|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-318 |
5.45e-159 |
|
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: 447.19 E-value: 5.45e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnQESIHIDDGNISFESEELTNLQESE 83
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGL-LPPPGITSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WNQIRGKDIAFIFQDPLSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRFEQYPHQLSGGMRQRI 163
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 164 CLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446453387 244 GSPKHPYTKSLLQAIPNIDDSEKVLRAIEGTTPSIETLNSfGCPFVNRCPVAIKECIHRFPERTTYSKEHSSHCW 318
Cdd:COG0444 240 ENPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPS-GCRFHPRCPYAMDRCREEEPPLREVGPGHRVACH 313
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-259 |
3.79e-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: 3.79e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHIDDGNISFESEELTNLQESE 83
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WNQIRGKDIAFIFQDPLSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRFEQYPHQLSGGMRQRI 163
Cdd:COG4172 86 LRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 164 CLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELF 245
|
250
....*....|....*.
gi 446453387 244 GSPKHPYTKSLLQAIP 259
Cdd:COG4172 246 AAPQHPYTRKLLAAEP 261
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-323 |
9.92e-109 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 320.13 E-value: 9.92e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHIDdGNISFESEELTNLQESEWNQIRGKDIAFIFQDPLSSL 103
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIG-GSATFNGREILNLPEKELNKLRAEQISMIFQDPMTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPTT 183
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 184 ALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTKSLLQAIPNIDD 263
Cdd:PRK09473 191 ALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPRLDA 270
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 264 SEKVLRAIEGTTPSIETLNSfGCPFVNRCPVAIKECiHRFPERTTYSKEHSSHCWQHVLE 323
Cdd:PRK09473 271 EGESLLTIPGNPPNLLRLPK-GCPFQPRCPHAMEIC-SSAPPLEEFGPGRLRACFKPVEE 328
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-237 |
2.24e-108 |
|
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: 315.21 E-value: 2.24e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNqesiHIDDGNISFESEELTNLQEsE 83
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL----KPTSGSIIFDGKDLLKLSR-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WNQIRGKDIAFIFQDPLSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAInLLNDLGIHEAEKRFEQYPHQLSGGMRQRI 163
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446453387 164 CLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKG 237
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-262 |
2.93e-102 |
|
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: 309.91 E-value: 2.93e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTL--AVEKENSKQAiVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQE 81
Cdd:COG1123 260 LLEVRNLSKryPVRGKGGVRA-VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL----LRPTSGSILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 82 SEWNQIRgKDIAFIFQDPLSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAekRFEQYPHQLSGGMRQ 161
Cdd:COG1123 335 RSLRELR-RRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPD--LADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 162 RICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEE 241
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
250 260
....*....|....*....|.
gi 446453387 242 VIGSPKHPYTKSLLQAIPNID 262
Cdd:COG1123 492 VFANPQHPYTRALLAAVPSLD 512
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-305 |
9.82e-98 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 292.03 E-value: 9.82e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHIDDGNISFESEELTNLQESE 83
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WNQIRGKDIAFIFQDPLSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRFEQYPHQLSGGMRQRI 163
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 164 CLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453387 244 GSPKHPYTKSLLQAIPNIDDSEKVLRAIEGTTPSIETLNSfGCPFVNRCPVAIKECIHRFPE 305
Cdd:PRK11022 243 RAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPN-GCLLNPRCPYATDRCRAEEPA 303
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-318 |
1.06e-94 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 284.32 E-value: 1.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEWNQIRgKDIAFIFQDPLSSL 103
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRL----EEPTSGEILFDGQDITGLSGRELRPLR-RRMQMVFQDPYASL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAekRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPTT 183
Cdd:COG4608 109 NPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPE--HADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 184 ALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTKSLLQAIPNIDD 263
Cdd:COG4608 187 ALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQALLSAVPVPDP 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446453387 264 SEKVLRAI-EGTTPSieTLN--SfGCPFVNRCPVAIKECIHRFPERTTYSKEHSSHCW 318
Cdd:COG4608 267 ERRRERIVlEGDVPS--PLNppS-GCRFHTRCPYAQDRCATEEPPLREVGPGHQVACH 321
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-278 |
9.76e-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: 280.25 E-value: 9.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 1 MGQLLSLENVTlaVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHIDdGNISFESEELTNLQ 80
Cdd:COG1123 1 MTPLLEVRDLS--VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIS-GEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 81 EsewnQIRGKDIAFIFQDPLSSLNPTmKVGRQITEViLQHEKKSKKEAKEIAINLLNDLGIheaEKRFEQYPHQLSGGMR 160
Cdd:COG1123 78 E----ALRGRRIGMVFQDPMTQLNPV-TVGDQIAEA-LENLGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 161 QRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIE 240
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 446453387 241 EVIGSPKhpytksLLQAIPNIDDSEKVLRAIEGTTPSI 278
Cdd:COG1123 229 EILAAPQ------ALAAVPRLGAARGRAAPAAAAAEPL 260
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
3-317 |
2.30e-89 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 270.62 E-value: 2.30e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 3 QLLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHIDDGNISFESEELTNLQES 82
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 83 EWNQIRGKDIAFIFQDPLSSLNPTMKVGRQITEVILQHEKKSK-----KEAKEIAINLLNDLGIHEAEKRFEQYPHQLSG 157
Cdd:COG4170 82 ERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIKDHKDIMNSYPHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 158 GMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKG 237
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 238 TIEEVIGSPKHPYTKSLLQAIPNIDDS---EKVLRAIEGTTPSIETLnSFGCPFVNRCPVAIKECIHRfPERTTYsKEHS 314
Cdd:COG4170 242 PTEQILKSPHHPYTKALLRSMPDFRQPlphKSRLNTLPGSIPPLQHL-PIGCRLGPRCPYAQKKCVET-PRLRKI-KGHE 318
|
...
gi 446453387 315 SHC 317
Cdd:COG4170 319 FAC 321
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-259 |
6.51e-85 |
|
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: 256.27 E-value: 6.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEELTNLQESE 83
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP----WSGEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WNqirgKDIAFIFQDPLSSLNPTMKVGRQITEVILQHEKKSKKEAkeiAINLLNDLGIHEAEKRfeQYPHQLSGGMRQRI 163
Cdd:COG1124 77 FR----RRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREER---IAELLEQVGLPPSFLD--RYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 164 CLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|....*.
gi 446453387 244 GSPKHPYTKSLLQAIP 259
Cdd:COG1124 228 AGPKHPYTRELLAASL 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
24-262 |
4.90e-84 |
|
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: 263.47 E-value: 4.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnQESihidDGNISFESEELTNLQESEWNQIRgKDIAFIFQDPLSSL 103
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPS----EGEIRFDGQDLDGLSRRALRPLR-RRMQVVFQDPFGSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMKVGRQITE-VILQHEKKSKKEAKEIAINLLNDLGIHEAekRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPT 182
Cdd:COG4172 376 SPRMTVGQIIAEgLRVHGPGLSAAERRARVAEALEEVGLDPA--ARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPT 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 183 TALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTKSLLQAIPNID 262
Cdd:COG4172 454 SALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-259 |
6.50e-81 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 255.40 E-value: 6.50e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGL-NQESIHIDDGNISFESEELTNLQES 82
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlPSPPVVYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 83 EWNQIRGKDIAFIFQDPLSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRFEQYPHQLSGGMRQR 162
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 163 ICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
250
....*....|....*..
gi 446453387 243 IGSPKHPYTKSLLQAIP 259
Cdd:PRK15134 245 FSAPTHPYTQKLLNSEP 261
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-317 |
3.79e-79 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 244.62 E-value: 3.79e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEWNQIRgKDIAFIFQDPLSSL 103
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGL----VKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDPLASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMKVGRQITEVILQHEKKSKKEAKEIAI-----------NLLNdlgiheaekrfeQYPHQLSGGMRQRICLAIAFACH 172
Cdd:PRK15079 112 NPRMTIGEIIAEPLRTYHPKLSRQEVKDRVkammlkvgllpNLIN------------RYPHEFSGGQCQRIGIARALILE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 173 PKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTK 252
Cdd:PRK15079 180 PKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 253 SLLQAIPnIDDSE----KVLRAIEGTTPSIETLNSfGCPFVNRCPVAIKECIHRFPERTTySKEHSSHC 317
Cdd:PRK15079 260 ALMSAVP-IPDPDlernKTIQLLEGELPSPINPPS-GCVFRTRCPIAGPECAKTRPVLEG-SFRHAVSC 325
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-261 |
1.42e-78 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 251.70 E-value: 1.42e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 2 GQLLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQES---IHIDDGNISFESEELTN 78
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAgglVQCDKMLLRRRSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 79 LQE---SEWNQIRGKDIAFIFQDPLSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRFEQYPHQL 155
Cdd:PRK10261 90 LSEqsaAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 156 SGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVE 235
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
250 260
....*....|....*....|....*.
gi 446453387 236 KGTIEEVIGSPKHPYTKSLLQAIPNI 261
Cdd:PRK10261 250 TGSVEQIFHAPQHPYTRALLAAVPQL 275
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-257 |
2.14e-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: 226.48 E-value: 2.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHIDDGNISFESEELTNLQesewnqIRGKDIAFIFQDPLSS 102
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 103 LNPTMKVGRQITEVILQHEKKSKKEAKEIAiNLLNDLGIHEAEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPT 182
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSLGKLSKQARALIL-EALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446453387 183 TALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTKSLLQA 257
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-317 |
1.03e-70 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 223.14 E-value: 1.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHIDDGNISFESEELTNLQESE 83
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WNQIRGKDIAFIFQDPLSSLNPTMKVGRQITEVI-----LQHEKKSKKEAKEIAINLLNDLGIHEAEKRFEQYPHQLSGG 158
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgwtyKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 159 MRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGT 238
Cdd:PRK15093 163 ECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 239 IEEVIGSPKHPYTKSLLQAIPNIDDS---EKVLRAIEGTTPSIETLnSFGCPFVNRCPVAIKECIHrfPERTTYSKEHSS 315
Cdd:PRK15093 243 SKELVTTPHHPYTQALIRAIPDFGSAmphKSRLNTLPGAIPLLEHL-PIGCRLGPRCPYAQRECIE--TPRLTGAKNHLY 319
|
..
gi 446453387 316 HC 317
Cdd:PRK15093 320 AC 321
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-299 |
2.14e-65 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 209.44 E-value: 2.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 19 SKQAIVKH---VSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQESEWNQIRgKDIAFI 95
Cdd:PRK11308 23 KPERLVKAldgVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPT----GGELYYQGQDLLKADPEAQKLLR-QKIQIV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 96 FQDPLSSLNPTMKVGRQITEvilqhekkskkeakEIAINllNDLGIHE-AEK----------RFEQ---YPHQLSGGMRQ 161
Cdd:PRK11308 98 FQNPYGSLNPRKKVGQILEE--------------PLLIN--TSLSAAErREKalammakvglRPEHydrYPHMFSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 162 RICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEE 241
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 242 VIGSPKHPYTKSLLQAIPNIDDSEKVLR-AIEGTTPSieTLN-SFGCPFVNRCPVAIKEC 299
Cdd:PRK11308 242 IFNNPRHPYTQALLSATPRLNPDDRRERiKLTGELPS--PLNpPPGCAFNARCPRAFGRC 299
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-233 |
3.79e-57 |
|
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: 184.23 E-value: 3.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSvTAQSIIGLnqesihIDD---GNISFESEELTNLQE 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGG------LDRptsGEVRVDGTDISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 82 SEWNQIRGKDIAFIFQDPlsSLNPTMKVGRQItEVILQHEKKSKKEAKEIAINLLNDLGIheaEKRFEQYPHQLSGGMRQ 161
Cdd:cd03255 74 KELAAFRRRHIGFVFQSF--NLLPDLTALENV-ELPLLLAGVPKKERRERAEELLERVGL---GDRLNHYPSELSGGQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453387 162 RICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREvADRVVVMYGGRV 233
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-235 |
1.96e-56 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 182.94 E-value: 1.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 1 MGQLLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSvTAQSIIGLnqesihID---DGNISFESEELT 77
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGG------LDrptSGEVLIDGQDIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 78 NLQESEWNQIRGKDIAFIFQDPlsSLNPTMKVGRQItEVILQHEKKSKKEAKEIAINLLNDLGIheaEKRFEQYPHQLSG 157
Cdd:COG1136 74 SLSERELARLRRRHIGFVFQFF--NLLPELTALENV-ALPLLLAGVSRKERRERARELLERVGL---GDRLDHRPSQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446453387 158 GMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVrEVADRVVVMYGGRVVE 235
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVS 224
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
24-257 |
3.18e-56 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 183.50 E-value: 3.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELtnlqESEWNQIRGKDIAFIFQDPLSSL 103
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPT----SGEILINGHKL----EYGDYKYRCKHIRMIFQDPNTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMKVGrQITEVILQhekkskkeakeiainLLNDLGIHEAEKRFEQ--------------YPHQLSGGMRQRICLAIAF 169
Cdd:COG4167 101 NPRLNIG-QILEEPLR---------------LNTDLTAEEREERIFAtlrlvgllpehanfYPHMLSSGQKQRVALARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 170 ACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHP 249
Cdd:COG4167 165 ILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHE 244
|
....*...
gi 446453387 250 YTKSLLQA 257
Cdd:COG4167 245 VTKRLIES 252
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-264 |
6.35e-54 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 186.60 E-value: 6.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEWNQIRgKDIAFIFQDPLSSL 103
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRL----VESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRfeQYPHQLSGGMRQRICLAIAFACHPKLVIADEPTT 183
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAW--RYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 184 ALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTKSLLQAIPNIDD 263
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVADP 572
|
.
gi 446453387 264 S 264
Cdd:PRK10261 573 S 573
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-258 |
1.83e-52 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 174.10 E-value: 1.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENV-----TLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEELTN 78
Cdd:PRK10419 3 LLNVSGLshhyaHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESP----SQGNVSWRGEPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 79 LQESEWNQIRgKDIAFIFQDPLSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLN--DLGIHEAEKRfeqyPHQLS 156
Cdd:PRK10419 79 LNRAQRKAFR-RDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRavDLDDSVLDKR----PPQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 157 GGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEK 236
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
250 260
....*....|....*....|..
gi 446453387 237 GTIEEVIGSpKHPYTKSLLQAI 258
Cdd:PRK10419 234 QPVGDKLTF-SSPAGRVLQNAV 254
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-255 |
2.59e-52 |
|
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: 172.47 E-value: 2.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKenskQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESE 83
Cdd:COG1127 5 MIEVRNLTKSFGD----RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGL----LRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WNQIRgKDIAFIFQDP--LSSLNptmkVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRfeqYPHQLSGGMRQ 161
Cdd:COG1127 77 LYELR-RRIGMLFQGGalFDSLT----VFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADK---MPSELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 162 RICLAIAFACHPKLVIADEPTTALD-VTiQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIE 240
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDpIT-SAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPE 227
|
250
....*....|....*
gi 446453387 241 EVIGSPkHPYTKSLL 255
Cdd:COG1127 228 ELLASD-DPWVRQFL 241
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-257 |
1.14e-51 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 171.42 E-value: 1.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 1 MGQLLSLENVTLAvekenSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHIDDGNISFESEELtnlq 80
Cdd:PRK10418 1 MPQQIELRNIALQ-----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPV---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 81 esEWNQIRGKDIAFIFQDPLSSLNPTMKVGRQITEVILQhekKSKKEAKEIAINLLNDLGIHEAEKRFEQYPHQLSGGMR 160
Cdd:PRK10418 72 --APCALRGRKIATIMQNPRSAFNPLHTMHTHARETCLA---LGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 161 QRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIE 240
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVE 226
|
250
....*....|....*..
gi 446453387 241 EVIGSPKHPYTKSLLQA 257
Cdd:PRK10418 227 TLFNAPKHAVTRSLVSA 243
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
20-258 |
7.10e-51 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 169.99 E-value: 7.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 20 KQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQESEWNQIRgKDIAFIFQDP 99
Cdd:TIGR02769 23 RAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPA----QGTVSFRGQDLYQLDRKQRRAFR-RDVQLVFQDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 LSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRfeQYPHQLSGGMRQRICLAIAFACHPKLVIAD 179
Cdd:TIGR02769 98 PSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDAD--KLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 180 EPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIgSPKHPYTKSLLQAI 258
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL-SFKHPAGRNLQSAV 253
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-253 |
4.17e-50 |
|
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: 166.91 E-value: 4.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKenskQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEW 84
Cdd:cd03261 1 IELRGLTKSFGG----RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGL----LRPDSGEVLIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIRgKDIAFIFQDP--LSSLNptmkVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKrfeQYPHQLSGGMRQR 162
Cdd:cd03261 73 YRLR-RRMGMLFQSGalFDSLT----VFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAED---LYPAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 163 ICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
250
....*....|.
gi 446453387 243 IGSPkHPYTKS 253
Cdd:cd03261 225 RASD-DPLVRQ 234
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
4-258 |
7.21e-50 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 166.91 E-value: 7.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlnqeSIHIDDGNISF-----ESEELTN 78
Cdd:COG4107 8 LLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYF----DLAPTSGSVYYrdrdgGPRDLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 79 LQESEWNQIRGKDIAFIFQDPLSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAekRFEQYPHQLSGG 158
Cdd:COG4107 84 LSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERLMAAGERHYGDIRARALEWLERVEIPLE--RIDDLPRTFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 159 MRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGT 238
Cdd:COG4107 162 MQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVESGL 241
|
250 260
....*....|....*....|
gi 446453387 239 IEEVIGSPKHPYTKSLLQAI 258
Cdd:COG4107 242 TDQVLEDPQHPYTQLLVSSV 261
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-271 |
1.25e-49 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 168.72 E-value: 1.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEELTNLQESEW 84
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERP----TSGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIRgKDIAFIFQDP--LSSLN-------PtMKV----GRQITEVILQhekkskkeakeiainLLNDLGIheAEKRfEQY 151
Cdd:COG1135 78 RAAR-RKIGMIFQHFnlLSSRTvaenvalP-LEIagvpKAEIRKRVAE---------------LLELVGL--SDKA-DAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 152 PHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGG 231
Cdd:COG1135 138 PSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446453387 232 RVVEKGTIEEVIGSPKHPYTKSLLQAIPNIDDSEKVLRAI 271
Cdd:COG1135 218 RIVEQGPVLDVFANPQSELTRRFLPTVLNDELPEELLARL 257
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-243 |
1.60e-48 |
|
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: 162.50 E-value: 1.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENskqAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEw 84
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL----LKPTSGEVLVDGKDITKKNLRE- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqIRgKDIAFIFQDPLSSL-NPT-----------MKVGRQitEVilqhekkskkeaKEIAINLLNDLGIHEAEKRfeqYP 152
Cdd:COG1122 73 --LR-RKVGLVFQNPDDQLfAPTveedvafgpenLGLPRE--EI------------RERVEEALELVGLEHLADR---PP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 153 HQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKeKQNTSILLITHDLALVREVADRVVVMYGGR 232
Cdd:COG1122 133 HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
250
....*....|.
gi 446453387 233 VVEKGTIEEVI 243
Cdd:COG1122 212 IVADGTPREVF 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-256 |
9.35e-48 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 168.35 E-value: 9.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihiddGNISFESEELTNLQESEWNQIRGKdIAFIFQDPLSS 102
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-----GEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQDPNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 103 LNPTMKVgRQITEVILQ--HEKKSKKEAKEIAINLLNDLGIhEAEKRFeQYPHQLSGGMRQRICLAIAFACHPKLVIADE 180
Cdd:PRK15134 375 LNPRLNV-LQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGL-DPETRH-RYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446453387 181 PTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTKSLLQ 256
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-232 |
3.09e-47 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 158.40 E-value: 3.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 6 SLENVTLAVEkeNSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTnlqESEWN 85
Cdd:cd03225 1 ELKNLSFSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT----SGEVLVDGKDLT---KLSLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 86 QIRGKdIAFIFQDPLSSL-NPTmkVGRqitEVI--LQHEKKSKKEAKEIAINLLNDLGIHEAEKRfeqYPHQLSGGMRQR 162
Cdd:cd03225 72 ELRRK-VGLVFQNPDDQFfGPT--VEE---EVAfgLENLGLPEEEIEERVEEALELVGLEGLRDR---SPFTLSGGQKQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 163 ICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITHDLALVREVADRVVVMYGGR 232
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-243 |
2.31e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.15 E-value: 2.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTnlqeSEW 84
Cdd:COG1131 1 IEVRGLT----KRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL----LRPTSGEVRVLGEDVA----RDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIRgKDIAFIFQDPlsSLNPTMKVgRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRfeqYPHQLSGGMRQRIC 164
Cdd:COG1131 69 AEVR-RRIGYVPQEP--ALYPDLTV-RENLRFFARLYGLPRKEARERIDELLELFGLTDAADR---KVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-258 |
4.96e-46 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 156.31 E-value: 4.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTnLQESE 83
Cdd:COG1126 1 MIEIENLH----KSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEE----PDSGTITVDGEDLT-DSKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WNQIRgKDIAFIFQdplsSLN--PTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIheAEKRfEQYPHQLSGGMRQ 161
Cdd:COG1126 72 INKLR-RKVGMVFQ----QFNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL--ADKA-DAYPAQLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 162 RICLAIAFACHPKLVIADEPTTALD------VTiqkQIMELLKerkeKQNTSILLITHDLALVREVADRVVVMYGGRVVE 235
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDpelvgeVL---DVMRDLA----KEGMTMVVVTHEMGFAREVADRVVFMDGGRIVE 216
|
250 260
....*....|....*....|...
gi 446453387 236 KGTIEEVIGSPKHPYTKSLLQAI 258
Cdd:COG1126 217 EGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-240 |
9.43e-46 |
|
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: 154.94 E-value: 9.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSvTAQSII-GLnqesIHIDDGNISFESEELTNlqese 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS-TLLRIIaGL----ERPTSGEVLVDGEPVTG----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 wnqiRGKDIAFIFQDPlsSLNPTMKVGRQItEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRfeqYPHQLSGGMRQRI 163
Cdd:cd03293 71 ----PGPDRGYVFQQD--ALLPWLTVLDNV-ALGLELQGVPKAEARERAEELLELVGLSGFENA---YPHQLSGGMRQRV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 164 CLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYG--GRVVEKGTIE 240
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVEVD 219
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
27-258 |
4.15e-45 |
|
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: 154.60 E-value: 4.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSVTAQSIIGlnqeSIHIDDGNISFESE-----ELTNLQESEWNQIRGKDIAFIFQDPLS 101
Cdd:TIGR02323 22 VSFDLYPGEVLGIVGESGSGKSTLLGCLAG----RLAPDHGTATYIMRsgaelELYQLSEAERRRLMRTEWGFVHQNPRD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 102 SLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAekRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEP 181
Cdd:TIGR02323 98 GLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDPT--RIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446453387 182 TTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTKSLLQAI 258
Cdd:TIGR02323 176 TGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-235 |
5.21e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 154.48 E-value: 5.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSvTAQSII-GLnqesIHIDDGNISFESEELTNLqes 82
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS-TLLRLIaGL----EKPTSGEVLVDGKPVTGP--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 83 ewnqirGKDIAFIFQDPlsSLNPTMKVGRQItEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRfeqYPHQLSGGMRQR 162
Cdd:COG1116 79 ------GPDRGVVFQEP--ALLPWLTVLDNV-ALGLELRGVPKAERRERARELLELVGLAGFEDA---YPHQLSGGMRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 163 ICLAIAFACHPKLVIADEPTTALDV----TIQKQIMELLKERKekqnTSILLITHDlalVRE---VADRVVVMYG--GRV 233
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDAltreRLQDELLRLWQETG----KTVLFVTHD---VDEavfLADRVVVLSArpGRI 219
|
..
gi 446453387 234 VE 235
Cdd:COG1116 220 VE 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-247 |
9.24e-45 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 152.74 E-value: 9.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQESE 83
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPT----SGSVLVDGTDLTLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WNQIRgKDIAFIFQ--DPLSSlnptmkvgRQITEVI---LQHEKKSKKEAKEIAINLLNDLGIheAEKRfEQYPHQLSGG 158
Cdd:cd03258 77 LRKAR-RRIGMIFQhfNLLSS--------RTVFENValpLEIAGVPKAEIEERVLELLELVGL--EDKA-DAYPAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 159 MRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGT 238
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
....*....
gi 446453387 239 IEEVIGSPK 247
Cdd:cd03258 225 VEEVFANPQ 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-242 |
1.38e-42 |
|
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: 147.33 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTlaVEKENSKQAIvKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNLQESEW 84
Cdd:cd03256 1 IEVENLS--KTYPNGKKAL-KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE----PTSGSVLIDGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIRgKDIAFIFQDP------------LSSLNPTMKVGRqiteVILQhekKSKKEAKEIAINLLNDLGIHE-AEKRFEqy 151
Cdd:cd03256 74 RQLR-RQIGMIFQQFnlierlsvlenvLSGRLGRRSTWR----SLFG---LFPKEEKQRALAALERVGLLDkAYQRAD-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 152 phQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGG 231
Cdd:cd03256 144 --QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
250
....*....|.
gi 446453387 232 RVVEKGTIEEV 242
Cdd:cd03256 222 RIVFDGPPAEL 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
27-257 |
3.86e-42 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 146.99 E-value: 3.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSVTAQSIiglnqeSIHI--DDGNISFESE-----ELTNLQESEWNQIRGKDIAFIFQDP 99
Cdd:PRK11701 25 VSFDLYPGEVLGIVGESGSGKTTLLNAL------SARLapDAGEVHYRMRdgqlrDLYALSEAERRRLLRTEWGFVHQHP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 LSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIheAEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIAD 179
Cdd:PRK11701 99 RDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEI--DAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 180 EPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTK----SLL 255
Cdd:PRK11701 177 EPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQllvsSVL 256
|
..
gi 446453387 256 QA 257
Cdd:PRK11701 257 QV 258
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
24-255 |
4.78e-42 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 146.86 E-value: 4.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESewnqIRGKDIAFIFQDPLSSL 103
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM----IEPTSGELLIDDHPLHFGDYS----YRSQRIRMIFQDPSTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMKVGrQITEVILQhekkskkeakeiainLLNDLGIHEAEKRFEQ--------------YPHQLSGGMRQRICLAIAF 169
Cdd:PRK15112 101 NPRQRIS-QILDFPLR---------------LNTDLEPEQREKQIIEtlrqvgllpdhasyYPHMLAPGQKQRLGLARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 170 ACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHP 249
Cdd:PRK15112 165 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHE 244
|
....*.
gi 446453387 250 YTKSLL 255
Cdd:PRK15112 245 LTKRLI 250
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
24-268 |
1.61e-41 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 147.64 E-value: 1.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIhiddGNISFESEELTNLQESEWNQIRgKDIAFIFQ--DPLS 101
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTS----GRVLVDGQDLTALSEKELRKAR-RQIGMIFQhfNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 102 SLN--------------PTMKVGRQITEvilqhekkskkeakeiainLLNDLGIheAEKRfEQYPHQLSGGMRQRICLAI 167
Cdd:PRK11153 96 SRTvfdnvalplelagtPKAEIKARVTE-------------------LLELVGL--SDKA-DRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 168 AFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPK 247
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
250 260
....*....|....*....|.
gi 446453387 248 HPYTKSLLQAIPNIDDSEKVL 268
Cdd:PRK11153 234 HPLTREFIQSTLHLDLPEDYL 254
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-259 |
3.31e-41 |
|
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: 144.71 E-value: 3.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 14 VEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEWNQIRGKDIA 93
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRL----IEPTSGKVLIDGQDIAAMSRKELRELRRKKIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 94 FIFQDplSSLNPTMKVGRQIT---EVilQHEKKSKKEAKeiAINLLNDLGIHEAEkrfEQYPHQLSGGMRQRICLAIAFA 170
Cdd:cd03294 106 MVFQS--FALLPHRTVLENVAfglEV--QGVPRAEREER--AAEALELVGLEGWE---HKYPDELSGGMQQRVGLARALA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 171 CHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPY 250
Cdd:cd03294 177 VDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
....*....
gi 446453387 251 TKSLLQAIP 259
Cdd:cd03294 257 VREFFRGVD 265
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-243 |
8.16e-41 |
|
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: 143.26 E-value: 8.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVekenSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESE 83
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGL----LKPSSGEVLLDGRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 wnqiRGKDIAFIFQDPLSSLNptMKVgrqiTEVILQ----HEKKSKKEA---KEIAINLLNDLGIHE-AEKRFeqypHQL 155
Cdd:COG1120 73 ----LARRIAYVPQEPPAPFG--LTV----RELVALgrypHLGLFGRPSaedREAVEEALERTGLEHlADRPV----DEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 156 SGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVE 235
Cdd:COG1120 139 SGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
....*...
gi 446453387 236 KGTIEEVI 243
Cdd:COG1120 219 QGPPEEVL 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-247 |
2.19e-40 |
|
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: 141.70 E-value: 2.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEwnqirgKDIAFIFQDplSSL 103
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGF----IKPDSGKILLNGKDITNLPPEK------RDISYVPQN--YAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMKVGRQItEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRfeqYPHQLSGGMRQRICLAIAFACHPKLVIADEPTT 183
Cdd:cd03299 83 FPHMTVYKNI-AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNR---KPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446453387 184 ALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPK 247
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
4-250 |
2.85e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 144.47 E-value: 2.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNLQESE 83
Cdd:COG3842 5 ALELENVS----KRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFET----PDSGRILLDGRDVTGLPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 wnqiRgkDIAFIFQDPlsSLNPTMKVGrqitEVI---LQHEKKSKKEAKEIAINLLNDLGIHEAEKRfeqYPHQLSGGMR 160
Cdd:COG3842 77 ----R--NVGMVFQDY--ALFPHLTVA----ENVafgLRMRGVPKAEIRARVAELLELVGLEGLADR---YPHQLSGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 161 QRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDL--ALVreVADRVVVMYGGRVVEKGT 238
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQeeALA--LADRIAVMNDGRIEQVGT 219
|
250
....*....|..
gi 446453387 239 IEEVIGSPKHPY 250
Cdd:COG3842 220 PEEIYERPATRF 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
24-255 |
4.45e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 143.75 E-value: 4.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEEL-TNL--QEsewnqiRGkdIAFIFQDPL 100
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGL----ETPDSGRIVLNGRDLfTNLppRE------RR--VGFVFQHYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 101 ssLNPTMKVG--------------RQITEVILQhekkskkeakeiainLLNDLGIHEAEKRfeqYPHQLSGGMRQRICLA 166
Cdd:COG1118 86 --LFPHMTVAeniafglrvrppskAEIRARVEE---------------LLELVQLEGLADR---YPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 167 IAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSP 246
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
....*....
gi 446453387 247 KHPYTKSLL 255
Cdd:COG1118 226 ATPFVARFL 234
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-235 |
4.83e-40 |
|
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: 140.65 E-value: 4.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSvTAQSII-GLNQesihIDDGNISFESEELTNLQES 82
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS-TLLGLLaGLDR----PTSGTVRLAGQDLFALDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 83 EWNQIRGKDIAFIFQDplSSLNPTMkvgrqiT--E-VILQHEKKSKKEAKEIAINLLNDLGIheaEKRFEQYPHQLSGGM 159
Cdd:COG4181 83 ARARLRARHVGFVFQS--FQLLPTL------TalEnVMLPLELAGRRDARARARALLERVGL---GHRLDHYPAQLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446453387 160 RQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREvADRVVVMYGGRVVE 235
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-233 |
8.34e-40 |
|
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: 137.91 E-value: 8.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTnlqeSEW 84
Cdd:cd03230 1 IEVRNLS----KRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGL----LKPDSGEIKVLGKDIK----KEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIRGKdIAFIFQDPlsSLNPTMKVGRQItevilqhekkskkeakeiainllndlgiheaekrfeqyphQLSGGMRQRIC 164
Cdd:cd03230 69 EEVKRR-IGYLPEEP--SLYENLTVRENL----------------------------------------KLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKeKQNTSILLITHDLALVREVADRVVVMYGGRV 233
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
24-255 |
3.27e-39 |
|
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: 138.63 E-value: 3.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEELTNLQesewnqIRGKDIAFIFQDplSSL 103
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERP----DSGTILFGGEDATDVP------VQERNVGFVFQH--YAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPTT 183
Cdd:cd03296 86 FRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453387 184 ALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTKSLL 255
Cdd:cd03296 166 ALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-237 |
6.21e-39 |
|
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: 137.27 E-value: 6.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKenskQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEw 84
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL----ERPDSGEILIDGRDVTGVPPER- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqirgKDIAFIFQDPlsSLNPTMKVGRQITEViLQHEKKSKKEAKEIAINLLNDLGIHEAEKRfeqYPHQLSGGMRQRIC 164
Cdd:cd03259 72 -----RNIGMVFQDY--ALFPHLTVAENIAFG-LKLRGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKG 237
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-235 |
6.88e-39 |
|
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: 137.10 E-value: 6.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTlAVEKENSKQAIV-KHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQES 82
Cdd:TIGR02211 1 LLKCENLG-KRYQEGKLDTRVlKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPT----SGEVLFNGQSLSKLSSN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 83 EWNQIRGKDIAFIFQ--------DPLSSLNPTMKVGRQ-ITEvilqhekkskkeAKEIAINLLNDLGIheaEKRFEQYPH 153
Cdd:TIGR02211 76 ERAKLRNKKLGFIYQfhhllpdfTALENVAMPLLIGKKsVKE------------AKERAYEMLEKVGL---EHRINHRPS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 154 QLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREvADRVVVMYGGRV 233
Cdd:TIGR02211 141 ELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKK-LDRVLEMKDGQL 219
|
..
gi 446453387 234 VE 235
Cdd:TIGR02211 220 FN 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-233 |
2.53e-38 |
|
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: 135.35 E-value: 2.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 14 VEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNlQESEWNQIRgKDIA 93
Cdd:cd03262 6 LHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEE----PDSGTIIIDGLKLTD-DKKNINELR-QKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 94 FIFQDplSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEaekRFEQYPHQLSGGMRQRICLAIAFACHP 173
Cdd:cd03262 80 MVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLAD---KADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 174 KLVIADEPTTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREVADRVVVMYGGRV 233
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMT-MVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-232 |
2.81e-38 |
|
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: 134.24 E-value: 2.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 13 AVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTnlQESEWNQIRGKDI 92
Cdd:cd03229 5 NVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE----PDSGSILIDGEDLT--DLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 93 AFIFQDPlsSLNPTMKVGRQITEVilqhekkskkeakeiainllndlgiheaekrfeqyphqLSGGMRQRICLAIAFACH 172
Cdd:cd03229 79 GMVFQDF--ALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 173 PKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGR 232
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-257 |
3.97e-38 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 135.89 E-value: 3.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTlavEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEw 84
Cdd:cd03295 1 IEFENVT---KRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRL----IEPTSGEIFIDGEDIREQDPVE- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqIRGKdIAFIFQDplSSLNPTMKVGRQITEViLQHEKKSKKEAKEIAINLLNDLGIHEAEKRfEQYPHQLSGGMRQRIC 164
Cdd:cd03295 73 --LRRK-IGYVIQQ--IGLFPHMTVEENIALV-PKLLKWPKEKIRERADELLALVGLDPAEFA-DRYPHELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIG 244
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
250
....*....|...
gi 446453387 245 SPKHPYTKSLLQA 257
Cdd:cd03295 226 SPANDFVAEFVGA 238
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-243 |
5.54e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.60 E-value: 5.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 1 MGQLLSLENVTLAVEKenskQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNlq 80
Cdd:COG1121 3 MMPAIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGL----LPPTSGTVRLFGKPPRR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 81 esewnqiRGKDIAFIFQdpLSSLNPTMkvgrQIT--EVILQHEKKSK-------KEAKEIAINLLNDLGIHE-AEKRFeq 150
Cdd:COG1121 73 -------ARRRIGYVPQ--RAEVDWDF----PITvrDVVLMGRYGRRglfrrpsRADREAVDEALERVGLEDlADRPI-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 151 ypHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKeKQNTSILLITHDLALVREVADRVVVMyG 230
Cdd:COG1121 138 --GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLL-N 213
|
250
....*....|...
gi 446453387 231 GRVVEKGTIEEVI 243
Cdd:COG1121 214 RGLVAHGPPEEVL 226
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
24-258 |
2.69e-37 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 133.77 E-value: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEELTNLQesewnqIRGKDIAFIFQDplSSL 103
Cdd:TIGR00968 16 LDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQP----DSGRIRLNGQDATRVH------ARDRKIGFVFQH--YAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMKVGRQIT--EVILQHEKKSKKEAKEiaiNLLNDLGIheaEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEP 181
Cdd:TIGR00968 84 FKHLTVRDNIAfgLEIRKHPKAKIKARVE---ELLELVQL---EGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446453387 182 TTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTKSLLQAI 258
Cdd:TIGR00968 158 FGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEV 234
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-243 |
7.26e-36 |
|
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: 137.27 E-value: 7.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENskQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNLQESEW 84
Cdd:COG2274 474 IELENVSFRYPGDS--PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE----PTSGRILIDGIDLRQIDPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIrgkdIAFIFQDP------------LSSLNPTMKvgrQITEVilqhekkskkeakeiainlLNDLGIHE-AEKRFEQY 151
Cdd:COG2274 548 RRQ----IGVVLQDVflfsgtirenitLGDPDATDE---EIIEA-------------------ARLAGLHDfIEALPMGY 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 152 PHQ-------LSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERkeKQNTSILLITHDLALVREvADR 224
Cdd:COG2274 602 DTVvgeggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRL-ADR 678
|
250
....*....|....*....
gi 446453387 225 VVVMYGGRVVEKGTIEEVI 243
Cdd:COG2274 679 IIVLDKGRIVEDGTHEELL 697
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-237 |
8.27e-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: 127.94 E-value: 8.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 6 SLENVTLAVekenSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNLQESEWN 85
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK----PSSGEILLDGKDLASLSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 86 QIrgkdIAFIFQdplsslnptmkvgrqitevilqhekkskkeakeiainLLNDLGI-HEAEKRFeqypHQLSGGMRQRIC 164
Cdd:cd03214 73 RK----IAYVPQ-------------------------------------ALELLGLaHLADRPF----NELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKG 237
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-232 |
1.00e-35 |
|
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: 127.50 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEkeNSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNLQESEW 84
Cdd:cd03228 1 IEFKNVSFSYP--GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD----PTSGEILIDGVDLRDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIrgkdIAFIFQDPlsslnptmkvgrqitevILQHEKkskkeakeIAINLLndlgiheaekrfeqyphqlSGGMRQRIC 164
Cdd:cd03228 75 RKN----IAYVPQDP-----------------FLFSGT--------IRENIL-------------------SGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLkeRKEKQNTSILLITHDLALVREvADRVVVMYGGR 232
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEAL--RALAKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-183 |
1.67e-35 |
|
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: 126.22 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQEsewnQIRGKDIAFIFQDPlsSL 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGL----LSPTEGTILLDGQDLTDDER----KSLRKEIGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMKVGRQITEViLQHEKKSKKEAKEIAINLLNDLGIHEAEKRF-EQYPHQLSGGMRQRICLAIAFACHPKLVIADEPT 182
Cdd:pfam00005 71 FPRLTVRENLRLG-LLLKGLSKREKDARAEEALEKLGLGDLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 446453387 183 T 183
Cdd:pfam00005 150 A 150
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
17-234 |
1.70e-35 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 128.21 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 17 ENSKQaIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNLQESEWNQIRgKDIAFIF 96
Cdd:TIGR02982 15 SLRKQ-VLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRS----VQEGSLKVLGQELHGASKKQLVQLR-RRIGYIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 97 Q--DPLSSLNPTMKVgrQITEVILQHEKKSKKEAKEIAInlLNDLGIheaEKRFEQYPHQLSGGMRQRICLAIAFACHPK 174
Cdd:TIGR02982 89 QahNLLGFLTARQNV--QMALELQPNLSYQEARERARAM--LEAVGL---GDHLNYYPHNLSGGQKQRVAIARALVHHPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 175 LVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVrEVADRVVVMYGGRVV 234
Cdd:TIGR02982 162 LVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRIL-DVADRILQMEDGKLL 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-241 |
2.56e-35 |
|
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: 134.89 E-value: 2.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKEnskQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNLQESEW 84
Cdd:COG4988 337 IELEDVSFSYPGG---RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP----PYSGSILINGVDLSDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQirgkDIAFIFQDP------------LSSLNPTMKvgrQITEVilqhekkskkeakeiainlLNDLGIHEaekrF-EQY 151
Cdd:COG4988 410 RR----QIAWVPQNPylfagtirenlrLGRPDASDE---ELEAA-------------------LEAAGLDE----FvAAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 152 PH-----------QLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERkeKQNTSILLITHDLALVRE 220
Cdd:COG4988 460 PDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHRLALLAQ 537
|
250 260
....*....|....*....|.
gi 446453387 221 vADRVVVMYGGRVVEKGTIEE 241
Cdd:COG4988 538 -ADRILVLDDGRIVEQGTHEE 557
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-242 |
2.74e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 129.36 E-value: 2.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 1 MGQLLSLENVTLAVeKENSKQAiVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTnlQ 80
Cdd:PRK13635 2 KEEIIRVEHISFRY-PDAATYA-LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL----LLPEAGTITVGGMVLS--E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 81 ESEWnQIRgKDIAFIFQDPLSSLnptmkVGRQITEvilqhekkskkeakEIAINLLNDlGI---------HEAEKR---- 147
Cdd:PRK13635 74 ETVW-DVR-RQVGMVFQNPDNQF-----VGATVQD--------------DVAFGLENI-GVpreemvervDQALRQvgme 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 148 --FEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREvADRV 225
Cdd:PRK13635 132 dfLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRV 210
|
250
....*....|....*..
gi 446453387 226 VVMYGGRVVEKGTIEEV 242
Cdd:PRK13635 211 IVMNKGEILEEGTPEEI 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-233 |
3.42e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 127.24 E-value: 3.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVekenSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEW 84
Cdd:COG4619 1 LELEGLSFRV----GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADL----DPPTSGEIYLDGKPLSAMPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqiRgKDIAFIFQDPLssLnPTMKVGRQITEVilqHEKKSKKEAKEIAINLLNDLGIHEA--EKRFEQyphqLSGGMRQR 162
Cdd:COG4619 73 ---R-RQVAYVPQEPA--L-WGGTVRDNLPFP---FQLRERKFDRERALELLERLGLPPDilDKPVER----LSGGERQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446453387 163 ICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRV 233
Cdd:COG4619 139 LALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-242 |
6.76e-35 |
|
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: 127.28 E-value: 6.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTnlqeSE 83
Cdd:COG4555 1 MIEVENLS----KKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGL----LKPDSGSILIDGEDVR----KE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WNQIRgKDIAFIFQDPlsSLNPTMKVGRQITEVILQHEKKSKKEAKEIAiNLLNDLGIHEAEKRfeqYPHQLSGGMRQRI 163
Cdd:COG4555 69 PREAR-RQIGVLPDER--GLYDRLTVRENIRYFAELYGLFDEELKKRIE-ELIELLGLEEFLDR---RVGELSTGMKKKV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 164 CLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKeKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:COG4555 142 ALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-235 |
1.18e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 126.32 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKensKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEW 84
Cdd:COG2884 2 IRFENVSKRYPG---GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE----ERPTSGQVLVNGQDLSRLKRREI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIRgKDIAFIFQDP--LSSLN-------PtMKVGRQITEVILQHekkskkeakeiAINLLNDLGIHEAEKRfeqYPHQL 155
Cdd:COG2884 75 PYLR-RRIGVVFQDFrlLPDRTvyenvalP-LRVTGKSRKEIRRR-----------VREVLDLVGLSDKAKA---LPHEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 156 SGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKeKQNTSILLITHDLALVREVADRVVVMYGGRVVE 235
Cdd:COG2884 139 SGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-232 |
4.04e-34 |
|
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: 122.74 E-value: 4.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 6 SLENVTLAVEKenskQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEWn 85
Cdd:cd00267 1 EIENLSFRYGG----RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGL----LKPTSGEILIDGKDIAKLPLEEL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 86 qirGKDIAFIFQdplsslnptmkvgrqitevilqhekkskkeakeiainllndlgiheaekrfeqyphqLSGGMRQRICL 165
Cdd:cd00267 72 ---RRRIGYVPQ---------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446453387 166 AIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREVADRVVVMYGGR 232
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRT-VIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
16-256 |
8.43e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 124.86 E-value: 8.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 16 KENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQ-ESIHIDDGNISFESEELTNLQESEWNQIRgKDIAF 94
Cdd:PRK11264 11 KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpEAGTIRVGDITIDTARSLSQQKGLIRQLR-QHVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 95 IFQDplSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEkrfEQYPHQLSGGMRQRICLAIAFACHPK 174
Cdd:PRK11264 90 VFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKE---TSYPRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 175 LVIADEPTTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTKSL 254
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQF 243
|
..
gi 446453387 255 LQ 256
Cdd:PRK11264 244 LE 245
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-247 |
2.15e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 123.64 E-value: 2.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 1 MGQLlSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQ 80
Cdd:COG3839 1 MASL-ELENVS----KSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGL----EDPTSGEILIGGRDVTDLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 81 ESEwnqiRgkDIAFIFQDPlsSLNPTMKVG------------------RQITEVilqhekkskkeakeiainlLNDLGIH 142
Cdd:COG3839 72 PKD----R--NIAMVFQSY--ALYPHMTVYeniafplklrkvpkaeidRRVREA-------------------AELLGLE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 143 EAEKRfeqYPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALD----VTIQKQIMELLKERKekqnTSILLITHD---- 214
Cdd:COG3839 125 DLLDR---KPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLG----TTTIYVTHDqvea 197
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446453387 215 LALvrevADRVVVMYGGRVVEKGTIEEV------------IGSPK 247
Cdd:COG3839 198 MTL----ADRIAVMNDGRIQQVGTPEELydrpanlfvagfIGSPP 238
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-242 |
3.10e-32 |
|
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: 119.98 E-value: 3.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVekeNSKQAIvKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHI-DDGNISFESEELTNLQESE 83
Cdd:cd03260 1 IELRDLNVYY---GDKHAL-KDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 wNQIRgKDIAFIFQDPlsslNP-TMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRfEQYPHQLSGGMRQR 162
Cdd:cd03260 77 -LELR-RRVGMVFQKP----NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKD-RLHALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 163 ICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERkeKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-237 |
8.05e-32 |
|
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: 118.51 E-value: 8.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNLQESEw 84
Cdd:cd03301 1 VELENVT----KRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEE----PTSGRIYIGGRDVTDLPPKD- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqirgKDIAFIFQDplSSLNPTMKVgrqitevilqhekkskkeAKEIAINL-LNDLGIHEAEKRFEQ------------- 150
Cdd:cd03301 72 -----RDIAMVFQN--YALYPHMTV------------------YDNIAFGLkLRKVPKDEIDERVREvaellqiehlldr 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 151 YPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYG 230
Cdd:cd03301 127 KPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND 206
|
....*..
gi 446453387 231 GRVVEKG 237
Cdd:cd03301 207 GQIQQIG 213
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-256 |
2.30e-31 |
|
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: 123.72 E-value: 2.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEkeNSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEW 84
Cdd:COG4987 334 LELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF----LDPQSGSITLGGVDLRDLDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIrgkdIAFIFQDP---LSSLNPTMKVGR------QITEVilqhekkskkeakeiainlLNDLGIHEAekrFEQYPH-- 153
Cdd:COG4987 408 RRR----IAVVPQRPhlfDTTLRENLRLARpdatdeELWAA-------------------LERVGLGDW---LAALPDgl 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 154 ---------QLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKER-KEKqntSILLITHDLALVrEVAD 223
Cdd:COG4987 462 dtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlAGR---TVLLITHRLAGL-ERMD 537
|
250 260 270
....*....|....*....|....*....|...
gi 446453387 224 RVVVMYGGRVVEKGTIEEVIGspKHPYTKSLLQ 256
Cdd:COG4987 538 RILVLEDGRIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
24-247 |
3.54e-31 |
|
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: 117.54 E-value: 3.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQEsewNQIRGKDIAFIFQDPlsSL 103
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF----LRPTSGSVLFDGEDITGLPP---HEIARLGIGRTFQIP--RL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMKV---------GRQITEVILQHEKKSKKEAKEIAINLLNDLGIheAEKRFEQyPHQLSGGMRQRICLAIAFACHPK 174
Cdd:cd03219 87 FPELTVlenvmvaaqARTGSGLLLARARREEREARERAEELLERVGL--ADLADRP-AGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446453387 175 LVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPK 247
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-247 |
5.78e-31 |
|
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: 117.45 E-value: 5.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTlavekensKQ----AIVKHVSFSINEGEIVALVGESGSGKSvTAQSII-GLnqesIHIDDGNISFESEELTN 78
Cdd:COG0411 4 LLEVRGLT--------KRfgglVAVDDVSLEVERGEIVGLIGPNGAGKT-TLFNLItGF----YRPTSGRILFDGRDITG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 79 LQEsewNQIRGKDIAFIFQdpLSSLNPTMKV------------GRQITEVILQHEKKSKKEAKEI--AINLLNDLGIHEa 144
Cdd:COG0411 71 LPP---HRIARLGIARTFQ--NPRLFPELTVlenvlvaaharlGRGLLAALLRLPRARREEREARerAEELLERVGLAD- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 145 ekRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADR 224
Cdd:COG0411 145 --RADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADR 222
|
250 260
....*....|....*....|...
gi 446453387 225 VVVMYGGRVVEKGTIEEVIGSPK 247
Cdd:COG0411 223 IVVLDFGRVIAEGTPAEVRADPR 245
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-248 |
1.15e-30 |
|
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: 115.68 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLaVEKENSKQAiVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQES---IHIDDGNISfeseeltnlqe 81
Cdd:cd03263 1 LQIRNLTK-TYKKGTKPA-VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTsgtAYINGYSIR----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 82 SEWNQIRgKDIAFIFQDplSSLNPTMKVgRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRFeqyPHQLSGGMRQ 161
Cdd:cd03263 68 TDRKAAR-QSLGYCPQF--DALFDELTV-REHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKR---ARTLSGGMKR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 162 RICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKerKEKQNTSILLITHDLALVREVADRVVVMYGGRVVekgtiee 241
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLIL--EVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR------- 211
|
....*..
gi 446453387 242 VIGSPKH 248
Cdd:cd03263 212 CIGSPQE 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-234 |
1.62e-30 |
|
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: 114.66 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 6 SLENVTlavEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQesewn 85
Cdd:cd03226 1 RIENIS---FSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES----SGSILLNGKPIKAKE----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 86 qiRGKDIAFIFQDPlsslnptmkvGRQIT------EVILqhEKKSKKEAKEIAINLLNDLGIHEAEkrfEQYPHQLSGGM 159
Cdd:cd03226 69 --RRKSIGYVMQDV----------DYQLFtdsvreELLL--GLKELDAGNEQAETVLKDLDLYALK---ERHPLSLSGGQ 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446453387 160 RQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKeKQNTSILLITHDLALVREVADRVVVMYGGRVV 234
Cdd:cd03226 132 KQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELA-AQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-247 |
3.84e-30 |
|
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: 114.64 E-value: 3.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNLQESEw 84
Cdd:cd03300 1 IELENVS----KFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFET----PTSGEILLDGKDITNLPPHK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqirgKDIAFIFQDplSSLNPTMKVGRQITeVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRfeqYPHQLSGGMRQRIC 164
Cdd:cd03300 72 -----RPVNTVFQN--YALFPHLTVFENIA-FGLRLKKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIG 244
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
...
gi 446453387 245 SPK 247
Cdd:cd03300 221 EPA 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-234 |
4.49e-30 |
|
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: 113.78 E-value: 4.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 6 SLENVTLAVEKENskqaIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLN---QESIHIDDGNISFESEELTNL-Q- 80
Cdd:cd03235 1 EVEDLTVSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkptSGSIRVFGKPLEKERKRIGYVpQr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 81 -ESEWN-QIRGKDIAfifqdpLSSLNPTMKVGRQITEvilqhekkskkEAKEIAINLLNDLGIHE-AEKRFEqyphQLSG 157
Cdd:cd03235 77 rSIDRDfPISVRDVV------LMGLYGHKGLFRRLSK-----------ADKAKVDEALERVGLSElADRQIG----ELSG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446453387 158 GMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREVADRVVVMyGGRVV 234
Cdd:cd03235 136 GQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMT-ILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-235 |
8.18e-30 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 114.57 E-value: 8.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNlqesew 84
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGF----LAPSSGEITLDGVPVTG------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqiRGKDIAFIFQDplSSLNPTMKVgRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRFeqyPHQLSGGMRQRIC 164
Cdd:COG4525 74 ---PGADRGVVFQK--DALLPWLNV-LDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRR---IWQLSGGMRQRVG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDL--ALVreVADRVVVMYG--GRVVE 235
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVeeALF--LATRLVVMSPgpGRIVE 217
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
14-258 |
1.81e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 116.67 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 14 VEKENSKQAI---------VKHVSFSINEGEIVALVGESGSGKSvtaqSIIGLNQESIHIDDGNISFESEELTNLQESEW 84
Cdd:PRK10070 25 IEQGLSKEQIlektglslgVKDASLAIEEGEIFVIMGLSGSGKS----TMVRLLNRLIEPTRGQVLIDGVDIAKISDAEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIRGKDIAFIFQDplSSLNPTMKVGRQiTEVILQHEKKSKKEAKEIAINLLNDLGIheaEKRFEQYPHQLSGGMRQRIC 164
Cdd:PRK10070 101 REVRRKKIAMVFQS--FALMPHMTVLDN-TAFGMELAGINAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIG 244
Cdd:PRK10070 175 LARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
250
....*....|....
gi 446453387 245 SPKHPYTKSLLQAI 258
Cdd:PRK10070 255 NPANDYVRTFFRGV 268
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-250 |
2.26e-29 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 115.52 E-value: 2.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 1 MGQLLSLENVtlavEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEELTNLQ 80
Cdd:TIGR03265 1 SSPYLSIDNI----RKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQ----TAGTIYQGGRDITRLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 81 ESEwnqirgKDIAFIFQDplSSLNPTMKVGRQItEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRfeqYPHQLSGGMR 160
Cdd:TIGR03265 73 PQK------RDYGIVFQS--YALFPNLTVADNI-AYGLKNRGMGRAEVAERVAELLDLVGLPGSERK---YPGQLSGGQQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 161 QRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDL--ALVreVADRVVVMYGGRVVEKGT 238
Cdd:TIGR03265 141 QRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQeeALS--MADRIVVMNHGVIEQVGT 218
|
250
....*....|..
gi 446453387 239 IEEVIGSPKHPY 250
Cdd:TIGR03265 219 PQEIYRHPATPF 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-239 |
2.88e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 112.22 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQESEWNQIRGKDIAFIFQdpLSS 102
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPT----SGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ--FHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 103 LNPTMKVGRQITEVILQHEKKSKKEAKEiAINLLNDLGIheaEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPT 182
Cdd:PRK11629 98 LLPDFTALENVAMPLLIGKKKPAEINSR-ALEMLAAVGL---EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446453387 183 TALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVaDRVVVMYGGRVVEKGTI 239
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELSL 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-243 |
2.88e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 117.96 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKEnskQAIVKHVSFSINEGEIVALVGESGSGKSvtaqSIIGL-------NQESIHIDDgnisfeseelT 77
Cdd:COG1132 340 IEFENVSFSYPGD---RPVLKDISLTIPPGETVALVGPSGSGKS----TLVNLllrfydpTSGRILIDG----------V 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 78 NLQESEWNQIRGKdIAFIFQDP------------LSSLNPTMKvgrQITEVilqhekkskkeakeiainlLNDLGIHEAE 145
Cdd:COG1132 403 DIRDLTLESLRRQ-IGVVPQDTflfsgtirenirYGRPDATDE---EVEEA-------------------AKAAQAHEFI 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 146 KRFEQ-YPHQ-------LSGGMRQRICLAIAFACHPKLVIADEPTTALDV----TIQKQIMELLKERkekqnTSIlLITH 213
Cdd:COG1132 460 EALPDgYDTVvgergvnLSGGQRQRIAIARALLKDPPILILDEATSALDTeteaLIQEALERLMKGR-----TTI-VIAH 533
|
250 260 270
....*....|....*....|....*....|
gi 446453387 214 DLALVREvADRVVVMYGGRVVEKGTIEEVI 243
Cdd:COG1132 534 RLSTIRN-ADRILVLDDGRIVEQGTHEELL 562
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-237 |
4.68e-29 |
|
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: 111.23 E-value: 4.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 25 KHVSFSIN-----EGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESeelTNLQESEWNQI---RGKDIAFIF 96
Cdd:cd03297 9 RLPDFTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGL----EKPDGGTIVLNG---TVLFDSRKKINlppQQRKIGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 97 QDplSSLNPTMKVGRQITEVILQHEKKSKKEAKEiaiNLLNDLGIHEAEKRfeqYPHQLSGGMRQRICLAIAFACHPKLV 176
Cdd:cd03297 82 QQ--YALFPHLNVRENLAFGLKRKRNREDRISVD---ELLDLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446453387 177 IADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKG 237
Cdd:cd03297 154 LLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-233 |
7.32e-29 |
|
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: 109.44 E-value: 7.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAvekenskqAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNLQESE 83
Cdd:cd03215 4 VLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP----PASGEITLDGKPVTRRSPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WnqiRGKDIAFIFQDplsslnptmkvgRQITEVILQHEkkskkeakeIAINLLNdlgiheaekrfeqyPHQLSGGMRQRI 163
Cdd:cd03215 72 A---IRAGIAYVPED------------RKREGLVLDLS---------VAENIAL--------------SSLLSGGNQQKV 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 164 CLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITHDLALVREVADRVVVMYGGRV 233
Cdd:cd03215 114 VLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
14-256 |
9.60e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.95 E-value: 9.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 14 VEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNLQESEwNQIRgKDIA 93
Cdd:PRK09493 7 VSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEE----ITSGDLIVDGLKVNDPKVDE-RLIR-QEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 94 FIFQDplSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEaekRFEQYPHQLSGGMRQRICLAIAFACHP 173
Cdd:PRK09493 81 MVFQQ--FYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAE---RAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 174 KLVIADEPTTALDVTIQKQIMELLKERKEKQNTSIlLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTKS 253
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMV-IVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
...
gi 446453387 254 LLQ 256
Cdd:PRK09493 235 FLQ 237
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
14-256 |
2.21e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 110.44 E-value: 2.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 14 VEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQES---IHIDDGNISFESEELTNLQESEWNQIR-- 88
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSegsIVVNGQTINLVRDKDGQLKVADKNQLRll 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 89 GKDIAFIFQDplSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKrfEQYPHQLSGGMRQRICLAIA 168
Cdd:PRK10619 91 RTRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ--GKYPVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 169 FACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKH 248
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
....*...
gi 446453387 249 PYTKSLLQ 256
Cdd:PRK10619 246 PRLQQFLK 253
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-256 |
3.47e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.57 E-value: 3.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 1 MGQLLSLENVTLAVEKENSKQAIvKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTnlQ 80
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQL-NGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEF----EGKVKIDGELLT--A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 81 ESEWNQIRgkDIAFIFQDPL-----SSLNPTMKVGRQiTEVILQHEKKSKKEAKEIAINLLnDLGIHEaekrfeqyPHQL 155
Cdd:PRK13642 74 ENVWNLRR--KIGMVFQNPDnqfvgATVEDDVAFGME-NQGIPREEMIKRVDEALLAVNML-DFKTRE--------PARL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 156 SGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREvADRVVVMYGGRVVE 235
Cdd:PRK13642 142 SGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIK 220
|
250 260
....*....|....*....|....*....
gi 446453387 236 KGTIEEVIGSPKH--------PYTKSLLQ 256
Cdd:PRK13642 221 EAAPSELFATSEDmveigldvPFSSNLMK 249
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-276 |
4.04e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 110.58 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTnlqESEW 84
Cdd:COG4152 2 LELKGLT----KRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGI----LAPDSGEVLWDGEPLD---PEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQI------RGkdiafifqdplssLNPTMKVGRQIT-----------EVILQhekkskkeakeiAINLLNDLGIHE-AEK 146
Cdd:COG4152 71 RRIgylpeeRG-------------LYPKMKVGEQLVylarlkglskaEAKRR------------ADEWLERLGLGDrANK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 147 RFEQyphqLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKqNTSILLITHDLALVREVADRVV 226
Cdd:COG4152 126 KVEE----LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIV 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453387 227 VMYGGRVVEKGTIEEV---IGSPKH----PYTKSLLQAIPNIDDSEK-----VLRAIEGTTP 276
Cdd:COG4152 201 IINKGRKVLSGSVDEIrrqFGRNTLrleaDGDAGWLRALPGVTVVEEdgdgaELKLEDGADA 262
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-246 |
7.57e-28 |
|
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: 111.35 E-value: 7.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELtnlQESEwnqiRGKD-------IAFIFQDP 99
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGL----ERPDSGRIRLGGEVL---QDSA----RGIFlpphrrrIGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 lsSLNPTMKV------GRQITEVILQHEKKSKkeakeiAINLLndlGIheaEKRFEQYPHQLSGGMRQRICLAIAFACHP 173
Cdd:COG4148 87 --RLFPHLSVrgnllyGRKRAPRAERRISFDE------VVELL---GI---GHLLDRRPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446453387 174 KLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSP 246
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
23-246 |
7.97e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 111.33 E-value: 7.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQEsewnqiRGKDIAFIFQDplSS 102
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT----SGHIRFHGTDVSRLHA------RDRKVGFVFQH--YA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 103 LNPTMKVGRQIT---EVILQHEKKSKKEAKEIAINLLNDLGI-HEAEKrfeqYPHQLSGGMRQRICLAIAFACHPKLVIA 178
Cdd:PRK10851 85 LFRHMTVFDNIAfglTVLPRRERPNAAAIKAKVTQLLEMVQLaHLADR----YPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446453387 179 DEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSP 246
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-242 |
8.29e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.75 E-value: 8.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGL---NQESIHIDDGNISFESEELTNLQesewnqirgKDIAFIFQDPl 100
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLlkpTSGKIIIDGVDITDKKVKLSDIR---------KKVGLVFQYP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 101 sslnptmkvgrqitevilQHEKKSKKEAKEIA---INL-LNDLGIHEAEKR--------FEQY----PHQLSGGMRQRIC 164
Cdd:PRK13637 93 ------------------EYQLFEETIEKDIAfgpINLgLSEEEIENRVKRamnivgldYEDYkdksPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
24-261 |
1.27e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.10 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTN-LQESEWNQIRgKDIAFIFQDPLSS 102
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPT----TGTVTVDDITITHkTKDKYIRPVR-KRIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 103 LNPTmKVGRQItEVILQHEKKSKKEAKEIAINLLNDLGIheAEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPT 182
Cdd:PRK13646 98 LFED-TVEREI-IFGPKNFKMNLDEVKNYAHRLLMDLGF--SRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 183 TALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKhpYTKSLLQAIPNI 261
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK--KLADWHIGLPEI 250
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-257 |
1.39e-27 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 109.41 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 7 LENVTlaveKE-NSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQEsewN 85
Cdd:COG1125 4 FENVT----KRyPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRL----IEPTSGRILIDGEDIRDLDP---V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 86 QIRgKDIAFIFQDplSSLNPTMKVGRQITeVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRfEQYPHQLSGGMRQRICL 165
Cdd:COG1125 73 ELR-RRIGYVIQQ--IGLFPHMTVAENIA-TVPRLLGWDKERIRARVDELLELVGLDPEEYR-DRYPHELSGGQQQRVGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 166 AIAFACHPKLVIADEPTTALD-VT---IQKQIMELLKERKekqnTSILLITHDL--ALvrEVADRVVVMYGGRVVEKGTI 239
Cdd:COG1125 148 ARALAADPPILLMDEPFGALDpITreqLQDELLRLQRELG----KTIVFVTHDIdeAL--KLGDRIAVMREGRIVQYDTP 221
|
250
....*....|....*...
gi 446453387 240 EEVIGSPKHPYTKSLLQA 257
Cdd:COG1125 222 EEILANPANDFVADFVGA 239
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-217 |
2.18e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 107.17 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQESE 83
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS----SGEVSLVGQPLHQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WNQIRGKDIAFIFQDPLssLNPTMKVGRQITEVILQHEKKSKKEAKEiAINLLNDLGIheaEKRFEQYPHQLSGGMRQRI 163
Cdd:PRK10584 82 RAKLRAKHVGFVFQSFM--LIPTLNALENVELPALLRGESSRQSRNG-AKALLEQLGL---GKRLDHLPAQLSGGEQQRV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446453387 164 CLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLAL 217
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQL 209
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-228 |
4.85e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 105.64 E-value: 4.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKenskQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHIDdGNISFESEELTNLQesew 84
Cdd:COG4136 2 LSLENLTITLGG----RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSAS-GEVLLNGRRLTALP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqIRGKDIAFIFQDPLssLNPTMKVGRqitevilqhekkskkeakeiaiNLLNDL--GIHEAEKR--------------- 147
Cdd:COG4136 73 --AEQRRIGILFQDDL--LFPHLSVGE----------------------NLAFALppTIGRAQRRarveqaleeaglagf 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 148 FEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVrEVADRVVV 227
Cdd:COG4136 127 ADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA-PAAGRVLD 205
|
.
gi 446453387 228 M 228
Cdd:COG4136 206 L 206
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-234 |
6.44e-27 |
|
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: 104.05 E-value: 6.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISfeseeltnlqesew 84
Cdd:cd03216 1 LELRGIT----KRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGL----YKPDSGEIL-------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqIRGKDIAFifqdplssLNPTMKvgrqitevilqhekkskkeakeiainllNDLGIheaekrfeQYPHQLSGGMRQRIC 164
Cdd:cd03216 59 --VDGKEVSF--------ASPRDA----------------------------RRAGI--------AMVYQLSVGERQMVE 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKeKQNTSILLITHDLALVREVADRVVVMYGGRVV 234
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAEVERLFKVIRRLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
24-242 |
6.71e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 106.76 E-value: 6.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELT--NLQEsewnqIRgKDIAFIFQDPLS 101
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK----SGEIFYNNQAITddNFEK-----LR-KHIGIVFQNPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 102 SLnptmkVGRQITEVI---LQHEKKSKKEAKEIAINLLNDLGIHEaekRFEQYPHQLSGGMRQRICLAIAFACHPKLVIA 178
Cdd:PRK13648 95 QF-----VGSIVKYDVafgLENHAVPYDEMHRRVSEALKQVDMLE---RADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446453387 179 DEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREvADRVVVMYGGRVVEKGTIEEV 242
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
11-237 |
8.13e-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: 104.99 E-value: 8.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 11 TLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLqESEWNQIrgk 90
Cdd:cd03268 3 TNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGL----IKPDSGEITFDGKSYQKN-IEALRRI--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 91 diAFIFQDPlsSLNPTMkVGRqitEVILQHEKKSKKEAKEIAiNLLNDLGIHEAE-KRFEQYphqlSGGMRQRICLAIAF 169
Cdd:cd03268 75 --GALIEAP--GFYPNL-TAR---ENLRLLARLLGIRKKRID-EVLDVVGLKDSAkKKVKGF----SLGMKQRLGIALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446453387 170 ACHPKLVIADEPTTALDVTIQKQIMELLKeRKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKG 237
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRELIL-SLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-278 |
8.31e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 106.61 E-value: 8.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 6 SLENVTLAVEkeNSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGL---NQESIHIDDGNISFEseeltNLqes 82
Cdd:PRK13632 9 KVENVSFSYP--NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLlkpQSGEIKIDGITISKE-----NL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 83 ewNQIRGKdIAFIFQDPLSSLnptmkVGRQITEVI---LQHEKKSKKEAKEIAINLLNDLGIheaEKRFEQYPHQLSGGM 159
Cdd:PRK13632 79 --KEIRKK-IGIIFQNPDNQF-----IGATVEDDIafgLENKKVPPKKMKDIIDDLAKKVGM---EDYLDKEPQNLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 160 RQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLalvREV--ADRVVVMYGGRVVEKG 237
Cdd:PRK13632 148 KQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDM---DEAilADKVIVFSEGKLIAQG 224
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446453387 238 TIEEVIGSpkhpytKSLLQAIpNIDD--SEKVLRAIEGTTPSI 278
Cdd:PRK13632 225 KPKEILNN------KEILEKA-KIDSpfIYKLSKKLKGIDPTY 260
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
23-242 |
9.86e-27 |
|
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: 105.21 E-value: 9.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEWNQiRGkdIAFIFQdplss 102
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGL----LPPRSGSIRFDGRDITGLPPHERAR-AG--IGYVPE----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 103 lnptmkvGRQI------TEVILqhekkskkeakeIAINLLNDLGIHEAEKR-FEQYP------HQ----LSGGMRQRICL 165
Cdd:cd03224 83 -------GRRIfpeltvEENLL------------LGAYARRRAKRKARLERvYELFPrlkerrKQlagtLSGGEQQMLAI 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446453387 166 AIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQnTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEG-VTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-242 |
3.21e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.17 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 1 MGQLLSLENVTLAVEKENSKQAI--VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEElTN 78
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEKlaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPS----EGKVYVDGLD-TS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 79 LQESEWNqIRGKdIAFIFQDPlsslnptmkvGRQITEVILQHEkkskkeakeIAINLLNdLGI---------HEAEKRFE 149
Cdd:PRK13633 76 DEENLWD-IRNK-AGMVFQNP----------DNQIVATIVEED---------VAFGPEN-LGIppeeirervDESLKKVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 150 QY------PHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREvAD 223
Cdd:PRK13633 134 MYeyrrhaPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-AD 212
|
250
....*....|....*....
gi 446453387 224 RVVVMYGGRVVEKGTIEEV 242
Cdd:PRK13633 213 RIIVMDSGKVVMEGTPKEI 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-248 |
4.98e-26 |
|
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: 103.70 E-value: 4.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNlqesewnqiRGKDIAFIFQDplSSL 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPT----SGGVILEGKQITE---------PGPDRMVVFQN--YSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMKVGRQIT----EVILQHEKKSKKEAKEIAINLLNdLGiHEAEKRfeqyPHQLSGGMRQRICLAIAFACHPKLVIAD 179
Cdd:TIGR01184 66 LPWLTVRENIAlavdRVLPDLSKSERRAIVEEHIALVG-LT-EAADKR----PGQLSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 180 EPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV-IGSPKH 248
Cdd:TIGR01184 140 EPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-237 |
5.11e-26 |
|
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: 102.74 E-value: 5.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEELTNLQESew 84
Cdd:cd03269 1 LEVENVT----KRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILP----DSGEVLFDGKPLDIAARN-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqirgkDIAFIFQDplSSLNPTMKVGRQItevilqhekkskkeakeIAINLLNDLGIHEAE-------KRFEQYPH---- 153
Cdd:cd03269 71 ------RIGYLPEE--RGLYPKMKVIDQL-----------------VYLAQLKGLKKEEARrridewlERLELSEYankr 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 154 --QLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKqNTSILLITHDLALVREVADRVVVMYGG 231
Cdd:cd03269 126 veELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKG 204
|
....*.
gi 446453387 232 RVVEKG 237
Cdd:cd03269 205 RAVLYG 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-255 |
7.18e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 102.91 E-value: 7.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENskqaivKHVSFSINEGEIVALVGESGSGKSvTAQSII-GLnqesIHIDDGNISFESEELTNLQESE 83
Cdd:COG3840 2 LRLDDLTYRYGDFP------LRFDLTIAAGERVAILGPSGAGKS-TLLNLIaGF----LPPDSGRILWNGQDLTALPPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 wnqiRGkdIAFIFQD----P-LS-------SLNPTMKVGR-QITEVIlqhekkskkeakeiaiNLLNDLGIHEAEKRfeq 150
Cdd:COG3840 71 ----RP--VSMLFQEnnlfPhLTvaqniglGLRPGLKLTAeQRAQVE----------------QALERVGLAGLLDR--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 151 YPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYG 230
Cdd:COG3840 126 LPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVAD 205
|
250 260
....*....|....*....|....*
gi 446453387 231 GRVVEKGTIEEVIGSPKHPYTKSLL 255
Cdd:COG3840 206 GRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-252 |
8.83e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 103.17 E-value: 8.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 20 KQAIVKHVSFSINEGEIVALVGESGSGKSV---------TAQSiiglnqESIHIDDGNISFEseelTNLQESEWNQIRGK 90
Cdd:COG4161 14 SHQALFDINLECPSGETLVLLGPSGAGKSSllrvlnlleTPDS------GQLNIAGHQFDFS----QKPSEKAIRLLRQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 91 dIAFIFQDplSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRFeqyPHQLSGGMRQRICLAIAFA 170
Cdd:COG4161 84 -VGMVFQQ--YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRF---PLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 171 CHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSIlLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIgspkHPY 250
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQV-IVTHEVEFARKVASQVVYMEKGRIIEQGDASHFT----QPQ 232
|
..
gi 446453387 251 TK 252
Cdd:COG4161 233 TE 234
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-242 |
1.06e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 103.73 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 18 NSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGL-----NQESIHIDDGnisfeseeLTNLQESEWNqIRGKdI 92
Cdd:PRK13640 17 DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddNPNSKITVDG--------ITLTAKTVWD-IREK-V 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 93 AFIFQDPLSSLnptmkVGRQITEVI---LQHEKKSKKEAKEIAINLLNDLGIHEAEKrfeQYPHQLSGGMRQRICLAIAF 169
Cdd:PRK13640 87 GIVFQNPDNQF-----VGATVGDDVafgLENRAVPRPEMIKIVRDVLADVGMLDYID---SEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446453387 170 ACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVrEVADRVVVMYGGRVVEKGTIEEV 242
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-234 |
1.35e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.24 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKE--NSKQAIvKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlnqeSIHIDDGNISFESEELTNLQES 82
Cdd:COG1101 2 LELKNLSKTFNPGtvNEKRAL-DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAG----SLPPDSGSILIDGKDVTKLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 83 EwnqiRGKDIAFIFQDPLSSLNPTMkvgrQITEVILQHEKKSKKEAKEIAIN---------LLNDLGIhEAEKRFEQYPH 153
Cdd:COG1101 77 K----RAKYIGRVFQDPMMGTAPSM----TIEENLALAYRRGKRRGLRRGLTkkrrelfreLLATLGL-GLENRLDTKVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 154 QLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDL--ALvrEVADRVVVMYGG 231
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMeqAL--DYGNRLIMMHEG 225
|
...
gi 446453387 232 RVV 234
Cdd:COG1101 226 RII 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
24-241 |
2.50e-25 |
|
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: 101.29 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGL---NQESIHIDDGNISFESEEltnlqesewnqIRgKDIAFIFQDPl 100
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLlkpTSGRATVAGHDVVREPRE-----------VR-RRIGIVFQDL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 101 sSLNPTMkVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRFEQYphqLSGGMRQRICLAIAFACHPKLVIADE 180
Cdd:cd03265 83 -SVDDEL-TGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446453387 181 PTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEE 241
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-234 |
3.06e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 106.35 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 1 MGQLLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSvTAQSIIG-LNQESihidDGNISFESEELTNL 79
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGcLDKPT----SGTYRVAGQDVATL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 80 QESEWNQIRGKDIAFIFQ--DPLSSLNPTMKVgrqitEVILQHEKKSKKEAKEIAINLLNDLGIHEaekRFEQYPHQLSG 157
Cdd:PRK10535 76 DADALAQLRREHFGFIFQryHLLSHLTAAQNV-----EVPAVYAGLERKQRLLRAQELLQRLGLED---RVEYQPSQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446453387 158 GMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSIlLITHDlALVREVADRVVVMYGGRVV 234
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVI-IVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-244 |
3.90e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.49 E-value: 3.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQEse 83
Cdd:COG3845 257 VLEVENLSV---RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGL----RPPASGSIRLDGEDITGLSP-- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 wNQIRGKDIAFIFQDPLSS-LNPTMKVgrqiTE-VILQHEKKSKKEAKEIainlLNDLGIHE-AEKRFEQY------PHQ 154
Cdd:COG3845 328 -RERRRLGVAYIPEDRLGRgLVPDMSV----AEnLILGRYRRPPFSRGGF----LDRKAIRAfAEELIEEFdvrtpgPDT 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 155 ----LSGGMRQRICLAIAFACHPKLVIADEPTTALDV----TIQKQIMELlkeRKekQNTSILLITHDLALVREVADRVV 226
Cdd:COG3845 399 parsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaieFIHQRLLEL---RD--AGAAVLLISEDLDEILALSDRIA 473
|
250 260
....*....|....*....|..
gi 446453387 227 VMYGGRVVE----KGTIEEVIG 244
Cdd:COG3845 474 VMYEGRIVGevpaAEATREEIG 495
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-250 |
5.29e-25 |
|
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: 103.27 E-value: 5.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEWNQIRGKDIAFIFQDplSSLNPT 106
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGL----TRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE--ARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 107 MKVgRQITEVILQHEKKSKKEAKEIAINLLndLGIheaEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALD 186
Cdd:TIGR02142 90 LSV-RGNLRYGMKRARPSERRISFERVIEL--LGI---GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446453387 187 VTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPY 250
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-270 |
5.59e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 103.76 E-value: 5.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQESE 83
Cdd:PRK11607 19 LLEIRNLT----KSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPT----AGQIMLDGVDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 wnqirgKDIAFIFQDplSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAiNLLNDLGIHEAEKRfeqYPHQLSGGMRQRI 163
Cdd:PRK11607 91 ------RPINMMFQS--YALFPHMTVEQNIAFGLKQDKLPKAEIASRVN-EMLGLVHMQEFAKR---KPHQLSGGQRQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 164 CLAIAFACHPKLVIADEPTTALDVTI----QKQIMELLkerkEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTI 239
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
250 260 270
....*....|....*....|....*....|.
gi 446453387 240 EEVIgspKHPYTKSLLQAIPNIDDSEKVLRA 270
Cdd:PRK11607 235 EEIY---EHPTTRYSAEFIGSVNVFEGVLKE 262
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-243 |
6.33e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.00 E-value: 6.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVekenSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlnqeSIHIDDGNISFESEELTNLQESE 83
Cdd:PRK13548 2 MLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG----ELSPDSGEVRLNGRPLADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WNQIRG-----KDIAFIFQdplsslnptmkvgrqITEVI---LQHEKKSKKEAKEIAINLLNDLGIHEAEKRFeqYPhQL 155
Cdd:PRK13548 74 LARRRAvlpqhSSLSFPFT---------------VEEVVamgRAPHGLSRAEDDALVAAALAQVDLAHLAGRD--YP-QL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 156 SGGMRQRICLAIAFA-CH-----PKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMY 229
Cdd:PRK13548 136 SGGEQQRVQLARVLAqLWepdgpPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLH 215
|
250
....*....|....
gi 446453387 230 GGRVVEKGTIEEVI 243
Cdd:PRK13548 216 QGRLVADGTPAEVL 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-266 |
6.55e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 101.71 E-value: 6.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 21 QAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQE-SIHIDDGNISFESEELTNLQESEWNQIRgkdIAFIFQDP 99
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvSGYRYSGDVLLGGRSIFNYRDVLEFRRR---VGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 lsslNP-TMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEK-RFEQYPHQLSGGMRQRICLAIAFACHPKLVI 177
Cdd:PRK14271 111 ----NPfPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 178 ADEPTTALDVTIQKQIMELLKERKEKqnTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTKSLLQA 257
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAG 264
|
250
....*....|
gi 446453387 258 IP-NIDDSEK 266
Cdd:PRK14271 265 LSgDVKDAKR 274
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-262 |
6.63e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 101.24 E-value: 6.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENskqaIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQESEW 84
Cdd:PRK11231 3 LRTENLTVGYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQ----SGTVFLGDKPISMLSSRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqirGKDIAFIFQDPLSslnPTmkvGRQITEVI-------LQHEKKSKKEAKEIAINLLNDLGIHE-AEKRFEQyphqLS 156
Cdd:PRK11231 75 ----ARRLALLPQHHLT---PE---GITVRELVaygrspwLSLWGRLSAEDNARVNQAMEQTRINHlADRRLTD----LS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 157 GGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLItHDLALVREVADRVVVMYGGRVVEK 236
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVL-HDLNQASRYCDHLVVLANGHVMAQ 219
|
250 260
....*....|....*....|....*.
gi 446453387 237 GTIEEVIgspkhpyTKSLLQAIPNID 262
Cdd:PRK11231 220 GTPEEVM-------TPGLLRTVFDVE 238
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-247 |
9.71e-25 |
|
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: 100.06 E-value: 9.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTL---AVEkenskqaIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLq 80
Cdd:COG0410 3 MLEVENLHAgygGIH-------VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGL----LPPRSGSIRFDGEDITGL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 81 esEWNQIRGKDIAF------IFqdplsslnPTMKVgrqiTEvilqhekkskkeakeiaiNLL-------NDLGIHEAEKR 147
Cdd:COG0410 71 --PPHRIARLGIGYvpegrrIF--------PSLTV----EE------------------NLLlgayarrDRAEVRADLER 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 148 -FEQYP------HQ----LSGGMRQRicLAIAFA--CHPKLVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITHD 214
Cdd:COG0410 119 vYELFPrlkerrRQragtLSGGEQQM--LAIGRAlmSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQN 195
|
250 260 270
....*....|....*....|....*....|...
gi 446453387 215 LALVREVADRVVVMYGGRVVEKGTIEEVIGSPK 247
Cdd:COG0410 196 ARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-243 |
1.14e-24 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 104.44 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEkeNSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIhiddGNISFESEELTNlqeseW 84
Cdd:COG4618 331 LSVENLTVVPP--GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTA----GSVRLDGADLSQ-----W 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIR-GKDIAFIFQDPlsSLNP-TmkvgrqitevilqhekkskkeakeIAINL--LNDL------------GIHEAEKRF 148
Cdd:COG4618 400 DREElGRHIGYLPQDV--ELFDgT------------------------IAENIarFGDAdpekvvaaaklaGVHEMILRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 149 EQ-Y-------PHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITHDLALVRe 220
Cdd:COG4618 454 PDgYdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPSLLA- 531
|
250 260
....*....|....*....|...
gi 446453387 221 VADRVVVMYGGRVVEKGTIEEVI 243
Cdd:COG4618 532 AVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
23-257 |
1.33e-24 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 102.38 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHidDGNISFESEELTNLQESEwnqirgKDIAFIFQDplSS 102
Cdd:TIGR03258 20 VLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGL--TGRIAIADRDLTHAPPHK------RGLALLFQN--YA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 103 LNPTMKVGRQITEVILQHEKKSKKEAKEIAiNLLNDLGIHEAEKRfeqYPHQLSGGMRQRICLAIAFACHPKLVIADEPT 182
Cdd:TIGR03258 90 LFPHLKVEDNVAFGLRAQKMPKADIAERVA-DALKLVGLGDAAAH---LPAQLSGGMQQRIAIARAIAIEPDVLLLDEPL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446453387 183 TALDVTIQKQIMELLKE-RKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTKSLLQA 257
Cdd:TIGR03258 166 SALDANIRANMREEIAAlHEELPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGA 241
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-233 |
1.68e-24 |
|
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: 97.67 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEkeNSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQESEW 84
Cdd:cd03246 1 LEVENVSFRYP--GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT----SGRVRLDGADISQWDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqirGKDIAFIFQDplsslnptmkvgrqiteVILqhekkskkEAKEIAINLLndlgiheaekrfeqyphqlSGGMRQRIC 164
Cdd:cd03246 75 ----GDHVGYLPQD-----------------DEL--------FSGSIAENIL-------------------SGGQRQRLG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSIlLITHDLALVREvADRVVVMYGGRV 233
Cdd:cd03246 107 LARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRI-VIAHRPETLAS-ADRILVLEDGRV 173
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-228 |
2.20e-24 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 103.52 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENskqAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEW 84
Cdd:TIGR02857 322 LEFSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF----VDPTEGSIAVNGVPLADADADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqirGKDIAFIFQdplsslNPTMKVGrQITEVILQHEKKSKKEAKEIAinlLNDLGIHEAEKRFEQY--------PHQLS 156
Cdd:TIGR02857 395 ----RDQIAWVPQ------HPFLFAG-TIAENIRLARPDASDAEIREA---LERAGLDEFVAALPQGldtpigegGAGLS 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453387 157 GGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLkeRKEKQNTSILLITHDLALVREvADRVVVM 228
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEAL--RALAQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
25-247 |
2.97e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.77 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 25 KHVSFSINEGEIVALVGESGSGKSVT---AQSIIGLNQESIHIDDGNISFESEELTNLQesewnqirgKDIAFIFQDPLS 101
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLflhFNGILKPTSGEVLIKGEPIKYDKKSLLEVR---------KTVGIVFQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 102 SL-NPTMKvgrqitevilqhekkskkeaKEIAINLLN-DLGIHEAEKR------------FEQY-PHQLSGGMRQRICLA 166
Cdd:PRK13639 90 QLfAPTVE--------------------EDVAFGPLNlGLSKEEVEKRvkealkavgmegFENKpPHHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 167 IAFACHPKLVIADEPTTALDVTIQKQIMELLKERKeKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSP 246
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
.
gi 446453387 247 K 247
Cdd:PRK13639 229 E 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-228 |
3.49e-24 |
|
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: 97.93 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKEnskqAIVKHVSFSINEGEIVALVGESGSGKSvTA-QSIIGLnqesIHIDDGNISFESEELTNLQES 82
Cdd:COG4133 2 MLEAENLSCRRGER----LLFSGLSFTLAAGEALALTGPNGSGKT-TLlRILAGL----LPPSAGEVLWNGEPIRDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 83 ewnqiRGKDIAFIFQDPLssLNPTMKVGRQITevILQHEKKSKKEAKEIAiNLLNDLGIHEAEkrfEQYPHQLSGGMRQR 162
Cdd:COG4133 73 -----YRRRLAYLGHADG--LKPELTVRENLR--FWAALYGLRADREAID-EALEAVGLAGLA---DLPVRQLSAGQKRR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446453387 163 ICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITHDLALVRevADRVVVM 228
Cdd:COG4133 140 VALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLA-RGGAVLLTTHQPLELA--AARVLDL 202
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-247 |
4.85e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.18 E-value: 4.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNL----- 79
Cdd:COG1137 4 LEAENLV----KSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGL----VKPDSGRIFLDGEDITHLpmhkr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 80 ---------QEsewnqirgkdiAFIFQDplsslnptMKVGRQItEVILQHEKKSKKEAKEIAINLLNDLGIheaEKRFEQ 150
Cdd:COG1137 76 arlgigylpQE-----------ASIFRK--------LTVEDNI-LAVLELRKLSKKEREERLEELLEEFGI---THLRKS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 151 YPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALD---VT-IQKQIMElLKERkekqNTSIlLIT-HDlalVRE---VA 222
Cdd:COG1137 133 KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiaVAdIQKIIRH-LKER----GIGV-LITdHN---VREtlgIC 203
|
250 260
....*....|....*....|....*
gi 446453387 223 DRVVVMYGGRVVEKGTIEEVIGSPK 247
Cdd:COG1137 204 DRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-260 |
4.91e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.42 E-value: 4.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 1 MGQLLSLENVTLAVeKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTnlQ 80
Cdd:PRK13650 1 MSNIIEVKNLTFKY-KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGL----LEAESGQIIIDGDLLT--E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 81 ESEWNqIRGKdIAFIFQDPLSSLnptmkVGRQITEVI---LQHEKKSKKEAKEIAINLLNDLGIHEAEKRfeqYPHQLSG 157
Cdd:PRK13650 74 ENVWD-IRHK-IGMVFQNPDNQF-----VGATVEDDVafgLENKGIPHEEMKERVNEALELVGMQDFKER---EPARLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 158 GMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLalvREVA--DRVVVMYGGRVVE 235
Cdd:PRK13650 144 GQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDL---DEVAlsDRVLVMKNGQVES 220
|
250 260 270
....*....|....*....|....*....|...
gi 446453387 236 KGTIEEVIGSPKH--------PYTKSLLQAIPN 260
Cdd:PRK13650 221 TSTPRELFSRGNDllqlgldiPFTTSLVQSLRQ 253
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-244 |
5.43e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 102.19 E-value: 5.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihiddgnisfeSEELTNLQESEW---------NQIRGKD-IA 93
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT-----------SGEVNVRVGDEWvdmtkpgpdGRGRAKRyIG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 94 FIFQDplSSLNPTMKVGRQITEVIlqHEKKSKKEAKEIAINLLNDLGIHE--AEKRFEQYPHQLSGGMRQRICLAIAFAC 171
Cdd:TIGR03269 369 ILHQE--YDLYPHRTVLDNLTEAI--GLELPDELARMKAVITLKMVGFDEekAEEILDKYPDELSEGERHRVALAQVLIK 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446453387 172 HPKLVIADEPTTALDVTIQKQIME-LLKERKEKQNTsILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIG 244
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQT-FIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-250 |
5.67e-24 |
|
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: 99.88 E-value: 5.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 39 LVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNLQEsewnQIRGkdIAFIFQDplSSLNPTMKVGRQITEVIL 118
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQ----PDSGSIMLDGEDVTNVPP----HLRH--INMVFQS--YALFPHMTVEENVAFGLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 119 QHEKKSKKeakeIAINLLNDLGIHEAEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLK 198
Cdd:TIGR01187 69 MRKVPRAE----IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446453387 199 ERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPY 250
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
5-243 |
7.04e-24 |
|
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: 102.04 E-value: 7.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNlqeseW 84
Cdd:TIGR01842 317 LSVENVTIV--PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPT----SGSVRLDGADLKQ-----W 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIR-GKDIAFIFQDplSSLNPTmkvgrQITEVILQHEKKSKKEAKEIAINLLndlGIHEAEKRFEQ-YPHQ-------L 155
Cdd:TIGR01842 386 DRETfGKHIGYLPQD--VELFPG-----TVAENIARFGENADPEKIIEAAKLA---GVHELILRLPDgYDTVigpggatL 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 156 SGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKeKQNTSILLITHDLALVrEVADRVVVMYGGRVVE 235
Cdd:TIGR01842 456 SGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALK-ARGITVVVITHRPSLL-GCVDKILVLQDGRIAR 533
|
....*...
gi 446453387 236 KGTIEEVI 243
Cdd:TIGR01842 534 FGERDEVL 541
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-243 |
7.78e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 101.96 E-value: 7.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 6 SLENVTLAVEKE-------NSKQAiVKHVSFSINEGEIVALVGESGSGKSVTaqsiIGLNQESIHIDDGNISFESEELTN 78
Cdd:PRK13657 327 DLGRVKGAVEFDdvsfsydNSRQG-VEDVSFEAKPGQTVAIVGPTGAGKSTL----INLLQRVFDPQSGRILIDGTDIRT 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 79 LQESewnQIRgKDIAFIFQDPL---SSLNPTMKVGRQ-ITEVILQHEKKSKKEAKEIAINLlNDLGIHEAEKrfeqyPHQ 154
Cdd:PRK13657 402 VTRA---SLR-RNIAVVFQDAGlfnRSIEDNIRVGRPdATDEEMRAAAERAQAHDFIERKP-DGYDTVVGER-----GRQ 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 155 LSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSIllITHDLALVREvADRVVVMYGGRVV 234
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTVRN-ADRILVFDNGRVV 548
|
....*....
gi 446453387 235 EKGTIEEVI 243
Cdd:PRK13657 549 ESGSFDELV 557
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-243 |
7.85e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 98.26 E-value: 7.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVekenSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESE 83
Cdd:COG4559 1 MLEAENLSVRL----GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGE----LTPSSGEVRLNGRPLAAWSPWE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WNQIRG-----KDIAFifqdPLSSLnptmkvgrqitEVI---LQHEKKSKKEAKEIAINLLNDLGIHEAEKRFeqYPhQL 155
Cdd:COG4559 73 LARRRAvlpqhSSLAF----PFTVE-----------EVValgRAPHGSSAAQDRQIVREALALVGLAHLAGRS--YQ-TL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 156 SGGMRQRICLAIAFA-------CHPKLVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITHDLALVREVADRVVVM 228
Cdd:COG4559 135 SGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLL 213
|
250
....*....|....*
gi 446453387 229 YGGRVVEKGTIEEVI 243
Cdd:COG4559 214 HQGRLVAQGTPEEVL 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-243 |
1.22e-23 |
|
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: 97.23 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSII---GLNQESIHIDDGNISFeseelTNLQEsewnqIRGKdIAFIFQDP 99
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfyDPTSGEILLDGVDIRD-----LNLRW-----LRSQ-IGLVSQEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 LssLNPTmkvgrQITEVILQHEKKSKKEAKEIAINLLNdlgIHE-AEKRFEQY-----PH--QLSGGMRQRICLAIAFAC 171
Cdd:cd03249 87 V--LFDG-----TIAENIRYGKPDATDEEVEEAAKKAN---IHDfIMSLPDGYdtlvgERgsQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453387 172 HPKLVIADEPTTALDVTIQKQIMELLKERKEkqNTSILLITHDLALVREvADRVVVMYGGRVVEKGTIEEVI 243
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELM 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-237 |
1.89e-23 |
|
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: 96.12 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 7 LENVTLAVEkeNSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQESEwnq 86
Cdd:cd03245 5 FRNVSFSYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT----SGSVLLDGTDIRQLDPAD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 87 IRgKDIAFIFQDPL---SSL--NPTMKVGRQITEVILQhekkskkeakeiAINLLndlGIHEAEKRfeqYPH-------- 153
Cdd:cd03245 76 LR-RNIGYVPQDVTlfyGTLrdNITLGAPLADDERILR------------AAELA---GVTDFVNK---HPNgldlqige 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 154 ---QLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQntSILLITHDLALVrEVADRVVVMYG 230
Cdd:cd03245 137 rgrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLL-DLVDRIIVMDS 213
|
....*..
gi 446453387 231 GRVVEKG 237
Cdd:cd03245 214 GRIVADG 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
24-270 |
4.11e-23 |
|
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: 97.08 E-value: 4.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTnlqeSEWNQIRgKDIAFIFQDPLSSL 103
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTL----LRPTSGTARVAGYDVV----REPRKVR-RSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTmkvGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRfeqYPHQLSGGMRQRICLAIAFACHPKLVIADEPTT 183
Cdd:TIGR01188 80 DLT---GRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADR---PVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 184 ALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVigspKHPYTKSLLQAIPNIDD 263
Cdd:TIGR01188 154 GLDPRTRRAIWDYIRALKEEGVT-ILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL----KRRLGKDTLESRPRDIQ 228
|
....*..
gi 446453387 264 SEKVLRA 270
Cdd:TIGR01188 229 SLKVEVS 235
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
24-228 |
4.35e-23 |
|
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: 95.58 E-value: 4.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEE----LTNLQESEWNQIRGKDIAFIFQdp 99
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYL----PDSGSILVRHDGgwvdLAQASPREILALRRRTIGYVSQ-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 lsSLN-----PTMKVgrqiteVI--LQHEKKSKKEAKEIAINLLNDLGIheAEKRFEQYPHQLSGGMRQRICLAIAFACH 172
Cdd:COG4778 101 --FLRviprvSALDV------VAepLLERGVDREEARARARELLARLNL--PERLWDLPPATFSGGEQQRVNIARGFIAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446453387 173 PKLVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITHDLALVREVADRVVVM 228
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEEAKA-RGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-247 |
5.71e-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: 95.30 E-value: 5.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVtlavEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLqesEW 84
Cdd:cd03218 1 LRAENL----SKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGL----VKPDSGKILLDGQDITKL---PM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIRGKDIAFIFQDPlsSLNPTMKVGRQItEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKrfeQYPHQLSGGMRQRIC 164
Cdd:cd03218 70 HKRARLGIGYLPQEA--SIFRKLTVEENI-LAVLEIRGLSKKEREEKLEELLEEFHITHLRK---SKASSLSGGERRRVE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKqNTSILLITHDlalVRE---VADRVVVMYGGRVVEKGTIEE 241
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDHN---VREtlsITDRAYIIYEGKVLAEGTPEE 219
|
....*.
gi 446453387 242 VIGSPK 247
Cdd:cd03218 220 IAANEL 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
27-238 |
8.08e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 95.08 E-value: 8.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSvTAQSIIGL----NQESIHIDDGNISFEseelTNLQESEWNQIRgKDIAFIFQDplSS 102
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKS-SLLRVLNLlempRSGTLNIAGNHFDFS----KTPSDKAIRELR-RNVGMVFQQ--YN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 103 LNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRFeqyPHQLSGGMRQRICLAIAFACHPKLVIADEPT 182
Cdd:PRK11124 93 LWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRF---PLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446453387 183 TALDVTIQKQIMELLKERkekQNTSI--LLITHDLALVREVADRVVVMYGGRVVEKGT 238
Cdd:PRK11124 170 AALDPEITAQIVSIIREL---AETGItqVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
25-242 |
1.39e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.18 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 25 KHVSFSINEGEIVALVGESGSGKSvTAQSII-GLnqesIHIDDGNISFESEELTnlqesewnqIRG-KD-----IAFIFQ 97
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKS-TLMKILyGL----YQPDSGEILIDGKPVR---------IRSpRDaialgIGMVHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 98 DPlsSLNPTMKVgrqiTE-VILQHEKKSKKEakeiainllndLGIHEAEKRF----EQYP---------HQLSGGMRQRI 163
Cdd:COG3845 88 HF--MLVPNLTV----AEnIVLGLEPTKGGR-----------LDRKAARARIrelsERYGldvdpdakvEDLSVGEQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 164 ----CLAiafaCHPKLVIADEPTTALdvTIQ--KQIMELLKERKEkQNTSILLITHDLALVREVADRVVVMYGGRVVEKG 237
Cdd:COG3845 151 eilkALY----RGARILILDEPTAVL--TPQeaDELFEILRRLAA-EGKSIIFITHKLREVMAIADRVTVLRRGKVVGTV 223
|
....*
gi 446453387 238 TIEEV 242
Cdd:COG3845 224 DTAET 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-252 |
1.48e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.52 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 13 AVEKEN-----SKQAIVKHVSFSINEGEIVALVGESGSGKSV---TAQSIIGLNQESIHIDDGNISFEseeltNLQESEW 84
Cdd:PRK14267 4 AIETVNlrvyyGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTllrTFNRLLELNEEARVEGEVRLFGR-----NIYSPDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIR-GKDIAFIFQDPlsslNP--------TMKVGRQITEVILQHEKKSKKEAKEIAINLLNDlgihEAEKRFEQYPHQL 155
Cdd:PRK14267 79 DPIEvRREVGMVFQYP----NPfphltiydNVAIGVKLNGLVKSKKELDERVEWALKKAALWD----EVKDRLNDYPSNL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 156 SGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEkqNTSILLITHDLALVREVADRVVVMYGGRVVE 235
Cdd:PRK14267 151 SGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
250
....*....|....*..
gi 446453387 236 KGTIEEVIGSPKHPYTK 252
Cdd:PRK14267 229 VGPTRKVFENPEHELTE 245
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-243 |
1.52e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 94.21 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 8 ENVTLAVEKENSkqaIVKHVSFSINEGEIVALVGESGSGKSvtaqSIIGLNQESIHIDDGNISFESEELTNLQESEWNqi 87
Cdd:cd03254 6 ENVNFSYDEKKP---VLKDINFSIKPGETVAIVGPTGAGKT----TLINLLMRFYDPQKGQILIDGIDIRDISRKSLR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 88 rgKDIAFIFQDPL---SSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKrfeqyPHQLSGGMRQRIC 164
Cdd:cd03254 77 --SMIGVVLQDTFlfsGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGEN-----GGNLSQGERQLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 165 LAIAFACHPKLVIADEPTTALDV----TIQKQIMELLKERkekqnTSIlLITHDLALVREvADRVVVMYGGRVVEKGTIE 240
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTetekLIQEALEKLMKGR-----TSI-IIAHRLSTIKN-ADKILVLDDGKIIEEGTHD 222
|
...
gi 446453387 241 EVI 243
Cdd:cd03254 223 ELL 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-242 |
1.52e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 25 KHVSFSINEGEIVALVGESGSGKSvTAQSII-GLNQesihIDDGNISFESEE--LTNLQESewnQIRGkdIAFIFQDPls 101
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKS-TLMKILsGVYQ----PDSGEILLDGEPvrFRSPRDA---QAAG--IAIIHQEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 102 SLNPTMKV------GRQITE-VILQHEKKSKKeakeiAINLLNDLGIHEAekrfeqyPHQ----LSGGMRQRICLAIAFA 170
Cdd:COG1129 89 NLVPNLSVaeniflGREPRRgGLIDWRAMRRR-----ARELLARLGLDID-------PDTpvgdLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446453387 171 CHPKLVIADEPTTALDVT-IQK--QIMELLKErkekQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:COG1129 157 RDARVLILDEPTASLTEReVERlfRIIRRLKA----QGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-242 |
1.56e-22 |
|
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: 93.36 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKEnskqAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqESIHIDDGNISFESEELTNLQESEw 84
Cdd:cd03217 1 LEIKDLHVSVGGK----EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYEVTEGEILFKGEDITDLPPEE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqiRGKDIAFI-FQDPLsslnptmkvgrQITEVILqhekkskkeakeiaINLLNDLGIheaekrfeqyphQLSGGMRQRI 163
Cdd:cd03217 74 ---RARLGIFLaFQYPP-----------EIPGVKN--------------ADFLRYVNE------------GFSGGEKKRN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 164 CLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKqNTSILLITHD---LALVRevADRVVVMYGGRVVEKGTIE 240
Cdd:cd03217 114 EILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYqrlLDYIK--PDRVHVLYDGRIVKSGDKE 190
|
..
gi 446453387 241 EV 242
Cdd:cd03217 191 LA 192
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-247 |
1.75e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 96.33 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNlqesew 84
Cdd:PRK11432 7 VVLKNIT----KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPT----EGQIFIDGEDVTH------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIRGKDIAFIFQDplSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINL-LNDLGIHEaekrfEQYPHQLSGGMRQRI 163
Cdd:PRK11432 73 RSIQQRDICMVFQS--YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALeLVDLAGFE-----DRYVDQISGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 164 CLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY 225
|
....
gi 446453387 244 GSPK 247
Cdd:PRK11432 226 RQPA 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-252 |
1.93e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 94.33 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVekeNSKQAiVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQE--------SIHIDDGNISFESEEL 76
Cdd:COG1117 12 IEVRNLNVYY---GDKQA-LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarvegEILLDGEDIYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 77 TNLqesewnqiRgKDIAFIFQDPlsslNP----------------TMKVGRQITEvilqhekkskkeakeIAINLLNDLG 140
Cdd:COG1117 88 VEL--------R-RRVGMVFQKP----NPfpksiydnvayglrlhGIKSKSELDE---------------IVEESLRKAA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 141 I-HEAEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKErkEKQNTSILLITHDLALVR 219
Cdd:COG1117 140 LwDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILE--LKKDYTIVIVTHNMQQAA 217
|
250 260 270
....*....|....*....|....*....|...
gi 446453387 220 EVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTK 252
Cdd:COG1117 218 RVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-244 |
2.40e-22 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 93.45 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKEnsKQAIVKHVSFSINEGEIVALVGESGSGKSvtaqSIIGLNQESIHIDDGNISFESeelTNLQESEW 84
Cdd:cd03251 1 VEFKNVTFRYPGD--GPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYDVDSGRILIDG---HDVRDYTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIRgKDIAFIFQDPLSsLNPTmkvgrqITEVILQHEKKSKKEAKEIAINLLNdlgIHEAEKRFEQYPH--------QLS 156
Cdd:cd03251 72 ASLR-RQIGLVSQDVFL-FNDT------VAENIAYGRPGATREEVEEAARAAN---AHEFIMELPEGYDtvigergvKLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 157 GGMRQRICLAIAFACHPKLVIADEPTTALDVT----IQKQIMELLKERkekqnTSIlLITHDLALVREvADRVVVMYGGR 232
Cdd:cd03251 141 GGQRQRIAIARALLKDPPILILDEATSALDTEserlVQAALERLMKNR-----TTF-VIAHRLSTIEN-ADRIVVLEDGK 213
|
250
....*....|..
gi 446453387 233 VVEKGTIEEVIG 244
Cdd:cd03251 214 IVERGTHEELLA 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
15-262 |
2.77e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.30 E-value: 2.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 15 EKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGL---NQESIHIDD----GNISFESEELTNLQES--EWN 85
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLiksKYGTIQVGDiyigDKKNNHELITNPYSKKikNFK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 86 QIRgKDIAFIFQDPLSSL-NPTMKVGRQITEVILQhekKSKKEAKEIAINLLNDLGIHEAekRFEQYPHQLSGGMRQRIC 164
Cdd:PRK13631 113 ELR-RRVSMVFQFPEYQLfKDTIEKDIMFGPVALG---VKKSEAKKLAKFYLNKMGLDDS--YLERSPFGLSGGQKRRVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKeKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIG 244
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFT 265
|
250
....*....|....*...
gi 446453387 245 SPkHPYTKSLLQAIPNID 262
Cdd:PRK13631 266 DQ-HIINSTSIQVPRVIQ 282
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-242 |
2.99e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.43 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSVTAQSIIGLN---QESIHIDDGNISFESEEltnlqeSEWNQIRgKDIAFIFQDPLSSL 103
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvptQGSVRVDDTLITSTSKN------KDIKQIR-KKVGLVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 nptmkvgrqITEVIL-------QHEKKSKKEAKEIAINLLNDLGIheAEKRFEQYPHQLSGGMRQRICLAIAFACHPKLV 176
Cdd:PRK13649 99 ---------FEETVLkdvafgpQNFGVSQEEAEALAREKLALVGI--SESLFEKNPFELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446453387 177 IADEPTTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMT-IVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-245 |
2.99e-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: 93.32 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEELTnLQESEWNQirgKDIAFIFQ----- 97
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVP----ENGRVLVDGHDLA-LADPAWLR---RQVGVVLQenvlf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 98 -----DPLSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIheaekrfeqyphQLSGGMRQRICLAIAFACH 172
Cdd:cd03252 89 nrsirDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGA------------GLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446453387 173 PKLVIADEPTTALDVTIQKQIMELLkeRKEKQNTSILLITHDLALVREvADRVVVMYGGRVVEKGTIEEVIGS 245
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNM--HDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
232-318 |
3.17e-22 |
|
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: 88.96 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 232 RVVEKGTIEEVIGSPKHPYTKSLLQAIPNIDDSEKVLRAIEGTTPSIETLNSfGCPFVNRCPVAIKECIHRFPERTTYSK 311
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPS-GCRFYPRCPYAQDECRKEPPALVEIAE 79
|
....*..
gi 446453387 312 EHSSHCW 318
Cdd:TIGR01727 80 GHRVACH 86
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-237 |
5.25e-22 |
|
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: 91.22 E-value: 5.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENSKqaIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlnqeSIHIDDGNISFESEELTNLQESew 84
Cdd:cd03247 1 LSINNVSFSYPEQEQQ--VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG----DLKPQQGEITLDGVPVSDLEKA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqiRGKDIAFIFQDPlsslnptmkvgrqitevilqhekkskkeaKEIAINLLNDLGIheaekrfeqyphQLSGGMRQRIC 164
Cdd:cd03247 73 ---LSSLISVLNQRP-----------------------------YLFDTTLRNNLGR------------RFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEkqNTSILLITHDLALVrEVADRVVVMYGGRVVEKG 237
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGI-EHMDKILFLENGKIIMQG 178
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-243 |
6.74e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.00 E-value: 6.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNIS------FEsEELTNLqesewnqirgKDIAFIF- 96
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGI----LVPTSGEVRvlgyvpFK-RRKEFA----------RRIGVVFg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 97 Q------D--PLSSLNpTMKVGRQITEVILQHEkkskkeakeiaINLLND-LGIHEaekrFEQYP-HQLSGGMRQRICLA 166
Cdd:COG4586 103 QrsqlwwDlpAIDSFR-LLKAIYRIPDAEYKKR-----------LDELVElLDLGE----LLDTPvRQLSLGQRMRCELA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446453387 167 IAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:COG4586 167 AALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELK 243
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-252 |
7.74e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.80 E-value: 7.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 21 QAIVKHVSFSINEGEIVALVGESGSGKSvtaqSIIGLNQESIHIDDGNISFESEEL---TNLQESEWNQIRgKDIAFIFQ 97
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKS----TLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLR-KEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 98 DPlsSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGI-HEAEKRFEQYPHQLSGGMRQRICLAIAFACHPKLV 176
Cdd:PRK14246 98 QP--NPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446453387 177 IADEPTTALDVTIQKQIMELLKERKEKqnTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTK 252
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-237 |
1.60e-21 |
|
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: 90.89 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFES-EELTNLQES 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL----LEPDAGFATVDGfDVVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 83 EWNqirgkdIAFIFQDplSSLNPTMKVGRQITEVILQHEKKSKKEAKeiAINLLND-LGIHE-AEKRFEQyphqLSGGMR 160
Cdd:cd03266 77 RRR------LGFVSDS--TGLYDRLTARENLEYFAGLYGLKGDELTA--RLEELADrLGMEElLDRRVGG----FSTGMR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446453387 161 QRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREVADRVVVMYGGRVVEKG 237
Cdd:cd03266 143 QKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKC-ILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-243 |
2.50e-21 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 90.75 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVekeNSKQAIVKHVSFSINEGEIVALVGESGSGKSvtaqSIIGL-------NQESIHIDDGNISfeseELT 77
Cdd:cd03253 1 IEFENVTFAY---DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKS----TILRLlfrfydvSSGSILIDGQDIR----EVT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 78 nlQESewnqIRgKDIAFIFQD-PLssLNPTM----KVGR------QITEVilqhekkskkeaKEIAInllndlgIHEAEK 146
Cdd:cd03253 70 --LDS----LR-RAIGVVPQDtVL--FNDTIgyniRYGRpdatdeEVIEA------------AKAAQ-------IHDKIM 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 147 RF-EQYPHQ-------LSGGMRQRICLAIAFACHPKLVIADEPTTALDVT----IQKQIMELLKERkekqnTSIlLITHD 214
Cdd:cd03253 122 RFpDGYDTIvgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHtereIQAALRDVSKGR-----TTI-VIAHR 195
|
250 260
....*....|....*....|....*....
gi 446453387 215 LALVREvADRVVVMYGGRVVEKGTIEEVI 243
Cdd:cd03253 196 LSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
27-233 |
4.94e-21 |
|
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: 89.39 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQESEWNQIRGKdIAFIFQDplSSLNPT 106
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPT----SGTIRVNGQDVSDLRGRAIPYLRRK-IGVVFQD--FRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 107 MKVGRQI--TEVILQHEKKSKKEAKEIAINLLnDLgiheaEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPTTA 184
Cdd:cd03292 93 RNVYENVafALEVTGVPPREIRKRVPAALELV-GL-----SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446453387 185 LDVTIQKQIMELLKErKEKQNTSILLITHDLALVREVADRVVVMYGGRV 233
Cdd:cd03292 167 LDPDTTWEIMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-246 |
5.55e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 91.23 E-value: 5.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 25 KHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTN-LQESEWNQIRgKDIAFIFQDPLSSL 103
Cdd:PRK13634 24 YDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPT----SGTVTIGERVITAgKKNKKLKPLR-KKVGIVFQFPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 nptmkvgrqITEVILQhekkskkeakEIAINLLNdLGIHEAEKR----------------FEQYPHQLSGGMRQRICLAI 167
Cdd:PRK13634 99 ---------FEETVEK----------DICFGPMN-FGVSEEDAKqkaremielvglpeelLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 168 AFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSP 246
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-240 |
5.60e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 90.13 E-value: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVE-KEnskqaIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqESIHIDDGNISFESEELTNLQESE 83
Cdd:COG0396 1 LEIKNLHVSVEgKE-----ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH--PKYEVTSGSILLDGEDILELSPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 wnqiR-GKDIAFIFQDPLSSlnPTMKVG---RQITEVILQHEKKSKKEAKEIAiNLLNDLGI-HEAEKR-----Feqyph 153
Cdd:COG0396 74 ----RaRAGIFLAFQYPVEI--PGVSVSnflRTALNARRGEELSAREFLKLLK-EKMKELGLdEDFLDRyvnegF----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 154 qlSGGMRQRICLAIAFACHPKLVIADEPTTALDV----TIQKQIMELLKErkekqNTSILLITHDLALVREV-ADRVVVM 228
Cdd:COG0396 142 --SGGEKKRNEILQMLLLEPKLAILDETDSGLDIdalrIVAEGVNKLRSP-----DRGILIITHYQRILDYIkPDFVHVL 214
|
250
....*....|..
gi 446453387 229 YGGRVVEKGTIE 240
Cdd:COG0396 215 VDGRIVKSGGKE 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-251 |
5.89e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.22 E-value: 5.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 18 NSKQAIvKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHID-DGNISFESEELTNlQESEWNQIRgKDIAFIF 96
Cdd:PRK14239 16 NKKKAL-NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTiTGSIVYNGHNIYS-PRTDTVDLR-KEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 97 QDPlsslNP-TMKV------GRQITEVILQHEKKSKKEAKEIAINLLNdlgihEAEKRFEQYPHQLSGGMRQRICLAIAF 169
Cdd:PRK14239 93 QQP----NPfPMSIyenvvyGLRLKGIKDKQVLDEAVEKSLKGASIWD-----EVKDRLHDSALGLSGGQQQRVCIARVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 170 ACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQntSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHP 249
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHK 241
|
..
gi 446453387 250 YT 251
Cdd:PRK14239 242 ET 243
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-252 |
5.94e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 90.36 E-value: 5.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQ---SIIGLNQESIhiDDGNISFESEELTNLQESEWNqirgKDIAFIFQ-- 97
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnRLIELYPEAR--VSGEVYLDGQDIFKMDVIELR----RRVQMVFQip 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 98 DPLSSLN--PTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDlgihEAEKRFEQYPHQLSGGMRQRICLAIAFACHPKL 175
Cdd:PRK14247 92 NPIPNLSifENVALGLKLNRLVKSKKELQERVRWALEKAQLWD----EVKDRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446453387 176 VIADEPTTALDVTIQKQIMELLKERkeKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSPKHPYTK 252
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTE 242
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-241 |
1.09e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.60 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 21 QAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIG-LNQEsihiddGNISFESEELTNLQESEWNQirgkDIAFIFQDP 99
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGfLPYQ------GSLKINGIELRELDPESWRK----HLSWVGQNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 L---SSLNPTMKVGR-QITEVILQHekkskkeakeiainLLNDLGIHEAEKRFEQ---YPHQ-----LSGGMRQRICLAI 167
Cdd:PRK11174 433 QlphGTLRDNVLLGNpDASDEQLQQ--------------ALENAWVSEFLPLLPQgldTPIGdqaagLSVGQAQRLALAR 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446453387 168 AFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTsiLLITHDLALVREVaDRVVVMYGGRVVEKGTIEE 241
Cdd:PRK11174 499 ALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTT--LMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAE 569
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-245 |
3.25e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 88.22 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTlaVEKENskQAIVKHVSFSINEGEIVALVGESGSGKS-----VTAQ---------SIIG--LNQESI----- 62
Cdd:COG1119 3 LLELRNVT--VRRGG--KTILDDISWTVKPGEHWAILGPNGAGKStllslITGDlpptygndvRLFGerRGGEDVwelrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 63 HIddGNISfeSEELTNLQESEwnqiRGKDIAfifqdpLSSLNPTMKVGRQITEVILQHekkskkeakeiAINLLNDLGI- 141
Cdd:COG1119 79 RI--GLVS--PALQLRFPRDE----TVLDVV------LSGFFDSIGLYREPTDEQRER-----------ARELLELLGLa 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 142 HEAEKRFeqypHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREV 221
Cdd:COG1119 134 HLADRPF----GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPG 209
|
250 260
....*....|....*....|....
gi 446453387 222 ADRVVVMYGGRVVEKGTIEEVIGS 245
Cdd:COG1119 210 ITHVLLLKDGRVVAAGPKEEVLTS 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-243 |
3.76e-20 |
|
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: 91.32 E-value: 3.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTlaVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSvtaqSIIGLNQESIHIDDGNISFESEELTNLQ-ES 82
Cdd:TIGR02203 330 DVEFRNVT--FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPRFYEPDSGQILLDGHDLADYTlAS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 83 EWNQIR--GKDIaFIFQDPLSSlNPTMKVGRQITEvilqhekkSKKEAKEIAINLLN-----DLGIHEaekRFEQYPHQL 155
Cdd:TIGR02203 404 LRRQVAlvSQDV-VLFNDTIAN-NIAYGRTEQADR--------AEIERALAAAYAQDfvdklPLGLDT---PIGENGVLL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 156 SGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLkERKEKQNTSiLLITHDLALVrEVADRVVVMYGGRVVE 235
Cdd:TIGR02203 471 SGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAAL-ERLMQGRTT-LVIAHRLSTI-EKADRIVVMDDGRIVE 547
|
....*...
gi 446453387 236 KGTIEEVI 243
Cdd:TIGR02203 548 RGTHNELL 555
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-234 |
5.08e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.85 E-value: 5.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 20 KQAIvKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQESEWNQIRgKDIAFIFQDP 99
Cdd:PRK10908 15 RQAL-QGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPS----AGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 LSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAinlLNDLGIHEAEKRFeqyPHQLSGGMRQRICLAIAFACHPKLVIAD 179
Cdd:PRK10908 89 HLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAA---LDKVGLLDKAKNF---PIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446453387 180 EPTTALDVTIQKQIMELLKERKeKQNTSILLITHDLALVREVADRVVVMYGGRVV 234
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-241 |
5.78e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 90.94 E-value: 5.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 19 SKQAIVKHVSFSINEGEIVALVGESGSGKSvtaqSIIGLNQESIHIDDGNISFESEELTnlqESEWNQIRGKdIAFIFQD 98
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKS----TVAALLQNLYQPTGGQVLLDGVPLV---QYDHHYLHRQ-VALVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 99 PLSslnptmkVGRQITEVILQHEKKSKKEAKEIAINLLN-DLGIHEAEKRF--EQYPH--QLSGGMRQRICLAIAFACHP 173
Cdd:TIGR00958 564 PVL-------FSGSVRENIAYGLTDTPDEEIMAAAKAANaHDFIMEFPNGYdtEVGEKgsQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446453387 174 KLVIADEPTTALDVtiqkQIMELLKERKEKQNTSILLITHDLALVREvADRVVVMYGGRVVEKGTIEE 241
Cdd:TIGR00958 637 RVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQ 699
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-233 |
1.40e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.34 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 25 KHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLqeSEWNQIRgKDIAFIFQDplssln 104
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPAR----GGRIMLNGKEINAL--STAQRLA-RGLVYLPED------ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 105 ptmkvgRQITEVILQhekkskkeaKEIAIN----LLNDLGIHEAEKR----FEQYPHQ--------------LSGGMRQR 162
Cdd:PRK15439 347 ------RQSSGLYLD---------APLAWNvcalTHNRRGFWIKPARenavLERYRRAlnikfnhaeqaartLSGGNQQK 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446453387 163 ICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKeRKEKQNTSILLITHDLALVREVADRVVVMYGGRV 233
Cdd:PRK15439 412 VLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIR-SIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
234-299 |
1.62e-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: 1.62e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446453387 234 VEKGTIEEVIGSPKHPYTKSLLQAIPNIDDSEKVLRAIEGTTPSIETLNSfGCPFVNRCPVAIKEC 299
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPE-GCPFAPRCPFATEEC 65
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-246 |
2.48e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 87.59 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEkenSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqESihIDDGNISFESEELTNLQESEw 84
Cdd:PRK11650 4 LKLQAVRKSYD---GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL--ER--ITSGEIWIGGRVVNELEPAD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqirgKDIAFIFQDplSSLNPTM-------------KVGR-QITEVILQhekkskkeakeiAINLLndlgihEAEKRFEQ 150
Cdd:PRK11650 76 -----RDIAMVFQN--YALYPHMsvrenmayglkirGMPKaEIEERVAE------------AARIL------ELEPLLDR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 151 YPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQiMELlkERKEKQ---NTSILLITHDLALVREVADRVVV 227
Cdd:PRK11650 131 KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRL--EIQRLHrrlKTTSLYVTHDQVEAMTLADRVVV 207
|
250 260 270
....*....|....*....|....*....|.
gi 446453387 228 MYGGRVVEKGTIEEV------------IGSP 246
Cdd:PRK11650 208 MNGGVAEQIGTPVEVyekpastfvasfIGSP 238
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
24-242 |
2.55e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.44 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQES---IHIDDGNISFESEELTNLQESewnqirgkdIAFIFQDPL 100
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSsgrILFDGKPIDYSRKGLMKLRES---------VGMVFQDPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 101 SSLNpTMKVGRQITEVILQHEKKSKKEAKEIAiNLLNDLGIHEAEkrfEQYPHQLSGGMRQRICLAIAFACHPKLVIADE 180
Cdd:PRK13636 93 NQLF-SASVYQDVSFGAVNLKLPEDEVRKRVD-NALKRTGIEHLK---DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453387 181 PTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:PRK13636 168 PTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-247 |
3.24e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.04 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENSKQAI-VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELT-NLQES 82
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPS----SGTITIAGYHITpETGNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 83 EWNQIRgKDIAFIFQDPLSSLnptmkvgrqITEVILQHEK-------KSKKEAKEIAINLLNDLGIheAEKRFEQYPHQL 155
Cdd:PRK13641 79 NLKKLR-KKVSLVFQFPEAQL---------FENTVLKDVEfgpknfgFSEDEAKEKALKWLKKVGL--SEDLISKSPFEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 156 SGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSIlLITHDLALVREVADRVVVMYGGRVVE 235
Cdd:PRK13641 147 SGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVI-LVTHNMDDVAEYADDVLVLEHGKLIK 225
|
250
....*....|..
gi 446453387 236 KGTIEEVIGSPK 247
Cdd:PRK13641 226 HASPKEIFSDKE 237
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-243 |
3.36e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.13 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNIsfeseeltnlqesewnQIRGKdIAFIFqDPLSS 102
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI----LEPTSGRV----------------EVNGR-VSALL-ELGAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 103 LNPTMkVGRQitevilqhekkskkeakEIAIN-LLNDLGIHEAEKRF---------EQYPHQ----LSGGMRQRICLAIA 168
Cdd:COG1134 99 FHPEL-TGRE-----------------NIYLNgRLLGLSRKEIDEKFdeivefaelGDFIDQpvktYSSGMRARLAFAVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446453387 169 FACHPKLVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:COG1134 161 TAVDPDILLVDEVLAVGDAAFQKKCLARIRELRE-SGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
5-237 |
3.40e-19 |
|
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: 84.63 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnQESIHIDDGNISFESEELTNLQeseW 84
Cdd:cd03234 4 LPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEGGGTTSGQILFNGQPRKPDQ---F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQIrgkdIAFIFQDplSSLNPTMKVGRQIT---EVILQHEKKSKKEAKEIAINLLNDLGI-HEAEKRFEQyphqLSGGMR 160
Cdd:cd03234 80 QKC----VAYVRQD--DILLPGLTVRETLTytaILRLPRKSSDAIRKKRVEDVLLRDLALtRIGGNLVKG----ISGGER 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446453387 161 QRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKG 237
Cdd:cd03234 150 RRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-233 |
3.55e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.50 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 2 GQLLSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQE 81
Cdd:PRK11247 10 GTPLLLNAVS----KRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPS----AGELLAGTAPLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 82 sewnqirgkDIAFIFQDplSSLNPTMKVgrqITEVILQHEKKSKKEakeiAINLLNDLGIheaEKRFEQYPHQLSGGMRQ 161
Cdd:PRK11247 82 ---------DTRLMFQD--ARLLPWKKV---IDNVGLGLKGQWRDA----ALQALAAVGL---ADRANEWPAALSGGQKQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453387 162 RICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRV 233
Cdd:PRK11247 141 RVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-237 |
3.58e-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: 84.47 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 26 HVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEELTNLQESEwnqirgKDIAFIFQDP-----L 100
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETP----QSGRVLINGVDVTAAPPAD------RPVSMLFQENnlfahL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 101 S-------SLNPTMK---VGRQITEVILQHekkskkeakeiainllndLGIHEAEKRFeqyPHQLSGGMRQRICLAIAFA 170
Cdd:cd03298 86 TveqnvglGLSPGLKltaEDRQAIEVALAR------------------VGLAGLEKRL---PGELSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446453387 171 CHPKLVIADEPTTALDVTIQKQIMELLKE-RKEKQNTsILLITHDLALVREVADRVVVMYGGRVVEKG 237
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVLDlHAETKMT-VLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
27-236 |
6.08e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 84.75 E-value: 6.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNlqesewnqiRGKDIAFIFQD----PLSS 102
Cdd:PRK11248 20 INLTLESGELLVVLGPSGCGKTTLLNLIAGF----VPYQHGSITLDGKPVEG---------PGAERGVVFQNegllPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 103 LNPTMKVGRQITEVilqhekkSKKEAKEIAINLLNDLGIHEAEKRFeqyPHQLSGGMRQRICLAIAFACHPKLVIADEPT 182
Cdd:PRK11248 87 VQDNVAFGLQLAGV-------EKMQRLEIAHQMLKKVGLEGAEKRY---IWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446453387 183 TALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMY--GGRVVEK 236
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVER 212
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
24-271 |
6.86e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.79 E-value: 6.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQESEwnqIRGKdIAFIFQDPLSSL 103
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQ----RGRVKVMGREVNAENEKW---VRSK-VGLVFQDPDDQV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 nptmkvgrqitevilqhekKSKKEAKEIAINLLN-DLGIHEAEKRFEQY-------------PHQLSGGMRQRICLAIAF 169
Cdd:PRK13647 93 -------------------FSSTVWDDVAFGPVNmGLDKDEVERRVEEAlkavrmwdfrdkpPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 170 ACHPKLVIADEPTTALDVTIQKQIMELLkERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIE--------- 240
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEIL-DRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSlltdedive 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 446453387 241 ------EVIGSPKHPYTKSLLQAIP-NIDDSEKVLRAI 271
Cdd:PRK13647 233 qaglrlPLVAQIFEDLPELGQSKLPlTVKEAVQIIRKL 270
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-258 |
6.90e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.19 E-value: 6.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEkeNSKQAIVKHVSFSINEGEIVALVGESGSGKSvtaqSIIGL-------NQESIHIDDGNISFESEel 76
Cdd:PRK11160 338 SLTLNNVSFTYP--DQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLltrawdpQQGEILLNGQPIADYSE-- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 77 TNLQESewnqirgkdIAFIFQ----------DPLSSLNPtmkvgrQITEVILqhekkskkeakeiaINLLNDLGIH---E 143
Cdd:PRK11160 410 AALRQA---------ISVVSQrvhlfsatlrDNLLLAAP------NASDEAL--------------IEVLQQVGLEkllE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 144 AEKRFEQY----PHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLkeRKEKQNTSILLITHDL-ALv 218
Cdd:PRK11160 461 DDKGLNAWlgegGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELL--AEHAQNKTVLMITHRLtGL- 537
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446453387 219 rEVADRVVVMYGGRVVEKGTIEEVIGspKHPYTKSLLQAI 258
Cdd:PRK11160 538 -EQFDRICVMDNGQIIEQGTHQELLA--QQGRYYQLKQRL 574
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
23-238 |
7.05e-19 |
|
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: 83.70 E-value: 7.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSI---IGLNQESIHIDDGNISfeseeltnlqesewnQIRGKD----IAFI 95
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALfrlVELSSGSILIDGVDIS---------------KIGLHDlrsrISII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 96 FQDPL-------SSLNPTmkvGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKrfeqyphQLSGGMRQRICLAIA 168
Cdd:cd03244 84 PQDPVlfsgtirSNLDPF---GEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGE-------NLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 169 FACHPKLVIADEPTTALDVTIQKQIMELLkeRKEKQNTSILLITHDLALVREvADRVVVMYGGRVVEKGT 238
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTI--REAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-280 |
9.75e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 85.77 E-value: 9.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNLQESE 83
Cdd:PRK09452 14 LVELRGIS----KSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFET----PDSGRIMLDGQDITHVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 wnqirgKDIAFIFQDplSSLNPTMKV------GRQITEVilqhekkskkEAKEIAINLLNDLGIHEAEKRFEQYPHQLSG 157
Cdd:PRK09452 86 ------RHVNTVFQS--YALFPHMTVfenvafGLRMQKT----------PAAEITPRVMEALRMVQLEEFAQRKPHQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 158 GMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDlalvREVA----DRVVVMYGGRV 233
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHD----QEEAltmsDRIVVMRDGRI 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446453387 234 VEKGTIEEVIGSPKHPYTKSLLQAIpNIDD-------SEKVLRA-IEGTTPSIET 280
Cdd:PRK09452 224 EQDGTPREIYEEPKNLFVARFIGEI-NIFDatvierlDEQRVRAnVEGRECNIYV 277
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-234 |
1.45e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.23 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAvekenskqAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELT--NLQE 81
Cdd:COG1129 256 VLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP----ADSGEIRLDGKPVRirSPRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 82 SewnqIRGKdIAFIFQDPLSS-LNPTMKVGRQITEVILQHEKKS----KKEAKEIAINLLNDLGIheaekRF---EQYPH 153
Cdd:COG1129 324 A----IRAG-IAYVPEDRKGEgLVLDLSIRENITLASLDRLSRGglldRRRERALAEEYIKRLRI-----KTpspEQPVG 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 154 QLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITHDLALVREVADRVVVMYGGRV 233
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAA-EGKAVIVISSELPELLGLSDRILVMREGRI 472
|
.
gi 446453387 234 V 234
Cdd:COG1129 473 V 473
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-237 |
1.53e-18 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 82.63 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTlaveKENSKQAIVKHVSFSINEGeIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEELTNLQESew 84
Cdd:cd03264 1 LQLENLT----KRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPP----SSGTIRIDGQDVLKQPQK-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqIRGKdIAFIFQDPlsSLNPTMKVGRQITEVILQHEKKSKKEAKEIaINLLNDLGIHEAEKRfeqYPHQLSGGMRQRIC 164
Cdd:cd03264 70 --LRRR-IGYLPQEF--GVYPNFTVREFLDYIAWLKGIPSKEVKARV-DEVLELVNLGDRAKK---KIGSLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEkqNTSILLITHDLALVREVADRVVVMYGGRVVEKG 237
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
8-233 |
1.56e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 82.90 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 8 ENVTLAVEKENSKQaIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNLQesewNQI 87
Cdd:cd03248 15 QNVTFAYPTRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ----PQGGQVLLDGKPISQYE----HKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 88 RGKDIAFIFQDPLSSlnptmkvGRQITEVI---LQHEKKSKKEAKEIAINllNDLGIHEAEKRFE----QYPHQLSGGMR 160
Cdd:cd03248 86 LHSKVSLVGQEPVLF-------ARSLQDNIaygLQSCSFECVKEAAQKAH--AHSFISELASGYDtevgEKGSQLSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446453387 161 QRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKErkEKQNTSILLITHDLALVrEVADRVVVMYGGRV 233
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYD--WPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-246 |
1.68e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.66 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 21 QAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlnqeSIHIDDGNISFESEELTNLQESEwnqiRGKDIAFIFQDPL 100
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAING----TLTPTAGTVLVAGDDVEALSARA----ASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 101 SSLNPTmkvGRQITEV-ILQHEKKSKKEAKEiainllNDLGIHEAEKRFE--QYPHQ----LSGGMRQRICLAIAFACHP 173
Cdd:PRK09536 88 LSFEFD---VRQVVEMgRTPHRSRFDTWTET------DRAAVERAMERTGvaQFADRpvtsLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446453387 174 KLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLItHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSP 246
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-243 |
2.20e-18 |
|
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: 85.62 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqESIHIDDGNI--------------- 69
Cdd:TIGR03269 1 IEVKNLT----KKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGM--DQYEPTSGRIiyhvalcekcgyver 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 70 -------------SFESEE--LTNLQESEWNQIRgKDIAFIFQDPLSsLNPTMKVGRQITEViLQHEKKSKKEAKEIAIN 134
Cdd:TIGR03269 75 pskvgepcpvcggTLEPEEvdFWNLSDKLRRRIR-KRIAIMLQRTFA-LYGDDTVLDNVLEA-LEEIGYEGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 135 LLNDLGIheaEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHD 214
Cdd:TIGR03269 152 LIEMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHW 228
|
250 260
....*....|....*....|....*....
gi 446453387 215 LALVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEGTPDEVV 257
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-262 |
2.21e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 83.21 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 6 SLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSvTAQSIIG-LnqesIHIDDGNISFESEELTnlqesew 84
Cdd:COG4604 3 EIKNVS----KRYGGKVVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMISrL----LPPDSGEVLVDGLDVA------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nQIRGKDIAFIF----QDPlsSLNPTMKV------GR------QITEVILQHEKKskkeakeiAINLLNdlgIHEAEKRf 148
Cdd:COG4604 67 -TTPSRELAKRLailrQEN--HINSRLTVrelvafGRfpyskgRLTAEDREIIDE--------AIAYLD---LEDLADR- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 149 eqYPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVM 228
Cdd:COG4604 132 --YLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAM 209
|
250 260 270
....*....|....*....|....*....|....
gi 446453387 229 YGGRVVEKGTIEEVIgspkhpyTKSLLQAIPNID 262
Cdd:COG4604 210 KDGRVVAQGTPEEII-------TPEVLSDIYDTD 236
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
23-238 |
3.73e-18 |
|
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: 81.30 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSI---IGLNQESIHIDDGNISfeSEELTNLQESewnqirgkdIAFIFQDP 99
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALfrfLEAEEGKIEIDGIDIS--TIPLEDLRSS---------LTIIPQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 L-------SSLNPtmkvgrqitevilqhekkskkeakeiaINLLNDLGIHEAeKRFEQYPHQLSGGMRQRICLAIAFACH 172
Cdd:cd03369 92 TlfsgtirSNLDP---------------------------FDEYSDEEIYGA-LRVSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453387 173 PKLVIADEPTTALDVT----IQKQImellkeRKEKQNTSILLITHDLalvREVAD--RVVVMYGGRVVEKGT 238
Cdd:cd03369 144 PRVLVLDEATASIDYAtdalIQKTI------REEFTNSTILTIAHRL---RTIIDydKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-246 |
1.15e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.57 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESI------HIDDGNISfeseeltNLQEsewnqIRgKDIAFIFQ 97
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKgkvlvsGIDTGDFS-------KLQG-----IR-KLVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 98 DPlsslnPTMKVGRQITEVILqhEKKSKKEAKEIAINLLNDLGIheAEKRFEQY----PHQLSGGMRQRICLAIAFACHP 173
Cdd:PRK13644 85 NP-----ETQFVGRTVEEDLA--FGPENLCLPPIEIRKRVDRAL--AEIGLEKYrhrsPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446453387 174 KLVIADEPTTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVrEVADRVVVMYGGRVVEKGTIEEVIGSP 246
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKT-IVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-233 |
3.03e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 7 LENVTLAVekenSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFEseeltnlqesewnq 86
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGE----LEPDSGEVSIP-------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 87 iRGKDIAFIFQDP------------LSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAI-NLLNDLGIHEAEKR------ 147
Cdd:COG0488 59 -KGLRIGYLPQEPpldddltvldtvLDGDAELRALEAELEELEAKLAEPDEDLERLAELqEEFEALGGWEAEARaeeils 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 148 ---FEQYPHQ-----LSGGMRQRICLAIAFACHPKLVIADEPTTALDV-TIQKqIMELLKERKekqnTSILLITHDLALV 218
Cdd:COG0488 138 glgFPEEDLDrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEW-LEEFLKNYP----GTVLVVSHDRYFL 212
|
250
....*....|....*
gi 446453387 219 REVADRVVVMYGGRV 233
Cdd:COG0488 213 DRVATRILELDRGKL 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-246 |
4.12e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.03 E-value: 4.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 14 VEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNIsfeseelTNLQESEWNQIRG--KD 91
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSP----DAGKI-------TVLGVPVPARARLarAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 92 IAFIFQdpLSSLNPTMKVgRQITEVILQHEKKSKKEAKEIAINLLNdlgIHEAEKRFEQYPHQLSGGMRQRICLAIAFAC 171
Cdd:PRK13536 116 IGVVPQ--FDNLDLEFTV-RENLLVFGRYFGMSTREIEAVIPSLLE---FARLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 172 HPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREVADRVVVMYGGRVVEKGT----IEEVIGSP 246
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVLEAGRKIAEGRphalIDEHIGCQ 267
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-252 |
4.47e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.70 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 21 QAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQ-ESIHIDDGNISFESEELTNlQESEWNQIRgKDIAFIFQDP 99
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElESEVRVEGRVEFFNQNIYE-RRVNLNRLR-RQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 lsSLNPtMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGI-HEAEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIA 178
Cdd:PRK14258 98 --NLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLwDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 179 DEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYG-----GRVVEKGTIEEVIGSPKHPYTK 252
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTR 253
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
29-238 |
4.67e-17 |
|
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: 78.74 E-value: 4.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 29 FSINEGEIVALVGESGSGKSVTAQSIIGL---NQESIHIDDGNISFESEELTNL-QESEwnqirgkdiaFIFQDPLSSLN 104
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLippAKGTVKVAGASPGKGWRHIGYVpQRHE----------FAWDFPISVAH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 105 PTMKvGRQITEVILQHEKKSKKEAKEIAinlLNDLGIHEAEKRfeqyP-HQLSGGMRQRICLAIAFACHPKLVIADEPTT 183
Cdd:TIGR03771 71 TVMS-GRTGHIGWLRRPCVADFAAVRDA---LRRVGLTELADR----PvGELSGGQRQRVLVARALATRPSVLLLDEPFT 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446453387 184 ALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREVADRvVVMYGGRVVEKGT 238
Cdd:TIGR03771 143 GLDMPTQELLTELFIELAGAGTA-ILMTTHDLAQAMATCDR-VVLLNGRVIADGT 195
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
28-233 |
5.46e-17 |
|
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: 78.36 E-value: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 28 SFSINEGEIVALVGESGSGKSVTAQSIIGLN---QESIHIDDGNIsfeseelTNLQESEwnqirgKDIAFIFQDplSSLN 104
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIepaSGSIKVNDQSH-------TGLAPYQ------RPVSMLFQE--NNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 105 PTMKVGRQITEVIlqhekkskkeAKEIAINLLNDLGIHEAEKR------FEQYPHQLSGGMRQRICLAIAFACHPKLVIA 178
Cdd:TIGR01277 83 AHLTVRQNIGLGL----------HPGLKLNAEQQEKVVDAAQQvgiadyLDRLPEQLSGGQRQRVALARCLVRPNPILLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446453387 179 DEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRV 233
Cdd:TIGR01277 153 DEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-228 |
7.41e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 77.27 E-value: 7.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 21 QAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIhiddGNISfeseeltnlqesewnQIRGKDIAFIFQdpL 100
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTS----GTVR---------------RAGGARVAYVPQ--R 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 101 SSLNPTMKVG-RQITEVIL-QHEKK---SKKEAKEIAINLLNDLGIHEAEKRfeQYpHQLSGGMRQRICLAIAFACHPKL 175
Cdd:NF040873 64 SEVPDSLPLTvRDLVAMGRwARRGLwrrLTRDDRAAVDDALERVGLADLAGR--QL-GELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446453387 176 VIADEPTTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREvADRVVVM 228
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHARGAT-VVVVTHDLELVRR-ADPCVLL 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-237 |
9.79e-17 |
|
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: 77.21 E-value: 9.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENSKQ--AIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlnQESIHIDDGNISFESeelTNLQES 82
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG--RRTGLGVSGEVLING---RPLDKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 83 EWNQIrgkdIAFIFQDplSSLNPTMKVgRQitevilqhekkskkeakeiaiNLLndlgiHEAEKRfeqyphQLSGGMRQR 162
Cdd:cd03213 79 SFRKI----IGYVPQD--DILHPTLTV-RE---------------------TLM-----FAAKLR------GLSGGERKR 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446453387 163 ICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKeRKEKQNTSILLITHDL-ALVREVADRVVVMYGGRVVEKG 237
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLR-RLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
24-237 |
2.09e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 77.37 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGnisfeseELTNLQESEWNQIRG--KDIAFIFQD--- 98
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGL----LQPTSG-------EVRVAGLVPWKRRKKflRRIGVVFGQktq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 99 ------PLSSLNptmkvgrqitevILQHEKKSKKEAKEIAINLLNDLgiHEAEKRFEQYPHQLSGGMRQRICLAIAFACH 172
Cdd:cd03267 106 lwwdlpVIDSFY------------LLAAIYDLPPARFKKRLDELSEL--LDLEELLDTPVRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446453387 173 PKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKG 237
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
7-246 |
2.48e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.92 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 7 LENVTLAVEKENSKQAIvKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELT--NLQEsew 84
Cdd:PRK13652 4 IETRDLCYSYSGSKEAL-NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPT----SGSVLIRGEPITkeNIRE--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqIRgKDIAFIFQDPLSSL-NPTMK-------VGRQITEVILQHEKKSKkeakeiainlLNDLGIHEAEKRFeqyPHQLS 156
Cdd:PRK13652 76 --VR-KFVGLVFQNPDDQIfSPTVEqdiafgpINLGLDEETVAHRVSSA----------LHMLGLEELRDRV---PHHLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 157 GGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEK 236
Cdd:PRK13652 140 GGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
250
....*....|
gi 446453387 237 GTIEEVIGSP 246
Cdd:PRK13652 220 GTVEEIFLQP 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-242 |
3.61e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.47 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSVTAQSIIGL---NQESIHIDDGNISFESeeltnlQESEWNQIRgKDIAFIFQDPLSSL 103
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlqpTEGKVTVGDIVVSSTS------KQKEIKPVR-KKVGVVFQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 nptmkvgrqITEVIL-------QHEKKSKKEAKEIAINLLNDLGIheAEKRFEQYPHQLSGGMRQRICLAIAFACHPKLV 176
Cdd:PRK13643 98 ---------FEETVLkdvafgpQNFGIPKEKAEKIAAEKLEMVGL--ADEFWEKSPFELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446453387 177 IADEPTTALDVTIQKQIMELLkERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLF-ESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-243 |
4.68e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.99 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENSkqaIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNLQESEW 84
Cdd:PRK10790 341 IDIDNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP----LTEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 NQirgkDIAFIFQDPL---SSLNPTMKVGRQITEVILQHEKKSKKeakeiainlLNDL------GIHeaeKRFEQYPHQL 155
Cdd:PRK10790 414 RQ----GVAMVQQDPVvlaDTFLANVTLGRDISEEQVWQALETVQ---------LAELarslpdGLY---TPLGEQGNNL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 156 SGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLkeRKEKQNTSILLITHDLALVREvADRVVVMYGGRVVE 235
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL--AAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
....*...
gi 446453387 236 KGTIEEVI 243
Cdd:PRK10790 555 QGTHQQLL 562
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-246 |
5.68e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.61 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 36 IVALVGESGSGKSVTAQSIIGLnqesIHIDDGNIS------FESEELTNLQEsewNQIRgkdIAFIFQDplSSLNPTMKV 109
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGL----TRPQKGRIVlngrvlFDAEKGICLPP---EKRR---IGYVFQD--ARLFPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 110 grqitEVILQHEKKSKKEAKEIAINLLndLGIheaEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTI 189
Cdd:PRK11144 94 -----RGNLRYGMAKSMVAQFDKIVAL--LGI---EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446453387 190 QKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGSP 246
Cdd:PRK11144 164 KRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-243 |
1.96e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.98 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVE-KENskqAIVKHVSFSINEGEIVALVGESGSGKSVTAQSII---GLNQESIHIDDGNIsfESEELTNLQ 80
Cdd:PRK11176 342 IEFRNVTFTYPgKEV---PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTrfyDIDEGEILLDGHDL--RDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 81 E-----SE----WNQIRGKDIAFIFQDPLSSlnptmkvgRQITEVI-LQHekkskkeakeiAINLLNDLgiheaEKRFEQ 150
Cdd:PRK11176 417 NqvalvSQnvhlFNDTIANNIAYARTEQYSR--------EQIEEAArMAY-----------AMDFINKM-----DNGLDT 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 151 YPHQ----LSGGMRQRICLAIAFACHPKLVIADEPTTALDV----TIQKQIMELLKERkekqnTSiLLITHDLALVrEVA 222
Cdd:PRK11176 473 VIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTeserAIQAALDELQKNR-----TS-LVIAHRLSTI-EKA 545
|
250 260
....*....|....*....|.
gi 446453387 223 DRVVVMYGGRVVEKGTIEEVI 243
Cdd:PRK11176 546 DEILVVEDGEIVERGTHAELL 566
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-236 |
2.64e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.84 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 13 AVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlnqesihiddgnisfeseELTNLQESEWNQIrgkdi 92
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG------------------ALKGTPVAGCVDV----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 93 afifqdplsslnPTMKVGRQITevILQHEKKSKKEAKeiAINLLNDLGIHEAEKRFEQYPHqLSGGMRQRICLAIAFACH 172
Cdd:COG2401 92 ------------PDNQFGREAS--LIDAIGRKGDFKD--AVELLNAVGLSDAVLWLRRFKE-LSTGQKFRFRLALLLAER 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 173 PKLVIADEPTTALDVTIQK----QIMELLKERKekqnTSILLITHDLALVREVADRVVVM--YGGRVVEK 236
Cdd:COG2401 155 PKLLVIDEFCSHLDRQTAKrvarNLQKLARRAG----ITLVVATHHYDVIDDLQPDLLIFvgYGGVPEEK 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-237 |
2.82e-15 |
|
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: 73.72 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISfeseeltnlqesewnqIRGKDIAFIfqDPLSS 102
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI----YPPDSGTVT----------------VRGRVSSLL--GLGGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 103 LNPTMkVGRQitevilqhekkskkeakEIAIN-LLNDLGIHEAEKRF---------EQYPHQ----LSGGMRQRICLAIA 168
Cdd:cd03220 95 FNPEL-TGRE-----------------NIYLNgRLLGLSRKEIDEKIdeiiefselGDFIDLpvktYSSGMKARLAFAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 169 FACHPKLVIADEPTTALDVTIQKQIMELLKERKeKQNTSILLITHDLALVREVADRVVVMYGGRVVEKG 237
Cdd:cd03220 157 TALEPDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-242 |
2.93e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.04 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 7 LENVTLAVEKENSKQ-AIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGL-NQESIHIDDGNISFESeeltNLQE-SE 83
Cdd:PRK13645 9 LDNVSYTYAKKTPFEfKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiISETGQTIVGDYAIPA----NLKKiKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WNQIRgKDIAFIFQDPLSSL-NPTMKVGRQITEVILQHEKKSKKEAKEIAINLlndlgIHEAEKRFEQYPHQLSGGMRQR 162
Cdd:PRK13645 85 VKRLR-KEIGLVFQFPEYQLfQETIEKDIAFGPVNLGENKQEAYKKVPELLKL-----VQLPEDYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 163 ICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
27-243 |
3.48e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 74.74 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEELTNLQESEWNQIRGKDIafIFQDPLSSLNPT 106
Cdd:PRK13651 26 VSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLP----DTGTIEWIFKDEKNKKKTKEKEKVLEKL--VIQKTRFKKIKK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 107 MKVGRQITEVILQ---HEKKSKKEAKEIAINLLNdLGI--HEAEKRFEQY--------------PHQLSGGMRQRICLAI 167
Cdd:PRK13651 100 IKEIRRRVGVVFQfaeYQLFEQTIEKDIIFGPVS-MGVskEEAKKRAAKYielvgldesylqrsPFELSGGQKRRVALAG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446453387 168 AFACHPKLVIADEPTTALDVTIQKQIMELLKERkEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-245 |
4.31e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.46 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 14 VEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTnlqeSEWNQIRGKdIA 93
Cdd:PRK13537 13 VEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL----THPDAGSISLCGEPVP----SRARHARQR-VG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 94 FIFQdpLSSLNPTMKVgRQITEVILQHEKKSKKEAKEIAINLLNdlgIHEAEKRFEQYPHQLSGGMRQRICLAIAFACHP 173
Cdd:PRK13537 84 VVPQ--FDNLDPDFTV-RENLLVFGRYFGLSAAAARALVPPLLE---FAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453387 174 KLVIADEPTTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVIGS 245
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-247 |
4.67e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.07 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 9 NVTLA-VEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTNLQESEwnqi 87
Cdd:PRK11000 3 SVTLRnVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGDLFIGEKRMNDVPPAE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 88 RGkdIAFIFQD----PLSSLNPTMKVG------------RQITEV--ILQhekkskkeakeiainllndLGiHEAEKRfe 149
Cdd:PRK11000 75 RG--VGMVFQSyalyPHLSVAENMSFGlklagakkeeinQRVNQVaeVLQ-------------------LA-HLLDRK-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 150 qyPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQI-MELLKERKEKQNTSIlLITHDLALVREVADRVVVM 228
Cdd:PRK11000 131 --PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMrIEISRLHKRLGRTMI-YVTHDQVEAMTLADKIVVL 207
|
250 260 270
....*....|....*....|....*....|.
gi 446453387 229 YGGRVVEKGTIEEV------------IGSPK 247
Cdd:PRK11000 208 DAGRVAQVGKPLELyhypanrfvagfIGSPK 238
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-243 |
5.46e-15 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 75.93 E-value: 5.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQESEWNQIrgkdIAFIFQDPLss 102
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR----SGEILLNGFSLKDIDRHTLRQF----INYLPQEPY-- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 103 lnptMKVGRQITEVILQHEKKSKKEAKEIAINllndlgIHEAEKRFEQYPH-----------QLSGGMRQRICLAIAFAC 171
Cdd:TIGR01193 559 ----IFSGSILENLLLGAKENVSQDEIWAACE------IAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453387 172 HPKLVIADEPTTALDVTIQKQIMELLKERKEKqntSILLITHDLAlVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGSHDELL 696
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-242 |
6.94e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.95 E-value: 6.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihiddGNISFESEELTNLQESEWNQIRgkdiAFIFQDplSSLNPT 106
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-----GEILLNGRPLSDWSAAELARHR----AYLSQQ--QSPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 107 MKVGRQITeviLQHEKKSKKEAKEIAIN-LLNDLGIheaEKRFEQYPHQLSGGMRQRICLAIAF-----ACHP--KLVIA 178
Cdd:COG4138 84 MPVFQYLA---LHQPAGASSEAVEQLLAqLAEALGL---EDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446453387 179 DEPTTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELCQQGIT-VVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-228 |
9.52e-15 |
|
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: 70.17 E-value: 9.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKenskQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlnqeSIHIDDGNISfeseeltnlqesew 84
Cdd:cd03221 1 IELENLSKTYGG----KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG----ELEPDEGIVT-------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqirgkdiafifqdplssLNPTMKVGrqitevilqhekkskkeakeiainllndlgiheaekrfeqYPHQLSGGMRQRIC 164
Cdd:cd03221 59 ------------------WGSTVKIG----------------------------------------YFEQLSGGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKErkekQNTSILLITHDLALVREVADRVVVM 228
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDLESIEALEEALKE----YPGTVILVSHDRYFLDQVATKIIEL 140
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
23-243 |
1.35e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.23 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEELTNLQESEwNQIRGkdIAFIFQDP--- 99
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPR----DAGNIIIDDEDISLLPLHA-RARRG--IGYLPQEAsif 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 --LSSLNPTMKVgRQITEVILQHEKKSKkeakeiAINLLNDLGIHEAEKRFEQyphQLSGGMRQRICLAIAFACHPKLVI 177
Cdd:PRK10895 91 rrLSVYDNLMAV-LQIRDDLSAEQREDR------ANELMEEFHIEHLRDSMGQ---SLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 178 ADEPTTALD---VTIQKQIMELLKERkekqNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:PRK10895 161 LDEPFAGVDpisVIDIKRIIEHLRDS----GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
24-252 |
1.84e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.12 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQ--ESIHIDdGNISFESEELtNLQESEWNQIRgKDIAFIFQDPls 101
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFRVE-GKVTFHGKNL-YAPDVDPVEVR-RRIGMVFQKP-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 102 slNPTMKvgrQITEVIL---QHEKKSKKEAKEIAINLLNDLGIHEAEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIA 178
Cdd:PRK14243 101 --NPFPK---SIYDNIAygaRINGYKGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 179 DEPTTALDVTIQKQIMELLKERKEKQntSILLITHDLALVREVADRV------VVMYGGRV---VEKGTIEEVIGSPKHP 249
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTaffnveLTEGGGRYgylVEFDRTEKIFNSPQQQ 253
|
...
gi 446453387 250 YTK 252
Cdd:PRK14243 254 ATR 256
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
24-246 |
2.25e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 71.94 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQEsewNQIRGKDIAFIFQDplssl 103
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPT----GGTILLRGQHIEGLPG---HQIARMGVVRTFQH----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 nptMKVGRQITEV----ILQHEKKSKKeakeIAINLLNDLGIHEAEKRFEQYPHQ-----------------LSGGMRQR 162
Cdd:PRK11300 89 ---VRLFREMTVIenllVAQHQQLKTG----LFSGLLKTPAFRRAESEALDRAATwlervgllehanrqagnLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 163 ICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
....
gi 446453387 243 IGSP 246
Cdd:PRK11300 242 RNNP 245
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-242 |
3.74e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 21 QAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELtNLQESEWNQIRgKDIAFIFQDPl 100
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL----LRPQKGAVLWQGKPL-DYSKRGLLALR-QQVATVFQDP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 101 sslnptmkvGRQI--TEVilqhekkskkeAKEIAINLLNdLGIHEAE--------------KRFEQYPHQ-LSGGMRQRI 163
Cdd:PRK13638 87 ---------EQQIfyTDI-----------DSDIAFSLRN-LGVPEAEitrrvdealtlvdaQHFRHQPIQcLSHGQKKRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 164 CLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKeRKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:PRK13638 146 AIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIR-RIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-235 |
3.75e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihIDDGNISFESEELTnlQESEWNQIRgKDIAFIFQD----- 98
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK----RAGGEIRLNGKDIS--PRSPLDAVK-KGMAYITESrrdng 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 99 --PLSSLNPTMKVGRQITEVILQHE--KKSKKEAKEIAINLLNDLGIHEAEkrFEQYPHQLSGGMRQRICLAIAFACHPK 174
Cdd:PRK09700 352 ffPNFSIAQNMAISRSLKDGGYKGAmgLFHEVDEQRTAENQRELLALKCHS--VNQNITELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446453387 175 LVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITHDLALVREVADRVVVMYGGRVVE 235
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-242 |
3.97e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.33 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlnqeSIHIDDGNISFESEELTNLQESEWNQIRgKDIAFIFQDplSS 102
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGG----QIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQS--GA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 103 LNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRFeqyPHQLSGGMRQRICLAIAFACHPKLVIADEPT 182
Cdd:PRK11831 95 LFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 183 TALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:PRK11831 172 VGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-241 |
4.30e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.16 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHIDdGNIsfeseeLTNLQESEWNQIRgKDIAFIFQDPLss 102
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGS-GSV------LLNGMPIDAKEMR-AISAYVQQDDL-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 103 LNPTM------------KVGRQITEVILQHEKKskkeakeiaiNLLNDLGIHEAEKRFEQYPHQ---LSGGMRQRIclai 167
Cdd:TIGR00955 110 FIPTLtvrehlmfqahlRMPRRVTKKEKRERVD----------EVLQALGLRKCANTRIGVPGRvkgLSGGERKRL---- 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446453387 168 AFACH----PKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEE 241
Cdd:TIGR00955 176 AFASElltdPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
5-238 |
4.67e-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: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKEnskQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGL---NQESIHIDDGNISfeseELTnlQE 81
Cdd:COG5265 358 VRFENVSFGYDPE---RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFydvTSGRILIDGQDIR----DVT--QA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 82 SewnqIRgKDIAFIFQDPLssL-NPTMKV----GR------QITEVI-LQHekkskkeakeiainllndlgIHEaekrF- 148
Cdd:COG5265 429 S----LR-AAIGIVPQDTV--LfNDTIAYniayGRpdaseeEVEAAArAAQ--------------------IHD----Fi 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 149 EQYPHQ-----------LSGGMRQRIclAIAFAC--HPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTsiLLITHDL 215
Cdd:COG5265 478 ESLPDGydtrvgerglkLSGGEKQRV--AIARTLlkNPPILIFDEATSALDSRTERAIQAALREVARGRTT--LVIAHRL 553
|
250 260
....*....|....*....|...
gi 446453387 216 ALVREvADRVVVMYGGRVVEKGT 238
Cdd:COG5265 554 STIVD-ADEILVLEAGRIVERGT 575
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-233 |
5.31e-14 |
|
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: 72.55 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTlAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGL----NQESIHIDDGNIsfeseELTNL 79
Cdd:TIGR02633 257 ILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAypgkFEGNVFINGKPV-----DIRNP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 80 QESewnqIRGKdIAFIFQD-PLSSLNPTMKVGRQITEVILQHEKKSKKeakeiaINLLNDLG-IHEAEKRFE---QYPH- 153
Cdd:TIGR02633 331 AQA----IRAG-IAMVPEDrKRHGIVPILGVGKNITLSVLKSFCFKMR------IDAAAELQiIGSAIQRLKvktASPFl 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 154 ---QLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKeKQNTSILLITHDLALVREVADRVVVMYG 230
Cdd:TIGR02633 400 pigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLA-QEGVAIIVVSSELAEVLGLSDRVLVIGE 478
|
...
gi 446453387 231 GRV 233
Cdd:TIGR02633 479 GKL 481
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
21-215 |
5.71e-14 |
|
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: 72.39 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 21 QAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEWNQIrgkdIAFIFQDP- 99
Cdd:TIGR02868 348 PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL----LDPLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQDAh 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 --LSSLNPTMKVGR------QITEVILqhekkskkeakeiAINLLNDLG---------IHEAEKRfeqyphqLSGGMRQR 162
Cdd:TIGR02868 420 lfDTTVRENLRLARpdatdeELWAALE-------------RVGLADWLRalpdgldtvLGEGGAR-------LSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446453387 163 ICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLkeRKEKQNTSILLITHDL 215
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-243 |
6.34e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.00 E-value: 6.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 26 HVSFSINEGEIVALVGESGSGKSVTAQSIIG-LNQESihiddGNISFESEELTNLQESEwnqirgKDIAFIFQDplSSLN 104
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGfLTPAS-----GSLTLNGQDHTTTPPSR------RPVSMLFQE--NNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 105 PTMKVGRQITEVI---LQHEKKSKKEAKEIAinllNDLGIHEAEKRFeqyPHQLSGGMRQRICLAIAFACHPKLVIADEP 181
Cdd:PRK10771 84 SHLTVAQNIGLGLnpgLKLNAAQREKLHAIA----RQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453387 182 TTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-218 |
8.47e-14 |
|
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: 68.92 E-value: 8.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 7 LENVTLAVEKenSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQEsewnq 86
Cdd:TIGR01189 1 LAARNLACSR--GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGL----LRPDSGEVRWNGTPLAEQRD----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 87 IRGKDIAFIFQdpLSSLNPTMKVGRQITevILQHEKKSKKEAKEIAINLLNDLGiheaekrFEQYP-HQLSGGMRQRICL 165
Cdd:TIGR01189 70 EPHENILYLGH--LPGLKPELSALENLH--FWAAIHGGAQRTIEDALAAVGLTG-------FEDLPaAQLSAGQQRRLAL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446453387 166 AIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNtSILLITH-DLALV 218
Cdd:TIGR01189 139 ARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGG-IVLLTTHqDLGLV 191
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-246 |
9.95e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 71.67 E-value: 9.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 19 SKQAIVKHVSFSINEGEIVALVGESGSGKSvtaqSIIGLNQESIHIDDGNISFESEELTNLQESEWnqiRGK-----DIA 93
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW---RSRlavvsQTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 94 FIFQDPLSSlnpTMKVGR------QITEVIlqhekkskkeakeiaiNLLNdlgIHEAEKRFEQ-YPHQ-------LSGGM 159
Cdd:PRK10789 399 FLFSDTVAN---NIALGRpdatqqEIEHVA----------------RLAS---VHDDILRLPQgYDTEvgergvmLSGGQ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 160 RQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQntSILLITHDLALVREvADRVVVMYGGRVVEKGTI 239
Cdd:PRK10789 457 KQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTE-ASEILVMQHGHIAQRGNH 533
|
....*..
gi 446453387 240 EEVIGSP 246
Cdd:PRK10789 534 DQLAQQS 540
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-233 |
1.80e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTlAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihiDDGNISFESEELT--NLQES 82
Cdd:PRK13549 260 LEVRNLT-AWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGR---WEGEIFIDGKPVKirNPQQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 83 EWNQI------RGKDiafifqdplsSLNPTMKVGRQITEVILQHEKKSKKeakeiaINLLNDLG-IHEAEKRF------- 148
Cdd:PRK13549 336 IAQGIamvpedRKRD----------GIVPVMGVGKNITLAALDRFTGGSR------IDDAAELKtILESIQRLkvktasp 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 149 EQYPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDV----TIQKQIMELLkerkeKQNTSILLITHDLALVREVADR 224
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQLV-----QQGVAIIVISSELPEVLGLSDR 474
|
....*....
gi 446453387 225 VVVMYGGRV 233
Cdd:PRK13549 475 VLVMHEGKL 483
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-242 |
2.07e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.58 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNIsfeseeltNLQESEWNQIRGKD-----IAFIFQ- 97
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT----KGTI--------TINNINYNKLDHKLaaqlgIGIIYQe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 98 ----DPLSSLNpTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHeaeKRFEQYPHQLSGGMRQRICLAIAFACHP 173
Cdd:PRK09700 89 lsviDELTVLE-NLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLK---VDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453387 174 KLVIADEPTTAL---DVTIQKQIMELLKerkeKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:PRK09700 165 KVIIMDEPTSSLtnkEVDYLFLIMNQLR----KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-226 |
2.31e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 1 MGQLLSLENVTLAVekenSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESeeltnlq 80
Cdd:PRK09544 1 MTSLVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGL----VAPDEGVIKRNG------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 81 esewnQIRgkdIAFIFQDplSSLNPTM--KVGRQITeviLQHEKKSKkeakeiaiNLLNDLGIHEAEKRFEQYPHQLSGG 158
Cdd:PRK09544 66 -----KLR---IGYVPQK--LYLDTTLplTVNRFLR---LRPGTKKE--------DILPALKRVQAGHLIDAPMQKLSGG 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446453387 159 MRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVV 226
Cdd:PRK09544 125 ETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-240 |
2.51e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFeseeltnLQESEWNQIRGKDIAFIFQD----- 98
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGF----VRLASGKISI-------LGQPTRQALQKNLVAYVPQSeevdw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 99 --PLSSLNPTMkVGRQITEVILQHEKKSKKEAKEIAINLLNDLgiheaEKRFEQYpHQLSGGMRQRICLAIAFACHPKLV 176
Cdd:PRK15056 92 sfPVLVEDVVM-MGRYGHMGWLRRAKKRDRQIVTAALARVDMV-----EFRHRQI-GELSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446453387 177 IADEPTTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREVADrVVVMYGGRVVEKGTIE 240
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRELRDEGKT-MLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTE 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-231 |
4.44e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.84 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 2 GQLLSLENVTLAvekENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesihiddgnisfeseeltnlqe 81
Cdd:COG4178 360 DGALALEDLTLR---TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL------------------------ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 82 seWN----QIR---GKDIAFIFQDP---LSSL-------NPTMKVGR-QITEVilqhekkskkeakeiainlLNDLGIHE 143
Cdd:COG4178 413 --WPygsgRIArpaGARVLFLPQRPylpLGTLreallypATAEAFSDaELREA-------------------LEAVGLGH 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 144 AEKRFEQ---YPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLkeRKEKQNTSILLITHDLALvRE 220
Cdd:COG4178 472 LAERLDEeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLL--REELPGTTVISVGHRSTL-AA 548
|
250
....*....|.
gi 446453387 221 VADRVVVMYGG 231
Cdd:COG4178 549 FHDRVLELTGD 559
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-242 |
5.07e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihiddGNISFESEELTNLQESEWNQIRgkdiAFIFQDplSSLNPT 106
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-----GSIQFAGQPLEAWSAAELARHR----AYLSQQ--QTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 107 MKVGRQITeviLQHEKKSKKEAKEIAINLLND-LGIheaEKRFEQYPHQLSGGMRQRICLAIAF-----ACHP--KLVIA 178
Cdd:PRK03695 84 MPVFQYLT---LHQPDKTRTEAVASALNEVAEaLGL---DDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446453387 179 DEPTTALDVTIQKQIMELLKERKEkQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-232 |
6.39e-13 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 66.72 E-value: 6.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENSKQA-IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlnqeSIHIDDGNISFeseeltnlqese 83
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG----ELEKLSGSVSV------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 wnqirGKDIAFIFQDP-LssLNPTMKvgrqitEVILQHEKKSKKEAKEI--AINLLNDLgiheaekrfEQYPHQ------ 154
Cdd:cd03250 65 -----PGSIAYVSQEPwI--QNGTIR------ENILFGKPFDEERYEKVikACALEPDL---------EILPDGdlteig 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 155 -----LSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIME--LLKERKEkqNTSILLITHDLALVREvADRVVV 227
Cdd:cd03250 123 ekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLPH-ADQIVV 199
|
....*
gi 446453387 228 MYGGR 232
Cdd:cd03250 200 LDNGR 204
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-235 |
8.34e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.05 E-value: 8.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHidDGNISFESEELT--NLQESEwnqirGKDIAFIFQD----PL 100
Cdd:NF040905 20 VNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSY--EGEILFDGEVCRfkDIRDSE-----ALGIVIIHQElaliPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 101 SSLNPTMKVGRQITE--VILQHEKKSKkeakeiAINLLNDLGIHEAekrfeqyPHQLSG----GMRQRICLAIAFACHPK 174
Cdd:NF040905 93 LSIAENIFLGNERAKrgVIDWNETNRR------ARELLAKVGLDES-------PDTLVTdigvGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446453387 175 LVIADEPTTALDVTIQKQIMELLKERKEKQNTSILlITHDLALVREVADRVVVMYGGRVVE 235
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELKAQGITSII-ISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-241 |
9.02e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.94 E-value: 9.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 3 QLLSLENVTLAVEKENskqaIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlnqeSIHIDDGNIsfeseeltnlqes 82
Cdd:COG0488 314 KVLELEGLSKSYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG----ELEPDSGTV------------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 83 ewnqIRGK--DIAFIFQDpLSSLNPTMKVgrqiTEVILQHEKKSKKEAkeiAINLLNDLGIHEAekRFEQYPHQLSGGMR 160
Cdd:COG0488 373 ----KLGEtvKIGYFDQH-QEELDPDKTV----LDELRDGAPGGTEQE---VRGYLGRFLFSGD--DAFKPVGVLSGGEK 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 161 QRICLAIAFACHPKLVIADEPTTALDV-TIQkQIMELLKERKEkqntSILLITHDLALVREVADRVVVMYGGRVVEK-GT 238
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDIeTLE-ALEEALDDFPG----TVLLVSHDRYFLDRVATRILEFEDGGVREYpGG 513
|
...
gi 446453387 239 IEE 241
Cdd:COG0488 514 YDD 516
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-234 |
1.51e-12 |
|
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: 65.75 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 2 GQLLSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHIDdGNISFEseeltNLQE 81
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVE-GDIHYN-----GIPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 82 SEWNQIRGKDIAFIFQDPLSslNPTMKVGRQItevilqhekkskkeakEIAINLLNDlgiheaekrfeQYPHQLSGGMRQ 161
Cdd:cd03233 75 KEFAEKYPGEIIYVSEEDVH--FPTLTVRETL----------------DFALRCKGN-----------EFVRGISGGERK 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446453387 162 RICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLAL-VREVADRVVVMYGGRVV 234
Cdd:cd03233 126 RVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQI 199
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-232 |
2.56e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 1 MGQLLSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesiHID-DGNISFESEELT-- 77
Cdd:PRK13549 2 MEYLLEMKNIT----KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP---HGTyEGEIIFEGEELQas 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 78 NLQESEwnqirGKDIAFIFQDplSSLNPTMKVGRQI--TEVILQHEKKSKKEAKEIAINLLNDLGIH-EAEKRFEQYphq 154
Cdd:PRK13549 75 NIRDTE-----RAGIAIIHQE--LALVKELSVLENIflGNEITPGGIMDYDAMYLRAQKLLAQLKLDiNPATPVGNL--- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446453387 155 lSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKqNTSILLITHDLALVREVADRVVVMYGGR 232
Cdd:PRK13549 145 -GLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-246 |
3.59e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.58 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 6 SLENVTLAVekenSKQAIVKHVSFSINEGEIVALVGESGSGKSvTAQSIIGLNQESihiDDGNISFESEELtnlqeSEWN 85
Cdd:PRK10575 13 ALRNVSFRV----PGRTLLHPLSLTFPAGKVTGLIGHNGSGKS-TLLKMLGRHQPP---SEGEILLDAQPL-----ESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 86 -QIRGKDIAFIFQDPLSSLNPTMK----VGRQITEVILQHEKKSKKEAKEIAINLLndlGIHEAEKRFEQyphQLSGGMR 160
Cdd:PRK10575 80 sKAFARKVAYLPQQLPAAEGMTVRelvaIGRYPWHGALGRFGAADREKVEEAISLV---GLKPLAHRLVD---SLSGGER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 161 QRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIE 240
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPA 233
|
....*.
gi 446453387 241 EVIGSP 246
Cdd:PRK10575 234 ELMRGE 239
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-243 |
6.60e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.01 E-value: 6.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 8 ENVTLAVekenSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQESEwnqi 87
Cdd:PRK10253 11 EQLTLGY----GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA----HGHVWLDGEHIQHYASKE---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 88 RGKDIAFIFQDPLSSLNPTMKV----GRQITEVILQHEKKSKKEAKEIAinlLNDLGIHEAEKrfeQYPHQLSGGMRQRI 163
Cdd:PRK10253 79 VARRIGLLAQNATTPGDITVQElvarGRYPHQPLFTRWRKEDEEAVTKA---MQATGITHLAD---QSVDTLSGGQRQRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 164 CLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:PRK10253 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-230 |
8.18e-12 |
|
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: 64.35 E-value: 8.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 30 SINEGEIVALVGESGSGKSVTAQSIIGL---NQESIHIDDGNISFESEELTNLQESEwnqirgkdiafiFQDPLSSLNPT 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVlkpDEGDIEIELDTVSYKPQYIKADYEGT------------VRDLLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 107 MKVGRQ-ITEVIlqhekkskkeakeiainllNDLGIheaEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPTTAL 185
Cdd:cd03237 89 FYTHPYfKTEIA-------------------KPLQI---EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446453387 186 DVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYG 230
Cdd:cd03237 147 DVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-234 |
9.30e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.13 E-value: 9.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 1 MGQLLSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQ 80
Cdd:PRK11614 2 EKVMLSFDKVS----AHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRAT----SGRIVFDGKDITDWQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 81 ESewnQIRGKDIAFIFQdplsslnptmkvGRQI------TEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRFeQYPHQ 154
Cdd:PRK11614 74 TA---KIMREAVAIVPE------------GRRVfsrmtvEENLAMGGFFAERDQFQERIKWVYELFPRLHERRI-QRAGT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 155 LSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITHDLALVREVADRVVVMYGGRVV 234
Cdd:PRK11614 138 MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-234 |
9.39e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 9.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVekenSKQAIVKHVSFSINEGEIVALVGESGSGKSvTAQSIigLNQEsIHIDDGNISFESE-ELTNLQES 82
Cdd:PRK11147 3 LISIHGAWLSF----SDAPLLDNAELHIEDNERVCLVGRNGAGKS-TLMKI--LNGE-VLLDDGRIIYEQDlIVARLQQD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 83 EWNQIRGKDIAFIFQDpLSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLG-------IHEAEKRFEQYPHQ- 154
Cdd:PRK11147 75 PPRNVEGTVYDFVAEG-IEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNlwqlenrINEVLAQLGLDPDAa 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 155 ---LSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKekqnTSILLITHDLALVREVADRVVVMYGG 231
Cdd:PRK11147 154 lssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ----GSIIFISHDRSFIRNMATRIVDLDRG 229
|
...
gi 446453387 232 RVV 234
Cdd:PRK11147 230 KLV 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
7-225 |
2.03e-11 |
|
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: 62.51 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 7 LENVTLAVEKEnsKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEELtNLQESEWNQ 86
Cdd:cd03231 1 LEADELTCERD--GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPP----LAGRVLLNGGPL-DFQRDSIAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 87 irgkDIAFIFQDP-----LSSL-NPTMKVGRQITEVILQhekkskkeakeiainLLNDLGIheaeKRFEQYP-HQLSGGM 159
Cdd:cd03231 74 ----GLLYLGHAPgikttLSVLeNLRFWHADHSDEQVEE---------------ALARVGL----NGFEDRPvAQLSAGQ 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446453387 160 RQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITH-DLALVREVADRV 225
Cdd:cd03231 131 QRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCA-RGGMVVLTTHqDLGLSEAGAREL 196
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-242 |
2.55e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIG-LNQESihiddGNISFESEELTNLQESEwnqirGKD--IAFIFQD-- 98
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGaLPRTS-----GYVTLDGHEVVTRSPQD-----GLAngIVYISEDrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 99 --------------PLSSLNPTMKVGRQItevilQHEKKSKKEAKEIaiNLLNdlgIHEAEKrfEQYPHQLSGGMRQRIC 164
Cdd:PRK10762 338 rdglvlgmsvkenmSLTALRYFSRAGGSL-----KHADEQQAVSDFI--RLFN---IKTPSM--EQAIGLLSGGNQQKVA 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446453387 165 LAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKeKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:PRK10762 406 IARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFK-AEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQA 482
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-243 |
3.21e-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: 64.58 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSVTAQSIIG-LNQESIHID-DGNISFESEEltnlqesewnqirgkdiAFIFQDplsSLN 104
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAeMDKVEGHVHmKGSVAYVPQQ-----------------AWIQND---SLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 105 PTMKVGRQITEVILQHEKKskkeakeiAINLLNDLGIHEAEKRFE--QYPHQLSGGMRQRICLAIAFACHPKLVIADEPT 182
Cdd:TIGR00957 717 ENILFGKALNEKYYQQVLE--------ACALLPDLEILPSGDRTEigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453387 183 TALDVTIQKQIME-LLKERKEKQNTSILLITHDLALVREVaDRVVVMYGGRVVEKGTIEEVI 243
Cdd:TIGR00957 789 SAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 849
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-213 |
3.49e-11 |
|
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: 61.02 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEkenSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFEseeltnlqesew 84
Cdd:cd03223 1 IELENLSLATP---DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL----WPWGSGRIGMP------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqiRGKDIAFIFQDPLsslnptMKVGRqITEVILqhekkskkeakeiainllndlgiheaekrfeqYP--HQLSGGMRQR 162
Cdd:cd03223 62 ---EGEDLLFLPQRPY------LPLGT-LREQLI--------------------------------YPwdDVLSGGEQQR 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446453387 163 ICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKekqnTSILLITH 213
Cdd:cd03223 100 LAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
135-298 |
4.57e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.26 E-value: 4.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 135 LLNDLGIHEaeKRFEQyPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLkeRKEKQNTSILLITHD 214
Cdd:TIGR01257 1045 MLEDTGLHH--KRNEE-AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHH 1119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 215 LALVREVADRVVVMYGGRVVEKGT---IEEVIGSpkhPYTKSLLQAIPNIDDSEkvlRAIEGTTpsieTLNSFGcpFVNR 291
Cdd:TIGR01257 1120 MDEADLLGDRIAIISQGRLYCSGTplfLKNCFGT---GFYLTLVRKMKNIQSQR---GGCEGTC----SCTSKG--FSTR 1187
|
....*..
gi 446453387 292 CPVAIKE 298
Cdd:TIGR01257 1188 CPARVDE 1194
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-234 |
7.14e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 62.92 E-value: 7.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHidDGNISFESEEL--TNLQESEwnqirGKDIAFIFQDplSSLN 104
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTW--DGEIYWSGSPLkaSNIRDTE-----RAGIVIIHQE--LTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 105 PTMKVGRQI---TEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKrfEQYPHQLSGGMRQRICLAIAFACHPKLVIADEP 181
Cdd:TIGR02633 91 PELSVAENIflgNEITLPGGRMAYNAMYLRAKNLLRELQLDADNV--TRPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446453387 182 TTALDVTIQKQIMELLKERKEKqNTSILLITHDLALVREVADRVVVMYGGRVV 234
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-217 |
1.13e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.27 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 22 AIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESEwnqirgkDIAFIfqDPLS 101
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGL----LPPAAGTIKLDGGDIDDPDVAE-------ACHYL--GHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 102 SLNPTMKVgrqitevilqhekkskkeakeiAINLL--------NDLGIHEAEKRFEQYP------HQLSGGMRQRICLAI 167
Cdd:PRK13539 83 AMKPALTV----------------------AENLEfwaaflggEELDIAAALEAVGLAPlahlpfGYLSAGQKRRVALAR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446453387 168 AFACHPKLVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITH-DLAL 217
Cdd:PRK13539 141 LLVSNRPIWILDEPTAALDAAAVALFAELIRAHLA-QGGIVIAATHiPLGL 190
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-214 |
2.62e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.73 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKenskQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLQESE 83
Cdd:PRK10247 7 LLQLQNVGYLAGD----AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL----ISPTSGTLLFEGEDISTLKPEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WNQirgkDIAFIFQDPL---SSLNPTMKVGRQITEvilQHEKKSKkeakeiainLLNDLGIHE-AEKRFEQYPHQLSGGM 159
Cdd:PRK10247 79 YRQ----QVSYCAQTPTlfgDTVYDNLIFPWQIRN---QQPDPAI---------FLDDLERFAlPDTILTKNIAELSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446453387 160 RQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHD 214
Cdd:PRK10247 143 KQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
26-243 |
3.35e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.06 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 26 HVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFE-SEELTNLQESEWNQIRGkdiafIFQDPLSSLN 104
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPN----KGTVDIKgSAALIAISSGLNGQLTG-----IENIELKGLM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 105 PTMKvGRQITEVILQhekkskkeakeiaINLLNDLG--IHEAEKRFeqyphqlSGGMRQRICLAIAFACHPKLVIADEPT 182
Cdd:PRK13545 113 MGLT-KEKIKEIIPE-------------IIEFADIGkfIYQPVKTY-------SSGMKSRLGFAISVHINPDILVIDEAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446453387 183 TALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:PRK13545 172 SVGDQTFTKKCLDKMNEFKEQGKT-IFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVV 231
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
151-252 |
3.39e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.58 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 151 YPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREvADRVVVM-- 228
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFnn 1433
|
90 100
....*....|....*....|....*..
gi 446453387 229 ---YGGRVVEKGTIEEVIGSPKHPYTK 252
Cdd:PTZ00265 1434 pdrTGSFVQAHGTHEELLSVQDGVYKK 1460
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
27-238 |
6.57e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.87 E-value: 6.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSVTAQSIIGLNQesihiddGNISFES--EELTNLQESEWNQIRgkDI-------AFIFQ 97
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT-------GDKSAGShiELLGRTVQREGRLAR--DIrksrantGYIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 98 -----DPLSSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLLNDLGI-HEAEKRFEQyphqLSGGMRQRICLAIAFAC 171
Cdd:PRK09984 94 qfnlvNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMvHFAHQRVST----LSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446453387 172 HPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGT 238
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
23-240 |
6.79e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.88 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlnQESIHIDDGNISFESEELTNLQESEWNQiRGkdIAFIFQDPLss 102
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAYKILEGDILFKGESILDLEPEERAH-LG--IFLAFQYPI-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 103 lnptmkvgrQITEVILQHEKKSKKEAKEIAINL--LNDLG----IHEAEKRFEQYPHQL--------SGGMRQR---ICL 165
Cdd:CHL00131 95 ---------EIPGVSNADFLRLAYNSKRKFQGLpeLDPLEfleiINEKLKLVGMDPSFLsrnvnegfSGGEKKRneiLQM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446453387 166 AIAfacHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNtSILLITHDLALVREVA-DRVVVMYGGRVVEKGTIE 240
Cdd:CHL00131 166 ALL---DSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDAE 237
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-241 |
1.02e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTlaveKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEELTNLQESE 83
Cdd:PRK15439 11 LLCARSIS----KQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPP----DSGTLEIGGNPCARLTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WNQIrgkDIAFIFQDPLSSLNPTMKvgrqitEVILQHEKKSKKEAKEIAiNLLNDLGIH----------EAEKRfeQYPH 153
Cdd:PRK15439 83 AHQL---GIYLVPQEPLLFPNLSVK------ENILFGLPKRQASMQKMK-QLLAALGCQldldssagslEVADR--QIVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 154 QLSGGMRQriclaiafachPKLVIADEPTTALDV----TIQKQIMELLKerkekQNTSILLITHDLALVREVADRVVVMY 229
Cdd:PRK15439 151 ILRGLMRD-----------SRILILDEPTASLTPaeteRLFSRIRELLA-----QGVGIVFISHKLPEIRQLADRISVMR 214
|
250
....*....|..
gi 446453387 230 GGRVVEKGTIEE 241
Cdd:PRK15439 215 DGTIALSGKTAD 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-231 |
1.08e-09 |
|
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: 57.73 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 22 AIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQE---SIHIDDGNISFESEELTNLQEsewnqiRGKdIAFIFQD 98
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTlegKVHWSNKNESEPSFEATRSRN------RYS-VAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 99 PLSsLNPTMKvgrqiTEVILQHEKKSKKEAKEI-AINLLNDLGI--HEAEKRFEQYPHQLSGGMRQRICLAIAFACHPKL 175
Cdd:cd03290 88 PWL-LNATVE-----ENITFGSPFNKQRYKAVTdACSLQPDIDLlpFGDQTEIGERGINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446453387 176 VIADEPTTALDV-----TIQKQIMELLKERKEkqntSILLITHDLALVREvADRVVVMYGG 231
Cdd:cd03290 162 VFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-243 |
1.08e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 20 KQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihiddgniSFESEELTNLQESEwNQIRgKDIAFIFQDP 99
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGN--------NFTGTILANNRKPT-KQIL-KRTGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 LssLNPTMKVGRQITEVILQH--EKKSKKEAKEIAINLLNDLGIHEAEKRF--EQYPHQLSGGMRQRICLAIAFACHPKL 175
Cdd:PLN03211 150 I--LYPHLTVRETLVFCSLLRlpKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446453387 176 VIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
12-251 |
1.19e-09 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 58.00 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 12 LAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGNISFESEELTNLqesEWNQIRGKd 91
Cdd:cd03288 25 LCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRM----VDIFDGKIVIDGIDISKL---PLHTLRSR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 92 IAFIFQDPL---SSLNPTMKVGRQITEVILQHEKKSKKEAKEI-AINLLNDLGIHEAEKRFEQyphqlsgGMRQRICLAI 167
Cdd:cd03288 97 LSIILQDPIlfsGSIRFNLDPECKCTDDRLWEALEIAQLKNMVkSLPGGLDAVVTEGGENFSV-------GQRQLFCLAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 168 AFACHPKLVIADEPTTALDVT----IQKQIMELLKERkekqntSILLITHDLALVREvADRVVVMYGGRVVEKGTIEEVI 243
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMAteniLQKVVMTAFADR------TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
....*...
gi 446453387 244 GSPKHPYT 251
Cdd:cd03288 243 AQEDGVFA 250
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
24-237 |
2.04e-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: 56.18 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHIDDgnisfeseeltnLQESEWNQIrgkdiafIFQDPLSSL 103
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISF------------LPKFSRNKL-------IFIDQLQFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 nptMKVGrqitevilqhekkskkeakeiaINLLndlgiheaekRFEQYPHQLSGGMRQRICLA--IAFACHPKLVIADEP 181
Cdd:cd03238 72 ---IDVG----------------------LGYL----------TLGQKLSTLSGGELQRVKLAseLFSEPPGTLFILDEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453387 182 TTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREvADRVVVM------YGGRVVEKG 237
Cdd:cd03238 117 STGLHQQDINQLLEVIKGLIDLGNT-VILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-243 |
2.62e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQS---IIGLNQESIHIDDGNISfeSEELTNLQesewnqirgKDIAFIFQDP 99
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNAlfrIVELERGRILIDGCDIS--KFGLMDLR---------KVLGIIPQAP 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 -LSS------LNPTmkvgRQITEVILQHEKKSKKEAKEIAINLLN-DLGIHEAEKRFeqyphqlSGGMRQRICLAIAFAC 171
Cdd:PLN03130 1323 vLFSgtvrfnLDPF----NEHNDADLWESLERAHLKDVIRRNSLGlDAEVSEAGENF-------SVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446453387 172 HPKLVIADEPTTALDV----TIQKQImellkeRKEKQNTSILLITHDLALVREvADRVVVMYGGRVVEKGTIEEVI 243
Cdd:PLN03130 1392 RSKILVLDEATAAVDVrtdaLIQKTI------REEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLL 1460
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-237 |
3.52e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.72 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 4 LLSLENVTLAVEKenskQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlnQESIHIDDGNISFESEELTNLQESE 83
Cdd:PRK09580 1 MLSIKDLHVSVED----KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--REDYEVTGGTVEFKGKDLLELSPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 WnqiRGKDIAFIFQDPL------------SSLNPTMKVGRQitEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRFeqy 151
Cdd:PRK09580 75 R---AGEGIFMAFQYPVeipgvsnqfflqTALNAVRSYRGQ--EPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGF--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 152 phqlSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKE-RKEKQntSILLITHDLALVREVA-DRVVVMY 229
Cdd:PRK09580 147 ----SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSlRDGKR--SFIIVTHYQRILDYIKpDYVHVLY 220
|
....*...
gi 446453387 230 GGRVVEKG 237
Cdd:PRK09580 221 QGRIVKSG 228
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
155-243 |
4.30e-09 |
|
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: 57.72 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 155 LSGGMRQRICLAIAF---ACHPKLVIADEPTTAL---DVtiqKQIMELLKERKEKQNTsILLITHDLALVReVADRVVVM 228
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDKGNT-VVVIEHNLDVIK-TADYIIDL 904
|
90 100
....*....|....*....|.
gi 446453387 229 ------YGGRVVEKGTIEEVI 243
Cdd:TIGR00630 905 gpeggdGGGTVVASGTPEEVA 925
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-267 |
4.94e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENSKQAIvKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlnqESIHIDDGNISFESEeLTNLQESEW 84
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTL-SDINLEIPVGSLVAIVGGTGEGKTSLISAMLG---ELSHAETSSVVIRGS-VAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 --NQIRGKDIAFifqdplSSLNPTMKVGRQITEVILQHekkskkeakeiainllnDLGIHEAEKRFE--QYPHQLSGGMR 160
Cdd:PLN03232 690 ifNATVRENILF------GSDFESERYWRAIDVTALQH-----------------DLDLLPGRDLTEigERGVNISGGQK 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 161 QRICLAIAFACHPKLVIADEPTTALDVTIQKQIME-LLKErkEKQNTSILLITHDLALVREVaDRVVVMYGGRVVEKGTI 239
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDsCMKD--ELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTF 823
|
250 260
....*....|....*....|....*...
gi 446453387 240 EEVigSPKHPYTKSLLQAIPNIDDSEKV 267
Cdd:PLN03232 824 AEL--SKSGSLFKKLMENAGKMDATQEV 849
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-243 |
7.40e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.59 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 1 MGQLLSLENVT-----LAVEKENSKQAIV-KH----------VSFSINEGEIVALVGESGSGKSvTAQSIIGlnqESIHI 64
Cdd:PRK13546 1 MNVSVNIKNVTkeyriYRTNKERMKDALIpKHknktffalddISLKAYEGDVIGLVGINGSGKS-TLSNIIG---GSLSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 65 DDGNISFESE-ELTNLQESEWNQIRG-KDIAFifqdPLSSLNPTMKVGRQITEVILQhekkskkeakeiainlLNDLG-- 140
Cdd:PRK13546 77 TVGKVDRNGEvSVIAISAGLSGQLTGiENIEF----KMLCMGFKRKEIKAMTPKIIE----------------FSELGef 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 141 IHEAEKRFeqyphqlSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITHDLALVRE 220
Cdd:PRK13546 137 IYQPVKKY-------SSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKE-QNKTIFFVSHNLGQVRQ 208
|
250 260
....*....|....*....|...
gi 446453387 221 VADRVVVMYGGRVVEKGTIEEVI 243
Cdd:PRK13546 209 FCTKIAWIEGGKLKDYGELDDVL 231
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-248 |
8.63e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.60 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 22 AIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHID----DGNISFESEELTNLQESEWNQIRG-----KDI 92
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRgarvTGDVTLNGEPLAAIDAPRLARLRAvlpqaAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 93 AFIFqdplsSLNPTMKVGRqiteviLQHEKKSKKEAKEIAINLLNDLGIHEAEKRFEQYPHQLSGGMRQRICLAIAFA-- 170
Cdd:PRK13547 95 AFAF-----SAREIVLLGR------YPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 171 -------CHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEVI 243
Cdd:PRK13547 164 wpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
....*
gi 446453387 244 gSPKH 248
Cdd:PRK13547 244 -TPAH 247
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-243 |
1.14e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.49 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQES---IHIDDGNISfeseeltnlqESEWNQIRGKdIAFIFQDP 99
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAegeIIIDGLNIA----------KIGLHDLRFK-ITIIPQDP 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 L---SSLNPTMKVGRQITE------VILQHEKKSkkeakeiaINLLNDLGIHEAEKRFEQyphqLSGGMRQRICLAIAFA 170
Cdd:TIGR00957 1370 VlfsGSLRMNLDPFSQYSDeevwwaLELAHLKTF--------VSALPDKLDHECAEGGEN----LSVGQRQLVCLARALL 1437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446453387 171 CHPKLVIADEPTTALDVTIQKQIMELLkeRKEKQNTSILLITHDLALVREVAdRVVVMYGGRVVEKGTIEEVI 243
Cdd:TIGR00957 1438 RKTKILVLDEATAAVDLETDNLIQSTI--RTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLL 1507
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
155-234 |
1.72e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 155 LSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITHDLALVREVADRVVVMYGGRVV 234
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-242 |
2.20e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 28 SFSINEGEIVALVGESGSGKSVTAQSIIG-LNQESIHIDDG-----NISFEseELTNLQESEWnQIRGKDIAFIFQDpls 101
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGeLPLLSGERQSQfshitRLSFE--QLQKLVSDEW-QRNNTDMLSPGED--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 102 slnptmKVGRQITEVILQHEKKSKKEAKEIAInllndLGI-HEAEKRFEQyphqLSGGMRQRICLAIAFACHPKLVIADE 180
Cdd:PRK10938 97 ------DTGRTTAEIIQDEVKDPARCEQLAQQ-----FGItALLDRRFKY----LSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453387 181 PTTALDVTIQKQIMELLkERKEKQNTSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:PRK10938 162 PFDGLDVASRQQLAELL-ASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-219 |
2.45e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSvtaqSIIGLNQESIHIDDGNISF-ESEELTNLQESEWnqiRGKdIAFIFQDPL- 100
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKS----TILKLIERLYDPTEGDIIInDSHNLKDINLKWW---RSK-IGVVSQDPLl 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 101 -------------SSLNPTMKVGRQITE--VILQHEKKSKKEAKEIAINLLNDL-------GIHEAEKRFE--------- 149
Cdd:PTZ00265 472 fsnsiknnikyslYSLKDLEALSNYYNEdgNDSQENKNKRNSCRAKCAGDLNDMsnttdsnELIEMRKNYQtikdsevvd 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 150 ----------------QY-------PHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNT 206
Cdd:PTZ00265 552 vskkvlihdfvsalpdKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 631
|
250
....*....|...
gi 446453387 207 SILLITHDLALVR 219
Cdd:PTZ00265 632 ITIIIAHRLSTIR 644
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
154-230 |
4.50e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.41 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 154 QLSGGMRQRICLAIAFACHPKLVIADEPTTALDV----TIQKQIMELLKERKekqntSILLITHDLALVREVADRVVVMY 229
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIyqrlNVARLIRELAEEGK-----YVLVVEHDLAILDYLADYVHILY 286
|
.
gi 446453387 230 G 230
Cdd:COG1245 287 G 287
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
155-230 |
6.75e-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: 51.80 E-value: 6.75e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446453387 155 LSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYG 230
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-219 |
7.97e-08 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 53.16 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 29 FSINEGEIVALVGESGSGKSVTAQSIIGLNQESIHIDDGNISFESEELTNLQESEWNQIRGKDIAFIFQDPLSSLNPTMK 108
Cdd:pfam13304 110 KFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 109 VGRQITEVILQHEKKSKKEAKEIAI-NLLNDLGIHEAEKRFEQYPHQLSGGMRQ--RICLAIAFACHP-KLVIADEPTTA 184
Cdd:pfam13304 190 RGLKLADLNLSDLGEGIEKSLLVDDrLRERGLILLENGGGGELPAFELSDGTKRllALLAALLSALPKgGLLLIDEPESG 269
|
170 180 190
....*....|....*....|....*....|....*
gi 446453387 185 LDVTIQKQIMELLKErKEKQNTSILLITHDLALVR 219
Cdd:pfam13304 270 LHPKLLRRLLELLKE-LSRNGAQLILTTHSPLLLD 303
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-235 |
1.08e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.05 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 3 QLLSLENVTLAVEKENSKqaiVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISFESEELTNLQES 82
Cdd:PRK10522 321 QTLELRNVTFAYQDNGFS---VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ----SGEILLDGKPVTAEQPE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 83 EWNQIrgkdIAFIFQD--PLSSLnptmkVGRQITEVilqhekkskkeAKEIAINLLNDLG----IHEAEKRFEQYphQLS 156
Cdd:PRK10522 394 DYRKL----FSAVFTDfhLFDQL-----LGPEGKPA-----------NPALVEKWLERLKmahkLELEDGRISNL--KLS 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 157 GGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQI-MELLKERKEKQNTsILLITHDLALVrEVADRVVVMYGGRVVE 235
Cdd:PRK10522 452 KGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEMGKT-IFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-228 |
1.49e-07 |
|
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: 50.06 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 34 GEIVALVGESGSGKSVTAQSIIglnqesihiddgnisfeseeltnlqesewNQIRGKDIAFIFQDPlsslnptmkvgrqi 113
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALA-----------------------------RELGPPGGGVIYIDG-------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 114 tevilqhekkskkeakeiaINLLNDLGIHEAEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQI 193
Cdd:smart00382 39 -------------------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALL 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446453387 194 MEL-----LKERKEKQNTSILLITHDL-----ALVREVADRVVVM 228
Cdd:smart00382 100 LLLeelrlLLLLKSEKNLTVILTTNDEkdlgpALLRRRFDRRIVL 144
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-243 |
1.51e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.82 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLnqesihiddgnisfeseeltnLQESEwnqirGKdiAFIFQDPL--S 101
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGL---------------------LPASE-----GE--AWLFGQPVdaG 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 102 SLNPTMKVG--------------RQitevilqhekkskkeakeiaiNL-----LNDLG-------IHEAEKRF------E 149
Cdd:NF033858 334 DIATRRRVGymsqafslygeltvRQ---------------------NLelharLFHLPaaeiaarVAEMLERFdladvaD 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 150 QYPHQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHdlaLVREVA--DRVVV 227
Cdd:NF033858 393 ALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTH---FMNEAErcDRISL 469
|
250
....*....|....*.
gi 446453387 228 MYGGRVVEKGTIEEVI 243
Cdd:NF033858 470 MHAGRVLASDTPAALV 485
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
154-230 |
1.58e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 154 QLSGGMRQRicLAIAfACHPK---LVIADEPTTALDV----TIQKQIMELLKERkekqntSILLITHDLALVREVADRVV 226
Cdd:PRK13409 212 ELSGGELQR--VAIA-AALLRdadFYFFDEPTSYLDIrqrlNVARLIRELAEGK------YVLVVEHDLAVLDYLADNVH 282
|
....
gi 446453387 227 VMYG 230
Cdd:PRK13409 283 IAYG 286
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-245 |
1.88e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENSKQAIvKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlnqESIHIDDGNISfeseeltnlqesew 84
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTL-SNINLDVPVGSLVAIVGSTGEGKTSLISAMLG---ELPPRSDASVV-------------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 85 nqIRGK-----DIAFIFQDPL-------SSLNPTmKVGRQITEVILQHEkkskkeakeiaINLLNDLGIHEAEKRfeqyP 152
Cdd:PLN03130 677 --IRGTvayvpQVSWIFNATVrdnilfgSPFDPE-RYERAIDVTALQHD-----------LDLLPGGDLTEIGER----G 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 153 HQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIME-LLKErkEKQNTSILLITHDLALVREVaDRVVVMYGG 231
Cdd:PLN03130 739 VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkCIKD--ELRGKTRVLVTNQLHFLSQV-DRIILVHEG 815
|
250
....*....|....
gi 446453387 232 RVVEKGTIEEVIGS 245
Cdd:PLN03130 816 MIKEEGTYEELSNN 829
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-237 |
2.00e-07 |
|
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: 51.10 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 25 KHVSFSINEGEIVALVGESGSGKSVTA-QSIIGLNQ----ESIHiddgniSFESEELTNLQESEWNQIRGKDIAFIFQDP 99
Cdd:cd03270 12 KNVDVDIPRNKLVVITGVSGSGKSSLAfDTIYAEGQrryvESLS------AYARQFLGQMDKPDVDSIEGLSPAIAIDQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 LSSLNPTMKVGrQITEvILQHEKKSKKEAKEIA-INLLNDLGIHEAekRFEQYPHQLSGGMRQRICLAIAFAChpKLV-- 176
Cdd:cd03270 86 TTSRNPRSTVG-TVTE-IYDYLRLLFARVGIRErLGFLVDVGLGYL--TLSRSAPTLSGGEAQRIRLATQIGS--GLTgv 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 177 --IADEPTTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREvADRVVVM------YGGRVVEKG 237
Cdd:cd03270 160 lyVLDEPSIGLHPRDNDRLIETLKRLRDLGNT-VLVVEHDEDTIRA-ADHVIDIgpgagvHGGEIVAQG 226
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-230 |
2.12e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.21 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 33 EGEIVALVGESGSGKSvTAQSIIGlnqesihiddgnisfeSEELTNL----QESEWNQI----RGKDIAFIFQDPLS-SL 103
Cdd:cd03236 25 EGQVLGLVGPNGIGKS-TALKILA----------------GKLKPNLgkfdDPPDWDEIldefRGSELQNYFTKLLEgDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMKVgrqitevilQHEKKSKKEAKEIAINLLN---DLGIH-------EAEKRFEQYPHQLSGGMRQRICLAIAFACHP 173
Cdd:cd03236 88 KVIVKP---------QYVDLIPKAVKGKVGELLKkkdERGKLdelvdqlELRHVLDRNIDQLSGGELQRVAIAAALARDA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446453387 174 KLVIADEPTTALDV----TIQKQIMELLKERKekqntSILLITHDLALVREVADRVVVMYG 230
Cdd:cd03236 159 DFYFFDEPSSYLDIkqrlNAARLIRELAEDDN-----YVLVVEHDLAVLDYLSDYIHCLYG 214
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-244 |
2.57e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 28 SFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEELT-----NLQES-------EWNQIRGKDIA-F 94
Cdd:PRK10762 24 ALNVYPGRVMALVGENGAGKSTMMKVLTGIYTR----DAGSILYLGKEVTfngpkSSQEAgigiihqELNLIPQLTIAeN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 95 IFqdplsslnptmkVGRQITEVI--LQHEKKSKKeakeiAINLLNDLGIHEAEKRFEQyphQLSGGMRQRICLAIAFACH 172
Cdd:PRK10762 100 IF------------LGREFVNRFgrIDWKKMYAE-----ADKLLARLNLRFSSDKLVG---ELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 173 PKLVIADEPTTALDVTIQKQIMELLKERKEkQNTSILLITHDLALVREVADRVVVMYGGRVV---------EKGTIEEVI 243
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELKS-QGRGIVYISHRLKEIFEICDDVTVFRDGQFIaerevadltEDSLIEMMV 238
|
.
gi 446453387 244 G 244
Cdd:PRK10762 239 G 239
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
132-242 |
2.59e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.66 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 132 AINLLNDLGIHEAEKRFEQyphQLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKeKQNTSILLI 211
Cdd:NF000106 125 ADELLERFSLTEAAGRAAA---KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLT 200
|
90 100 110
....*....|....*....|....*....|.
gi 446453387 212 THDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:NF000106 201 TQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-230 |
4.16e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.32 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 30 SINEGEIVALVGESGSGKSVTAQSIIGLnqesIHIDDGN------ISFESEELTNLQESEwnqirgkdiafiFQDPLSSL 103
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGV----LKPDEGEvdedlkISYKPQYISPDYDGT------------VEEFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMkvgrqITEVILQHekkskkeakeiaiNLLNDLGIHeaeKRFEQYPHQLSGGMRQRicLAIAfACHPK---LVIADE 180
Cdd:COG1245 426 NTDD-----FGSSYYKT-------------EIIKPLGLE---KLLDKNVKDLSGGELQR--VAIA-ACLSRdadLYLLDE 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446453387 181 PTTALDVTIQKQIMELLKERKEKQNTSILLITHDLALVREVADRVVVMYG 230
Cdd:COG1245 482 PSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-218 |
4.31e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 7 LENVTLAVEKENskqaIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIG-LNQESIHIDDGnisfeseelTNLQESEWN 85
Cdd:PRK11147 322 MENVNYQIDGKQ----LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGqLQADSGRIHCG---------TKLEVAYFD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 86 QIRgkdiafifqdplSSLNPTMKV------GRQITEV--ILQHekkskkeakeiAINLLNDLGIHEaeKRFEQYPHQLSG 157
Cdd:PRK11147 389 QHR------------AELDPEKTVmdnlaeGKQEVMVngRPRH-----------VLGYLQDFLFHP--KRAMTPVKALSG 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446453387 158 GMRQRICLAIAFACHPKLVIADEPTTALDVtiqkQIMELLKERKEKQNTSILLITHDLALV 218
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-217 |
5.12e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.42 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 26 HVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEELTNLQEsEWNQirgkDIAFI---------- 95
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARP----DAGEVLWQGEPIRRQRD-EYHQ----DLLYLghqpgiktel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 96 -------FQDPLSSLnptmkVGRQITEVILQhekkskkeakeiAINLlndlgiheaeKRFEQYP-HQLSGGMRQRICLAI 167
Cdd:PRK13538 90 talenlrFYQRLHGP-----GDDEALWEALA------------QVGL----------AGFEDVPvRQLSAGQQRRVALAR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446453387 168 AFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLITHDLAL 217
Cdd:PRK13538 143 LWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPV 192
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
155-247 |
5.28e-07 |
|
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: 51.17 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 155 LSGGMRQRICLA--IAFACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVREvADRVVVM---- 228
Cdd:TIGR00630 489 LSGGEAQRIRLAtqIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNT-LIVVEHDEDTIRA-ADYVIDIgpga 566
|
90 100
....*....|....*....|.
gi 446453387 229 --YGGRVVEKGTIEEVIGSPK 247
Cdd:TIGR00630 567 geHGGEVVASGTPEEILANPD 587
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
153-229 |
7.08e-07 |
|
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: 48.51 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 153 HQLSGGMRQRICLAIAFACHPK----LVIADEPTTALDVTIQKQIMELLKERKEKQNTSIlLITHDLALVrEVADRVVVM 228
Cdd:cd03227 76 LQLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVI-VITHLPELA-ELADKLIHI 153
|
.
gi 446453387 229 Y 229
Cdd:cd03227 154 K 154
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
30-226 |
7.21e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 30 SINEGEIVALVGESGSGKSvtaqSIIGLNQESIHIDDGNISFES--------EELTNLQESEWNQIRGKDIAF-IFQDPL 100
Cdd:PRK10636 23 TINPGQKVGLVGKNGCGKS----TLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPALEYVIDGDREYrQLEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 101 SSLNPTMKvGRQITEVILQHEKKSKKEAKEIAINLLNDLGIheAEKRFEQYPHQLSGGMRQRICLAIAFACHPKLVIADE 180
Cdd:PRK10636 99 HDANERND-GHAIATIHGKLDAIDAWTIRSRAASLLHGLGF--SNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446453387 181 PTTALDVtiqKQIMELLKERKEKQNTSIlLITHDLALVREVADRVV 226
Cdd:PRK10636 176 PTNHLDL---DAVIWLEKWLKSYQGTLI-LISHDRDFLDPIVDKII 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
135-230 |
1.14e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 135 LLNDLGIheaEKRFEQYPHQLSGGMRQRicLAIAfACHPK---LVIADEPTTALDVTIQKQIMELLKERKEKQNTSILLI 211
Cdd:PRK13409 437 IIKPLQL---ERLLDKNVKDLSGGELQR--VAIA-ACLSRdadLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVV 510
|
90
....*....|....*....
gi 446453387 212 THDLALVREVADRVVVMYG 230
Cdd:PRK13409 511 DHDIYMIDYISDRLMVFEG 529
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
12-262 |
1.43e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.08 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 12 LAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihidDGNISFESEELTNLQESEWNQIRG-- 89
Cdd:cd03289 8 LTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-----EGDIQIDGVSWNSVPLQKWRKAFGvi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 90 KDIAFIFQDPL-SSLNPTmkvGRQITEVILQhekkskkeakeiainLLNDLGIHEAekrFEQYPHQ-----------LSG 157
Cdd:cd03289 83 PQKVFIFSGTFrKNLDPY---GKWSDEEIWK---------------VAEEVGLKSV---IEQFPGQldfvlvdggcvLSH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 158 GMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKErkEKQNTSILLITHDLALVREvADRVVVMYGGRVVEKG 237
Cdd:cd03289 142 GHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ--AFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYD 218
|
250 260
....*....|....*....|....*
gi 446453387 238 TIEEVIGSpkhpyTKSLLQAIPNID 262
Cdd:cd03289 219 SIQKLLNE-----KSHFKQAISPSD 238
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
27-243 |
1.49e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 27 VSFSINEGEIVALVGESGSGKSVTAQS---IIGLNQESIHIDDGNISfeSEELTNLQESewnqirgkdIAFIFQDPLSsL 103
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNAlfrIVELEKGRIMIDDCDVA--KFGLTDLRRV---------LSIIPQSPVL-F 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMKVGrqiTEVILQHekkskkeakeiainllNDLGIHEAEKR------FEQYPHQL-----------SGGMRQRICLA 166
Cdd:PLN03232 1323 SGTVRFN---IDPFSEH----------------NDADLWEALERahikdvIDRNPFGLdaevseggenfSVGQRQLLSLA 1383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446453387 167 IAFACHPKLVIADEPTTALDVTIQKQIMELLKErkEKQNTSILLITHDLALVREvADRVVVMYGGRVVEKGTIEEVI 243
Cdd:PLN03232 1384 RALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
155-238 |
1.61e-06 |
|
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: 48.76 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 155 LSGGMRQRICLAIAF---ACHPKLVIADEPTTALDVTIQKQIMELLKERKEKQNTsILLITHDLALVReVADRVVVM--- 228
Cdd:cd03271 170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNT-VVVIEHNLDVIK-CADWIIDLgpe 247
|
90
....*....|...
gi 446453387 229 ---YGGRVVEKGT 238
Cdd:cd03271 248 ggdGGGQVVASGT 260
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
139-229 |
1.75e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 49.16 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 139 LGIHEAEKRFEQYPHQLSGGMRQRICLAIAFAC--HPKLVIADEPTTALDVTIQKQIMELLKERKEKqnTSILLITHDLA 216
Cdd:COG4637 243 LEFREKGLDRPFPARELSDGTLRFLALLAALLSprPPPLLCIEEPENGLHPDLLPALAELLREASER--TQVIVTTHSPA 320
|
90
....*....|....
gi 446453387 217 LVREVA-DRVVVMY 229
Cdd:COG4637 321 LLDALEpEEVLVLE 334
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-235 |
1.89e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.14 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 26 HVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQEsihiDDGNISFESEEL--TNLQESewnqiRGKDIAFIFQDplSSL 103
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQP----DAGSILIDGQEMrfASTTAA-----LAAGVAIIYQE--LHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 NPTMKVGRQITEVILQHEKKSKKEAKEI--AINLLNDLGIH---EAEKRFeqyphqLSGGMRQRICLAIAFACHPKlVIA 178
Cdd:PRK11288 91 VPEMTVAENLYLGQLPHKGGIVNRRLLNyeAREQLEHLGVDidpDTPLKY------LSIGQRQMVEIAKALARNAR-VIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446453387 179 -DEPTTALDVTIQKQIMELLKERKeKQNTSILLITHDLALVREVADRVVVMYGGRVVE 235
Cdd:PRK11288 164 fDEPTSSLSAREIEQLFRVIRELR-AEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
154-242 |
2.19e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 154 QLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKE-RKEKQNTSILLIThdlALVREVA--DRVVVMYG 230
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRiRAERPGMSVLVAT---AYMEEAErfDWLVAMDA 212
|
90
....*....|..
gi 446453387 231 GRVVEKGTIEEV 242
Cdd:NF033858 213 GRVLATGTPAEL 224
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
24-271 |
3.07e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKS-------VTA--QSIIGLNQESIHIDDGNI-------------SFESEELT---- 77
Cdd:PRK00635 611 LKDLTISLPLGRLTVVTGVSGSGKSslindtlVPAveEFIEQGFCSNLSIQWGAIsrlvhitrdlpgrSQRSIPLTyika 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 78 --NLQESEWNQIRGKDIA-----FIFQDPLSSLNPTMKVGR----------------------QITEVILQHEKkskkea 128
Cdd:PRK00635 691 fdDLRELFAEQPRSKRLGltkshFSFNTPLGACAECQGLGSitttdnrtsipcpsclgkrflpQVLEVRYKGKN------ 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 129 keIAINLlnDLGIHEAEKRFEQYPH-----------------------QLSGGMRQRICLA---IAFACHPKLVIADEPT 182
Cdd:PRK00635 765 --IADIL--EMTAYEAEKFFLDEPSihekihalcslgldylplgrplsSLSGGEIQRLKLAyelLAPSKKPTLYVLDEPT 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 183 TALDVTIQKQIMELLKERKEkQNTSILLITHDLALVReVADRVVVM------YGGRVVEKGTIEEVIGSPKH------PY 250
Cdd:PRK00635 841 TGLHTHDIKALIYVLQSLTH-QGHTVVIIEHNMHVVK-VADYVLELgpeggnLGGYLLASCSPEELIHLHTPtakalrPY 918
|
330 340
....*....|....*....|....
gi 446453387 251 TKSlLQAIPNIDD---SEKVLRAI 271
Cdd:PRK00635 919 LSS-PQELPYLPDpspKPPVPADI 941
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
155-247 |
4.33e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.48 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 155 LSGGMRQRICLAiAF----ACHPKLVIADEPTTAL---DVtiqKQIMELLKERKEKQNTsILLITHDLALVReVADRVVV 227
Cdd:COG0178 827 LSGGEAQRVKLA-SElskrSTGKTLYILDEPTTGLhfhDI---RKLLEVLHRLVDKGNT-VVVIEHNLDVIK-TADWIID 900
|
90 100
....*....|....*....|....*.
gi 446453387 228 M------YGGRVVEKGTIEEVIGSPK 247
Cdd:COG0178 901 LgpeggdGGGEIVAEGTPEEVAKVKA 926
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
155-251 |
9.11e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 47.37 E-value: 9.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 155 LSGGMRQRICLAiafachpK----------LVIADEPTTAL---DVtiqKQIMELLKERKEKQNTsILLITHDLALVReV 221
Cdd:PRK00349 831 LSGGEAQRVKLA-------KelskrstgktLYILDEPTTGLhfeDI---RKLLEVLHRLVDKGNT-VVVIEHNLDVIK-T 898
|
90 100 110
....*....|....*....|....*....|....*.
gi 446453387 222 ADRVVVM------YGGRVVEKGTIEEVIGSPKhPYT 251
Cdd:PRK00349 899 ADWIIDLgpeggdGGGEIVATGTPEEVAKVEA-SYT 933
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-305 |
1.02e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.21 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGLNQESihidDGNISfESEELTNLQESEW---NQIRGKDIAFIFQDP 99
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPS----EGKIK-HSGRISFSPQTSWimpGTIKDNIIFGLSYDE 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 100 LsslnptmkvgrQITEVI----LQHEKKSKKEAKEIainLLNDLGIheaekrfeqyphQLSGGMRQRICLAIAFACHPKL 175
Cdd:TIGR01271 516 Y-----------RYTSVIkacqLEEDIALFPEKDKT---VLGEGGI------------TLSGGQRARISLARAVYKDADL 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 176 VIADEPTTALDVTIQKQIMELLKERKEKQNTSIlLITHDLALVREvADRVVVMYGGRVVEKGTIEEVIGspKHPYTKSLL 255
Cdd:TIGR01271 570 YLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRI-LVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQA--KRPDFSSLL 645
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446453387 256 QAIPNIDDSekvlraiegttpSIETLNSFGCPFVNRCPVAIKECIHRFPE 305
Cdd:TIGR01271 646 LGLEAFDNF------------SAERRNSILTETLRRVSIDGDSTVFSGPE 683
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
155-233 |
3.74e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 3.74e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 155 LSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKeKQNTSILLITHDLALVREVADRVVVMYGGRV 233
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELA-KKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-242 |
4.09e-05 |
|
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: 45.39 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlnQESIHIDDGNISFESEeLTNLqeSEWNQIRGKDIAFIFQDPLSSl 103
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG--DTTVTSGDATVAGKSI-LTNI--SDVHQNMGYCPQFDAIDDLLT- 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 104 nptmkvGRQITEVILQHEKKSKKEAKEIAINLLNDLGIHEAEKRFEQyphQLSGGMRQRICLAIAFACHPKLVIADEPTT 183
Cdd:TIGR01257 2029 ------GREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAG---TYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446453387 184 ALDVTIQKQ----IMELLKERKekqntSILLITHDLALVREVADRVVVMYGGRVVEKGTIEEV 242
Cdd:TIGR01257 2100 GMDPQARRMlwntIVSIIREGR-----AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
154-219 |
5.61e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.36 E-value: 5.61e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446453387 154 QLSGGMRQRICLAIAFA--------ChpKLVIADEPTTALDV-TIQKQIMELLKERKEKQNTSILLITHDLALVR 219
Cdd:cd03240 115 RCSGGEKVLASLIIRLAlaetfgsnC--GILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVD 187
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-190 |
5.70e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.90 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 12 LAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGL--NQESIHIDdgNISFESEELtnlqeSEWNQIRG 89
Cdd:TIGR01271 1223 LTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLlsTEGEIQID--GVSWNSVTL-----QTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 90 --KDIAFIFQDPL-SSLNPtmkvgrqitevilqHEKKSKKEAKEIAinllNDLGIHEAekrFEQYPHQ-----------L 155
Cdd:TIGR01271 1296 viPQKVFIFSGTFrKNLDP--------------YEQWSDEEIWKVA----EEVGLKSV---IEQFPDKldfvlvdggyvL 1354
|
170 180 190
....*....|....*....|....*....|....*.
gi 446453387 156 SGGMRQRICLAIAFACHPKLVIADEPTTALD-VTIQ 190
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLDpVTLQ 1390
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-336 |
8.81e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 15 EKENSKQAIVKHVSFSINEGEIVALVGESGSGKSVTAQSIIGlNQESIHID-DGNISFESEELTNLQesewNQIRGkDIA 93
Cdd:TIGR00956 68 FRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS-NTDGFHIGvEGVITYDGITPEEIK----KHYRG-DVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 94 FIFQDPLSSlnPTMKVG-------------------------RQITEVI-----LQHEKKSkkeakeiaiNLLNDL--GI 141
Cdd:TIGR00956 142 YNAETDVHF--PHLTVGetldfaarcktpqnrpdgvsreeyaKHIADVYmatygLSHTRNT---------KVGNDFvrGV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 142 heaekrfeqyphqlSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKErkekqntsILLITHDLALVR-- 219
Cdd:TIGR00956 211 --------------SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKT--------SANILDTTPLVAiy 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 220 -------EVADRVVVMYGGRVVEKGTIEEV------IG--SPKHPYTKSLLQAIpniddsekvlraiegTTPSIETLNSf 284
Cdd:TIGR00956 269 qcsqdayELFDKVIVLYEGYQIYFGPADKAkqyfekMGfkCPDRQTTADFLTSL---------------TSPAERQIKP- 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446453387 285 gcPFVNRCPVAIKECI---HRFPERTTYSKEHSshcwQHVLEHNKAKSKEKVNAS 336
Cdd:TIGR00956 333 --GYEKKVPRTPQEFEtywRNSPEYAQLMKEID----EYLDRCSESDTKEAYRES 381
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-244 |
1.01e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 26 HVSFSINEGEIVALVGESGSGKSVTAQSIIGL---NQESIHIDDGNISFES--EELTN---LQESEWNQIRGKdiafifq 97
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIyqkDSGSILFQGKEIDFKSskEALENgisMVHQELNLVLQR------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 98 dplsSLNPTMKVGRQITEVILQHEKKSKKEAKEIAINLlnDLGIHEAEKRFEqyphqLSGGMRQRICLAIAFACHPKLVI 177
Cdd:PRK10982 89 ----SVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDEL--DIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446453387 178 ADEPTTAL---DVTIQKQIMELLKERkekqNTSILLITHDLALVREVADRVVVMYGG-----RVVEKGTIEEVIG 244
Cdd:PRK10982 158 MDEPTSSLtekEVNHLFTIIRKLKER----GCGIVYISHKMEEIFQLCDEITILRDGqwiatQPLAGLTMDKIIA 228
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-242 |
1.68e-04 |
|
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: 42.54 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 23 IVKHVSFSINEGEIVALVGESGSGKSVTAQSIIG--LNQESIHIDDGNISFESEeltnlqeSEW---NQIRGKDIAFIFQ 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGelEPSEGKIKHSGRISFSSQ-------FSWimpGTIKENIIFGVSY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 98 DPLSSLNPTMKVgrQITEVILQHEKKSKKeakeiainLLNDLGIheaekrfeqyphQLSGGMRQRICLAIAFACHPKLVI 177
Cdd:cd03291 125 DEYRYKSVVKAC--QLEEDITKFPEKDNT--------VLGEGGI------------TLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446453387 178 ADEPTTALDVTIQKQIMELLKERKEKQNTSIlLITHDLALVREvADRVVVMYGGRVVEKGTIEEV 242
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFESCVCKLMANKTRI-LVTSKMEHLKK-ADKILILHEGSSYFYGTFSEL 245
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
155-246 |
2.72e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 155 LSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELL-------KERkekqntsiLLITHDLALVrEVADRVVV 227
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECflgalagKTR--------VLATHQVHVV-PRADYVVA 853
|
90
....*....|....*....
gi 446453387 228 MYGGRVVEKGTIEEVIGSP 246
Cdd:PTZ00243 854 LGDGRVEFSGSSADFMRTS 872
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
155-247 |
3.25e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 155 LSGGMRQRICLAIAFAChpKLV----IADEPTTAL---DVTiqkQIMELLKERKEKQNTsILLITHDLALVREvADRVVV 227
Cdd:COG0178 486 LSGGEAQRIRLATQIGS--GLVgvlyVLDEPSIGLhqrDND---RLIETLKRLRDLGNT-VIVVEHDEDTIRA-ADYIID 558
|
90 100
....*....|....*....|....*.
gi 446453387 228 M------YGGRVVEKGTIEEVIGSPK 247
Cdd:COG0178 559 IgpgageHGGEVVAQGTPEEILKNPD 584
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
155-213 |
5.35e-04 |
|
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: 41.66 E-value: 5.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446453387 155 LSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKErkekQNTSILLITH 213
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE----FGITLFSVSH 637
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
154-233 |
7.28e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 154 QLSGGMRQRICLAIAFACHPKLVIADEPTTALDVTIQKQIMELLKERKekqnTSILLITHDLALVREVADRVVVMYGGRV 233
Cdd:PRK10636 430 RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFE----GALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
5-198 |
1.13e-03 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 39.53 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 5 LSLENVTLAVEKENSKQAIVKHVSFSINEGEIVALVGESGSGKSvTAQSIIGLNQESIHIdDGNISFESEELT-NLQESe 83
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKT-TLLDVLAGRKTAGVI-TGEILINGRPLDkNFQRS- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 84 wnqirgkdIAFIFQDPLssLNPTMKVgrqiTEVILQHEkkskkeakeiainLLNDLGIHEaekrfeqyphqlsggmRQRI 163
Cdd:cd03232 81 --------TGYVEQQDV--HSPNLTV----REALRFSA-------------LLRGLSVEQ----------------RKRL 117
|
170 180 190
....*....|....*....|....*....|....*
gi 446453387 164 CLAIAFACHPKLVIADEPTTALDVTIQKQIMELLK 198
Cdd:cd03232 118 TIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
24-258 |
3.05e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 38.83 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 24 VKHVSFSINEGeIVALVGESGSGKSvtaqSIIglnqESIHI---DDGNISFESEELTNLQESEWNQIRgkdIAFIFQDPL 100
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKS----SIL----EALRLllgPSSSRKFDEEDFYLGDDPDLPEIE---IELTFGSLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 101 S--------------------SLNPTMKVGRQITEVILQHEKKSKKEAKEIAI--------NLLNDLGIHEAEKrfEQYP 152
Cdd:COG3593 82 SrllrlllkeedkeeleealeELNEELKEALKALNELLSEYLKELLDGLDLELelsldeleDLLKSLSLRIEDG--KELP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 153 -HQLSGGMRQRICLAIAFACH-------PKLVIADEPTTALDVTIQKQIMELLKERKEKqNTSILLITHDLALVREV-AD 223
Cdd:COG3593 160 lDRLGSGFQRLILLALLSALAelkrapaNPILLIEEPEAHLHPQAQRRLLKLLKELSEK-PNQVIITTHSPHLLSEVpLE 238
|
250 260 270
....*....|....*....|....*....|....*
gi 446453387 224 RVVVMyggRVVEKGTIEEVIGSPKHPYTKSLLQAI 258
Cdd:COG3593 239 NIRRL---RRDSGGTTSTKLIDLDDEDLRKLLRYL 270
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
162-218 |
5.51e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 38.87 E-value: 5.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446453387 162 RICLAIAFACHPKLVIADEPTTALD----VTIQKQIMELLKERKEKQNTSILLITHDLALV 218
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDreniESLAHALVEIIKSRSQQRNFQLLVITHDEDFV 1273
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
154-187 |
7.29e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.30 E-value: 7.29e-03
10 20 30
....*....|....*....|....*....|....
gi 446453387 154 QLSGGMRQRICLAIAFACHPKLVIADEPTTALDV 187
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
36-120 |
9.24e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 35.78 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453387 36 IVALVGESGSGKSVTAQSIIGLNQESihiDDGNISFeseELTNLqeSEWNQIRgKDIAFIFQDPLSSLNPTMKVGRQITE 115
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLLEQLPEV---RDSVVFV---DLPSG--TSPKDLL-RALLRALGLPLSGRLSKEELLAALQQ 77
|
....*
gi 446453387 116 VILQH 120
Cdd:pfam13401 78 LLLAL 82
|
|
| |
