfdgtIAEN------------IARFGD---ADPEKVVAaaklagvh 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 152 ----RYP-----------FELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHkARASGTSVLFISHD 216
Cdd:COG4618 448 emilRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRA-LKARGATVVVITHR 526
|
250 260
....*....|....*....|...
gi 505383390 217 MAVVSQlCDRMYVMYAGSVIESG 239
Cdd:COG4618 527 PSLLAA-VDKLLVLRDGRVQAFG 548
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-278 |
7.73e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.06 E-value: 7.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 2 SDSVLSIEDLHLSFPiFRGDVHALnhvSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLlgedvlna 81
Cdd:PRK10575 8 SDTTFALRNVSFRVP-GRTLLHPL---SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSE-----GEILL-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 82 SEKQLRQWRG---AR-VAMIFQ-----EPMTAlnptrrigRQMVEVIRQ--HQSLSR-----RDAQQKAIALLGEMqiPD 145
Cdd:PRK10575 71 DAQPLESWSSkafARkVAYLPQqlpaaEGMTV--------RELVAIGRYpwHGALGRfgaadREKVEEAISLVGLK--PL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 146 AAQVMDrypfELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCD 225
Cdd:PRK10575 141 AHRLVD----SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCD 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 226 RMYVMYAGSVIESGITQTLIHHPV--HPYSIgllrcapengePREILPAIPGTVP 278
Cdd:PRK10575 217 YLVALRGGEMIAQGTPAELMRGETleQIYGI-----------PMGILPHPAGAAP 260
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-239 |
8.65e-17 |
|
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: 78.02 E-value: 8.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 21 DVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDvlnasekqLRQWRGARVamifqe 100
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTS-----GSVLLDGTD--------IRQLDPADL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 101 pmtalnpTRRIGRQMVEV------IRQHQSLSRRDAQQKAIalLGEMQIPDAAQVMDRYP-----------FELSGGMRQ 163
Cdd:cd03245 77 -------RRNIGYVPQDVtlfygtLRDNITLGAPLADDERI--LRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 164 RVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkhKARASGTSVLFISHDMAVVsQLCDRMYVMYAGSVIESG 239
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERL--RQLLGDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
25-235 |
1.00e-16 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 76.49 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGsyhvhHGRVTLLGEDVLNASEKQLRQwrgarvamifqepmta 104
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT-----SGRVRLDGADISQWDPNELGD---------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 105 lnptrRIGRQMVEVIrqhqslsrrdaqqkaiaLLgemqipdAAQVMDRYpfeLSGGMRQRVMIALAFSCEPELIIADEPT 184
Cdd:cd03246 77 -----HVGYLPQDDE-----------------LF-------SGSIAENI---LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505383390 185 TALDVTVQRQVLRLLKHkARASGTSVLFISHDMAVVSQlCDRMYVMYAGSV 235
Cdd:cd03246 125 SHLDVEGERALNQAIAA-LKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-244 |
1.10e-16 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 77.58 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 30 LEIGRGEIVGVVGESGSGKS--VTAMLAMRLLPEGSYHVhhgrvtllgedvlnASEKQLRQWRG-----ARVAMIFQEPM 102
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTtlLRAILGLIPPAKGTVKV--------------AGASPGKGWRHigyvpQRHEFAWDFPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 103 ----TALN-PTRRIGrqmvevirqhqsLSRRDAQQKAIALLGEMQIPDAAQVMDRYPFELSGGMRQRVMIALAFSCEPEL 177
Cdd:TIGR03771 67 svahTVMSgRTGHIG------------WLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383390 178 IIADEPTTALDVTVQRQVLRLLKHKArASGTSVLFISHDMAVVSQLCDRMyVMYAGSVIESGITQTL 244
Cdd:TIGR03771 135 LLLDEPFTGLDMPTQELLTELFIELA-GAGTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQL 199
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-247 |
1.15e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.78 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 8 IEDLHLSFPiFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRllpegSYHVHHGRVTLLGEDVLNASEKQLR 87
Cdd:PRK13657 335 VEFDDVSFS-YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQR-----VFDPQSGRILIDGTDIRTVTRASLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 88 QwrgaRVAMIFQEPMTaLNPTrrigrqmvevIRQHQSLSRRDAQQKAIALLGEmqipdAAQVMD-------RYPF----- 155
Cdd:PRK13657 409 R----NIAVVFQDAGL-FNRS----------IEDNIRVGRPDATDEEMRAAAE-----RAQAHDfierkpdGYDTvvger 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 156 --ELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVlfISHDMAVVSQlCDRMYVMYAG 233
Cdd:PRK13657 469 grQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTVRN-ADRILVFDNG 545
|
250
....*....|....
gi 505383390 234 SVIESGITQTLIHH 247
Cdd:PRK13657 546 RVVESGSFDELVAR 559
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
4-239 |
1.23e-16 |
|
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: 77.70 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 4 SVLSIEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhgrvTLLGEDVLNASE 83
Cdd:cd03234 2 RVLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGG--------TTSGQILFNGQP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 84 KQLRQWRgARVAMIFQEPMTALNPTRRIGRQMVEVIRQHQSLSRRdAQQKAIALLGEMQIPDAaQVMDRYPFELSGGMRQ 163
Cdd:cd03234 74 RKPDQFQ-KCVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDA-IRKKRVEDVLLRDLALT-RIGGNLVKGISGGERR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 164 RVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:cd03234 151 RVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-242 |
1.36e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.96 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 28 VSLEIGRGEIVGVVGESGSGKSvTAMLAMR-LLPegsyhvHHGRVTLLGEDVLNASEKQLRQWRgarvAMIFQEPMTALn 106
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKS-TLLARMAgLLP------GQGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPF- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 107 ptrrigrQM--VEVIRQHQSLS-RRDAQQKAIAllgemQIPDAAQVMDRYP---FELSGGMRQRVMIALAF-----SCEP 175
Cdd:COG4138 83 -------AMpvFQYLALHQPAGaSSEAVEQLLA-----QLAEALGLEDKLSrplTQLSGGEWQRVRLAAVLlqvwpTINP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383390 176 E--LIIADEPTTALDVTVQRQVLRLLKHKARAsGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQ 242
Cdd:COG4138 151 EgqLLLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
24-241 |
1.41e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.97 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 24 ALNHVSLEIGRGEIVGVVGESGSGKS--VTAMLAMrLLPE-GS-----YHVHHGRVTLLGEDVLNASE---------KQL 86
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTtfIEHLNAL-LLPDtGTiewifKDEKNKKKTKEKEKVLEKLViqktrfkkiKKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 87 RQWRgARVAMIFQ--EpmtalnptRRIGRQMVE--VIRQHQSL--SRRDAQQKA---IALLGemqIPDaaQVMDRYPFEL 157
Cdd:PRK13651 101 KEIR-RRVGVVFQfaE--------YQLFEQTIEkdIIFGPVSMgvSKEEAKKRAakyIELVG---LDE--SYLQRSPFEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 158 SGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIE 237
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIF-DNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIK 245
|
....
gi 505383390 238 SGIT 241
Cdd:PRK13651 246 DGDT 249
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-247 |
1.74e-16 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 80.15 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 8 IEDLHLSFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLlpegsYHVHHGRVTLLGEDVLNASEKQLR 87
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRF-----YEPDSGQILLDGHDLADYTLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 88 qwrgARVAMIFQEPM---------TALNPTRRIGRQMVEvirqhqslsrrDAQQKAIALLGEMQIPDAAQ-VMDRYPFEL 157
Cdd:TIGR02203 406 ----RQVALVSQDVVlfndtiannIAYGRTEQADRAEIE-----------RALAAAYAQDFVDKLPLGLDtPIGENGVLL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 158 SGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARasGTSVLFISHDMAVVsQLCDRMYVMYAGSVIE 237
Cdd:TIGR02203 471 SGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTI-EKADRIVVMDDGRIVE 547
|
250
....*....|
gi 505383390 238 SGITQTLIHH 247
Cdd:TIGR02203 548 RGTHNELLAR 557
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-246 |
2.38e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.78 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKSVT-AMLAmRLLPEGSyhvhhGRVTLLGEDVlNASEKQLRQwrgaRV---- 94
Cdd:NF033858 277 GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTmKMLT-GLLPASE-----GEAWLFGQPV-DAGDIATRR----RVgyms 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 95 ------------------AMIFQEPmtalnpTRRIGRQMVEVIRQHqslsrrdaqqkaiallgemqipDAAQVMDRYPFE 156
Cdd:NF033858 346 qafslygeltvrqnlelhARLFHLP------AAEIAARVAEMLERF----------------------DLADVADALPDS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 LSGGMRQRVMIALAFSCEPELIIADEPTTALDvTVQR-QVLRLLKHKARASGTSVlFIS-HDM--AvvsQLCDRMYVMYA 232
Cdd:NF033858 398 LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD-PVARdMFWRLLIELSREDGVTI-FIStHFMneA---ERCDRISLMHA 472
|
250
....*....|....
gi 505383390 233 GSVIESGITQTLIH 246
Cdd:NF033858 473 GRVLASDTPAALVA 486
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-235 |
2.53e-16 |
|
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: 76.74 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 3 DSVLSIEDLHLSFPIfRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLlpegsYHVHHGRVTLLGEDVLNAS 82
Cdd:cd03248 9 KGIVKFQNVTFAYPT-RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENF-----YQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 83 EKQLRQwrgaRVAMIFQEPMTAlnpTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAQV-MDRYPFELSGGM 161
Cdd:cd03248 83 HKYLHS----KVSLVGQEPVLF---ARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTeVGEKGSQLSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383390 162 RQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARAsgTSVLFISHDMAVVSQlCDRMYVMYAGSV 235
Cdd:cd03248 156 KQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-243 |
3.23e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.23 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFpifRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMrllpeGSYHVHHGRVTLLGEDVLN 80
Cdd:PRK15056 2 MQQAGIVVNDVTVTW---RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALM-----GFVRLASGKISILGQPTRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQLRQWRGARVAMIFQEPMTaLNPTRRIGRQmvevirQHQSLSRRDAQQKAIALLGEMQIPDAAQVMDRYPFELSGG 160
Cdd:PRK15056 74 ALQKNLVAYVPQSEEVDWSFPVL-VEDVVMMGRY------GHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 161 MRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMyVMYAGSVIESGI 240
Cdd:PRK15056 147 QKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLR-ELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGP 224
|
...
gi 505383390 241 TQT 243
Cdd:PRK15056 225 TET 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-239 |
3.52e-16 |
|
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: 75.67 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 4 SVLSIEDLHLSFPIFRGDVHA--LNHVSLEIGRGEIVGVVGESGSGKSvTAM--LAMRLLPEGsyhvhhgrvtLLGEDVL 79
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKS-TLLnaLAGRRTGLG----------VSGEVLI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 80 NASEKQLRQWRgARVAMIFQEPMTalnptrrigrqmvevirqHQSLSRRDAQQKAIALLGemqipdaaqvmdrypfeLSG 159
Cdd:cd03213 71 NGRPLDKRSFR-KIIGYVPQDDIL------------------HPTLTVRETLMFAAKLRG-----------------LSG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 160 GMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARaSGTSVLFISHD-MAVVSQLCDRMYVMYAGSVIES 238
Cdd:cd03213 115 GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYF 193
|
.
gi 505383390 239 G 239
Cdd:cd03213 194 G 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-276 |
4.27e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.94 E-value: 4.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 19 RGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAM--LAMRLLP--EGSyhvhhGRVTLLGEdVLNAseKQLRQWRG--- 91
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKT-TLMnaLAFRSPKgvKGS-----GSVLLNGM-PIDA--KEMRAISAyvq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 92 ----------ARVAMIFQEPMtalnptrRIGRQMVEVIRQH------QSLSRRDAQQKAIALLGEMQipdaaqvmdrypf 155
Cdd:TIGR00955 106 qddlfiptltVREHLMFQAHL-------RMPRRVTKKEKRErvdevlQALGLRKCANTRIGVPGRVK------------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 156 ELSGGMRQRvmiaLAFSCE----PELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMY 231
Cdd:TIGR00955 166 GLSGGERKR----LAFASElltdPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 505383390 232 AGSVIESGITqtliHHPVHPYSIGLLRCaPENGEPRE----ILPAIPGT 276
Cdd:TIGR00955 242 EGRVAYLGSP----DQAVPFFSDLGHPC-PENYNPADfyvqVLAVIPGS 285
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-242 |
4.56e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.67 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLpEGSYHVHHGRVTLLGEDVLN 80
Cdd:PRK09700 1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTL----MKVL-SGIHEPTKGTITINNINYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQLRQwrgARVAMIFQE-----PMTALNpTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLgemQIPDAAQVMDRYPF 155
Cdd:PRK09700 72 LDHKLAAQ---LGIGIIYQElsvidELTVLE-NLYIGRHLTKKVCGVNIIDWREMRVRAAMML---LRVGLKVDLDEKVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 156 ELSGGMRQRVMIALAFSCEPELIIADEPTTALdvtVQRQV--LRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAG 233
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVdyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
....*....
gi 505383390 234 SVIESGITQ 242
Cdd:PRK09700 222 SSVCSGMVS 230
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-239 |
6.13e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.18 E-value: 6.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAmrllpeGSYHVHHGRVTLLGEDVL 79
Cdd:PRK11300 1 MSQPLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTtVFNCLT------GFYKPTGGTILLRGQHIE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 80 NASEKQLrqwrgARVAMI--FQEPmtalnptrRIGRQMVEV----IRQHQSL----------------SRRDAQQKAIAL 137
Cdd:PRK11300 71 GLPGHQI-----ARMGVVrtFQHV--------RLFREMTVIenllVAQHQQLktglfsgllktpafrrAESEALDRAATW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 138 LGEMQIPDAAqvmDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDM 217
Cdd:PRK11300 138 LERVGLLEHA---NRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDM 214
|
250 260
....*....|....*....|..
gi 505383390 218 AVVSQLCDRMYVMYAGSVIESG 239
Cdd:PRK11300 215 KLVMGISDRIYVVNQGTPLANG 236
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-248 |
7.36e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 77.07 E-value: 7.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKsvTAMLamRLLPeGSYHVHHGRVTLLGEDVLNASEKQlRQwrgarVAMIFQ 99
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGK--TTVL--RLVA-GLEKPTEGQIFIDGEDVTHRSIQQ-RD-----ICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 100 EpmTALNPTRRIGRQmVEVIRQHQSLSRRDAQQK---AIALLgemqipDAAQVMDRYPFELSGGMRQRVMIALAFSCEPE 176
Cdd:PRK11432 86 S--YALFPHMSLGEN-VGYGLKMLGVPKEERKQRvkeALELV------DLAGFEDRYVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505383390 177 LIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHP 248
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-233 |
1.20e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.40 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 27 HVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQL-----------RQWRGA--- 92
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG-----GRIMLNGKEINALSTAQRlarglvylpedRQSSGLyld 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 93 ------RVAMIFQEPMTALNPTRRigRQMVEviRQHQSLSRR--DAQQKAIALlgemqipdaaqvmdrypfelSGGMRQR 164
Cdd:PRK15439 356 aplawnVCALTHNRRGFWIKPARE--NAVLE--RYRRALNIKfnHAEQAARTL--------------------SGGNQQK 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383390 165 VMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKArASGTSVLFISHDMAVVSQLCDRMYVMYAG 233
Cdd:PRK15439 412 VLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-233 |
1.98e-15 |
|
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: 76.79 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSYhvhHGRVTLLGEDvLNASekQLRQWRGARVAMIFQ 99
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTW---DGEIYWSGSP-LKAS--NIRDTERAGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 100 EPMTALNPTRRIGRQMVEVIRQHQSLSRRDAQ-QKAIALLGEMQI---PDAAQVMDrypfeLSGGMRQRVMIALAFSCEP 175
Cdd:TIGR02633 86 ELTLVPELSVAENIFLGNEITLPGGRMAYNAMyLRAKNLLRELQLdadNVTRPVGD-----YGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505383390 176 ELIIADEPTTALdVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAG 233
Cdd:TIGR02633 161 RLLILDEPSSSL-TEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-245 |
2.12e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.23 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 27 HVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPegsyhVHHGRVTLLGEDVLNASEKQlrqwrgaR-VAMIFQEP--MT 103
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLT-----PASGSLTLNGQDHTTTPPSR-------RpVSMLFQENnlFS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 104 ALNPTRRIGRQMvevirqHQSLsRRDAQQKAI--ALLGEMQIPDaaqVMDRYPFELSGGMRQRVMIALAFSCEPELIIAD 181
Cdd:PRK10771 85 HLTVAQNIGLGL------NPGL-KLNAAQREKlhAIARQMGIED---LLARLPGQLSGGQRQRVALARCLVREQPILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383390 182 EPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLI 245
Cdd:PRK10771 155 EPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-237 |
3.27e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 75.37 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKsvTAMLamRLLpEGSYHVHHGRVTLLGEDVLN 80
Cdd:PRK09452 10 SLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGK--TTVL--RLI-AGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQlRQwrgarVAMIFQEpmTALNPTRRI------GRQMvevirqhQSLSRRDAQQKAIALLGEMQIPDAAQvmdRYP 154
Cdd:PRK09452 81 VPAEN-RH-----VNTVFQS--YALFPHMTVfenvafGLRM-------QKTPAAEITPRVMEALRMVQLEEFAQ---RKP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 155 FELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGs 234
Cdd:PRK09452 143 HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG- 221
|
...
gi 505383390 235 VIE 237
Cdd:PRK09452 222 RIE 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-245 |
4.10e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.87 E-value: 4.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSV--LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGsyhvhHGRVTLLGEDV 78
Cdd:PRK10253 1 MTESVarLRGEQLTLGY----GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA-----HGHVWLDGEHI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 79 LNASEKQLRQwrgaRVAMIFQEPMTalnPTRRIGRQMVEVIR-QHQSLSRRDAQQKAIALLGEMQIPDAAQVMDRYPFEL 157
Cdd:PRK10253 72 QHYASKEVAR----RIGLLAQNATT---PGDITVQELVARGRyPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 158 SGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIE 237
Cdd:PRK10253 145 SGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
|
....*...
gi 505383390 238 SGITQTLI 245
Cdd:PRK10253 225 QGAPKEIV 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
18-233 |
4.88e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.99 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 18 FRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMrllpeGSYHVHHGRVTLLGEDVLNASEKQLRQWRgARVAMI 97
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLIC-----GIERPSAGKIWFSGHDITRLKNREVPFLR-RQIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 98 FQEPMTALNPTRRIGRQMVEVIrqhQSLSRRDAQQKAIALLGEMQIPDAAQvmdRYPFELSGGMRQRVMIALAFSCEPEL 177
Cdd:PRK10908 85 FQDHHLLMDRTVYDNVAIPLII---AGASGDDIRRRVSAALDKVGLLDKAK---NFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 178 IIADEPTTALDVTVQRQVLRLLKHKARAsGTSVLFISHDMAVVSQLCDRMYVMYAG 233
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-236 |
4.88e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.35 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLL----PEGSYhvhHGRVTLLGE 76
Cdd:PRK13549 1 MMEYLLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTL----MKVLsgvyPHGTY---EGEIIFEGE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 77 DvLNAseKQLRQWRGARVAMIFQEPMtaLNPTRRIGRQMV--EVIRQHQSLSRRDAQQKAIALLGEMQ--IPDAAQVMDr 152
Cdd:PRK13549 70 E-LQA--SNIRDTERAGIAIIHQELA--LVKELSVLENIFlgNEITPGGIMDYDAMYLRAQKLLAQLKldINPATPVGN- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 153 ypfeLSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYA 232
Cdd:PRK13549 144 ----LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIR-DLKAHGIACIYISHKLNEVKAISDTICVIRD 218
|
....
gi 505383390 233 GSVI 236
Cdd:PRK13549 219 GRHI 222
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-235 |
5.46e-15 |
|
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: 72.59 E-value: 5.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 29 SLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQlrqwrgARVAMIFQEP--MTALN 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPAS-----GSIKVNDQSHTGLAPYQ------RPVSMLFQENnlFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 107 PTRRIGRQMvevirqHQSLS-RRDAQQKAIALLGEMQIPDaaqVMDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTT 185
Cdd:TIGR01277 87 VRQNIGLGL------HPGLKlNAEQQEKVVDAAQQVGIAD---YLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505383390 186 ALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSV 235
Cdd:TIGR01277 158 ALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-249 |
5.59e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.53 E-value: 5.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKS--VTAMLAMRLLpEGSYHVHhGRVTLLGEDVLnasEKQLRQWRGAR-VAMIFQEP 101
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKStfLKCLNRMNEL-ESEVRVE-GRVEFFNQNIY---ERRVNLNRLRRqVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 102 mtALNPTRRIGRQM--VEVIRQHQSLSRRDAQQKAIA---LLGEMQipdaaQVMDRYPFELSGGMRQRVMIALAFSCEPE 176
Cdd:PRK14258 98 --NLFPMSVYDNVAygVKIVGWRPKLEIDDIVESALKdadLWDEIK-----HKIHKSALDLSGGQQQRLCIARALAVKPK 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505383390 177 LIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYA-----GSVIESGITQTLIHHPV 249
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPH 248
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-230 |
1.45e-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: 69.78 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvtamlamrllpegsyhvhhgrvTLLgedvlnasekq 85
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKS----------------------TLL----------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 lrqwrgarvamifqepmtalnptrrigRQMVEVIRQHQslsrrdaqqkaiallGEMQIPDAAQVmdRYpFE-LSGGMRQR 164
Cdd:cd03221 44 ---------------------------KLIAGELEPDE---------------GIVTWGSTVKI--GY-FEqLSGGEKMR 78
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 165 VMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARAsgtsVLFISHDMAVVSQLCDRMYVM 230
Cdd:cd03221 79 LALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGT----VILVSHDRYFLDQVATKIIEL 140
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-239 |
1.49e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.35 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 21 DVHALNHVSLEIGRGEIVGVVGESGSGKSVTAM-LAMRLLPEgsyhvhHGRVTLLGEdVLNASEKQLRQWRgARVAMIFQ 99
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMnLSGLLRPQ------KGAVLWQGK-PLDYSKRGLLALR-QQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 100 EPMTALNPT----------RRIGRQMVEVIRQ-HQSLSRRDAQQkaiallgemqipdaaqvMDRYPFE-LSGGMRQRVMI 167
Cdd:PRK13638 85 DPEQQIFYTdidsdiafslRNLGVPEAEITRRvDEALTLVDAQH-----------------FRHQPIQcLSHGQKKRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505383390 168 ALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKArASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIV-AQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
5-235 |
2.73e-14 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 73.54 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFPIFRGDVhaLNHVSLEIGRGEIVGVVGESGSGKSVTAmlamRLLpEGSYHVHHGRVTLLGEDvlnasek 84
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKPT--LRGISFSLQAGEALAIIGPSGSGKSTLA----RLI-VGIWPPTSGSVRLDGAD------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 qLRQWRgarvamifQEPMTalnptRRIGR--QMVEV----IRQHQSLSRRDAQ-QKAIAllgEMQIPDAAQVMDRYP--- 154
Cdd:TIGR01842 382 -LKQWD--------RETFG-----KHIGYlpQDVELfpgtVAENIARFGENADpEKIIE---AAKLAGVHELILRLPdgy 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 155 --------FELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHkARASGTSVLFISHDMAVVSQLcDR 226
Cdd:TIGR01842 445 dtvigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKA-LKARGITVVVITHRPSLLGCV-DK 522
|
....*....
gi 505383390 227 MYVMYAGSV 235
Cdd:TIGR01842 523 ILVLQDGRI 531
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-248 |
2.94e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.75 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAmrllpeGSYHVHHGRVtLLGEDVLNASEKQLRQwrgarVAMIF 98
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKStLLRMIA------GLEDITSGDL-FIGEKRMNDVPPAERG-----VGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 99 QEpmTALNPTRRIGRQMVEVIRQhQSLSRRDAQQKAIALLGEMQIpdaAQVMDRYPFELSGGMRQRVMIALAFSCEPELI 178
Cdd:PRK11000 82 QS--YALYPHLSVAENMSFGLKL-AGAKKEEINQRVNQVAEVLQL---AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383390 179 IADEPTTALD----VTVQRQVLRLlkHKARasGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHHP 248
Cdd:PRK11000 156 LLDEPLSNLDaalrVQMRIEISRL--HKRL--GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-229 |
2.94e-14 |
|
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: 73.28 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFPIFRGDVHALnhvslEIGRGEIVGVVGESGSGKSVTA-MLAMRLLP-EGSYHvhhGRVTL----- 73
Cdd:COG1245 337 EEETLVEYPDLTKSYGGFSLEVEGG-----EIREGEVLGIVGPNGIGKTTFAkILAGVLKPdEGEVD---EDLKIsykpq 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 74 -LGEDVLNASEKQLRQWRGARV-AMIFQEpmtalnptrrigrqmvEVIRQhqslsrrdaqqkaiallgeMQIPdaaQVMD 151
Cdd:COG1245 409 yISPDYDGTVEEFLRSANTDDFgSSYYKT----------------EIIKP-------------------LGLE---KLLD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383390 152 RYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTvQR-QVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYV 229
Cdd:COG1245 451 KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE-QRlAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-233 |
3.00e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLpEGSYHVHHGRVTLLGEDVLNASEKQL-----------RQWRGAR 93
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTEL----MKVL-YGALPRTSGYVTLDGHEVVTRSPQDGlangivyisedRKRDGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 94 VAMIFQEPM--TALNPTRRIGRQMvevirqhqslsRRDAQQKAIA---LLGEMQIPDAAQVMDrypfELSGGMRQRVMIA 168
Cdd:PRK10762 343 LGMSVKENMslTALRYFSRAGGSL-----------KHADEQQAVSdfiRLFNIKTPSMEQAIG----LLSGGNQQKVAIA 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 169 LAFSCEPELIIADEPTTALDVTVQRQVLRLLkHKARASGTSVLFISHDMAVVSQLCDRMYVMYAG 233
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLI-NQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
24-247 |
3.26e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 73.13 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 24 ALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLlpegsYHVHHGRVTLLGEDVLNASEKQLRQwrgaRVAMIFQEpMT 103
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRF-----YDIDEGEILLDGHDLRDYTLASLRN----QVALVSQN-VH 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 104 ALNPTrrIGRQMVEVIRQHQSlsrRDAQQKAIALLGEMQ-IPDAAQVMDRYPFE----LSGGMRQRVMIALAFSCEPELI 178
Cdd:PRK11176 428 LFNDT--IANNIAYARTEQYS---REQIEEAARMAYAMDfINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505383390 179 IADEPTTALDVTVQRQVLRLLK--HKARasgtSVLFISHDMAVVSQlCDRMYVMYAGSVIESGITQTLIHH 247
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDelQKNR----TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQ 568
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-239 |
4.12e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 72.93 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLlpegsYHVHHGRVTLLGEDVLNASEKQLRqwrgARVAMIFQEpmTA 104
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF-----YDVTSGRILIDGQDIRDVTQASLR----AAIGIVPQD--TV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 105 L-NPTrrigrqmvevIRQHQSLSRRDAQQKAI------ALLGE--MQIPD--AAQVMDRyPFELSGGMRQRVMIALAFSC 173
Cdd:COG5265 443 LfNDT----------IAYNIAYGRPDASEEEVeaaaraAQIHDfiESLPDgyDTRVGER-GLKLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 174 EPELIIADEPTTALDVTVQRQVLRLLKHKARasGTSVLFISHDMAVVSQlCDRMYVMYAGSVIESG 239
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
20-239 |
5.14e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 71.69 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGsyhvhhGRvtllgedvlnaSEKQLRQW----RGARVA 95
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDA------GR-----------RPWRF*TWcanrRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 96 MIFQEPMTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAqvmDRYPFELSGGMRQRVMIALAFSCEP 175
Cdd:NF000106 87 IG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAA---GRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383390 176 ELIIADEPTTALDVTVQRQVLRLLKHKARaSGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-238 |
6.24e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.13 E-value: 6.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 22 VHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLL----PEGSYHvhhGRVTLLGEDV----LNASEKqlrqwRGar 93
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTL----MKVLsgvyPHGSYE---GEILFDGEVCrfkdIRDSEA-----LG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 94 VAMIFQE----PMTAL-------NPTRRIGrqmveVIrqhqslSRRDAQQKAIALLGE--MQIPDAAQVMDrypfeLSGG 160
Cdd:NF040905 80 IVIIHQElaliPYLSIaeniflgNERAKRG-----VI------DWNETNRRARELLAKvgLDESPDTLVTD-----IGVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383390 161 MRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHkARASG-TSVLfISHDMAVVSQLCDRMYVMYAGSVIES 238
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLE-LKAQGiTSII-ISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-229 |
9.47e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 69.74 E-value: 9.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 31 EIGRGEIVGVVGESGSGKSVTA-MLAMRLLPEGsyhvhhGRVTLLGEDVlnASEKQlrqwrgarvAMIFQEPMTAlnptr 109
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIkMLAGVLKPDE------GDIEIELDTV--SYKPQ---------YIKADYEGTV----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 110 rigRQMV-EVIRQHQSLSrrdaqQKAIALLGEMQIpdaAQVMDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALD 188
Cdd:cd03237 79 ---RDLLsSITKDFYTHP-----YFKTEIAKPLQI---EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505383390 189 VTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYV 229
Cdd:cd03237 148 VEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
150-239 |
1.04e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.06 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 150 MDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYV 229
Cdd:PRK11144 122 LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVV 201
|
90
....*....|
gi 505383390 230 MYAGSVIESG 239
Cdd:PRK11144 202 LEQGKVKAFG 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-242 |
1.21e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.66 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 4 SVLSIEDLHLSFPIFRgdvhALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMRLLPEGSyHVHHGRVTLLGEDVLNASE 83
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKS-TLLRHLSGLITGD-KSAGSHIELLGRTVQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 84 --KQLRQWRgARVAMIFQE-----PMTALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIpdaAQVMDRYPFE 156
Cdd:PRK09984 77 laRDIRKSR-ANTGYIFQQfnlvnRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGM---VHFAHQRVST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 LSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVI 236
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVF 232
|
....*.
gi 505383390 237 ESGITQ 242
Cdd:PRK09984 233 YDGSSQ 238
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-238 |
2.53e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 22 VHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLpEGSYHVHHGRVTLLGEDVLNASekqLRQWRGARVAMIFQE- 100
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTL----LKIL-SGNYQPDAGSILIDGQEMRFAS---TTAALAAGVAIIYQEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 101 ---P-MT-ALN------PTRRigrqmvEVIRqhqslsRRDAQQKAIALLGEMQI---PDAaqvmdryPF-ELSGGMRQRV 165
Cdd:PRK11288 89 hlvPeMTvAENlylgqlPHKG------GIVN------RRLLNYEAREQLEHLGVdidPDT-------PLkYLSIGQRQMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505383390 166 MIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIES 238
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIR-ELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-229 |
3.02e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 2 SDSVLSIEDLHLSFPIFRGDVHALnhvslEIGRGEIVGVVGESGSGKSVTA-MLAMRLLP-EG--------SY------H 65
Cdd:PRK13409 337 RETLVEYPDLTKKLGDFSLEVEGG-----EIYEGEVIGIVGPNGIGKTTFAkLLAGVLKPdEGevdpelkiSYkpqyikP 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 66 VHHGRVtllgEDVLnasekqlrqwrgarvamifqepmtalnptRRIGRQM------VEVIRQhqslsrrdaqqkaiallg 139
Cdd:PRK13409 412 DYDGTV----EDLL-----------------------------RSITDDLgssyykSEIIKP------------------ 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 140 eMQIPDaaqVMDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTvQR-QVLRLLKHKARASGTSVLFISHDMA 218
Cdd:PRK13409 441 -LQLER---LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE-QRlAVAKAIRRIAEEREATALVVDHDIY 515
|
250
....*....|.
gi 505383390 219 VVSQLCDRMYV 229
Cdd:PRK13409 516 MIDYISDRLMV 526
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-242 |
3.58e-13 |
|
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: 69.85 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 3 DSVLSIEDLHLSFPIFRgDVHALNHVSLEIGRGEIVGVVGESGSGKS--VTAMLamrllpeGSYH-VHHGRVTLLGEDVl 79
Cdd:TIGR02633 255 DVILEARNLTCWDVINP-HRKRVDDVSFSLRRGEILGVAGLVGAGRTelVQALF-------GAYPgKFEGNVFINGKPV- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 80 naSEKQLRQWRGARVAMIFQE-PMTALNPTRRIGRQM-VEVIRQHQSLSRRDAQQKAIALLGEMQipdAAQVMDRYPF-- 155
Cdd:TIGR02633 326 --DIRNPAQAIRAGIAMVPEDrKRHGIVPILGVGKNItLSVLKSFCFKMRIDAAAELQIIGSAIQ---RLKVKTASPFlp 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 156 --ELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARaSGTSVLFISHDMAVVSQLCDRMYVMYAG 233
Cdd:TIGR02633 401 igRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
250
....*....|...
gi 505383390 234 ----SVIESGITQ 242
Cdd:TIGR02633 480 klkgDFVNHALTQ 492
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-236 |
9.03e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.83 E-value: 9.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKsvTAMLAMRLlpeGSYHVHHGRVTLLGEDVlnasekqlRQWRGARvamIFQ 99
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGK--TTLLGTLC---GDPRATSGRIVFDGKDI--------TDWQTAK---IMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 100 EPMTALNPTRRIGRQMV--EVIRQHQSLSRRDAQQKAIALLGEMqIPDAAQVMDRYPFELSGGMRQRVMIALAFSCEPEL 177
Cdd:PRK11614 80 EAVAIVPEGRRVFSRMTveENLAMGGFFAERDQFQERIKWVYEL-FPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505383390 178 IIADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVI 236
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIE-QLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-239 |
1.00e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.74 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSF---PIFRGdvhalnhVSLEIGRGEIVGVVGESGSGKS-VTAMLAMRllpeGSYHVHHGRVTLLGEDVLN 80
Cdd:PRK09580 1 MLSIKDLHVSVedkAILRG-------LNLEVRPGEVHAIMGPNGSGKStLSATLAGR----EDYEVTGGTVEFKGKDLLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQLRqwrGARVAMIFQEPM------------TALNPTRRIgrqmveviRQHQSLSRRDAQ---QKAIALLgemQIPd 145
Cdd:PRK09580 70 LSPEDRA---GEGIFMAFQYPVeipgvsnqfflqTALNAVRSY--------RGQEPLDRFDFQdlmEEKIALL---KMP- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 146 aAQVMDR-YPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLkHKARASGTSVLFISHDMAVVSQL- 223
Cdd:PRK09580 135 -EDLLTRsVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGV-NSLRDGKRSFIIVTHYQRILDYIk 212
|
250
....*....|....*.
gi 505383390 224 CDRMYVMYAGSVIESG 239
Cdd:PRK09580 213 PDYVHVLYQGRIVKSG 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-225 |
2.16e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.96 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 2 SDSVLSIEDLHlsfpIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRL--LPEGSYHvhHGRVTLLGEDvL 79
Cdd:PRK14243 7 TETVLRTENLN----VYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFRV--EGKVTFHGKN-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 80 NASEKQLRQWRgARVAMIFQEPmtalNP------------TRRIGRQ--MVEVIRQhqslSRRDAqqkaiALLGEmqipd 145
Cdd:PRK14243 80 YAPDVDPVEVR-RRIGMVFQKP----NPfpksiydniaygARINGYKgdMDELVER----SLRQA-----ALWDE----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 146 aaqVMDRYP---FELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARAsgTSVLFISHDMAVVSQ 222
Cdd:PRK14243 141 ---VKDKLKqsgLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAAR 215
|
...
gi 505383390 223 LCD 225
Cdd:PRK14243 216 VSD 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-235 |
2.60e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.85 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLPeGSYHVHHGRVtLLGEDVLNASEKQ 85
Cdd:PRK11247 13 LLLNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTL----LRLLA-GLETPSAGEL-LAGTAPLAEARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 86 LRqwrgarvaMIFQEpmTALNPTRRIGRQMVEVIRQHQslsrRDAQQKAIALLGemqIPDAAQvmdRYPFELSGGMRQRV 165
Cdd:PRK11247 83 TR--------LMFQD--ARLLPWKKVIDNVGLGLKGQW----RDAALQALAAVG---LADRAN---EWPAALSGGQKQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 166 MIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSV 235
Cdd:PRK11247 143 ALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-237 |
2.64e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.79 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPifrGDVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAmrllpeGSYHVHHGRVTLLGEDVLNASEK 84
Cdd:PRK11650 4 LKLQAVRKSYD---GKTQVIKGIDLDVADGEFIVLVGPSGCGKStLLRMVA------GLERITSGEIWIGGRVVNELEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QlrqwRGarVAMIFQEpmTALNP-------------TRRIGRQMVEvirqhqslsRRDAQQKAIALLGEMqipdaaqvMD 151
Cdd:PRK11650 75 D----RD--IAMVFQN--YALYPhmsvrenmayglkIRGMPKAEIE---------ERVAEAARILELEPL--------LD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 152 RYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQvLRL-LKHKARASGTSVLFISHDMAVVSQLCDRMYVM 230
Cdd:PRK11650 130 RKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLeIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVM 208
|
....*..
gi 505383390 231 YAGsVIE 237
Cdd:PRK11650 209 NGG-VAE 214
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-230 |
2.72e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.98 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 23 HALNHVSLEIGRGEIVGVVGESGSGKSvtamlamrllpegsyhvhhgrvTLLgedvlnasEKQLRQWRGARVAMIFQEPM 102
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKS----------------------TLL--------RLLAGALKGTPVAGCVDVPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 103 TALNPTRRIgrqmVEvirqhqSLSRRDAQQKAIALLGEMQIPDAAQVMDRYPfELSGGMRQRVMIALAFSCEPELIIADE 182
Cdd:COG2401 94 NQFGREASL----ID------AIGRKGDFKDAVELLNAVGLSDAVLWLRRFK-ELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505383390 183 PTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVM 230
Cdd:COG2401 163 FCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
24-239 |
3.29e-12 |
|
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: 64.82 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 24 ALNHVSLEIGRGEIVGVVGESGSGKSvTAMLA-MRLlpegsYHVHHGRVTLLGEDVLNASEKQLRQwrgaRVAMIFQEPm 102
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKS-SLLLAlFRL-----VELSSGSILIDGVDISKIGLHDLRS----RISIIPQDP- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 103 TALNPTrrigrqmvevIR-------QHQSLSRRDAQQKA--IALLGEMQIPDAAQVMDRyPFELSGGMRQRVMIALAFSC 173
Cdd:cd03244 88 VLFSGT----------IRsnldpfgEYSDEELWQALERVglKEFVESLPGGLDTVVEEG-GENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 174 EPELIIADEPTTALDVTVQRQVLRLLKHKarASGTSVLFISHDMAVVSQlCDRMYVMYAGSVIESG 239
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREA--FKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-242 |
3.41e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.34 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 28 VSLEIGRGEIVGVVGESGSGKSvTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQLRQWRgarvAMIFQEPMTALNp 107
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKS-TLLARMAGLLPGS-----GSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 108 trrigrqmVEVIrQHQSLSRRDAQQKAIALLGEMQIPDAAQVMDRYPF---ELSGGMRQRVMIALAF-----SCEPE--L 177
Cdd:PRK03695 84 --------MPVF-QYLTLHQPDKTRTEAVASALNEVAEALGLDDKLGRsvnQLSGGEWQRVRLAAVVlqvwpDINPAgqL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 178 IIADEPTTALDVTVQRQVLRLLKHKARAsGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQ 242
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRD 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-237 |
4.84e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 17 IFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTaMLAMRllpeGSYHVHHGRVTLLGEDVLNASEKQlrqwrgarvam 96
Cdd:PRK09700 271 VTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTEL-MNCLF----GVDKRAGGEIRLNGKDISPRSPLD----------- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 97 IFQEPMTALNPTRR-IGRQMVEVIRQHQSLSR--RDAQQK-AIALLG---EMQIPDAAQ--------VMDRYPFELSGGM 161
Cdd:PRK09700 335 AVKKGMAYITESRRdNGFFPNFSIAQNMAISRslKDGGYKgAMGLFHevdEQRTAENQRellalkchSVNQNITELSGGN 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 162 RQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARaSGTSVLFISHDMAVVSQLCDRMYVMYAGSVIE 237
Cdd:PRK09700 415 QQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-245 |
9.30e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 65.89 E-value: 9.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 7 SIEDLHLSFPiFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMrllpeGSYHVHHGRVTLLGEDVLNASEKQL 86
Cdd:PRK10790 340 RIDIDNVSFA-YRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLM-----GYYPLTEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 87 RQwrgaRVAMIFQEPMTalnptrrigrqMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAQVMDRYPF--------ELS 158
Cdd:PRK10790 414 RQ----GVAMVQQDPVV-----------LADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYtplgeqgnNLS 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 159 GGMRQRVMIALAFSCEPELIIADEPTTALDV-TVQ--RQVLRLLKHKarasgTSVLFISHDMAVVSQlCDRMYVMYAGSV 235
Cdd:PRK10790 479 VGQKQLLALARVLVQTPQILILDEATANIDSgTEQaiQQALAAVREH-----TTLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
250
....*....|
gi 505383390 236 IESGITQTLI 245
Cdd:PRK10790 553 VEQGTHQQLL 562
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-231 |
1.02e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.58 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 34 RGEIVGVVGESGSGKSvTAM--LAMRLLPE-GSYH--------VHHGRVTLLGEDVLNASEKQLRqwrgarvamifqepm 102
Cdd:COG1245 98 KGKVTGILGPNGIGKS-TALkiLSGELKPNlGDYDeepswdevLKRFRGTELQDYFKKLANGEIK--------------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 103 TALNPtrrigrQMVEVIRQH------QSLSRRDAQQKAIALLGEMQIpdaAQVMDRYPFELSGGMRQRVMIALAFSCEPE 176
Cdd:COG1245 162 VAHKP------QYVDLIPKVfkgtvrELLEKVDERGKLDELAEKLGL---ENILDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 177 LIIADEPTTALDVTvQR-QVLRLLKHKARaSGTSVLFISHDMAVVSQLCDRMYVMY 231
Cdd:COG1245 233 FYFFDEPSSYLDIY-QRlNVARLIRELAE-EGKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-216 |
1.22e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.19 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQLRQwrgaRVAMIFQ 99
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS-----GTLLFEGEDISTLKPEIYRQ----QVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 100 EPMTalnptrrIGRQMVE-VIRQHQSLSRRDAQQKAIALLGEMQIPDaaQVMDRYPFELSGGMRQRVMIALAFSCEPELI 178
Cdd:PRK10247 89 TPTL-------FGDTVYDnLIFPWQIRNQQPDPAIFLDDLERFALPD--TILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 505383390 179 IADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHD 216
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-236 |
1.43e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.14 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 14 SFPifrgDVHALNHVSLEIGRGEIVGVVGESGSGKSVTamlaMRLLpEGSYHVHHGRVTLLGEDVLNASEKQLRQwrgAR 93
Cdd:PRK10982 7 SFP----GVKALDNVNLKVRPHSIHALMGENGAGKSTL----LKCL-FGIYQKDSGSILFQGKEIDFKSSKEALE---NG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 94 VAMIFQEpmtaLNPTRR--------IGRQMVEVIRQHQSLSRRDAqqKAIALLGEMQIPDAAQVMDrypfeLSGGMRQRV 165
Cdd:PRK10982 75 ISMVHQE----LNLVLQrsvmdnmwLGRYPTKGMFVDQDKMYRDT--KAIFDELDIDIDPRAKVAT-----LSVSQMQMI 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505383390 166 MIALAFSCEPELIIADEPTTALdvtVQRQVLRLLK--HKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVI 236
Cdd:PRK10982 144 EIAKAFSYNAKIVIMDEPTSSL---TEKEVNHLFTiiRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-231 |
2.82e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 34 RGEIVGVVGESGSGKSvTAM--LAMRLLPEgsyhvhhgrvtlLGEDVLNAS-EKQLRQWRGARVAMIFQ-----EPMTAL 105
Cdd:PRK13409 98 EGKVTGILGPNGIGKT-TAVkiLSGELIPN------------LGDYEEEPSwDEVLKRFRGTELQNYFKklyngEIKVVH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 106 NPtrrigrQMVEVIRQH------QSLSRRDAQQKAIALLGEMQIpdaAQVMDRYPFELSGGMRQRVMIALAFSCEPELII 179
Cdd:PRK13409 165 KP------QYVDLIPKVfkgkvrELLKKVDERGKLDEVVERLGL---ENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505383390 180 ADEPTTALDVtVQR-QVLRLLKHkaRASGTSVLFISHDMAVVSQLCDRMYVMY 231
Cdd:PRK13409 236 FDEPTSYLDI-RQRlNVARLIRE--LAEGKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-265 |
4.04e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 2 SDSVLSIEDLHLSF-----PIFRGdvhalnhVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLpegsyHVHHGRVTLLGE 76
Cdd:PLN03232 1231 SRGSIKFEDVHLRYrpglpPVLHG-------LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIV-----ELEKGRIMIDDC 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 77 DVLNASEKQLRqwrgaRVAMIFQEPMTALNPTRRIGrqmVEVIRQHQSLSRRDAQQKAiallgemQIPDaaqVMDRYPFE 156
Cdd:PLN03232 1299 DVAKFGLTDLR-----RVLSIIPQSPVLFSGTVRFN---IDPFSEHNDADLWEALERA-------HIKD---VIDRNPFG 1360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 L-----------SGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARAsgTSVLFISHDMAVVSQlCD 225
Cdd:PLN03232 1361 LdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS--CTMLVIAHRLNTIID-CD 1437
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 505383390 226 RMYVMYAGSVIESGITQTLIHHPVHPYSIGLLRCAPENGE 265
Cdd:PLN03232 1438 KILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPANAQ 1477
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-245 |
6.15e-11 |
|
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: 63.43 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 14 SFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKS--VTAMLAMRLLPEGsyHVHhgrvtlLGEDVLNASEKQLRQWRG 91
Cdd:TIGR00957 643 TFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSslLSALLAEMDKVEG--HVH------MKGSVAYVPQQAWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 92 ARVAMIFQEPmtaLNPTRRigRQMVEvirqhqslsrrdaqqkAIALLGEMQI-PDAAQV-MDRYPFELSGGMRQRVMIAL 169
Cdd:TIGR00957 715 LRENILFGKA---LNEKYY--QQVLE----------------ACALLPDLEIlPSGDRTeIGEKGVNLSGGQKQRVSLAR 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 170 AFSCEPELIIADEPTTALDVTVQRQVLR-------LLKHKARasgtsvLFISHDMAVVSQLcDRMYVMYAGSVIESGITQ 242
Cdd:TIGR00957 774 AVYSNADIYLFDDPLSAVDAHVGKHIFEhvigpegVLKNKTR------ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQ 846
|
...
gi 505383390 243 TLI 245
Cdd:TIGR00957 847 ELL 849
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
24-239 |
7.50e-11 |
|
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: 60.89 E-value: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 24 ALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLpegsyHVHHGRVTLLGEDVLNASEKQLRQwrgaRVAMIFQEPmT 103
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFL-----EAEEGKIEIDGIDISTIPLEDLRS----SLTIIPQDP-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 104 ALNPTRRigrqmvevirqhQSLSRRDAQQkaiallgEMQIPDAAQVMDRyPFELSGGMRQRVMIALAFSCEPELIIADEP 183
Cdd:cd03369 93 LFSGTIR------------SNLDPFDEYS-------DEEIYGALRVSEG-GLNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 184 TTALDVTVQRQVLRLLKHKarASGTSVLFISHDMAVVSQlCDRMYVMYAGSVIESG 239
Cdd:cd03369 153 TASIDYATDALIQKTIREE--FTNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-215 |
9.06e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.52 E-value: 9.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 3 DSVLSIEDLHLSFPifrgDVHAL-NHVSLEIGRGEIVGVVGESGSGKSvtamlamRLL-------PEGSyhvhhGRVTLL 74
Cdd:COG4178 360 DGALALEDLTLRTP----DGRPLlEDLSLSLKPGERLLITGPSGSGKS-------TLLraiaglwPYGS-----GRIARP 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 75 gedvlnasekqlrqwRGARVAMIFQEP-------MTAL---NPTRRIGR-QMVEVIRQ---HQSLSRRDAQQkaiallge 140
Cdd:COG4178 424 ---------------AGARVLFLPQRPylplgtlREALlypATAEAFSDaELREALEAvglGHLAERLDEEA-------- 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 141 mqipDAAQVmdrypfeLSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHkaRASGTSVLFISH 215
Cdd:COG4178 481 ----DWDQV-------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-234 |
9.54e-11 |
|
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: 60.18 E-value: 9.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPIFRGDVH-ALNHVSLEIGRGEIVGVVGESGSGKSvtaMLAMRLLpeGSYHVHHGRVTLLGedvlnasek 84
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKS---SLLSALL--GELEKLSGSVSVPG--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 qlrqwrgaRVAMIFQEPMtALNPTRRigrqmvEVIRQHQSLSRRDAQQ--KAIALLGEMQI-P--DAAQVMDRyPFELSG 159
Cdd:cd03250 67 --------SIAYVSQEPW-IQNGTIR------ENILFGKPFDEERYEKviKACALEPDLEIlPdgDLTEIGEK-GINLSG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 160 GMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVL-RLLKHKARASGTSVLfISHDMAVVSQlCDRMYVMYAGS 234
Cdd:cd03250 131 GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRIL-VTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-248 |
9.72e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.55 E-value: 9.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 28 VSLEIGRGEIVGVVGESGSGKS--VTAMLAmrLLP-EGSYHVhhGRVTLlgedvlnaSEKQLRQWRgARVAMIFQEPMTa 104
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTslLNALLG--FLPyQGSLKI--NGIEL--------RELDPESWR-KHLSWVGQNPQL- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 105 LNPTrrigrqmvevIRQHQSLSRRDAQQKAIALLgeMQIPDAAQVMDRYPF-----------ELSGGMRQRVMIALAFSC 173
Cdd:PRK11174 435 PHGT----------LRDNVLLGNPDASDEQLQQA--LENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQ 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 174 EPELIIADEPTTALDVTVQRQVLRLLKHKARasGTSVLFISHDMAVVSQlCDRMYVMYAGSVIESGITQTLIHHP 248
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-211 |
2.25e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.18 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 11 LHLSFPIFR-GDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAM-LAMRLLP-EGSYHVHHGRVTLLgedvlnaSEKQLR 87
Cdd:PRK10938 4 LQISQGTFRlSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARaLAGELPLlSGERQSQFSHITRL-------SFEQLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 88 QwrgaRVAMIFQEPMT-ALNPTRR-IGRQMVEVIRQHQS---LSRRDAQQKAIALLgemqipdaaqvMDRyPFE-LSGGM 161
Cdd:PRK10938 77 K----LVSDEWQRNNTdMLSPGEDdTGRTTAEIIQDEVKdpaRCEQLAQQFGITAL-----------LDR-RFKyLSTGE 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505383390 162 RQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVL 211
Cdd:PRK10938 141 TRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVL 190
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
8-248 |
3.08e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.88 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 8 IEDLHLSFPIFRG--------------DVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLlpegsYHVHHGRVTL 73
Cdd:PRK10789 300 VKDGSEPVPEGRGeldvnirqftypqtDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRH-----FDVSEGDIRF 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 74 LGedvLNASEKQLRQWRGaRVAMIFQEPMTalnptrrigrqMVEVIRQHQSLSRRDAQQKAI---ALLGE-----MQIPD 145
Cdd:PRK10789 375 HD---IPLTKLQLDSWRS-RLAVVSQTPFL-----------FSDTVANNIALGRPDATQQEIehvARLASvhddiLRLPQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 146 AAQ-------VMdrypfeLSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARasGTSVLFISHDMA 218
Cdd:PRK10789 440 GYDtevgergVM------LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLS 511
|
250 260 270
....*....|....*....|....*....|
gi 505383390 219 VVSQlCDRMYVMYAGSVIESGITQTLIHHP 248
Cdd:PRK10789 512 ALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-239 |
4.26e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.27 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVtamLAMRLLPEGSYHVHHGRVTLLGEDVLN 80
Cdd:CHL00131 3 KNKPILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKST---LSKVIAGHPAYKILEGDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 AsEKQLRQWRGARVAmiFQEP------------MTALNpTRRIGRQMVEVirqhQSLSRRDAQQKAIALLGeMQipdaAQ 148
Cdd:CHL00131 76 L-EPEERAHLGIFLA--FQYPieipgvsnadflRLAYN-SKRKFQGLPEL----DPLEFLEIINEKLKLVG-MD----PS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 149 VMDRYPFE-LSGGMRQR----VMIALafscEPELIIADEPTTALDVTVQRQVLRLLkHKARASGTSVLFISHDMAVVSQL 223
Cdd:CHL00131 143 FLSRNVNEgFSGGEKKRneilQMALL----DSELAILDETDSGLDIDALKIIAEGI-NKLMTSENSIILITHYQRLLDYI 217
|
250
....*....|....*..
gi 505383390 224 C-DRMYVMYAGSVIESG 239
Cdd:CHL00131 218 KpDYVHVMQNGKIIKTG 234
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-231 |
5.63e-10 |
|
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: 58.92 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 35 GEIVGVVGESGSGKSvTAM--LAMRLLPEgsyhvhhgrvtlLGEDVLNAS-EKQLRQWRGARVAMIFQepmtalnptrRI 111
Cdd:cd03236 26 GQVLGLVGPNGIGKS-TALkiLAGKLKPN------------LGKFDDPPDwDEILDEFRGSELQNYFT----------KL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 112 GRQMVEVIRQHQSLSR--RDAQQKAIALLGE----------MQIPDAAQVMDRYPFELSGGMRQRVMIALAFSCEPELII 179
Cdd:cd03236 83 LEGDVKVIVKPQYVDLipKAVKGKVGELLKKkdergkldelVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 180 ADEPTTALDV----TVQRQVLRLLKHkarasGTSVLFISHDMAVVSQLCDRMYVMY 231
Cdd:cd03236 163 FDEPSSYLDIkqrlNAARLIRELAED-----DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-247 |
1.03e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.52 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVH-ALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAMRLLPegsyhvHHGRVTLLGEDVLNASEKQLrqwrgarvami 97
Cdd:PRK13545 34 GEYHyALNNISFEVPEGEIVGIIGLNGSGKStLSNLIAGVTMP------NKGTVDIKGSAALIAISSGL----------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 98 fQEPMTALNPTRRIGRQMvevirqhqSLSRRDAQQKAIALLgemQIPDAAQVMDRYPFELSGGMRQRVMIALAFSCEPEL 177
Cdd:PRK13545 97 -NGQLTGIENIELKGLMM--------GLTKEKIKEIIPEII---EFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 178 IIADEPTTALDVTVQRQVLRLLkHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTLIHH 247
Cdd:PRK13545 165 LVIDEALSVGDQTFTKKCLDKM-NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-233 |
1.14e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMrllpEGSYHVHHGRVTLLgedvlnASEKQLRQWRGARVAMIFQEPMTA 104
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKS-TLLNAL----AGRIQGNNFTGTIL------ANNRKPTKQILKRTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 105 LNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAQVMDRYPF--ELSGGMRQRVMIALAFSCEPELIIADE 182
Cdd:PLN03211 153 PHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505383390 183 PTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMYAG 233
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEG 283
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-239 |
1.37e-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: 59.64 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 24 ALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVlNASEKQLRQWRG--ARVAMIFQEP 101
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS-----GTVLVGGKDI-ETNLDAVRQSLGmcPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 102 MTAlnptrrigrQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAQVMDRypfELSGGMRQRVMIALAFSCEPELIIAD 181
Cdd:TIGR01257 1019 TVA---------EHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQ---DLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505383390 182 EPTTALDVTVQRQVLR-LLKHKaraSGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDlLLKYR---SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-235 |
1.72e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.77 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 28 VSLEIGRGEIVGVVGESGSGKSVTamlaMRLLpEGSYHVHHGRVTLLGEDVlnasekQLRQWRGARVAMIfqepmtALNP 107
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSEL----MKLL-YGATRRTAGQVYLDGKPI------DIRSPRDAIRAGI------MLCP 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 108 TRR----I--GRQMVEVI----RQHQS-----LSRRDAQQKAIALLGEMQI--PDAAQVMdrypFELSGGMRQRVMIALA 170
Cdd:PRK11288 335 EDRkaegIipVHSVADNInisaRRHHLragclINNRWEAENADRFIRSLNIktPSREQLI----MNLSGGNQQKAILGRW 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 171 FSCEPELIIADEPTTALDVTVQRQVLRLLkHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSV 235
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDVGAKHEIYNVI-YELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-244 |
5.60e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.44 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvtAMLAmrlLPEGSYHVHHGRVTLLGEDVlnaSEK 84
Cdd:NF033858 1 VARLEGVSHRY----GKTVALDDVSLDIPAGCMVGLIGPDGVGKS--SLLS---LIAGARKIQQGRVEVLGGDM---ADA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 85 QLRQWRGARVAMIFQEPMTALNPTRRIgrqmVEVIRQHQSLSRRDAQQKaiallgEMQIPDAAQVMDRYPF------ELS 158
Cdd:NF033858 69 RHRRAVCPRIAYMPQGLGKNLYPTLSV----FENLDFFGRLFGQDAAER------RRRIDELLRATGLAPFadrpagKLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 159 GGMRQRvmiaLAFSC----EPELIIADEPTTALDVTVQRQVLRLLKH-KARASGTSVLFISHDM--AvvsQLCDRMYVMY 231
Cdd:NF033858 139 GGMKQK----LGLCCalihDPDLLILDEPTTGVDPLSRRQFWELIDRiRAERPGMSVLVATAYMeeA---ERFDWLVAMD 211
|
250
....*....|...
gi 505383390 232 AGSVIESGITQTL 244
Cdd:NF033858 212 AGRVLATGTPAEL 224
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-239 |
5.63e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 54.64 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 22 VHALNHVSLEIGRGEIVGVVGESGSGKSvtamlamrllpegsyhvhhgrvTLLGEDVlnASEKQLRQWRGarvamifqep 101
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKS----------------------TLVNEGL--YASGKARLISF---------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 102 mtalnpTRRIGRQMVEVIRQHQSLsrrdaqqkaIAL-LGEMQIPDAAQVmdrypfeLSGGMRQRVMIA--LAFSCEPELI 178
Cdd:cd03238 54 ------LPKFSRNKLIFIDQLQFL---------IDVgLGYLTLGQKLST-------LSGGELQRVKLAseLFSEPPGTLF 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383390 179 IADEPTTALDVTVQRQVLRLLKhKARASGTSVLFISHDMAVVSQlCDRMYVM------YAGSVIESG 239
Cdd:cd03238 112 ILDEPSTGLHQQDINQLLEVIK-GLIDLGNTVILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6-246 |
1.06e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.67 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 6 LSIEDLHLSFPIfRGDVHALNHVSLEIGRGEIVGVVGESGSGKS--VTAMLAMRLLPEGSYHVHHGRVTLLGED--VLNA 81
Cdd:PLN03130 615 ISIKNGYFSWDS-KAERPTLSNINLDVPVGSLVAIVGSTGEGKTslISAMLGELPPRSDASVVIRGTVAYVPQVswIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 82 SekqlrqwrgARVAMIFQEPmtaLNPTRRigRQMVEVIRQHQSLSrrdaqqkaiALLGEmqipDAAQVMDRyPFELSGGM 161
Cdd:PLN03130 694 T---------VRDNILFGSP---FDPERY--ERAIDVTALQHDLD---------LLPGG----DLTEIGER-GVNISGGQ 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 162 RQRVMIALAFSCEPELIIADEPTTALDVTVQRQVL-----RLLKHKARASGTSVL-FISHdmavvsqlCDRMYVMYAGSV 235
Cdd:PLN03130 746 KQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdkcikDELRGKTRVLVTNQLhFLSQ--------VDRIILVHEGMI 817
|
250
....*....|.
gi 505383390 236 IESGITQTLIH 246
Cdd:PLN03130 818 KEEGTYEELSN 828
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
153-215 |
1.15e-08 |
|
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: 53.70 E-value: 1.15e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 153 YPF--ELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKhkarASGTSVLFISH 215
Cdd:cd03223 86 YPWddVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-233 |
1.18e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.95 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 3 DSVLSIEDLHLSFPIFRgDVHALNHVSLEIGRGEIVGVVGESGSGKSvtaMLAMRLLpeG-SYHVHH-GRVTLLGE--DV 78
Cdd:NF040905 255 EVVFEVKNWTVYHPLHP-ERKVVDDVSLNVRRGEIVGIAGLMGAGRT---ELAMSVF--GrSYGRNIsGTVFKDGKevDV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 79 LNASE-------------KQLrqwrgarvAMIFQEPM---TALNPTRRIGRQMVevIRQHQSLS-----RRDAQQKAial 137
Cdd:NF040905 329 STVSDaidaglayvtedrKGY--------GLNLIDDIkrnITLANLGKVSRRGV--IDENEEIKvaeeyRKKMNIKT--- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 138 lgemqiPDAAQVMDRypfeLSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKArASGTSVLFISHDM 217
Cdd:NF040905 396 ------PSVFQKVGN----LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELA-AEGKGVIVISSEL 464
|
250
....*....|....*.
gi 505383390 218 AVVSQLCDRMYVMYAG 233
Cdd:NF040905 465 PELLGMCDRIYVMNEG 480
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
156-231 |
1.52e-08 |
|
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: 53.73 E-value: 1.52e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 156 ELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVMY 231
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-242 |
2.38e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 26 NHVSLEIGRGEIVGVVGESGSGKS--VTAMLamrllpeGSYH-VHHGRVTLLGEDV-LNASEKQLRQwrgaRVAMIFQE- 100
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTelVQCLF-------GAYPgRWEGEIFIDGKPVkIRNPQQAIAQ----GIAMVPEDr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 101 PMTALNPTRRIGRQM-VEVIRQHQSLSRRDAQQKAIALLGEMQ-----IPDAAQVMDRypfeLSGGMRQRVMIALAFSCE 174
Cdd:PRK13549 348 KRDGIVPVMGVGKNItLAALDRFTGGSRIDDAAELKTILESIQrlkvkTASPELAIAR----LSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505383390 175 PELIIADEPTTALDVTVQRQVLRLLKHKARaSGTSVLFISHDMAVVSQLCDRMYVMYAGSV----IESGITQ 242
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKLkgdlINHNLTQ 494
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-220 |
2.47e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.96 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 1 MSDSVlSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAmlamrllpegsyhvhhgRVTLlgeDVLN 80
Cdd:PRK09544 1 MTSLV-SLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLV-----------------RVVL---GLVA 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 81 ASEKQLRQWRGARVAMIFQEpmTALNPTR--RIGRQMveviRQHQSLSRRDaqqkaiaLLGEMQIPDAAQVMDRYPFELS 158
Cdd:PRK09544 56 PDEGVIKRNGKLRIGYVPQK--LYLDTTLplTVNRFL----RLRPGTKKED-------ILPALKRVQAGHLIDAPMQKLS 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505383390 159 GGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVV 220
Cdd:PRK09544 123 GGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-216 |
5.08e-08 |
|
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: 54.17 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 3 DSVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSVT-AMLAMRLLPEGsyhvhhGRVTLlGEDVLNA 81
Cdd:TIGR03719 320 DKVIEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLfRMITGQEQPDS------GTIEI-GETVKLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 82 SEKQLRQwrgarvamifqepmtALNPTRRIgrqmVEVIRQHQSlsrrdaqqkaIALLGEMQIPDAAQVmDRYPF------ 155
Cdd:TIGR03719 389 YVDQSRD---------------ALDPNKTV----WEEISGGLD----------IIKLGKREIPSRAYV-GRFNFkgsdqq 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 156 ----ELSGGMRQRVMIALAFSCEPELIIADEPTTALDVtvqrQVLRLLKHKARASGTSVLFISHD 216
Cdd:TIGR03719 439 kkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHD 499
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-244 |
8.05e-08 |
|
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: 53.86 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 24 ALNHVSLEIGRGEIVGVVGESGSGKSVT-AMLAmrllpeGSYHVHHGRVTLLGEDVL-NASEkqlrqwrgARVAMIFQEP 101
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTfKMLT------GDTTVTSGDATVAGKSILtNISD--------VHQNMGYCPQ 2019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 102 MTALNPTRrIGRQMVEVIRQHQSLSRRDAQQKA---IALLGemqipdAAQVMDRYPFELSGGMRQRVMIALAFSCEPELI 178
Cdd:TIGR01257 2020 FDAIDDLL-TGREHLYLYARLRGVPAEEIEKVAnwsIQSLG------LSLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 179 IADEPTTALDVTVQRQVLRLLKHKARaSGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESGITQTL 244
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-216 |
9.45e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 9.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 34 RGEIVGVVGESGSGKSVTAMLAMRLLPEGSYHVHhgrvtllgedVLNASEKQLRQWRGARVAMIfqepmtalnptrrigr 113
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI----------YIDGEDILEEVLDQLLLIIV---------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 114 qmvevirqhqslsrrdaqqkaiallgemqipdaaqvmDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQR 193
Cdd:smart00382 55 -------------------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
170 180
....*....|....*....|....*...
gi 505383390 194 QVL-----RLLKHKARASGTSVLFISHD 216
Cdd:smart00382 98 LLLlleelRLLLLLKSEKNLTVILTTND 125
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-244 |
1.16e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAM--LAMRLLPEGsyhvhhGRVTLLGEDVLNAS 82
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKS-TLMkiIAGIVPPDS------GTLEIGGNPCARLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 83 EKQLRQWRgarVAMIFQEPMtaLNPTRRIGRQMVEVIRQHQslsrrDAQQKAIALLGEMQI---PDAA----QVMDRYPF 155
Cdd:PRK15439 80 PAKAHQLG---IYLVPQEPL--LFPNLSVKENILFGLPKRQ-----ASMQKMKQLLAALGCqldLDSSagslEVADRQIV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 156 E-LSGGMRqrvmialafscEPELIIADEPTTALdvtVQRQVLRLLKH--KARASGTSVLFISHDMAVVSQLCDRMYVMYA 232
Cdd:PRK15439 150 EiLRGLMR-----------DSRILILDEPTASL---TPAETERLFSRirELLAQGVGIVFISHKLPEIRQLADRISVMRD 215
|
250
....*....|..
gi 505383390 233 GSVIESGITQTL 244
Cdd:PRK15439 216 GTIALSGKTADL 227
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-239 |
1.86e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.75 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 17 IFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGsyhVHHGRVTLLGEDVLNAsekqlrqwrgarvam 96
Cdd:PRK13547 9 VARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGG---GAPRGARVTGDVTLNG--------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 97 ifqEPMTALNPTRRIGRQMV--------------EVI--------RQHQSLSRRDAQQKAIALlgemQIPDAAQVMDRYP 154
Cdd:PRK13547 71 ---EPLAAIDAPRLARLRAVlpqaaqpafafsarEIVllgryphaRRAGALTHRDGEIAWQAL----ALAGATALVGRDV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 155 FELSGGMRQRVMIALAFS---------CEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCD 225
Cdd:PRK13547 144 TTLSGGELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHAD 223
|
250
....*....|....
gi 505383390 226 RMYVMYAGSVIESG 239
Cdd:PRK13547 224 RIAMLADGAIVAHG 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
157-243 |
2.16e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 LSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARaSGTSVLFISHDMAVVSQLCDRMYVMYAGSVi 236
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLV- 469
|
....*..
gi 505383390 237 eSGITQT 243
Cdd:PRK10982 470 -AGIVDT 475
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-239 |
2.65e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.97 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 21 DVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAMRLLPEGSYHVHHGRVTLLGEDV-LNASEKQLRQWRGARVAMIF 98
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKStLSNIIGGSLSPTVGKVDRNGEVSVIAISAgLSGQLTGIENIEFKMLCMGF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 99 QEpmtalnptRRIGRQMVEVIRqhqslsrrdaqqkaIALLGEMqipdAAQVMDRYpfelSGGMRQRVMIALAFSCEPELI 178
Cdd:PRK13546 116 KR--------KEIKAMTPKIIE--------------FSELGEF----IYQPVKKY----SSGMRAKLGFSINITVNPDIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505383390 179 IADEPTTALDVTVQRQVLRLLkHKARASGTSVLFISHDMAVVSQLCDRMYVMYAGSVIESG 239
Cdd:PRK13546 166 VIDEALSVGDQTFAQKCLDKI-YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
25-239 |
7.26e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 49.18 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMRLLPEGSYHVHhGRVTLLGEDVLNASEKQLRQwrgarVAMIFQE---- 100
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCS-TLLKALANRTEGNVSVE-GDIHYNGIPYKEFAEKYPGE-----IIYVSEEdvhf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 101 -PMTAlnptrrigRQMVEVirqhqslsrrdaqqkAIALLGemqipdaaqvmDRYPFELSGGMRQRVMIALAFSCEPELII 179
Cdd:cd03233 96 pTLTV--------RETLDF---------------ALRCKG-----------NEFVRGISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383390 180 ADEPTTALDVTVQRQVLRLLKHKARASGTSVLFIshdmavVSQ-------LCDRMYVMYAGSVIESG 239
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS------LYQasdeiydLFDKVLVLYEGRQIYYG 202
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
5-222 |
7.94e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.03 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 5 VLSIEDLHLSfpifRGDvHAL-NHVSLEIGRGEIVGVVGESGSGKsvTAMLamRLL-----PEGsyhvhhGRVTLLGEDV 78
Cdd:PRK13538 1 MLEARNLACE----RDE-RILfSGLSFTLNAGELVQIEGPNGAGK--TSLL--RILaglarPDA------GEVLWQGEPI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 79 LNASEKQLRQ--WRGaRVAMIFQEpMTALnptrrigrqmvEVIR----QHQSLSRRDAQQ--KAIALLGEMQIPdAAQvm 150
Cdd:PRK13538 66 RRQRDEYHQDllYLG-HQPGIKTE-LTAL-----------ENLRfyqrLHGPGDDEALWEalAQVGLAGFEDVP-VRQ-- 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383390 151 drypfeLSGGMRQRVmiALA--FSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQ 222
Cdd:PRK13538 130 ------LSAGQQRRV--ALArlWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVASD 195
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-285 |
8.03e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.98 E-value: 8.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 LSGGMRQRVMIA---LAFSCEPELIIADEPTTAL---DVTVQRQVLRLLKHKarasGTSVLFISHDMAVVsQLCDrmYVM 230
Cdd:PRK00635 810 LSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQ----GHTVVIIEHNMHVV-KVAD--YVL 882
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505383390 231 --------YAGSVIESGITQTLIHHPVhPYSIGLlrcAPENGEPREiLPAIPGTVPNlSHLPR 285
Cdd:PRK00635 883 elgpeggnLGGYLLASCSPEELIHLHT-PTAKAL---RPYLSSPQE-LPYLPDPSPK-PPVPA 939
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-217 |
9.62e-07 |
|
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: 48.87 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 21 DVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMLAMRllpeGSYHVHHGRVTLLGEDVLNASEKQLRQWRGARVAMIFQE 100
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKS-SLLLAIL----GEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 101 PMTaLNPTRR--------IGRQMVEVIRQHQSLsrrdaqQKAIALLgemQIPDAAQVMDRyPFELSGGMRQRVMIALAFS 172
Cdd:cd03290 88 PWL-LNATVEenitfgspFNKQRYKAVTDACSL------QPDIDLL---PFGDQTEIGER-GINLSGGQRQRICVARALY 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505383390 173 CEPELIIADEPTTALDV-----TVQRQVLRLLKHKARasgtSVLFISHDM 217
Cdd:cd03290 157 QNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKL 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-226 |
1.10e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 4 SVLSIEDLHLSFpifrGDVHALNHVSLEIGRGEIVGVVGESGSGKSvTAMlamrllpegsyhvhhgRVtLLGEDVLNASE 83
Cdd:PRK11147 2 SLISIHGAWLSF----SDAPLLDNAELHIEDNERVCLVGRNGAGKS-TLM----------------KI-LNGEVLLDDGR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 84 KQLRQwrGARVAMIFQEPMTALNPT------RRIGRQmVEVIRQHQSLSRRDAQQKAIALLGEMqipdaAQVMDR----- 152
Cdd:PRK11147 60 IIYEQ--DLIVARLQQDPPRNVEGTvydfvaEGIEEQ-AEYLKRYHDISHLVETDPSEKNLNEL-----AKLQEQldhhn 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 153 -YPFE--------------------LSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHkarASGtSVL 211
Cdd:PRK11147 132 lWQLEnrinevlaqlgldpdaalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT---FQG-SII 207
|
250
....*....|....*
gi 505383390 212 FISHDMAVVSQLCDR 226
Cdd:PRK11147 208 FISHDRSFIRNMATR 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-239 |
1.37e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKS--VTAMLAMRLLPEGSYHVHHGRVTLLGED--VLNASekqlrqwrgARVAMIFQE 100
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTslISAMLGELSHAETSSVVIRGSVAYVPQVswIFNAT---------VRENILFGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 101 PMTalnpTRRIGRQMVEVIRQHQS--LSRRDAQQkaialLGEMQIpdaaqvmdrypfELSGGMRQRVMIALAFSCEPELI 178
Cdd:PLN03232 704 DFE----SERYWRAIDVTALQHDLdlLPGRDLTE-----IGERGV------------NISGGQKQRVSMARAVYSNSDIY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505383390 179 IADEPTTALDVTVQRQVL-RLLKHKARasGTSVLFISHDMAVVSQLcDRMYVMYAGSVIESG 239
Cdd:PLN03232 763 IFDDPLSALDAHVAHQVFdSCMKDELK--GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEG 821
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
8-189 |
2.52e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 8 IEDLHL-SFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSV----TAMLAMRLLPEGSyHVHHGRVTLLGED----- 77
Cdd:PLN03073 175 IKDIHMeNFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTflryMAMHAIDGIPKNC-QILHVEQEVVGDDttalq 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 78 -VLNA---------SEKQL-RQWRGARVAMIFQEPMTALNPTRR---IGRQMVEVIRQHQSLSRRDAQQKAIALLGEMQI 143
Cdd:PLN03073 254 cVLNTdiertqlleEEAQLvAQQRELEFETETGKGKGANKDGVDkdaVSQRLEEIYKRLELIDAYTAEARAASILAGLSF 333
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505383390 144 PDAAQVMDRYPFelSGGMRQRVMIALAFSCEPELIIADEPTTALDV 189
Cdd:PLN03073 334 TPEMQVKATKTF--SGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-237 |
3.07e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.43 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 24 ALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMrllpeGSYHVHHGRVTLLGEDVlnaSEKQLRQWRGARVAM-----IF 98
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLT-----GLYQPQSGEILLDGKPV---TAEQPEDYRKLFSAVftdfhLF 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 99 QEpmtALNPtrriGRQMVEVIRQHQSLSRRDAQQKaiallgeMQIPDaAQVMDrypFELSGGMRQRVMIALAFSCEPELI 178
Cdd:PRK10522 410 DQ---LLGP----EGKPANPALVEKWLERLKMAHK-------LELED-GRISN---LKLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505383390 179 IADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQlCDRMYVMYAGSVIE 237
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
25-254 |
4.81e-06 |
|
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: 47.21 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLpegsyHVHHGRVTLLGEDVLNASEKQLRqwrgARVAMIFQEPMT- 103
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMV-----DIFDGKIVIDGIDISKLPLHTLR----SRLSIILQDPILf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 104 ------ALNPTRRIGRQmveviRQHQSLSRRDAQQKAIALLGEMqipDAaqVMDRYPFELSGGMRQRVMIALAFSCEPEL 177
Cdd:cd03288 108 sgsirfNLDPECKCTDD-----RLWEALEIAQLKNMVKSLPGGL---DA--VVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383390 178 IIADEPTTALDVTVQrQVLRLLKHKARASGTsVLFISHDMAVVSQlCDRMYVMYAGSVIESGITQTLIHHPVHPYSI 254
Cdd:cd03288 178 LIMDEATASIDMATE-NILQKVVMTAFADRT-VVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFAS 251
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-220 |
6.73e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 19 RGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLlpegsYHVHHGRVTLlgEDVLNASEKQLRQWRgARVAMIF 98
Cdd:PTZ00265 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERL-----YDPTEGDIII--NDSHNLKDINLKWWR-SKIGVVS 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 99 QEPMTALNPTRRIGRQMVEVIRQHQSLS----------------RRDAQQKAIALLGEM----------------QIPDA 146
Cdd:PTZ00265 467 QDPLLFSNSIKNNIKYSLYSLKDLEALSnyynedgndsqenknkRNSCRAKCAGDLNDMsnttdsneliemrknyQTIKD 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 147 AQVM----------------DRY-------PFELSGGMRQRVMIALAFSCEPELIIADEPTTALD----VTVQRQVLRLL 199
Cdd:PTZ00265 547 SEVVdvskkvlihdfvsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDnkseYLVQKTINNLK 626
|
250 260
....*....|....*....|.
gi 505383390 200 KHKARASgtsvLFISHDMAVV 220
Cdd:PTZ00265 627 GNENRIT----IIIAHRLSTI 643
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
157-216 |
7.70e-06 |
|
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: 45.43 E-value: 7.70e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383390 157 LSGGMRQRVMIALAF---SCEPE-LIIADEPTTALDVTVQRQVLRLLKHKaRASGTSVLFISHD 216
Cdd:cd03227 78 LSGGEKELSALALILalaSLKPRpLYILDEIDRGLDPRDGQALAEAILEH-LVKGAQVIVITHL 140
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
17-220 |
1.49e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 45.68 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 17 IFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSvtAMLAMRLLPEGSYHVHHGRVTLLGEDVLNASEKQlrqwrgARVAM 96
Cdd:cd03271 3 LKGARENNLKNIDVDIPLGVLTCVTGVSGSGKS--SLINDTLYPALARRLHLKKEQPGNHDRIEGLEHI------DKVIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 97 IFQEPM---TALNP-------------------TRRIGRQMVEVIRQHQSlsrrdaqqkaIALLGEMQIPDAAQVMDRYP 154
Cdd:cd03271 75 IDQSPIgrtPRSNPatytgvfdeirelfcevckGKRYNRETLEVRYKGKS----------IADVLDMTVEEALEFFENIP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 155 -----------------------FELSGGMRQRVMIA--LAF-SCEPELIIADEPTTAL---DVtvqRQVLRLLkHKARA 205
Cdd:cd03271 145 kiarklqtlcdvglgyiklgqpaTTLSGGEAQRIKLAkeLSKrSTGKTLYILDEPTTGLhfhDV---KKLLEVL-QRLVD 220
|
250
....*....|....*
gi 505383390 206 SGTSVLFISHDMAVV 220
Cdd:cd03271 221 KGNTVVVIEHNLDVI 235
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-215 |
1.62e-05 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 45.04 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 19 RGDVHALNHVSLEIGRGEIVGVVGESGSGK-SVTAMLAMRLLPEGsyhvhhGRVTLLGEDVLNASEKQLRQ--WRGARVA 95
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKtTLLRILAGLLRPDS------GEVRWNGTPLAEQRDEPHENilYLGHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 96 MifqepMTALNPTrrigrqmvEVIRQHQSLSRrDAQQKAIALLGEMQIPDAAQVMDRYpfeLSGGMRQRVMIALAFSCEP 175
Cdd:TIGR01189 84 L-----KPELSAL--------ENLHFWAAIHG-GAQRTIEDALAAVGLTGFEDLPAAQ---LSAGQQRRLALARLWLSRR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505383390 176 ELIIADEPTTALDVTVQRQVLRLLK-HKARasGTSVLFISH 215
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLLRaHLAR--GGIVLLTTH 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-216 |
1.88e-05 |
|
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: 46.08 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 17 IFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSvtamlamrllpegsyhvhhgrvTLL----GEDvlNASEKQLRQWRGA 92
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKS----------------------TLLrimaGVD--KDFNGEARPQPGI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 93 RVAMIFQEPmtALNPTRRIgRQMVE--VIRQHQSLSRRDAQQKAIA--------LLGEM----QIPDAA----------Q 148
Cdd:TIGR03719 69 KVGYLPQEP--QLDPTKTV-RENVEegVAEIKDALDRFNEISAKYAepdadfdkLAAEQaelqEIIDAAdawdldsqleI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 149 VMD--RYP------FELSGGMRQRVMIALAFSCEPELIIADEPTTALDVtvqRQVLRLLKHKARASGTsVLFISHD 216
Cdd:TIGR03719 146 AMDalRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA---ESVAWLERHLQEYPGT-VVAVTHD 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-265 |
1.98e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKSVtamLAMRLLpeGSYHVHHGRVtllgedvlnasekqlrqWRGARVAMIFQEPMTa 104
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKST---LLQSLL--SQFEISEGRV-----------------WAERSIAYVPQQAWI- 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 105 LNPTRRIG---------RQMVEVIRQHQSlsRRDAQQKAIAL---LGEMQIpdaaqvmdrypfELSGGMRQRVMIALAFS 172
Cdd:PTZ00243 733 MNATVRGNilffdeedaARLADAVRVSQL--EADLAQLGGGLeteIGEKGV------------NLSGGQKARVSLARAVY 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 173 CEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLfISHDMAVVSqLCDRMYVMYAGSVIESGITQTLIHHPVHPY 252
Cdd:PTZ00243 799 ANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVL-ATHQVHVVP-RADYVVALGDGRVEFSGSSADFMRTSLYAT 876
|
250
....*....|...
gi 505383390 253 SIGLLRCAPENGE 265
Cdd:PTZ00243 877 LAAELKENKDSKE 889
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-220 |
2.56e-05 |
|
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: 44.41 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 19 RGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSyhvhhGRVTLLGEDVLNASEKQLRQ--WRGARVAM 96
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLA-----GRVLLNGGPLDFQRDSIARGllYLGHAPGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 97 ifqepMTALNPtrrigrqmVEVIRQHQSLSRRDAQQKAIALLGemqipdAAQVMDRYPFELSGGMRQRVMIALAFSCEPE 176
Cdd:cd03231 85 -----KTTLSV--------LENLRFWHADHSDEQVEEALARVG------LNGFEDRPVAQLSAGQQRRVALARLLLSGRP 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505383390 177 LIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVV 220
Cdd:cd03231 146 LWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-234 |
3.26e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 44.85 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKSVTAMLAM-RLLPEGSYHVHHGRVTLLGedvlnasekqlrQWRGARVAMIFQEPMT 103
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSGRISFSS------------QFSWIMPGTIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 104 ALNPTRRIGRQMVEVIRQHQSLSRRDAQQKAIalLGEMQIpdaaqvmdrypfELSGGMRQRVMIALAFSCEPELIIADEP 183
Cdd:cd03291 121 GVSYDEYRYKSVVKACQLEEDITKFPEKDNTV--LGEGGI------------TLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505383390 184 TTALDVTVQRQVLRLLKHKARASGTSVLFISHdmavVSQL--CDRMYVMYAGS 234
Cdd:cd03291 187 FGYLDVFTEKEIFESCVCKLMANKTRILVTSK----MEHLkkADKILILHEGS 235
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
157-222 |
4.67e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 4.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505383390 157 LSGGMRQRVMIALAFSCE---PELIIADEPTTAL---DVTVQRQVLRLLKHKarasGTSVLFISHDMAVVSQ 222
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIKKLLEVLQRLVDK----GNTVVVIEHNLDVIKT 897
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-222 |
1.09e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 3 DSVLSIEDLHLSFpIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPEGSYHV---------------- 66
Cdd:PTZ00265 1163 KGKIEIMDVNFRY-ISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 67 ---------------------------------HHGRVTLLGEDVLNASEKQLRQWrgarVAMIFQEPM---TALNPTRR 110
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNL----FSIVSQEPMlfnMSIYENIK 1317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 111 IGRQmvevirqhqSLSRRDAQQKA-IALLGEM--QIPDAAQV-MDRYPFELSGGMRQRVMIALAFSCEPELIIADEPTTA 186
Cdd:PTZ00265 1318 FGKE---------DATREDVKRACkFAAIDEFieSLPNKYDTnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSS 1388
|
250 260 270
....*....|....*....|....*....|....*.
gi 505383390 187 LDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQ 222
Cdd:PTZ00265 1389 LDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR 1424
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-248 |
1.14e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 25 LNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLpegsyHVHHGRVTLLGEDVLNASEKQLRQwrgaRVAMIFQEPM-- 102
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMV-----EVCGGEIRVNGREIGAYGLRELRR----QFSMIPQDPVlf 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 103 ---TALNPTRRIGRQMVEVIRqhqslsrrdaqqkAIALLG-EMQIPDAAQVMDRYPFE----LSGGMRQRVMIALA-FSC 173
Cdd:PTZ00243 1397 dgtVRQNVDPFLEASSAEVWA-------------ALELVGlRERVASESEGIDSRVLEggsnYSVGQRQLMCMARAlLKK 1463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 174 EPELIIADEPTTALDVTVQRQVLRLLkhKARASGTSVLFISHDMAVVSQlCDRMYVMYAGSVIESGITQTLIHHP 248
Cdd:PTZ00243 1464 GSGFILMDEATANIDPALDRQIQATV--MSAFSAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-78 |
1.19e-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: 43.63 E-value: 1.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 505383390 28 VSLEIGRGEIVGVVGESGSGKSVTAMLamrLLpeGSYHVHHGRVTLLGEDV 78
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKL---LT--GLYRPESGEILLDGQPV 396
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
158-239 |
2.73e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 158 SGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLfishdMAVV--SQ----LCDRMYVMY 231
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPL-----VAIYqcSQdayeLFDKVIVLY 285
|
....*...
gi 505383390 232 AGSVIESG 239
Cdd:TIGR00956 286 EGYQIYFG 293
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-216 |
2.96e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 8 IEDLHLSF-PifrgdvhalnhvsleigrGEIVGVVGESGSGKSvtamlamrllpegsyhvhhgrvTLL----GEDVLNAS 82
Cdd:PRK11819 23 LKDISLSFfP------------------GAKIGVLGLNGAGKS----------------------TLLrimaGVDKEFEG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 83 EKQLRQwrGARVAMIFQEPmtALNPTRRIgRQMVE--VIRQHQSLSRRDA-----------QQKAIALLGEMQ-IPDAA- 147
Cdd:PRK11819 63 EARPAP--GIKVGYLPQEP--QLDPEKTV-RENVEegVAEVKAALDRFNEiyaayaepdadFDALAAEQGELQeIIDAAd 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 148 ---------QVMD--RYP------FELSGGMRQRVmiALafsC-----EPELIIADEPTTALDVTvqrQVLRLLKHKARA 205
Cdd:PRK11819 138 awdldsqleIAMDalRCPpwdakvTKLSGGERRRV--AL---CrllleKPDMLLLDEPTNHLDAE---SVAWLEQFLHDY 209
|
250
....*....|.
gi 505383390 206 SGTsVLFISHD 216
Cdd:PRK11819 210 PGT-VVAVTHD 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
157-220 |
3.22e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.24 E-value: 3.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383390 157 LSGGMRQRVMIALAFSCEPELIIADEPTTALDVtvqrQVLRLLKHK-ARASGTsVLFISHDMAVV 220
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELlDSYQGT-VLLVSHDRQFV 500
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-216 |
4.95e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 14 SFPIFRGDVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAMRLLPEGsyhvhhGRVTLLGedvlnasekqlrQWRga 92
Cdd:PRK10636 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKStLLALLKNEISADG------GSYTFPG------------NWQ-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 93 rVAMIFQE----PMTALNPTRRIGRQMVEVIRQHQSLSRRDaQQKAIALL-GEMQIPDAAQVMDRYPFEL---------- 157
Cdd:PRK10636 66 -LAWVNQEtpalPQPALEYVIDGDREYRQLEAQLHDANERN-DGHAIATIhGKLDAIDAWTIRSRAASLLhglgfsneql 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383390 158 -------SGGMRQRVMIALAFSCEPELIIADEPTTALDVTVqrqVLRLLKHKARASGTSVLfISHD 216
Cdd:PRK10636 144 erpvsdfSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQGTLIL-ISHD 205
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
129-215 |
7.97e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 129 DAQQKA----IALLG-EMQIPDAaqvmdryPFE-LSGGMRQRVMIALAFSCEPELIIADEPTTALDvTVQRQ-VLRLLKH 201
Cdd:PRK10938 375 DRQQKLaqqwLDILGiDKRTADA-------PFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLD-PLNRQlVRRFVDV 446
|
90
....*....|....
gi 505383390 202 KARASGTSVLFISH 215
Cdd:PRK10938 447 LISEGETQLLFVSH 460
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-211 |
9.01e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 39.86 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 19 RGDVHALNHVSLEIGRGEIVGVVGESGSGKSVTAMLAMRLLPegsyhVHHGRVTLLGEDVLNASEKQLRQWRGARVAMif 98
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP-----PAAGTIKLDGGDIDDPDVAEACHYLGHRNAM-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 99 qepmtalnptrrigrqmvevirqHQSLSRRDAQQKAIALLG--EMQIPDAAQVMDRY-----PF-ELSGGMRQRVMIA-L 169
Cdd:PRK13539 85 -----------------------KPALTVAENLEFWAAFLGgeELDIAAALEAVGLAplahlPFgYLSAGQKRRVALArL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505383390 170 AFSCEPeLIIADEPTTALDVTVQRQVLRLLKHKARASGTSVL 211
Cdd:PRK13539 142 LVSNRP-IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIA 182
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
131-235 |
1.27e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 131 QQKAIALLGEMQIPD--AAQVMdrypFELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVqrqVLRLLKHKARASGt 208
Cdd:PLN03073 604 EQKLRAHLGSFGVTGnlALQPM----YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLFQG- 675
|
90 100
....*....|....*....|....*..
gi 505383390 209 SVLFISHDMAVVSQLCDRMYVMYAGSV 235
Cdd:PLN03073 676 GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
156-215 |
1.89e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 40.12 E-value: 1.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 156 ELSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKarasGTSVLFISH 215
Cdd:TIGR00954 582 VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF----GITLFSVSH 637
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
157-220 |
3.02e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 3.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 LSGGMRQRVMIALAFS---CEPELIIADEPTTAL---DVtvqRQVLRLLkHKARASGTSVLFISHDMAVV 220
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLhfhDI---RKLLEVL-HRLVDKGNTVVVIEHNLDVI 892
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
32-215 |
4.35e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 38.34 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 32 IGRGEIVGVVGESGSGKSvtaMLAMRLlpegSYHVHHGRvTLLGEDVlnasekqlrqwRGARVAMIFQEpmtalNPTRRI 111
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKS---FLALQL----AAAVAAGG-PWLGRRV-----------PPGKVLYLAAE-----DDRGEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 112 GRQMvEVIRQHQSLSRRDAQQKaIALLGEMQIPDAAQVMDRypfelsggmrqrvMIALAFSCEPELIIADePTTAL---- 187
Cdd:COG3598 66 RRRL-KALGADLGLPFADLDGR-LRLLSLAGDLDDTDDLEA-------------LERAIEEEGPDLVVID-PLARVfggd 129
|
170 180 190
....*....|....*....|....*....|
gi 505383390 188 --DVTVQRQVLRLLKHKARASGTSVLFISH 215
Cdd:COG3598 130 enDAEEMRAFLNPLDRLAERTGAAVLLVHH 159
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-216 |
5.16e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 37.62 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 22 VHALNHVSLEIGRGEIVGVVGESGSGKSvtaMLAMRLL-PEGSYHVHHGRVTLLGEDVLNASEKQLRQWRGARVAMIFQE 100
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKS---SLAFDTIyAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAIAIDQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 101 PMTALNPTRRIGrQMVEVIRQHQSLSRRDAQQKAIALLGEMQIPDAAqvMDRYPFELSGGMRQRvmIALAFSCEPELI-- 178
Cdd:cd03270 85 KTTSRNPRSTVG-TVTEIYDYLRLLFARVGIRERLGFLVDVGLGYLT--LSRSAPTLSGGEAQR--IRLATQIGSGLTgv 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505383390 179 --IADEPTTALDvtvQRQVLRLLK--HKARASGTSVLFISHD 216
Cdd:cd03270 160 lyVLDEPSIGLH---PRDNDRLIEtlKRLRDLGNTVLVVEHD 198
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
157-239 |
9.24e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.90 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 157 LSGGMRQRVMIALAFSCEPELIIADEPTTALDVTVQRQVLRLLKHKARASGTSVLFISHDMAVVSQLCDRMYVM-YAGSV 235
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMkRGGQV 1099
|
....
gi 505383390 236 IESG 239
Cdd:PLN03140 1100 IYSG 1103
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-235 |
9.41e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.84 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 20 GDVHALNHVSLEIGRGEIVGVVGESGSGKS-VTAMLAMRLLPEgsyhvhHGRVTLLgedvlnasekqlrqwRGARVAMIF 98
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKStLIKLLAGELAPV------SGEIGLA---------------KGIKLGYFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383390 99 QEPMTALNPTrrigrqmvEVIRQHQS-LSRRDAQQKAIALLGE--MQIPDAAQVMDRYpfelSGGMRQRVMIALAFSCEP 175
Cdd:PRK10636 382 QHQLEFLRAD--------ESPLQHLArLAPQELEQKLRDYLGGfgFQGDKVTEETRRF----SGGEKARLVLALIVWQRP 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505383390 176 ELIIADEPTTALDVTVqRQVLR--LLKHKArasgtSVLFISHDMAVVSQLCDRMYVMYAGSV 235
Cdd:PRK10636 450 NLLLLDEPTNHLDLDM-RQALTeaLIDFEG-----ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| |
