|
Name |
Accession |
Description |
Interval |
E-value |
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-339 |
0e+00 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 582.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKA 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRF 240
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 241 VQQLTDSEDTNETIESLIEKYPDGKVIRLQFIGEAVERPVLQRLMQRSDIEVSILQGNIAQTNNGSYGSLVVHLNGEETA 320
Cdd:COG1135 241 LPTVLNDELPEELLARLREAAGGGRLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDDAA 320
|
330
....*....|....*....
gi 446524434 321 IQQAIEGIHQDQVELEVIA 339
Cdd:COG1135 321 IDAALAYLREQGVVVEVLG 339
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-340 |
5.52e-172 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 481.22 E-value: 5.52e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKA 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRF 240
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 241 VQQLTDSEDTNETIESLIEKYP--DGKVIRLQFIGEAVERPVLQRLMQRSDIEVSILQGNIAQTNNGSYGSLVVHLNGEE 318
Cdd:PRK11153 241 IQSTLHLDLPEDYLARLQAEPTtgSGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGDP 320
|
330 340
....*....|....*....|..
gi 446524434 319 TAIQQAIEGIHQDQVELEVIAH 340
Cdd:PRK11153 321 GDIQAAIAYLQEHGVKVEVLGY 342
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-233 |
6.45e-150 |
|
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: 421.22 E-value: 6.45e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKA 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPK 233
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
1-340 |
1.67e-114 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 335.70 E-value: 1.67e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKA 80
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:TIGR02314 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRF 240
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 241 VQQLTDSEDTNETIESLIEK-----YPdgkVIRLQFIGEAVERPVLQRLMQRSDIEVSILQGNIAQTNNGSYGSLVVHLN 315
Cdd:TIGR02314 241 IRSTLHLSIPEDYQERLQATpfadsVP---MVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMH 317
|
330 340
....*....|....*....|....*
gi 446524434 316 GEETAIQQAIEGIHQDQVELEVIAH 340
Cdd:TIGR02314 318 GTQQDTQAAIAYLQEHNVKVEVLGY 342
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-244 |
1.52e-97 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 288.43 E-value: 1.52e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAiTGSELRKA 80
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENI-EFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNP 159
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVtLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 160 QVLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKR 239
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234
|
....*
gi 446524434 240 FVQQL 244
Cdd:COG1126 235 FLSKV 239
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-239 |
1.55e-97 |
|
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: 297.97 E-value: 1.55e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYKAKS-GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKARQ 82
Cdd:COG1123 263 VRNLSKRYPVRGkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 83 EIGMIFQH----FNLLWsrTVRENIEFPLEIAGV-DKAKRRKRVDELIHLVGL-EGRGDAYPSQLSGGQKQRVGIARALA 156
Cdd:COG1123 343 RVQMVFQDpyssLNPRM--TVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 157 NNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDI 236
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPY 500
|
...
gi 446524434 237 TKR 239
Cdd:COG1123 501 TRA 503
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-221 |
1.33e-92 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 275.38 E-value: 1.33e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKA 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 R-QEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNP 159
Cdd:COG1136 84 RrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 160 QVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRkICNRVAVMERGKIVE 221
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVS 224
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
13-242 |
3.41e-90 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 275.06 E-value: 3.41e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 13 AKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKARQE-IGMIFQHF 91
Cdd:COG4175 35 EKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELRELRRKkMSMVFQHF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 92 NLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSAL 171
Cdd:COG4175 115 ALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSAL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524434 172 DPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRFVQ 242
Cdd:COG4175 195 DPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVE 265
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-221 |
9.97e-89 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 265.38 E-value: 9.97e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKA 80
Cdd:COG2884 1 MIRFENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:COG2884 78 RRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINkRLGLTIVLITHEMHVIRKICNRVAVMERGKIVE 221
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-233 |
4.08e-88 |
|
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: 267.30 E-value: 4.08e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 3 LLE--NVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKP---TSGQITIANRVISAITGSEL 77
Cdd:COG0444 1 LLEvrNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 78 RKAR-QEIGMIFQH----FNLLWsrTVRENIEFPLEI-AGVDKAKRRKRVDELIHLVGL---EGRGDAYPSQLSGGQKQR 148
Cdd:COG0444 81 RKIRgREIQMIFQDpmtsLNPVM--TVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 149 VGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDV 228
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*
gi 446524434 229 FRNPK 233
Cdd:COG0444 239 FENPR 243
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-242 |
3.66e-87 |
|
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: 263.35 E-value: 3.66e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 14 KSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKAR-QEIGMIFQHFN 92
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRrKKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 93 LLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALD 172
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 173 PETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRFVQ 242
Cdd:cd03294 193 PLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFR 262
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-242 |
1.57e-85 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 258.48 E-value: 1.57e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIAnrvisaitGSELRKA 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD--------GKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLL-WsRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNP 159
Cdd:COG1116 79 GPDRGVVFQEPALLpW-LTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 160 QVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMH-VIRkICNRVAVMER--GKIVETGPV-LDVFRNPKQD 235
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVF-LADRVVVLSArpGRIVEEIDVdLPRPRDRELR 236
|
....*..
gi 446524434 236 ITKRFVQ 242
Cdd:COG1116 237 TSPEFAA 243
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-241 |
2.23e-85 |
|
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: 257.60 E-value: 2.23e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKA 80
Cdd:COG1127 5 MIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENIEFPL-EIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNP 159
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 160 QVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVlDVFRNPKQDITKR 239
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP-EELLASDDPWVRQ 239
|
..
gi 446524434 240 FV 241
Cdd:COG1127 240 FL 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-219 |
1.54e-84 |
|
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: 254.72 E-value: 1.54e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKAR 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 -QEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRkICNRVAVMERGKI 219
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-223 |
8.05e-83 |
|
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: 250.50 E-value: 8.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKA 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQH----FNLLWsrTVRENIEFPLEIAGV--DKAKRRKRVDELIHLVGL-EGRGDAYPSQLSGGQKQRVGIAR 153
Cdd:cd03257 81 RKEIQMVFQDpmssLNPRM--TIGEQIAEPLRIHGKlsKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 154 ALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-242 |
5.71e-81 |
|
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: 246.64 E-value: 5.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRvisAITGSELRKA 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR---PVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQH----FNLLWsrTVRENIEFPLEIAGVDKakRRKRVDELIHLVGLEGR-GDAYPSQLSGGQKQRVGIARAL 155
Cdd:COG1124 78 RRRVQMVFQDpyasLHPRH--TVDRILAEPLRIHGLPD--REERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 156 ANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQD 235
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
....*..
gi 446524434 236 ITKRFVQ 242
Cdd:COG1124 234 YTRELLA 240
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-233 |
1.65e-80 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 248.11 E-value: 1.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 3 LLE--NVKKIY-------KAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAIT 73
Cdd:COG4608 7 LLEvrDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 74 GSELRKARQEIGMIFQH-FNLLWSR-TVRENIEFPLEIAGV-DKAKRRKRVDELIHLVGL-EGRGDAYPSQLSGGQKQRV 149
Cdd:COG4608 87 GRELRPLRRRMQMVFQDpYASLNPRmTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 150 GIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVF 229
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELY 246
|
....
gi 446524434 230 RNPK 233
Cdd:COG4608 247 ARPL 250
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-225 |
2.20e-79 |
|
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: 241.61 E-value: 2.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAitgselrkAR 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG--------PG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLL-WsRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:cd03293 73 PDRGYVFQQDALLpW-LTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMH-VIRkICNRVAVMER--GKIVETGPV 225
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDeAVF-LADRVVVLSArpGRIVAEVEV 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-233 |
6.97e-79 |
|
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: 240.70 E-value: 6.97e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkakSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAitgSELRKAR 81
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQH-FNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:COG1122 75 RKVGLVFQNpDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPK 233
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-233 |
2.32e-78 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 243.47 E-value: 2.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITgSELRka 80
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP-PEKR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 rqEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:COG3842 78 --NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITH------EMhvirkiCNRVAVMERGKIVETGPVLDVFRNPK 233
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHdqeealAL------ADRIAVMNDGRIEQVGTPEEIYERPA 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-219 |
3.96e-75 |
|
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: 230.49 E-value: 3.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAiTGSELRKAR 81
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENI-EFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENItLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKI 219
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-230 |
5.41e-75 |
|
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: 230.85 E-value: 5.41e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKAR 81
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENIEFPL-EIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFR 230
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-225 |
7.52e-75 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 230.34 E-value: 7.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVIsaitGSELRKAR 81
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPV 225
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-223 |
2.17e-74 |
|
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: 228.56 E-value: 2.17e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITgselrKAR 81
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-----PER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-245 |
1.44e-72 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 224.89 E-value: 1.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVI---SAITGSELR 78
Cdd:PRK11124 3 IQLNGINCFY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 79 KARQEIGMIFQHFNLLWSRTVREN-IEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALAN 157
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLLDINKrLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVlDVFRNPKqdiT 237
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQ---T 233
|
....*...
gi 446524434 238 KRFVQQLT 245
Cdd:PRK11124 234 EAFKNYLS 241
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-250 |
2.77e-72 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 224.55 E-value: 2.77e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkakSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKA 80
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENI----------------EFPLEiagvDKAkrrkRVDELIHLVGLEGRGDAYPSQLSGG 144
Cdd:COG3638 79 RRRIGMIFQQFNLVPRLSVLTNVlagrlgrtstwrsllgLFPPE----DRE----RALEALERVGLADKAYQRADQLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 145 QKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIvetgp 224
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV----- 225
|
250 260
....*....|....*....|....*.
gi 446524434 225 vldVFRNPKQDITKRFVQQLTDSEDT 250
Cdd:COG3638 226 ---VFDGPPAELTDAVLREIYGGEAE 248
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-243 |
2.96e-71 |
|
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: 221.41 E-value: 2.96e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKar 81
Cdd:cd03295 1 IEFENVTKRYG---GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 qEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLE--GRGDAYPSQLSGGQKQRVGIARALANNP 159
Cdd:cd03295 76 -KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 160 QVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKR 239
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAE 234
|
....
gi 446524434 240 FVQQ 243
Cdd:cd03295 235 FVGA 238
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-233 |
4.80e-69 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 216.93 E-value: 4.80e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKSG-DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKA 80
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQhF--NLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGL-EGRGDAYPSQLSGGQKQRVGIARALAN 157
Cdd:TIGR04521 81 RKKVGLVFQ-FpeHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPK 233
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
15-234 |
5.30e-69 |
|
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: 224.01 E-value: 5.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 15 SGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPT---SGQITIANRVISAITGSELRKarqEIGMIFQHF 91
Cdd:COG1123 16 GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR---RIGMVFQDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 92 -NLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSA 170
Cdd:COG1123 93 mTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524434 171 LDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQ 234
Cdd:COG1123 173 LDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-244 |
1.51e-68 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 214.49 E-value: 1.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVIS---AITGSELR 78
Cdd:COG4161 3 IQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 79 KARQEIGMIFQHFNLLWSRTVREN-IEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALAN 157
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLLDInKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPvLDVFRNPKqdiT 237
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ---T 233
|
....*..
gi 446524434 238 KRFVQQL 244
Cdd:COG4161 234 EAFAHYL 240
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-218 |
2.36e-68 |
|
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: 211.66 E-value: 2.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVIsAITGSELRKAR 81
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL-TDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENIEFPLeiagvdkakrrkrvdelihlvglegrgdaypsqlSGGQKQRVGIARALANNPQV 161
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGK 218
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-245 |
3.33e-68 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 217.32 E-value: 3.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKar 81
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 qeIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:COG1118 77 --VGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKqditKRFV 241
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA----TPFV 230
|
....
gi 446524434 242 QQLT 245
Cdd:COG1118 231 ARFL 234
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-233 |
1.19e-67 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 216.09 E-value: 1.19e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgsELRKA 80
Cdd:COG3839 3 SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-----DLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:COG3839 74 DRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHE----MhvirKICNRVAVMERGKIVETGPVLDVFRNPK 233
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaM----TLADRIAVMNDGRIQQVGTPEELYDRPA 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-239 |
2.33e-67 |
|
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: 220.33 E-value: 2.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 8 KKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEkPTSGQITIANRVISAITGSELRKARQEIGMI 87
Cdd:COG4172 289 RGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 88 FQH-FNLLWSR-TVRENIEFPLEI--AGVDKAKRRKRVDELIHLVGL-EGRGDAYPSQLSGGQKQRVGIARALANNPQVL 162
Cdd:COG4172 368 FQDpFGSLSPRmTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 163 LCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKR 239
Cdd:COG4172 448 VLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRA 524
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-241 |
2.48e-66 |
|
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: 208.63 E-value: 2.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSElrkaR 81
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QeIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:cd03300 73 P-VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRFV 241
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-242 |
3.45e-66 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 208.41 E-value: 3.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANrvISAITGS-ELRK 79
Cdd:PRK09493 1 MIEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKvDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 80 ARQEIGMIFQHFNLLWSRTVRENIEF-PLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANN 158
Cdd:PRK09493 75 IRQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 159 PQVLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITK 238
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQ 233
|
....
gi 446524434 239 RFVQ 242
Cdd:PRK09493 234 EFLQ 237
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-219 |
3.70e-66 |
|
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: 207.65 E-value: 3.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkakSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKAR 81
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKI 219
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-248 |
4.48e-66 |
|
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: 216.86 E-value: 4.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKS----SLIRLFNQLEKPTSGQITIANRVISAITGSELRKAR-QEIGMIFQH 90
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRgNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 91 ----FNLLWsrTVRENIEFPLEI-AGVDKAKRRKRVDELIHLVGL---EGRGDAYPSQLSGGQKQRVGIARALANNPQVL 162
Cdd:COG4172 101 pmtsLNPLH--TIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 163 LCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITkrfvQ 242
Cdd:COG4172 179 IADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYT----R 254
|
....*.
gi 446524434 243 QLTDSE 248
Cdd:COG4172 255 KLLAAE 260
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-224 |
3.04e-65 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 206.38 E-value: 3.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkakSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKA 80
Cdd:TIGR02315 1 MLEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENI--------EFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIA 152
Cdd:TIGR02315 78 RRRIGMIFQHYNLIERLTVLENVlhgrlgykPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 153 RALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGP 224
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGA 229
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-218 |
3.23e-65 |
|
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: 205.01 E-value: 3.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYKakSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAitgSELRKARQE 83
Cdd:cd03225 2 LKNLSFSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK---LSLKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQHFNL-LWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVL 162
Cdd:cd03225 77 VGLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446524434 163 LCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGK 218
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-244 |
4.05e-64 |
|
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: 203.18 E-value: 4.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkakSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKAR 81
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENIEFPL--------EIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIAR 153
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 154 ALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIvetgpvldVFRNPK 233
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI--------VFDGPP 229
|
250
....*....|.
gi 446524434 234 QDITKRFVQQL 244
Cdd:cd03256 230 AELTDEVLDEI 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-224 |
2.30e-63 |
|
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: 201.12 E-value: 2.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAitGSELRKA 80
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA--LDEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 R---QEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRvdELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALAN 157
Cdd:COG4181 86 RlraRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARAR--ALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKiCNRVAVMERGKIVETGP 224
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTA 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-243 |
6.03e-63 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 200.75 E-value: 6.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKsgdvTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITI------ANRVISAITG 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 75 sELRKARQEIGMIFQHFNLLWSRTVREN-IEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIAR 153
Cdd:PRK11264 79 -LIRQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 154 ALANNPQVLLCDEATSALDPETTDQILDLL--LDINKRlglTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRN 231
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIrqLAQEKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
250
....*....|..
gi 446524434 232 PKQDITKRFVQQ 243
Cdd:PRK11264 235 PQQPRTRQFLEK 246
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
16-244 |
6.61e-63 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 200.44 E-value: 6.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSE----------LRKARQEIG 85
Cdd:TIGR03005 11 GILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNgplvpadekhLRQMRNKIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 86 MIFQHFNLLWSRTVRENI-EFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLC 164
Cdd:TIGR03005 91 MVFQSFNLFPHKTVLDNVtEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAMRPKVMLF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 165 DEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRFVQQL 244
Cdd:TIGR03005 171 DEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKEERTREFLSKV 250
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
26-240 |
6.67e-62 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 198.10 E-value: 6.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 26 LKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGS----------ELRKARQEIGMIFQHFNLlW 95
Cdd:COG4598 29 LTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRdgelvpadrrQLQRIRTRLGMVFQSFNL-W 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 S-RTVREN-IEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDP 173
Cdd:COG4598 108 ShMTVLENvIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 174 ETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRF 240
Cdd:COG4598 188 ELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQF 253
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-231 |
1.11e-61 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 198.04 E-value: 1.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKakSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANrvISAITGSELRKAR 81
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQH-FNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:TIGR04520 77 KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKiCNRVAVMERGKIVETGPVLDVFRN 231
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-233 |
1.60e-60 |
|
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: 194.49 E-value: 1.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLE--NVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELr 78
Cdd:COG0411 2 DPLLEvrGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 79 kARQEIGMIFQHFNLLWSRTVRENIE----------FPLEIAGVDKAKR-----RKRVDELIHLVGLEGRGDAYPSQLSG 143
Cdd:COG0411 77 -ARLGIARTFQNPRLFPELTVLENVLvaaharlgrgLLAALLRLPRARReereaRERAEELLERVGLADRADEPAGNLSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 144 GQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
250
....*....|
gi 446524434 224 PVLDVFRNPK 233
Cdd:COG0411 236 TPAEVRADPR 245
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-225 |
1.06e-59 |
|
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: 191.24 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEK-----PTSGQITIANRVISA--ITGSE 76
Cdd:cd03260 3 LRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 77 LRKarqEIGMIFQHFNLLWSrTVRENIEFPLEIAGV-DKAKRRKRVDELIHLVGLEGRGD--AYPSQLSGGQKQRVGIAR 153
Cdd:cd03260 79 LRR---RVGMVFQKPNPFPG-SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 154 ALANNPQVLLCDEATSALDPETTDQILDLLLDINKRlgLTIVLITHEMHVIRKICNRVAVMERGKIVETGPV 225
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-241 |
8.02e-59 |
|
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: 189.47 E-value: 8.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSElrkar 81
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENIEFPLEI----AGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALAN 157
Cdd:cd03296 74 RNVGFVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDIT 237
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFV 233
|
....
gi 446524434 238 KRFV 241
Cdd:cd03296 234 YSFL 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-233 |
4.27e-57 |
|
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: 184.95 E-value: 4.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAItgSELRKARQE 83
Cdd:cd03219 3 VRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL--PPHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQHFNLLWSRTVRENIE----------FPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIAR 153
Cdd:cd03219 77 IGRTFQIPRLFPELTVLENVMvaaqartgsgLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 154 ALANNPQVLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPK 233
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-199 |
9.84e-57 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 185.07 E-value: 9.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRvisAITGSElrka 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPG---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 rQEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:COG4525 76 -ADRGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITH 199
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-219 |
2.40e-56 |
|
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: 181.06 E-value: 2.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVIsaitGSELRKAR 81
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENIEfpleiagvdkakrrkrvdelihlvglegrgdaypsqLSGGQKQRVGIARALANNPQV 161
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKI 219
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-232 |
4.10e-56 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 183.73 E-value: 4.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILL--ENVKKIYK-----AKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAIT 73
Cdd:PRK10419 1 MTLLnvSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 74 GSELRKARQEIGMIFQH----FNLlwSRTVRENIEFPLE-IAGVDKAKRRKRVDELIHLVGL-EGRGDAYPSQLSGGQKQ 147
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDsisaVNP--RKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 148 RVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPV-- 225
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVgd 238
|
....*..
gi 446524434 226 LDVFRNP 232
Cdd:PRK10419 239 KLTFSSP 245
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-242 |
4.14e-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: 4.14e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLE--NVKKIYKAKSG-----DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaiT 73
Cdd:COG4167 2 SALLEvrNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLE--Y 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 74 GSELRKARQeIGMIFQHFN--LLWSRTVRENIEFPLEIA-GVDKAKRRKRVDELIHLVGL-EGRGDAYPSQLSGGQKQRV 149
Cdd:COG4167 80 GDYKYRCKH-IRMIFQDPNtsLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 150 GIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVF 229
Cdd:COG4167 159 ALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVF 238
|
250
....*....|...
gi 446524434 230 RNPKQDITKRFVQ 242
Cdd:COG4167 239 ANPQHEVTKRLIE 251
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-226 |
1.12e-55 |
|
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: 180.78 E-value: 1.12e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKakSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgSELRKAR 81
Cdd:cd03263 1 LQIRNLTKTYK--KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDInkRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVL 226
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-223 |
3.80e-55 |
|
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: 179.37 E-value: 3.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgsELRKAR 81
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-----DLPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-230 |
8.38e-55 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 179.51 E-value: 8.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIAnrvisaitGSELRKA 80
Cdd:COG1121 6 AIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLF--------GKPPRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSrtvrenieFPL---EI--AGVD---------KAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQK 146
Cdd:COG1121 74 RRRIGYVPQRAEVDWD--------FPItvrDVvlMGRYgrrglfrrpSRADREAVDEALERVGLEDLADRPIGELSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 147 QRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVEtGPVL 226
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPE 223
|
....
gi 446524434 227 DVFR 230
Cdd:COG1121 224 EVLT 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
1.22e-53 |
|
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: 175.64 E-value: 1.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgSELRKAR 81
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:cd03265 73 RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-262 |
2.69e-53 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 180.23 E-value: 2.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 8 KKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKAR-QEIGM 86
Cdd:PRK10070 31 KEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 87 IFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDE 166
Cdd:PRK10070 111 VFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 167 ATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRF-----V 241
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFfrgvdI 270
|
250 260
....*....|....*....|..
gi 446524434 242 QQLTDSED-TNETIESLIEKYP 262
Cdd:PRK10070 271 SQVFSAKDiARRTPNGLIRKTP 292
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6-242 |
3.22e-53 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 175.93 E-value: 3.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 6 NVKKIYKaKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGS---------- 75
Cdd:PRK10619 7 NVIDLHK-RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 76 ELRKARQEIGMIFQHFNLLWSRTVRENI-EFPLEIAGVDKAKRRKRVDELIHLVGLEGRG-DAYPSQLSGGQKQRVGIAR 153
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 154 ALANNPQVLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPK 233
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQ 244
|
....*....
gi 446524434 234 QDITKRFVQ 242
Cdd:PRK10619 245 SPRLQQFLK 253
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-241 |
1.18e-52 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 174.07 E-value: 1.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQL--EKP---TSGQITIANRVISAITGS--ELRKarqEIGMIF 88
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDIYDPDVDvvELRR---RVGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 89 QHFNLLwSRTVRENIEFPLEIAGV-DKAKRRKRVDELIHLVGL----EGRGDAYPSQLSGGQKQRVGIARALANNPQVLL 163
Cdd:COG1117 99 QKPNPF-PKSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 164 CDEATSALDPETTDQILDLLLDINKRlgLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRFV 241
Cdd:COG1117 178 MDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-232 |
1.83e-52 |
|
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: 174.22 E-value: 1.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKA-----KSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGS 75
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 76 ELRKARQEIGMIFQH----FNLlwSRTVRENIEFPLE-IAGVDKAKRRKRVDELIHLVGLEGR-GDAYPSQLSGGQKQRV 149
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDspsaVNP--RMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEdADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 150 GIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPV--LD 227
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVaqLL 239
|
....*
gi 446524434 228 VFRNP 232
Cdd:TIGR02769 240 SFKHP 244
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
22-219 |
1.91e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 172.31 E-value: 1.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 22 DNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKarqEIGMIFQHfNLLWSRTVRE 101
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRR---QVAYVPQE-PALWGGTVRD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 102 NIEFPLEIAgvDKAKRRKRVDELIHLVGLEGRG-DAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQIL 180
Cdd:COG4619 93 NLPFPFQLR--ERKFDRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 446524434 181 DLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKI 219
Cdd:COG4619 171 ELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-240 |
3.94e-52 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 172.25 E-value: 3.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkaksGDVTAvdNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAitgseLRKA 80
Cdd:COG3840 1 MLRLDDLTYRY----GDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-----LPPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENIEFpleiaGVDKAKR-----RKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARAL 155
Cdd:COG3840 70 ERPVSMLFQENNLFPHLTVAQNIGL-----GLRPGLKltaeqRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 156 ANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQD 235
Cdd:COG3840 145 VRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
....*
gi 446524434 236 ITKRF 240
Cdd:COG3840 225 ALAAY 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-233 |
4.29e-51 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 172.46 E-value: 4.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 6 NVKKIYKAKSG------DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRK 79
Cdd:PRK11308 10 DLKKHYPVKRGlfkperLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 80 ARQEIGMIFQH-FNLLWSR-TVRENIEFPLEI-AGVDKAKRRKRVDELIHLVGLEGR-GDAYPSQLSGGQKQRVGIARAL 155
Cdd:PRK11308 90 LRQKIQIVFQNpYGSLNPRkKVGQILEEPLLInTSLSAAERREKALAMMAKVGLRPEhYDRYPHMFSGGQRQRIAIARAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 156 ANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPK 233
Cdd:PRK11308 170 MLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-231 |
6.22e-51 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 170.61 E-value: 6.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKSG-DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAiTGSELRKA 80
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNL-LWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGL--EGRGDAYPSQLSGGQKQRVGIARALAN 157
Cdd:PRK13637 82 RKKVGLVFQYPEYqLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRN 231
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-267 |
7.29e-51 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 173.10 E-value: 7.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 3 LLEnVKKIYKAKSGDvTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQItianrVISAITGSELRKARQ 82
Cdd:PRK11607 19 LLE-IRNLTKSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-----MLDGVDLSHVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 83 EIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVL 162
Cdd:PRK11607 92 PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 163 LCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPkqdiTKRFVQ 242
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP----TTRYSA 247
|
250 260
....*....|....*....|....*
gi 446524434 243 QLTDSEDTNETIesLIEKYPDGKVI 267
Cdd:PRK11607 248 EFIGSVNVFEGV--LKERQEDGLVI 270
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-232 |
1.27e-49 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 167.50 E-value: 1.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKSG-DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGS-ELRK 79
Cdd:PRK13634 3 ITFQKVEHRYQYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 80 ARQEIGMIFQhF--NLLWSRTVRENIEF-PLEIaGVDKAKRRKRVDELIHLVGL-EGRGDAYPSQLSGGQKQRVGIARAL 155
Cdd:PRK13634 83 LRKKVGIVFQ-FpeHQLFEETVEKDICFgPMNF-GVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 156 ANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNP 232
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
16-229 |
1.57e-49 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 165.99 E-value: 1.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELrkARQeIGMIFQHFNLLW 95
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL--ARR-IAYVPQEPPAPF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 SRTVRENIE---FP-LEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSAL 171
Cdd:COG1120 89 GLTVRELVAlgrYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 172 DPETTDQILDLLLDINKRLGLTIVLITHEM-HVIRkICNRVAVMERGKIVETGPVLDVF 229
Cdd:COG1120 169 DLAHQLEVLELLRRLARERGRTVVMVLHDLnLAAR-YADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-218 |
5.42e-49 |
|
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: 161.78 E-value: 5.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKakSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKAr 81
Cdd:cd03228 1 IEFKNVSFSYP--GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 qeIGMIFQHFnLLWSRTVRENIefpleiagvdkakrrkrvdelihlvglegrgdaypsqLSGGQKQRVGIARALANNPQV 161
Cdd:cd03228 78 --IAYVPQDP-FLFSGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKrlGLTIVLITHEMHVIRKiCNRVAVMERGK 218
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-219 |
8.52e-49 |
|
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: 162.70 E-value: 8.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIAnrvisaitGSELRKARQE 83
Cdd:cd03235 2 VEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF--------GKPLEKERKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQHFNLLWSR--TVRENIEFPL----EIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALAN 157
Cdd:cd03235 70 IGYVPQRRSIDRDFpiSVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLLDINkRLGLTIVLITHEMHVIRKICNRVAVMERGKI 219
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-220 |
9.06e-49 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 163.12 E-value: 9.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKA 80
Cdd:PRK10908 1 MIRFEHVSKAYL---GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:PRK10908 78 RRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINkRLGLTIVLITHEMHVIRKICNRVAVMERGKIV 220
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-291 |
2.12e-48 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 164.51 E-value: 2.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgselRKA 80
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIG-----------MifqhfnllwsrTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRV 149
Cdd:COG4152 70 RRRIGylpeerglypkM-----------KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 150 GIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVf 229
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI- 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 230 rnpKQDITKRFVQ-QLTDSEDTNETIESLIEKYPDGKVIRLQFIGEAVERPVLQRLMQRSDIE 291
Cdd:COG4152 217 ---RRQFGRNTLRlEADGDAGWLRALPGVTVVEEDGDGAELKLEDGADAQELLRALLARGPVR 276
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
2.24e-48 |
|
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: 172.71 E-value: 2.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKkiYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKAr 81
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 qeIGMIFQHfNLLWSRTVRENIEF--P----------LEIAGVDkakrrkrvdELI--------HLVGLEGRGdaypsqL 141
Cdd:COG2274 551 --IGVVLQD-VFLFSGTIRENITLgdPdatdeeiieaARLAGLH---------DFIealpmgydTVVGEGGSN------L 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 142 SGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKrlGLTIVLITHEMHVIRKiCNRVAVMERGKIVE 221
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVE 689
|
...
gi 446524434 222 TGP 224
Cdd:COG2274 690 DGT 692
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-169 |
2.49e-47 |
|
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: 157.04 E-value: 2.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 21 VDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRvisAITGSELRKARQEIGMIFQHFNLLWSRTVR 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQ---DLTDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 101 ENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGD----AYPSQLSGGQKQRVGIARALANNPQVLLCDEATS 169
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-233 |
4.16e-47 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 162.58 E-value: 4.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRvisAITGSELRKarQE 83
Cdd:PRK11432 9 LKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE---DVTHRSIQQ--RD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLL 163
Cdd:PRK11432 80 ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 164 CDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPK 233
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-241 |
4.76e-47 |
|
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: 159.04 E-value: 4.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYKAKSgdvtaVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgsELRKARQE 83
Cdd:cd03299 3 VENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-----NLPPEKRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLL 163
Cdd:cd03299 73 ISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 164 CDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRFV 241
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-223 |
7.68e-47 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 157.84 E-value: 7.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 22 DNANLKIE---KGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRV-----ISAITGSELRKarqeIGMIFQHFNL 93
Cdd:cd03297 11 PDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrKKINLPPQQRK----IGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 94 LWSRTVRENIEFPLEiaGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDP 173
Cdd:cd03297 87 FPHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524434 174 ETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
13-238 |
9.42e-47 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 161.03 E-value: 9.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 13 AKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKARQEIGMIFQhfN 92
Cdd:PRK15079 29 QPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQ--D 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 93 LLWS----RTVRENIEFPLEI--AGVDKAKRRKRVDELIHLVGL-EGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCD 165
Cdd:PRK15079 107 PLASlnprMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 166 EATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITK 238
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-201 |
1.37e-46 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 158.71 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSgdvtAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRvisAITGSElrka 80
Cdd:PRK11248 1 MLQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVEGPG---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 rQEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:PRK11248 70 -AERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEM 201
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-230 |
1.56e-46 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 159.03 E-value: 1.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKkiYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKar 81
Cdd:PRK13635 6 IRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 qEIGMIFQH-FNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:PRK13635 82 -QVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKiCNRVAVMERGKIVETGPVLDVFR 230
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-224 |
1.68e-46 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 166.82 E-value: 1.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKARQE 83
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 -IGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVL 162
Cdd:PRK10535 87 hFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 163 LCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKiCNRVAVMERGKIVETGP 224
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPP 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-232 |
1.70e-46 |
|
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: 161.04 E-value: 1.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 23 NANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVI-SAITGSELRKARQEIGMIFQHFNLLWSRTVRE 101
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqDSARGIFLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 102 NIEFPLEIAGvdKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILD 181
Cdd:COG4148 97 NLLYGRKRAP--RAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446524434 182 LLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNP 232
Cdd:COG4148 175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-241 |
1.78e-46 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 161.65 E-value: 1.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITgSELRkar 81
Cdd:PRK09452 15 VELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AENR--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 qEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:PRK09452 87 -HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRFV 241
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFI 245
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-233 |
2.12e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 158.70 E-value: 2.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 3 LLENVKKIYKAKSGDVtAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaITGSELRKARQ 82
Cdd:PRK13639 1 ILETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 83 EIGMIFQHF-NLLWSRTVRENIEF-PLEIaGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:PRK13639 79 TVGIVFQNPdDQLFAPTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPK 233
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
4.44e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 157.85 E-value: 4.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKkiYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITgseLRKA 80
Cdd:PRK13632 7 MIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN---LKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQH-FNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNP 159
Cdd:PRK13632 82 RKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 160 QVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKiCNRVAVMERGKIVETGPVLDVFRN 231
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-224 |
7.83e-46 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 164.18 E-value: 7.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKArqeIGMIFQHFnLLW 95
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ---IGVVPQDT-FLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 SRTVRENIEFPLEIAG---VDKAKRRKRVDELIH--------LVGLEGrgdaypSQLSGGQKQRVGIARALANNPQVLLC 164
Cdd:COG1132 427 SGTIRENIRYGRPDATdeeVEEAAKAAQAHEFIEalpdgydtVVGERG------VNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 165 DEATSALDPETTDQILDLLLDINKrlGLTIVLITHEMHVIRKiCNRVAVMERGKIVETGP 224
Cdd:COG1132 501 DEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-241 |
9.47e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 156.23 E-value: 9.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 12 KAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQL-----EKPTSGQITIANRVISAITGSELRKARQeigM 86
Cdd:PRK14247 10 KVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRRRVQ---M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 87 IFQHFNLLWSRTVRENIEFPLEIAGVDKAKR--RKRVDELIHLVGL----EGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:PRK14247 87 VFQIPNPIPNLSIFENVALGLKLNRLVKSKKelQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRlgLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRF 240
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKY 244
|
.
gi 446524434 241 V 241
Cdd:PRK14247 245 V 245
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-225 |
2.43e-45 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 161.35 E-value: 2.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaITGSelRKARQE 83
Cdd:COG3845 8 LRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-IRSP--RDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 -IGMIFQHFNLLWSRTVRENI----EfPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANN 158
Cdd:COG3845 81 gIGMVHQHFMLVPNLTVAENIvlglE-PTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 159 PQVLLCDEATSALDPETTDQildlLLDINKRL---GLTIVLITHEMHVIRKICNRVAVMERGKIVETGPV 225
Cdd:COG3845 160 ARILILDEPTAVLTPQEADE----LFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDT 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-260 |
3.36e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 155.76 E-value: 3.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKSG-DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSE-LRK 79
Cdd:PRK13641 3 IKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 80 ARQEIGMIFQhF--NLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGL-EGRGDAYPSQLSGGQKQRVGIARALA 156
Cdd:PRK13641 83 LRKKVSLVFQ-FpeAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 157 NNPQVLLCDEATSALDPETTDQILDLLLDInKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPK--- 233
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwlk 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 446524434 234 -----QDITKRFVQQLTDS----EDTNETIESLIEK 260
Cdd:PRK13641 241 khyldEPATSRFASKLEKGgfkfSEMPLTIDELVDG 276
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-223 |
1.57e-44 |
|
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: 151.58 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKsgdvTAVDNANLKIEKGeIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAitgsELRKAR 81
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK----QPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKrlGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
15-232 |
2.78e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 153.03 E-value: 2.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 15 SGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRvisAITGSELRKARQEIGMIFQHFN-L 93
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE---PITKENIREVRKFVGLVFQNPDdQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 94 LWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDP 173
Cdd:PRK13652 91 IFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 174 ETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNP 232
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-241 |
3.38e-44 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 160.41 E-value: 3.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 17 DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKARQEIGMIFQ--HFNLL 94
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQdpYASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 95 WSRTVRENIEFPLEIAGV-DKAKRRKRVDELIHLVGLEGRGD-AYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALD 172
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 173 PETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRFV 241
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-219 |
1.34e-43 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 149.97 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGS---EL 77
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 78 RKarQEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALAN 157
Cdd:PRK11629 85 RN--QKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKIcNRVAVMERGKI 219
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-231 |
1.72e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 151.39 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVkkIYKAKSGD----VTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANrvISAITGSE 76
Cdd:PRK13633 4 MIKCKNV--SYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 77 LRKARQEIGMIFQH-FNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARAL 155
Cdd:PRK13633 80 LWDIRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524434 156 ANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKiCNRVAVMERGKIVETGPVLDVFRN 231
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-218 |
2.90e-43 |
|
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: 146.62 E-value: 2.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAItgsELRKARQE 83
Cdd:cd00267 2 IENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKL---PLEELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQhfnllwsrtvreniefpleiagvdkakrrkrvdelihlvglegrgdaypsqLSGGQKQRVGIARALANNPQVLL 163
Cdd:cd00267 75 IGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446524434 164 CDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGK 218
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-241 |
7.27e-43 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 151.77 E-value: 7.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRkar 81
Cdd:PRK10851 3 IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 qeIGMIFQHFNLLWSRTVRENIEFPLEI----AGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALAN 157
Cdd:PRK10851 76 --VGFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPkqdiT 237
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP----A 229
|
....
gi 446524434 238 KRFV 241
Cdd:PRK10851 230 TRFV 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-228 |
1.24e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 154.02 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKARqe 83
Cdd:COG1129 7 MRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQHFNLLWSRTVRENIEFPLEIAG---VDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDInKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDV 228
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-223 |
1.87e-42 |
|
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: 146.21 E-value: 1.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgsELRKAR 81
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-----KNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENiefpLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:cd03268 72 RRIGALIEAPGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-223 |
6.38e-42 |
|
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: 152.99 E-value: 6.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkakSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKAr 81
Cdd:COG4988 337 IELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 qeIGMIFQHfNLLWSRTVRENIEFPLEIAG---VDKAKRRKRVDELI--------HLVGLEGRGdaypsqLSGGQKQRVG 150
Cdd:COG4988 413 --IAWVPQN-PYLFAGTIRENLRLGRPDASdeeLEAALEAAGLDEFVaalpdgldTPLGEGGRG------LSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 151 IARALANNPQVLLCDEATSALDPETTDQILDLLLDINKrlGLTIVLITHEMHVIRkICNRVAVMERGKIVETG 223
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLA-QADRILVLDDGRIVEQG 553
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-257 |
6.59e-42 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 148.35 E-value: 6.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 20 AVDNANLKIEKGEIFGVIGYSGAGKS----SLIRLFNQLEKPTSGQITIANRVISAITGSELRK-ARQEIGMIFQH--FN 92
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNlVGAEVAMIFQDpmTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 93 LLWSRTVRENIEFPLEI-AGVDKAKRRKRVDELIHLVGL---EGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEAT 168
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 169 SALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRFVQQLTDSE 248
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALPEFA 261
|
....*....
gi 446524434 249 DTNETIESL 257
Cdd:PRK11022 262 QDKARLASL 270
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-231 |
8.28e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 147.08 E-value: 8.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKSG-DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGS--ELR 78
Cdd:PRK13645 7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 79 KARQEIGMIFQHFNL-LWSRTVRENIEF-PLEIaGVDKAKRRKRVDELIHLVGL-EGRGDAYPSQLSGGQKQRVGIARAL 155
Cdd:PRK13645 87 RLRKEIGLVFQFPEYqLFQETIEKDIAFgPVNL-GENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524434 156 ANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRN 231
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-234 |
1.05e-41 |
|
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: 144.92 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 21 VDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIanrvisaiTGSELRKARQEIGMIFQHFNLLWSRTVR 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL--------EGKQITEPGPDRMVVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 101 ENIEFPLEIAGVD--KAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQ 178
Cdd:TIGR01184 73 ENIALAVDRVLPDlsKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 179 ILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDV-FRNPKQ 234
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-223 |
1.40e-41 |
|
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: 144.43 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgSELRKA 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDInKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-219 |
1.05e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 143.72 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGDVTaVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANrviSAITGSELRKA 80
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQH-FNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNP 159
Cdd:PRK13650 80 RHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 160 QVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIrKICNRVAVMERGKI 219
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-223 |
1.90e-40 |
|
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: 140.26 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELrkarqe 83
Cdd:cd03214 2 VENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 igmifqhfnllwsrtvreniefpleiagvdkAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLL 163
Cdd:cd03214 72 -------------------------------ARKIAYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 164 CDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-241 |
2.03e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 142.29 E-value: 2.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQL-----EKPTSGQITIANRVISAITGSELRkARQEIGMIFQH 90
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIE-VRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 91 FNLLWSRTVRENIEFPLEIAGVdkAKRRKRVDELIHLV--------GLEGRGDAYPSQLSGGQKQRVGIARALANNPQVL 162
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGL--VKSKKELDERVEWAlkkaalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 163 LCDEATSALDPETTDQILDLLLDINKRlgLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRFV 241
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-223 |
2.07e-40 |
|
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: 141.85 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKSGDVtaVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKar 81
Cdd:cd03252 1 ITFEHVRFRYKPDGPVI--LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 qEIGMIFQHfNLLWSRTVRENIefpleiAGVDKAKRRKRVDELIHLVGL--------EGRGDAYPSQ---LSGGQKQRVG 150
Cdd:cd03252 77 -QVGVVLQE-NVLFNRSIRDNI------ALADPGMSMERVIEAAKLAGAhdfiselpEGYDTIVGEQgagLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 151 IARALANNPQVLLCDEATSALDPETTDQILDLLLDINKrlGLTIVLITHEMHVIRKiCNRVAVMERGKIVETG 223
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-291 |
2.34e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 144.07 E-value: 2.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGD-----------------VTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQIT 63
Cdd:COG4586 1 IIEVENLSKTYRVYEKEpglkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 64 IANRVISaitgsELRKA-RQEIGMIF-QHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEG------Rgd 135
Cdd:COG4586 81 VLGYVPF-----KRRKEfARRIGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGElldtpvR-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 136 aypsQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVME 215
Cdd:COG4586 154 ----QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVID 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 216 RGKIVETGPV---LDVFRNPKQdITKRFVQQLTDsedtnETIESLIE-KYPDGKVIRLQFIGEAVERPVLQRLMQRSDIE 291
Cdd:COG4586 230 HGRIIYDGSLeelKERFGPYKT-IVLELAEPVPP-----LELPRGGEvIEREGNRVRLEVDPRESLAEVLARLLARYPVR 303
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-223 |
2.53e-40 |
|
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: 140.71 E-value: 2.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 26 LKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAitgseLRKARQEIGMIFQHFNLLWSRTVRENIEF 105
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA-----APPADRPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 106 PLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLD 185
Cdd:cd03298 94 GLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 446524434 186 INKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-222 |
3.04e-40 |
|
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: 139.10 E-value: 3.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKARqe 83
Cdd:cd03216 3 LRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQhfnllwsrtvreniefpleiagvdkakrrkrvdelihlvglegrgdaypsqLSGGQKQRVGIARALANNPQVLL 163
Cdd:cd03216 77 IAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 164 CDEATSALDPETTDQILDLLLDInKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVET 222
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-333 |
3.52e-40 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 144.79 E-value: 3.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgsELRKARQE 83
Cdd:PRK11000 6 LRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-----DVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLL 163
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 164 CDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQditkRFVQQ 243
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPAN----RFVAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 244 LTDSEDTN--------ETIESLIEKYPDGKVIRLQFIGEAVE---------RPvlQRLMQRSDIEVSiLQGNIaqtnngs 306
Cdd:PRK11000 233 FIGSPKMNflpvkvtaTAIEQVQVELPNRQQVWLPVEGRGVQvganmslgiRP--EHLLPSDIADVT-LEGEV------- 302
|
330 340
....*....|....*....|....*..
gi 446524434 307 ygsLVVHLNGEETAIQQAIEGIHQDQV 333
Cdd:PRK11000 303 ---QVVEQLGNETQIHIQIPAIRQNLV 326
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-223 |
4.51e-40 |
|
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: 140.11 E-value: 4.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAitgselrKARQE 83
Cdd:cd03269 3 VENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-------AARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLL 163
Cdd:cd03269 72 IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 164 CDEATSALDPETTDQILDLLLDInKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-223 |
6.21e-40 |
|
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: 140.55 E-value: 6.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 3 LLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVisaiTGSELRKARQ 82
Cdd:cd03267 19 LIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV----PWKRRKKFLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 83 EIGMIF-QHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:cd03267 95 RIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
1.76e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 141.48 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgSELRKAR 81
Cdd:PRK13537 8 IDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP----SRARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERG-KIVETGP 224
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGrKIAEGAP 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-224 |
2.69e-39 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 146.06 E-value: 2.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKArqeIGMIFQHfNLLW 95
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR---IAVVPQR-PHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 SRTVRENIEF--P----------LEIAGVDKAkrrkrVDELIHlvGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLL 163
Cdd:COG4987 422 DTTLRENLRLarPdatdeelwaaLERVGLGDW-----LAALPD--GLDTWLGEGGRRLSGGERRRLALARALLRDAPILL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524434 164 CDEATSALDPETTDQILDLLLDINKrlGLTIVLITHEMHVIRKiCNRVAVMERGKIVETGP 224
Cdd:COG4987 495 LDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGT 552
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-246 |
3.23e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 139.88 E-value: 3.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKSG-DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAIT-GSELRK 79
Cdd:PRK13649 3 INLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSkNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 80 ARQEIGMIFQhF--NLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGL-EGRGDAYPSQLSGGQKQRVGIARALA 156
Cdd:PRK13649 83 IRKKVGLVFQ-FpeSQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 157 NNPQVLLCDEATSALDPETTDQILDLLLDINkRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRN----- 231
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDvdfle 240
|
250 260
....*....|....*....|.
gi 446524434 232 ------PKqdITKrFVQQLTD 246
Cdd:PRK13649 241 ekqlgvPK--ITK-FAQRLAD 258
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-232 |
3.24e-39 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 141.79 E-value: 3.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 24 ANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVI-SAITGSELRKARQEIGMIFQHFNLLWSRTVREN 102
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 103 IEFPLEIAgvDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDL 182
Cdd:TIGR02142 96 LRYGMKRA--RPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524434 183 LLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNP 232
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-229 |
3.87e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 139.98 E-value: 3.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 20 AVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaITGSELRKARQEIGMIFQH-FNLLWSRT 98
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKLRESVGMVFQDpDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 99 VRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQ 178
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446524434 179 ILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVF 229
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-230 |
5.64e-39 |
|
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: 144.56 E-value: 5.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIY-KAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIA---NRVISAITGSE 76
Cdd:TIGR03269 279 IIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 77 LR-KARQEIGMIFQHFNLLWSRTVREN------IEFPLEIAgvdkakRRKRVDELIhLVGLEGRG-----DAYPSQLSGG 144
Cdd:TIGR03269 359 GRgRAKRYIGILHQEYDLYPHRTVLDNlteaigLELPDELA------RMKAVITLK-MVGFDEEKaeeilDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 145 QKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGP 224
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....*.
gi 446524434 225 VLDVFR 230
Cdd:TIGR03269 512 PEEIVE 517
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-223 |
1.00e-38 |
|
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: 137.29 E-value: 1.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKSgDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAItgsELRKAR 81
Cdd:cd03249 1 IEFKNVSFRYPSRP-DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL---NLRWLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHfNLLWSRTVRENIEF---PLEIAGVDKAKRRKRVDELIhlVGLEGRGD----AYPSQLSGGQKQRVGIARA 154
Cdd:cd03249 77 SQIGLVSQE-PVLFDGTIAENIRYgkpDATDEEVEEAAKKANIHDFI--MSLPDGYDtlvgERGSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 155 LANNPQVLLCDEATSALDPETTDQILDLLLDInkRLGLTIVLITHEMHVIRKiCNRVAVMERGKIVETG 223
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQG 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-224 |
1.57e-38 |
|
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: 136.41 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELrkARQE 83
Cdd:cd03224 3 VENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQHFNLLWSRTVRENIEfpLEIAGVDKAKRRKRVDELIHLV-GLEGRGDAYPSQLSGGQKQRVGIARALANNPQVL 162
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLL--LGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 163 LCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGP 224
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-246 |
3.68e-38 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 138.50 E-value: 3.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 15 SGDVTAVDNANLKIEKGEIFGVIGYSGAGKS----SLIRLFNQLEKPTSGQITIANRVISAITGSELRK-ARQEIGMIFQ 89
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSPRERRKiIGREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 90 HFN--LLWSRTVRENIEFPLEiAGVDKAK-------RRKRVDELIHLVGLEGRGD---AYPSQLSGGQKQRVGIARALAN 157
Cdd:COG4170 97 EPSscLDPSAKIGDQLIEAIP-SWTFKGKwwqrfkwRKKRAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMAIAN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDIT 237
Cdd:COG4170 176 QPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYT 255
|
....*....
gi 446524434 238 KRFVQQLTD 246
Cdd:COG4170 256 KALLRSMPD 264
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-232 |
3.83e-38 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 139.21 E-value: 3.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkakSGDVTAVDNANLKIEKGEiFGVI-GYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgsELRK 79
Cdd:PRK11650 3 GLKLQAVRKSY---DGKTQVIKGIDLDVADGE-FIVLvGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN-----ELEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 80 ARQEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNP 159
Cdd:PRK11650 74 ADRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 160 QVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHE----MhvirKICNRVAVMERGKIVETGPVLDVFRNP 232
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDqveaM----TLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
3.83e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 137.04 E-value: 3.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSgdvTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIanRVISAITGSELRKA 80
Cdd:PRK13644 1 MIRLENVSYSYPDGT---PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV--SGIDTGDFSKLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLW-SRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNP 159
Cdd:PRK13644 76 RKLVGIVFQNPETQFvGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524434 160 QVLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITH---EMHVirkiCNRVAVMERGKIVETGPVLDVFRNP 232
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHnleELHD----ADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-230 |
4.15e-38 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 135.98 E-value: 4.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIY------------------KAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQI 62
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 63 TIANRVISAItgselrkarqEIGMIFQHfnllwSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDA----YP 138
Cdd:COG1134 84 EVNGRVSALL----------ELGAGFHP-----ELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQpvktYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 139 SqlsgGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGK 218
Cdd:COG1134 149 S----GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
250
....*....|..
gi 446524434 219 IVETGPVLDVFR 230
Cdd:COG1134 224 LVMDGDPEEVIA 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-224 |
9.54e-38 |
|
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: 134.67 E-value: 9.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAksgDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKAr 81
Cdd:cd03253 1 IEFENVTFAYDP---GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 qeIGMIFQHfNLLWSRTVRENIEFPLEIAG---VDKAKRRKRVDELIhlvglEGRGDAYPSQ-------LSGGQKQRVGI 151
Cdd:cd03253 77 --IGVVPQD-TVLFNDTIGYNIRYGRPDATdeeVIEAAKAAQIHDKI-----MRFPDGYDTIvgerglkLSGGEKQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 152 ARALANNPQVLLCDEATSALDPETTDQILDLLLDINKrlGLTIVLITHEMHVIRKiCNRVAVMERGKIVETGP 224
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-233 |
9.68e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 136.75 E-value: 9.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKSG-DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANR------------- 67
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 68 -----VISAITGSELRKA---RQEIGMIFQHFNL-LWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGL-EGRGDAY 137
Cdd:PRK13651 83 vleklVIQKTRFKKIKKIkeiRRRVGVVFQFAEYqLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 138 PSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERG 217
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
250
....*....|....*.
gi 446524434 218 KIVETGPVLDVFRNPK 233
Cdd:PRK13651 242 KIIKDGDTYDILSDNK 257
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-234 |
1.40e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 136.06 E-value: 1.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIY-KAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAIT-GSELRK 79
Cdd:PRK13646 3 IRFDNVSYTYqKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 80 ARQEIGMIFQhF--NLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEgRG--DAYPSQLSGGQKQRVGIARAL 155
Cdd:PRK13646 83 VRKRIGMVFQ-FpeSQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS-RDvmSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 156 ANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQ 234
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-223 |
2.18e-37 |
|
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: 133.43 E-value: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIY------------------KAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQIT 63
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 64 IANRVISAItgselrkarqEIGMIFQHfnllwSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSG 143
Cdd:cd03220 81 VRGRVSSLL----------GLGGGFNP-----ELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 144 GQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-233 |
3.51e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 133.23 E-value: 3.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKsgdvTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAitgseL--- 77
Cdd:COG1137 3 TLEAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH-----Lpmh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 78 RKARQEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALAN 157
Cdd:COG1137 74 KRARLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLLDINKR-LGltiVLIT-HEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPK 233
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKIIRHLKERgIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-241 |
4.07e-37 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 134.15 E-value: 4.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 3 LLE--NVKKIYKAKSG-----DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRvisAITGS 75
Cdd:PRK15112 4 LLEvrNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 76 ELRKARQEIGMIFQHFNLlwSRTVRENI----EFPLEI-AGVDKAKRRKRVDELIHLVGL-EGRGDAYPSQLSGGQKQRV 149
Cdd:PRK15112 81 DYSYRSQRIRMIFQDPST--SLNPRQRIsqilDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 150 GIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVF 229
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
250
....*....|..
gi 446524434 230 RNPKQDITKRFV 241
Cdd:PRK15112 239 ASPLHELTKRLI 250
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-262 |
4.16e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 135.36 E-value: 4.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 6 NVKKIYKAK-SGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSE-------- 76
Cdd:PRK13631 26 NLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHelitnpys 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 77 -----LRKARQEIGMIFQHFNL-LWSRTVRENIEFPLEIAGVDKAKRRKRVDelIHLVGLeGRGDAY----PSQLSGGQK 146
Cdd:PRK13631 106 kkiknFKELRRRVSMVFQFPEYqLFKDTIEKDIMFGPVALGVKKSEAKKLAK--FYLNKM-GLDDSYlersPFGLSGGQK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 147 QRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDiNKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVL 226
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPY 261
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446524434 227 DVFRNP----KQDITK-RFVQQLTDSEDTNETIESLIEKYP 262
Cdd:PRK13631 262 EIFTDQhiinSTSIQVpRVIQVINDLIKKDPKYKKLYQKQP 302
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-219 |
4.37e-37 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 133.65 E-value: 4.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQItianrvisaITGSE-LRKA 80
Cdd:PRK11247 13 LLLNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL---------LAGTApLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENIEFPLeiagvdKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:PRK11247 80 REDTRLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKI 219
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-223 |
6.09e-37 |
|
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: 132.33 E-value: 6.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKsgDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRkar 81
Cdd:cd03245 3 IEFRNVSFSYPNQ--EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHfNLLWSRTVRENIEF------------PLEIAGVDK-AKRRKRVDELihLVGLEGRGdaypsqLSGGQKQR 148
Cdd:cd03245 78 RNIGYVPQD-VTLFYGTLRDNITLgapladderilrAAELAGVTDfVNKHPNGLDL--QIGERGRG------LSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 149 VGIARALANNPQVLLCDEATSALDPETTDQILDLLldinKRL--GLTIVLITHEMHVIrKICNRVAVMERGKIVETG 223
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERL----RQLlgDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
1.13e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 132.95 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKkiYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANrviSAITGSELRKA 80
Cdd:PRK13648 7 IIVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN---QAITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQH-FNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNP 159
Cdd:PRK13648 82 RKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 160 QVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEM-------HVIrkicnrvaVMERGKIVETGPVLDVF 229
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLseameadHVI--------VMNKGTVYKEGTPTEIF 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-241 |
1.77e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 132.09 E-value: 1.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 17 DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVI---SAITGSELRKARQEIGMIFQHFNL 93
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 94 LWSRTVRENIEFPLEIAGV-DKAKRRKRVDELIHLVGL----EGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEAT 168
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIkEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 169 SALDPETTDQILDLLLDINKRlgLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRFV 241
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
16-233 |
2.69e-36 |
|
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: 130.87 E-value: 2.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLeKPTSGQITIANRVISAITGSELrkARQEIGM------IF 88
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLL-PPRSGSIRFDGEDITGLPPHRI--ARLGIGYvpegrrIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 89 QHFnllwsrTVRENIEFPLEIAGvDKAKRRKRVDELIHL--VgLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDE 166
Cdd:COG0410 91 PSL------TVEENLLLGAYARR-DRAEVRADLERVYELfpR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 167 ATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPK 233
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-220 |
3.23e-36 |
|
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: 130.07 E-value: 3.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 7 VKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAitgSELRKArqeIGM 86
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKS---IGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 87 IFQHFNL-LWSRTVRENIEFPLEIAGVDKAKrrkrVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCD 165
Cdd:cd03226 76 VMQDVDYqLFTDSVREELLLGLKELDAGNEQ----AETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446524434 166 EATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIV 220
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-233 |
3.67e-36 |
|
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: 130.36 E-value: 3.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYKAKsgdvTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSelRKARQE 83
Cdd:cd03218 3 AENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH--KRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLL 163
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 164 CDEATSALDPETTDQILDLLLDINKR-LGltiVLIT-HEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPK 233
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRgIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
3.91e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 133.42 E-value: 3.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITianrVISAITGSELRKAR 81
Cdd:PRK13536 42 IDLAGVSKSY----GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKIT----VLGVPVPARARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERG-KIVETGP 224
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGRP 256
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-223 |
7.07e-36 |
|
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: 130.04 E-value: 7.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 20 AVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKarqEIGMIFQHfNLLWSRTV 99
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRR---QIGLVSQD-VFLFNDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 100 RENIEFPLEIAG---VDKAKRRKRVDELIH--------LVGLEGrgdaypSQLSGGQKQRVGIARALANNPQVLLCDEAT 168
Cdd:cd03251 93 AENIAYGRPGATreeVEEAARAANAHEFIMelpegydtVIGERG------VKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446524434 169 SALDPETTDQILDLLLDINKrlGLTIVLITHEMHVIRKIcNRVAVMERGKIVETG 223
Cdd:cd03251 167 SALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENA-DRIVVLEDGKIVERG 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
3.92e-35 |
|
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: 127.21 E-value: 3.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgSELRKA 80
Cdd:COG4133 2 MLEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR----DAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFqHFNLLWSR-TVRENIEFPLEIAGVDKAkrRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNP 159
Cdd:COG4133 74 RRRLAYLG-HADGLKPElTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524434 160 QVLLCDEATSALDPETTDQILDLLLDiNKRLGLTIVLITHE 200
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-232 |
4.50e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 129.15 E-value: 4.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 20 AVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKARQEIGMIFQH-FNLLWSRT 98
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKVGIVFQNpDNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 99 VRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQ 178
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446524434 179 ILDLLLDINKRLGLTIVLITHEMHVIrKICNRVAVMERGKIVETGPVLDVFRNP 232
Cdd:PRK13640 182 ILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-232 |
7.62e-35 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 134.46 E-value: 7.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 17 DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAItgsELRKARQEIGMIFQHfNLLWS 96
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY---DHHYLHRQVALVGQE-PVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 97 RTVRENIEFPL---EIAGVDKAKRRKRVDELIH--------LVGLEGrgdaypSQLSGGQKQRVGIARALANNPQVLLCD 165
Cdd:TIGR00958 569 GSVRENIAYGLtdtPDEEIMAAAKAANAHDFIMefpngydtEVGEKG------SQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 166 EATSALDPettdQILDLLLDINKRLGLTIVLITHEMHVIRKiCNRVAVMERGKIVETGPVLDVFRNP 232
Cdd:TIGR00958 643 EATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
16-199 |
8.99e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 126.06 E-value: 8.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLEKP--TSGQITIANRVISAITgSELRKarqeIGMIFQ--- 89
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALP-AEQRR----IGILFQddl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 90 ---HFNllwsrtVRENIEFPLEiAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDE 166
Cdd:COG4136 87 lfpHLS------VGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190
....*....|....*....|....*....|...
gi 446524434 167 ATSALDPETTDQILDLLLDINKRLGLTIVLITH 199
Cdd:COG4136 160 PFSKLDAALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
16-230 |
1.63e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 126.81 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKARqeiGMIFQHFNLLW 95
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR---AVLPQHSSLSF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 SRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEG-RGDAYPsQLSGGQKQRVGIARALA------NNPQVLLCDEAT 168
Cdd:PRK13548 90 PFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHlAGRDYP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 169 SALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFR 230
Cdd:PRK13548 169 SALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
16-241 |
1.97e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 126.81 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQL-----EKPTSGQITI-ANRVISAITGS-ELRKarqEIGMIF 88
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYnGHNIYSPRTDTvDLRK---EIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 89 QHFNLlWSRTVRENIEFPLEIAGVdkaKRRKRVDELIH--LVG------LEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:PRK14239 93 QQPNP-FPMSIYENVVYGLRLKGI---KDKQVLDEAVEksLKGasiwdeVKDRLHDSALGLSGGQQQRVCIARVLATSPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRlgLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRF 240
Cdd:PRK14239 169 IILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDY 246
|
.
gi 446524434 241 V 241
Cdd:PRK14239 247 I 247
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-221 |
2.13e-34 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 125.66 E-value: 2.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 26 LKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKAR-QEIGMIFQHFNLLWSRTVRENIE 104
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQSFMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 105 FPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLL 184
Cdd:PRK10584 111 LPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 446524434 185 DINKRLGLTIVLITHEMHVIRKiCNRVAVMERGKIVE 221
Cdd:PRK10584 191 SLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-230 |
2.30e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 127.54 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGDVT-AVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGS-ELR 78
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 79 KARQEIGMIFQH-FNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGR-GDAYPSQLSGGQKQRVGIARALA 156
Cdd:PRK13643 81 PVRKKVGVVFQFpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524434 157 NNPQVLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFR 230
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-242 |
3.29e-34 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 125.97 E-value: 3.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 17 DVTAVDNANLKIEKGEIFGVIGYSGAGKS----SLIRLFNQLEKPTSGQITIANRvisAITGSELRKarQEIGMIFQH-- 90
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGK---PVAPCALRG--RKIATIMQNpr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 91 --FNLLwsRTVRENIEFPLEIAGvdKAKRRKRVDELIHLVGLEGRG---DAYPSQLSGGQKQRVGIARALANNPQVLLCD 165
Cdd:PRK10418 90 saFNPL--HTMHTHARETCLALG--KPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 166 EATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRFVQ 242
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-228 |
3.91e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 125.97 E-value: 3.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGD-VTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAItgSELRK 79
Cdd:COG1101 1 MLELKNLSKTFNPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL--PEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 80 ARQeIGMIFQH------FNLlwsrTVRENiefpLEIA-----------GVDKAKR---RKRVDELiHLvGLEGRGDAYPS 139
Cdd:COG1101 79 AKY-IGRVFQDpmmgtaPSM----TIEEN----LALAyrrgkrrglrrGLTKKRRelfRELLATL-GL-GLENRLDTKVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 140 QLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKI 219
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
....*....
gi 446524434 220 vetgpVLDV 228
Cdd:COG1101 228 -----ILDV 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-223 |
4.07e-34 |
|
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: 125.03 E-value: 4.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKsgdVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKar 81
Cdd:cd03254 3 IEFENVNFSYDEK---KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 qEIGMIFQHfNLLWSRTVRENIEFPLEIAGVD---KAKRRKRVDELIhlVGLEGRGDAYPSQ----LSGGQKQRVGIARA 154
Cdd:cd03254 78 -MIGVVLQD-TFLFSGTIMENIRLGRPNATDEeviEAAKEAGAHDFI--MKLPNGYDTVLGEnggnLSQGERQLLAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 155 LANNPQVLLCDEATSALDPETTDQILDLLLDINKrlGLTIVLITHEMHVIRKiCNRVAVMERGKIVETG 223
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-242 |
8.55e-34 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 130.21 E-value: 8.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 8 KKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSS----LIRLFNqlekpTSGQITIANRVISAITGSELRKARQE 83
Cdd:PRK15134 289 KGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQHFN-LLWSR-TVRENIEFPLEI--AGVDKAKRRKRVDELIHLVGL--EGRgDAYPSQLSGGQKQRVGIARALAN 157
Cdd:PRK15134 364 IQVVFQDPNsSLNPRlNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdpETR-HRYPAEFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDIT 237
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
....*
gi 446524434 238 KRFVQ 242
Cdd:PRK15134 523 RQLLA 527
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-232 |
1.27e-33 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 126.38 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 3 LLENVKKI---YKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKS-SLIRLFNQLEKP--TSGQITIANRVISAITGSE 76
Cdd:PRK09473 11 ALLDVKDLrvtFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 77 LRKAR-QEIGMIFQ----------------------HFNLLWSRTVRENIEFpLEIAGVDKAKRRKRVdelihlvglegr 133
Cdd:PRK09473 91 LNKLRaEQISMIFQdpmtslnpymrvgeqlmevlmlHKGMSKAEAFEESVRM-LDAVKMPEARKRMKM------------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 134 gdaYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAV 213
Cdd:PRK09473 158 ---YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLV 234
|
250
....*....|....*....
gi 446524434 214 MERGKIVETGPVLDVFRNP 232
Cdd:PRK09473 235 MYAGRTMEYGNARDVFYQP 253
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-219 |
1.74e-33 |
|
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: 121.55 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKkiYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRkar 81
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLwSRTVRENIefpleiagvdkakrrkrvdelihlvglegrgdaypsqLSGGQKQRVGIARALANNPQV 161
Cdd:cd03246 76 DHVGYLPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRkICNRVAVMERGKI 219
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-252 |
5.69e-33 |
|
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: 128.00 E-value: 5.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKiykaKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLE--KPTSGQI----------------- 62
Cdd:TIGR03269 1 IEVKNLTK----KFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 63 -----------TIANRVISAITGSE--LRKARQEIGMIFQH-FNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLV 128
Cdd:TIGR03269 77 kvgepcpvcggTLEPEEVDFWNLSDklRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 129 GLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKIC 208
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446524434 209 NRVAVMERGKIVETGPVLDVfrnpkqdiTKRFVQQLTDSEDTNE 252
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEV--------VAVFMEGVSEVEKECE 272
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-287 |
6.35e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 127.90 E-value: 6.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 19 TAVDNANLKIEKGEIFGVIGYSGAGKS----SLIRLfnqLEKP----TSGQITIANRVISAITGSELRKAR-QEIGMIFQ 89
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRL---LPSPpvvyPSGDIRFHGESLLHASEQTLRGVRgNKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 90 H----FNLLwsrtvrENIEFPL-EIAGVDKAKRRK--RVDELIHL--VGLE---GRGDAYPSQLSGGQKQRVGIARALAN 157
Cdd:PRK15134 100 EpmvsLNPL------HTLEKQLyEVLSLHRGMRREaaRGEILNCLdrVGIRqaaKRLTDYPHQLSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDIT 237
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYT 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446524434 238 krfvQQLTDSEDTNETIESLIEKYPDGKVIRLQfigeaVERPVLQRLMQR 287
Cdd:PRK15134 254 ----QKLLNSEPSGDPVPLPEPASPLLDVEQLQ-----VAFPIRKGILKR 294
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-243 |
1.10e-32 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 121.35 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 5 ENVKKIYKAKsgdvTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgselRKARQEI 84
Cdd:TIGR03740 4 KNLSKRFGKQ----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT-------RKDLHKI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 85 GMIFQHFNLLWSRTVRENIEFPLEIAGVDKAkrrkRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLC 164
Cdd:TIGR03740 73 GSLIESPPLYENLTARENLKVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLIL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 165 DEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVldvfrNPKQDITKRFVQQ 243
Cdd:TIGR03740 149 DEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLGYQGKI-----NKSENLEKLFVEV 221
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-224 |
2.55e-32 |
|
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: 119.91 E-value: 2.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 20 AVDNANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLEkPTSGQITIANRVISAItgsELRKARQEIGMIFQHfNLLWSRT 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLaLFRLVE-LSSGSILIDGVDISKI---GLHDLRSRISIIPQD-PVLFSGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 99 VRENIEfPLEIAG-------VDKAKRRKRVDELihLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSAL 171
Cdd:cd03244 94 IRSNLD-PFGEYSdeelwqaLERVGLKEFVESL--PGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446524434 172 DPETTDQILDLLLdiNKRLGLTIVLITHEMHVIRKiCNRVAVMERGKIVETGP 224
Cdd:cd03244 171 DPETDALIQKTIR--EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
16-232 |
1.69e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 119.06 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELrkARQeIGMIFQHFNLLW 95
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWEL--ARR-RAVLPQHSSLAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 SRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGD-AYPsQLSGGQKQRVGIARALA-------NNPQVLLCDEA 167
Cdd:COG4559 89 PFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524434 168 TSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNP 232
Cdd:COG4559 168 TSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDE 231
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-224 |
1.73e-31 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 124.68 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKSGDVtaVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRkaR 81
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLI--LDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVR--R 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QeIGMIFQHFNLLwSRTVRENIefpleIAG----VDKAKrrkrvdELIHLVGLEGRGDAYP-----------SQLSGGQK 146
Cdd:TIGR03797 528 Q-LGVVLQNGRLM-SGSIFENI-----AGGapltLDEAW------EAARMAGLAEDIRAMPmgmhtviseggGTLSGGQR 594
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 147 QRVGIARALANNPQVLLCDEATSALDPETTDQILDLLldinKRLGLTIVLITHEMHVIRKiCNRVAVMERGKIVETGP 224
Cdd:TIGR03797 595 QRLLIARALVRKPRILLFDEATSALDNRTQAIVSESL----ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGT 667
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-217 |
1.97e-31 |
|
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: 117.92 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 18 VTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITI--ANRVISAITGSE-----LRkaRQEIGMIFQH 90
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPreilaLR--RRTIGYVSQF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 91 FNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGL-EGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATS 169
Cdd:COG4778 102 LRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524434 170 ALDPETTDQILDLLLDInKRLGLTIVLITHEMHVIRKICNRVAVMERG 217
Cdd:COG4778 182 SLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-223 |
1.98e-31 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 124.30 E-value: 1.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 20 AVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKArqeIGMIFQHfNLLWSRTV 99
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN---IAVVFQD-AGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 100 RENIEFPLEIAG----VDKAKR-------RKRVDELIHLVGLEGRgdaypsQLSGGQKQRVGIARALANNPQVLLCDEAT 168
Cdd:PRK13657 426 EDNIRVGRPDATdeemRAAAERaqahdfiERKPDGYDTVVGERGR------QLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446524434 169 SALDPETTDQILDLLLDINKrlGLTIVLITHEMHVIRKiCNRVAVMERGKIVETG 223
Cdd:PRK13657 500 SALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-224 |
2.75e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 117.76 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 25 NLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITgselrKARQEIGMIFQHFNLLWSRTVRENIE 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP-----PSRRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 105 FPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLL 184
Cdd:PRK10771 94 LGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524434 185 DINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGP 224
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-246 |
4.51e-31 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 119.52 E-value: 4.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLE--NVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKpTSGQITiANRV------ISAI 72
Cdd:PRK15093 1 MPLLDirNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVT-ADRMrfddidLLRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 73 TGSELRK-ARQEIGMIFQHFNLLWSRTVRENIEFPLEIAG-VDKAK-------RRKRVDELIHLVGLEGRGDA---YPSQ 140
Cdd:PRK15093 79 SPRERRKlVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGwTYKGRwwqrfgwRKRRAIELLHRVGIKDHKDAmrsFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 141 LSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIV 220
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250 260
....*....|....*....|....*.
gi 446524434 221 ETGPVLDVFRNPKQDITKRFVQQLTD 246
Cdd:PRK15093 239 ETAPSKELVTTPHHPYTQALIRAIPD 264
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-238 |
5.41e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 123.04 E-value: 5.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKS----SLIRLFNQL-EKPTSGQITIANR---VI--S 70
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAgGLVQCDKMLLRRRsrqVIelS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 71 AITGSELRKAR-QEIGMIFQH----FNLLWsrTVRENIEFPLEI---AGVDKAKRR-KRVDELIHLVGLEGRGDAYPSQL 141
Cdd:PRK10261 92 EQSAAQMRHVRgADMAMIFQEpmtsLNPVF--TVGEQIAESIRLhqgASREEAMVEaKRMLDQVRIPEAQTILSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 142 SGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVE 221
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
250
....*....|....*..
gi 446524434 222 TGPVLDVFRNPKQDITK 238
Cdd:PRK10261 250 TGSVEQIFHAPQHPYTR 266
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
16-224 |
7.84e-31 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 116.47 E-value: 7.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSElrKARQEIG------MIFQ 89
Cdd:TIGR03410 11 GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE--RARAGIAyvpqgrEIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 90 HFnllwsrTVRENIEFPLEIAGvdkaKRRKRVDELIH-----LVGLEGR--GDaypsqLSGGQKQRVGIARALANNPQVL 162
Cdd:TIGR03410 89 RL------TVEENLLTGLAALP----RRSRKIPDEIYelfpvLKEMLGRrgGD-----LSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 163 LCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGP 224
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-224 |
1.80e-30 |
|
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: 121.36 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 17 DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITgseLRKARQEIGMIFQHFnLLWS 96
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLRRQVALVSQDV-VLFN 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 97 RTVRENIEFPlEIAGVDKAKRRK------------RVDELIHL-VGLEGrgdaypSQLSGGQKQRVGIARALANNPQVLL 163
Cdd:TIGR02203 420 DTIANNIAYG-RTEQADRAEIERalaaayaqdfvdKLPLGLDTpIGENG------VLLSGGQRQRLAIARALLKDAPILI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 164 CDEATSALDPETTDQILDLLldinKRL--GLTIVLITHEMHVIRKiCNRVAVMERGKIVETGP 224
Cdd:TIGR02203 493 LDEATSALDNESERLVQAAL----ERLmqGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGT 550
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-229 |
2.56e-30 |
|
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: 115.57 E-value: 2.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQ-ITIANRVISAITGSELRK 79
Cdd:COG1119 3 LLELRNVTVRR----GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 80 arqEIGMI--FQHFNLLWSRTVRE--------NIEFPLEIAGVDkakrRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRV 149
Cdd:COG1119 79 ---RIGLVspALQLRFPRDETVLDvvlsgffdSIGLYREPTDEQ----RERARELLELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 150 GIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVF 229
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-228 |
3.01e-30 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 120.27 E-value: 3.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSElrKA 80
Cdd:PRK09700 5 YISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL--AA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENI---EFPLE----IAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIAR 153
Cdd:PRK09700 79 QLGIGIIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524434 154 ALANNPQVLLCDEATSALDPETTDQILdLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDV 228
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLF-LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-232 |
4.46e-30 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 117.28 E-value: 4.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 33 IFGVigySGAGKSSLIRLFNQLEKPTSGQITIANRVIS-AITGSELRKARQEIGMIFQHFNLLWSRTVRENIEFpleiaG 111
Cdd:PRK11144 29 IFGR---SGAGKTSLINAISGLTRPQKGRIVLNGRVLFdAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRY-----G 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 112 VdKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLG 191
Cdd:PRK11144 101 M-AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREIN 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446524434 192 LTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNP 232
Cdd:PRK11144 180 IPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
20-223 |
7.76e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 114.72 E-value: 7.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 20 AVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQL---EKPTSGQITIANRVI--SAITGSELRKARQEIGMIFQHFNLL 94
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVqrEGRLARDIRKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 95 WSRTVRENI------EFPLEIAGVD--KAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDE 166
Cdd:PRK09984 99 NRLSVLENVligalgSTPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 167 ATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-243 |
8.01e-30 |
|
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: 119.47 E-value: 8.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVkkIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKArqe 83
Cdd:COG4618 333 VENL--TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH--- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQHFNLLwSRTVRENI-EFP-LEIAGVDKAKRRKRVDELI-HL-------VGLEGRGdaypsqLSGGQKQRVGIAR 153
Cdd:COG4618 408 IGYLPQDVELF-DGTIAENIaRFGdADPEKVVAAAKLAGVHEMIlRLpdgydtrIGEGGAR------LSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 154 ALANNPQVLLCDEATSALDPEtTDQILDLLLDINKRLGLTIVLITHEMHVIRkICNRVAVMERGKIVETGpvldvfrnPK 233
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDE-GEAALAAAIRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFG--------PR 550
|
250
....*....|
gi 446524434 234 QDITKRFVQQ 243
Cdd:COG4618 551 DEVLARLARP 560
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-246 |
1.53e-29 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 114.09 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKARQEIGMIFQHFNLLW 95
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 SRTVRENIEFPL-EIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPE 174
Cdd:PRK11831 98 DMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 175 TTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDItKRFVQQLTD 246
Cdd:PRK11831 178 TMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRV-RQFLDGIAD 248
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
16-223 |
3.20e-29 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 118.30 E-value: 3.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAitgSELrKARQEIGMIFQHFNLLW 95
Cdd:NF033858 277 GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA---GDI-ATRRRVGYMSQAFSLYG 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 SRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPET 175
Cdd:NF033858 353 ELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVA 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524434 176 TDQILDLLLDINKRLGLTIVLITHEMH-VIRkiCNRVAVMERGKIVETG 223
Cdd:NF033858 433 RDMFWRLLIELSREDGVTIFISTHFMNeAER--CDRISLMHAGRVLASD 479
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-223 |
3.55e-29 |
|
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: 118.00 E-value: 3.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 25 NLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKArqeIGMIFQH---FNllwsRTVRE 101
Cdd:COG5265 378 SFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA---IGIVPQDtvlFN----DTIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 102 NIEFPLEIAG---VDKAKRRKRVDELIH--------LVGlEgRGdaypSQLSGGQKQRVGIARALANNPQVLLCDEATSA 170
Cdd:COG5265 451 NIAYGRPDASeeeVEAAARAAQIHDFIEslpdgydtRVG-E-RG----LKLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446524434 171 LDPETTDQILDLLLDINKrlGLTIVLITHEMHVIRKiCNRVAVMERGKIVETG 223
Cdd:COG5265 525 LDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-223 |
3.58e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 113.29 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKar 81
Cdd:PRK13647 5 IEVEDLHFRYK---DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 qEIGMIFQH-FNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:PRK13647 80 -KVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-214 |
4.07e-29 |
|
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: 117.00 E-value: 4.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 20 AVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKarqEIGMIFQHfNLLWSRTV 99
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD---QIAWVPQH-PFLFAGTI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 100 RENIEFPLEIAG---VDKAKRRKRVDELIHLV--GLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPE 174
Cdd:TIGR02857 413 AENIRLARPDASdaeIREALERAGLDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524434 175 TTDQILDLLLDINKrlGLTIVLITHEMHVIRKiCNRVAVM 214
Cdd:TIGR02857 493 TEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-223 |
8.20e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 116.46 E-value: 8.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 20 AVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKArqeIGMIFQHFNLLwSRTV 99
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA---ISVVSQRVHLF-SATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 100 RENIEFpleiagvdkAKRRKRVDELIHL---VGLE----------------GRgdaypsQLSGGQKQRVGIARALANNPQ 160
Cdd:PRK11160 431 RDNLLL---------AAPNASDEALIEVlqqVGLEklleddkglnawlgegGR------QLSGGEQRRLGIARALLHDAP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDINKrlGLTIVLITHEMHVIRKIcNRVAVMERGKIVETG 223
Cdd:PRK11160 496 LLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQG 555
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
14-229 |
9.94e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.11 E-value: 9.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 14 KSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRvisAITGSELRKARQEIGMIFQH-FN 92
Cdd:PRK13642 16 KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNLRRKIGMVFQNpDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 93 LLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALD 172
Cdd:PRK13642 93 QFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 173 PETTDQILDLLLDINKRLGLTIVLITHEMHVIRKiCNRVAVMERGKIVETGPVLDVF 229
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-245 |
1.54e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 111.73 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 19 TAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSG-----QITIANRviSAITGSELRKARQEIGMIFQHFNL 93
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGR--SIFNYRDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 94 lWSRTVRENIefpleIAGVDKAK----------RRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLL 163
Cdd:PRK14271 113 -FPMSIMDNV-----LAGVRAHKlvprkefrgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 164 CDEATSALDPETTDQILDLLLDINKRlgLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRFVQQ 243
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAG 264
|
..
gi 446524434 244 LT 245
Cdd:PRK14271 265 LS 266
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-219 |
3.43e-28 |
|
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: 109.48 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 5 ENVKKIYKAKSgDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAItgsELRKARQEI 84
Cdd:cd03248 15 QNVTFAYPTRP-DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY---EHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 85 GMIFQHfNLLWSRTVRENIEFPLE-------IAGVDKAKRRKRVDELIHlvGLEGRGDAYPSQLSGGQKQRVGIARALAN 157
Cdd:cd03248 91 SLVGQE-PVLFARSLQDNIAYGLQscsfecvKEAAQKAHAHSFISELAS--GYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLLDINKRlgLTIVLITHEMHVIRKiCNRVAVMERGKI 219
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-241 |
4.77e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 109.87 E-value: 4.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 5 ENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEK-----PTSGQITIANRVISA--ITGSEL 77
Cdd:PRK14243 14 ENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYApdVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 78 RKarqEIGMIFQHFNLlWSRTVRENIEFPLEIAG--------VDKAKRRKRV-DELIHLVGLEGrgdaypSQLSGGQKQR 148
Cdd:PRK14243 90 RR---RIGMVFQKPNP-FPKSIYDNIAYGARINGykgdmdelVERSLRQAALwDEVKDKLKQSG------LSLSGGQQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 149 VGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRlgLTIVLITHEMHVIRKICNRVA-----VMERGK----I 219
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAffnveLTEGGGrygyL 237
|
250 260
....*....|....*....|..
gi 446524434 220 VETGPVLDVFRNPKQDITKRFV 241
Cdd:PRK14243 238 VEFDRTEKIFNSPQQQATRDYV 259
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
4-223 |
5.97e-28 |
|
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: 108.51 E-value: 5.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQL---EKPTSGQITIAnrvisaitGSELRKA 80
Cdd:cd03234 6 WWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFN--------GQPRKPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 --RQEIGMIFQHFNLLWSRTVRENIEFPLEIAG---VDKAKRRKRV-DELIHLVGLEGRGDAYPSQLSGGQKQRVGIARA 154
Cdd:cd03234 78 qfQKCVAYVRQDDILLPGLTVRETLTYTAILRLprkSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 155 LANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETG 223
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
16-228 |
2.03e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 111.09 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGselRKARQEIGMIFQHFNLLW 95
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA---RAASRRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 SRTVRENIEF---P--LEIAGVDKAKRRKrVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSA 170
Cdd:PRK09536 91 EFDVRQVVEMgrtPhrSRFDTWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 171 LDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDV 228
Cdd:PRK09536 170 LDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-219 |
2.04e-27 |
|
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: 105.98 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 20 AVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKA--------RQEIGmifqhf 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedRKREG------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 92 nLLWSRTVRENIefpleiagvdkakrrkrvdelihlvglegrgdAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSAL 171
Cdd:cd03215 89 -LVLDLSVAENI--------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446524434 172 DPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKI 219
Cdd:cd03215 136 DVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
16-248 |
2.32e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.10 E-value: 2.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELrkARQeIGMIFQHFNLLW 95
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL--ARR-LALLPQHHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 SRTVRENIEF---P-LEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSAL 171
Cdd:PRK11231 90 GITVRELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 172 DPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGpvldvfrNPKQDITKRFVQQLTDSE 248
Cdd:PRK11231 170 DINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG-------TPEEVMTPGLLRTVFDVE 238
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-223 |
2.46e-26 |
|
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: 102.78 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 19 TAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIaNRVISAITGSELRKArqeIGMIFQHFNLlWSRT 98
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL-DGVPVSDLEKALSSL---ISVLNQRPYL-FDTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 99 VRENIefpleiagvdkakrrkrvdelihlvgleGRgdaypsQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQ 178
Cdd:cd03247 91 LRNNL----------------------------GR------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446524434 179 ILDLLLDINKrlGLTIVLITHEMHVIRKIcNRVAVMERGKIVETG 223
Cdd:cd03247 137 LLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-232 |
3.52e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 104.69 E-value: 3.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLirlFNQLE---KPTSGQITIANRVISAITGSELrkARQEIGMIFQHFN 92
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTV---FNCLTgfyKPTGGTILLRGQHIEGLPGHQI--ARMGVVRTFQHVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 93 LLWSRTVREN--------IEFPLeIAGVDK--AKRRKRVDEL------IHLVGLEGRGDAYPSQLSGGQKQRVGIARALA 156
Cdd:PRK11300 91 LFREMTVIENllvaqhqqLKTGL-FSGLLKtpAFRRAESEALdraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMV 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524434 157 NNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNP 232
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-241 |
3.94e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 104.73 E-value: 3.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 21 VDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQL-----EKPTSGQITIANRVISAiTGSELRKARQEIGMIFQHFNLlW 95
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYE-RRVNLNRLRRQVSMVHPKPNL-F 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 SRTVRENIEFPLEIAG----------VDKAKRRKRV-DEL---IHLVGLEgrgdaypsqLSGGQKQRVGIARALANNPQV 161
Cdd:PRK14258 101 PMSVYDNVAYGVKIVGwrpkleiddiVESALKDADLwDEIkhkIHKSALD---------LSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMER-----GKIVETGPVLDVFRNPKQDI 236
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSR 251
|
....*
gi 446524434 237 TKRFV 241
Cdd:PRK14258 252 TREYV 256
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-220 |
1.11e-25 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 101.47 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 21 VDNANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLEKP-TSGQITIANRVISaitgseLRKARQEIGMIFQHFNLLWSRT 98
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNaLAGRRTGLgVSGEVLINGRPLD------KRSFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 99 VRENIEFPLEIAGvdkakrrkrvdelihlvglegrgdaypsqLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQ 178
Cdd:cd03213 99 VRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446524434 179 ILDLLldinKRL---GLTIVLITHEM-HVIRKICNRVAVMERGKIV 220
Cdd:cd03213 150 VMSLL----RRLadtGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
23-218 |
2.03e-25 |
|
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: 101.39 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 23 NANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLEKpTSGQITIANRVisAItgselrkARQEIgmifqhfnllW--SRTV 99
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSVPGSI--AY-------VSQEP----------WiqNGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 100 RENIEFPLEIagvDKakrrKRVDELIHLVGLE---------------GRGdaypSQLSGGQKQRVGIARALANNPQVLLC 164
Cdd:cd03250 83 RENILFGKPF---DE----ERYEKVIKACALEpdleilpdgdlteigEKG----INLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446524434 165 DEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKiCNRVAVMERGK 218
Cdd:cd03250 152 DDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-226 |
6.70e-25 |
|
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: 105.87 E-value: 6.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAkSGDvTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgSELRKAR 81
Cdd:TIGR01257 929 VCVKNLVKIFEP-SGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE----TNLDAVR 1002
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:TIGR01257 1003 QSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524434 162 LLCDEATSALDPETTDQILDLLLdiNKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVL 226
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLL--KYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPL 1145
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-227 |
8.42e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 101.16 E-value: 8.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 5 ENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANR-----VISAITGSELRK 79
Cdd:PRK11701 10 RGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 80 -ARQEIGMIFQHF--NLLWSRTVRENIEFPLEIAGVDK--AKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARA 154
Cdd:PRK11701 86 lLRTEWGFVHQHPrdGLRMQVSAGGNIGERLMAVGARHygDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524434 155 LANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETG---PVLD 227
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGltdQVLD 241
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-221 |
9.14e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.76 E-value: 9.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVisaitgselrka 80
Cdd:COG0488 315 VLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV------------ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 rqEIGMIFQHFNLL-WSRTVRENIEfpleiAGVDKAKRrkrvdelIHLVGLEGR----GD---AYPSQLSGGQKQRVGIA 152
Cdd:COG0488 379 --KIGYFDQHQEELdPDKTVLDELR-----DGAPGGTE-------QEVRGYLGRflfsGDdafKPVGVLSGGEKARLALA 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 153 RALANNPQVLLCDEATSALDPETTDQILDLLLDINkrlGlTIVLITHEMHVIRKICNRVAVMERGKIVE 221
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-219 |
1.04e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.38 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVisaitgselrkarqE 83
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL--------------R 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQHFNLLWSRTVRENIEFPL-EIAGVDKAKRR------------KRVDELIH-----------------LVGL--- 130
Cdd:COG0488 63 IGYLPQEPPLDDDLTVLDTVLDGDaELRALEAELEEleaklaepdedlERLAELQEefealggweaearaeeiLSGLgfp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 131 EGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKrlglTIVLITHEMHVIRKICNR 210
Cdd:COG0488 143 EEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG----TVLVVSHDRYFLDRVATR 218
|
....*....
gi 446524434 211 VAVMERGKI 219
Cdd:COG0488 219 ILELDRGKL 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-223 |
1.86e-24 |
|
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: 104.44 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 20 AVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRkarQEIGMIFQHfNLLWSRTV 99
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR---QFINYLPQE-PYIFSGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 100 RENIEF----PLEIAGVDKAKRRKRVDELIHLV--GLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDP 173
Cdd:TIGR01193 565 LENLLLgakeNVSQDEIWAACEIAEIKDDIENMplGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524434 174 ETTDQILDLLLDINKRlglTIVLITHEMHVIRKIcNRVAVMERGKIVETG 223
Cdd:TIGR01193 645 ITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQG 690
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
31-232 |
5.14e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 99.09 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 31 GEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELrkARqEIGMIFQHFNLLWSRTVRENI---EFPL 107
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF--AR-KVAYLPQQLPAAEGMTVRELVaigRYPW 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 108 EIA-GVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDI 186
Cdd:PRK10575 114 HGAlGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446524434 187 NKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNP 232
Cdd:PRK10575 194 SQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-224 |
2.29e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 100.51 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 3 LLEnVKKIYKAKSGdVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSelrKARQ 82
Cdd:PRK15439 11 LLC-ARSISKQYSG-VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA---KAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 83 -EIGMIFQHFNLLWSRTVRENIEFPLEiagvDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:PRK15439 86 lGIYLVPQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 162 LLCDEATSALDPETTD----QILDLLldinkRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGP 224
Cdd:PRK15439 162 LILDEPTASLTPAETErlfsRIRELL-----AQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-224 |
3.26e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 100.00 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 3 LLEnVKKIYKAkSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLeKPT---SGQITIANRVISA--ITGSEl 77
Cdd:PRK13549 5 LLE-MKNITKT-FGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQAsnIRDTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 78 rkaRQEIGMIFQHFNLLWSRTVRENIEFPLEI--AGV-DKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARA 154
Cdd:PRK13549 81 ---RAGIAIIHQELALVKELSVLENIFLGNEItpGGImDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 155 LANNPQVLLCDEATSALDPETTDQILDLLLDInKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGP 224
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRP 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-231 |
4.75e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 95.73 E-value: 4.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 5 ENVKKIYKAKsgdvTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSElrKARQEI 84
Cdd:PRK10895 7 KNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 85 GMIFQHFNLLWSRTVRENIEFPLEI-AGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLL 163
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 164 CDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRN 231
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-220 |
5.72e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.32 E-value: 5.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 20 AVDNANLKIEKGEIFGVIGYSGAGKSSLIR-LFNqLEKPTSGQITIANRVISaitgseLRKARQEI--GMIF-----QHF 91
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARaLFG-ADPADSGEIRLDGKPVR------IRSPRDAIraGIAYvpedrKGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 92 NLLWSRTVRENIEFP----LEIAG-VDKAKRRKRVDELIHLVGLEGRGDAYP-SQLSGGQKQRVGIARALANNPQVLLCD 165
Cdd:COG1129 340 GLVLDLSIRENITLAsldrLSRGGlLDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446524434 166 EATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIV 220
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-199 |
1.01e-22 |
|
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: 98.59 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKArqeIGMIFQ--Hfnl 93
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR---VSVCAQdaH--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 94 LWSRTVRENIEFPLEIAG---VDKAKRRKR----VDELIHlvGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDE 166
Cdd:TIGR02868 420 LFDTTVRENLRLARPDATdeeLWAALERVGladwLRALPD--GLDTVLGEGGARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|...
gi 446524434 167 ATSALDPETTDQILDLLLDINKrlGLTIVLITH 199
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLAALS--GRTVVLITH 528
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-223 |
1.02e-22 |
|
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: 94.02 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKSGDVtaVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAItgsELRKAR 81
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLwSRTVRENiefpleiagVDKAKRRKRVDELIHLVGLEGrgdayPSQLSGGQKQRVGIARALANNPQV 161
Cdd:cd03369 82 SSLTIIPQDPTLF-SGTIRSN---------LDPFDEYSDEEIYGALRVSEG-----GLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKrlGLTIVLITHEMHVIRKiCNRVAVMERGKIVETG 223
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-223 |
3.80e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.01 E-value: 3.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKsgDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKar 81
Cdd:PRK11176 342 IEFRNVTFTYPGK--EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN-- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 qEIGMIFQHFNLlWSRTVRENIEFPLE----IAGVDKAKRRKRVDELIH--------LVGLEGrgdaypSQLSGGQKQRV 149
Cdd:PRK11176 418 -QVALVSQNVHL-FNDTIANNIAYARTeqysREQIEEAARMAYAMDFINkmdngldtVIGENG------VLLSGGQRQRI 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524434 150 GIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKrlGLTIVLITHEMHVIRKiCNRVAVMERGKIVETG 223
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-222 |
3.59e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 94.21 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 18 VTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKArqEIGMIFQHFNLLWSR 97
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAA--GVAIIYQELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 98 TVRENI---EFPLEIAGVDKAKRRKRV-DELIHLvGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDP 173
Cdd:PRK11288 95 TVAENLylgQLPHKGGIVNRRLLNYEArEQLEHL-GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524434 174 ETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVET 222
Cdd:PRK11288 174 REIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-199 |
3.70e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 90.02 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 19 TAVDNANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLE-KPTSGQITIanrvisaitgselrkarqeigmifqhfnllws 96
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRlLAGALKgTPVAGCVDV-------------------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 97 rtvrENIEFPLEIAGVDKAKRRKRVD---ELIHLVGLegrGDAY-----PSQLSGGQKQRVGIARALANNPQVLLCDEAT 168
Cdd:COG2401 92 ----PDNQFGREASLIDAIGRKGDFKdavELLNAVGL---SDAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|.
gi 446524434 169 SALDPETTDQILDLLLDINKRLGLTIVLITH 199
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| NIL |
smart00930 |
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ... |
263-338 |
4.54e-21 |
|
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins; This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.
Pssm-ID: 197998 [Multi-domain] Cd Length: 76 Bit Score: 85.64 E-value: 4.54e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524434 263 DGKVIRLQFIGEAVERPVLQRLMQRSDIEVSILQGNIAQTNNGSYGSLVVHLNGEETAIQQAIEGIHQDQVELEVI 338
Cdd:smart00930 1 DGRLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGDEEDIEAALAYLREQGVEVEVL 76
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-224 |
6.66e-21 |
|
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: 93.35 E-value: 6.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 3 LLEnVKKIYKaKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQL--EKPTSGQITIANRVISAITGSELRka 80
Cdd:TIGR02633 1 LLE-MKGIVK-TFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENI----EFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYP-SQLSGGQKQRVGIARAL 155
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 156 ANNPQVLLCDEATSALDPETTDQILDLLLDInKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGP 224
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKD 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-200 |
9.69e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.00 E-value: 9.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 14 KSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRkarQEIGMIFQHfNL 93
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR---QQVSYCAQT-PT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 94 LWSRTVRENIEFPLEIagvdkakRRKRVDELIHLVGLEGRG------DAYPSQLSGGQKQRVGIARALANNPQVLLCDEA 167
Cdd:PRK10247 92 LFGDTVYDNLIFPWQI-------RNQQPDPAIFLDDLERFAlpdtilTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190
....*....|....*....|....*....|...
gi 446524434 168 TSALDPETTDQILDLLLDINKRLGLTIVLITHE 200
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-228 |
1.20e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.40 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 18 VTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKA--------RQEIGMI-- 87
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipedRLGRGLVpd 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 88 FqhfnllwsrTVRENI------EFPLEIAG-VDKAKRRKRVDELIHLVGLEGRGDAYP-SQLSGGQKQRVGIARALANNP 159
Cdd:COG3845 351 M---------SVAENLilgryrRPPFSRGGfLDRKAIRAFAEELIEEFDVRTPGPDTPaRSLSGGNQQKVILARELSRDP 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 160 QVLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDV 228
Cdd:COG3845 422 KLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-266 |
1.25e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.80 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 27 KIEKGEIFGVIGYSGAGKSSLI-----RLFNQLEKptSGQITIANRVIsaitgsELRKARQEIGMIFQHFNLLWSRTVRE 101
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKG--SGSVLLNGMPI------DAKEMRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 102 NIEFPLEI---AGVDKAKRRKRVDELIHLVGLE-------GRGDAYPSqLSGGQKQRVGIARALANNPQVLLCDEATSAL 171
Cdd:TIGR00955 119 HLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRkcantriGVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 172 DPETTDQILDLLLDINKRlGLTIVLITHE-----MHVIRKICnrvaVMERGKIVETGPV---LDVFRN-----PKQDITK 238
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQK-GKTIICTIHQpsselFELFDKII----LMAEGRVAYLGSPdqaVPFFSDlghpcPENYNPA 272
|
250 260 270
....*....|....*....|....*....|...
gi 446524434 239 RFVQQL--TDSEDTNE---TIESLIEKYPDGKV 266
Cdd:TIGR00955 273 DFYVQVlaVIPGSENEsreRIEKICDSFAVSDI 305
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-218 |
1.90e-20 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 85.96 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVisaitgselrkar 81
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 qEIGmifqhfnllwsrtvreniefpleiagvdkakrrkrvdelihlvglegrgdaYPSQLSGGQKQRVGIARALANNPQV 161
Cdd:cd03221 64 -KIG---------------------------------------------------YFEQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKrlglTIVLITHEMHVIRKICNRVAVMERGK 218
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-229 |
1.98e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.30 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 17 DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaITGSELRKARQEIGMIFQHFNL-LW 95
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQVATVFQDPEQqIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 SRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPET 175
Cdd:PRK13638 92 YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446524434 176 TDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVF 229
Cdd:PRK13638 172 RTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-223 |
6.98e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.29 E-value: 6.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 25 NLKIEKGEIFGVIGYSGAGKSSLIrlfNQLEK--PTSGQITIanrvisaiTGSELRKA-----RQEIGMIFQHFNLLWSr 97
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLL---NALLGflPYQGSLKI--------NGIELRELdpeswRKHLSWVGQNPQLPHG- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 98 TVRENI---EFPLEIAGVDKAKRRKRVDELIHLV--GLEGR-GDAyPSQLSGGQKQRVGIARALANNPQVLLCDEATSAL 171
Cdd:PRK11174 438 TLRDNVllgNPDASDEQLQQALENAWVSEFLPLLpqGLDTPiGDQ-AAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446524434 172 DPETTDQILDLLLDINKrlGLTIVLITHEMHVIRKiCNRVAVMERGKIVETG 223
Cdd:PRK11174 517 DAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-227 |
7.34e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.06 E-value: 7.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 3 LLEnVKKIYKAKSGdVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaITGSelrKARQ 82
Cdd:PRK10762 4 LLQ-LKGIDKAFPG-VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-FNGP---KSSQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 83 E--IGMIFQHFNLLWSRTVRENI----EFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALA 156
Cdd:PRK10762 78 EagIGIIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524434 157 NNPQVLLCDEATSAL-DPETTdqilDLLLDIN--KRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLD 227
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTETE----SLFRVIRelKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVAD 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-217 |
7.50e-20 |
|
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: 90.84 E-value: 7.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYKAKSGdvTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgSELRKA 80
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL----TNISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQ 160
Cdd:TIGR01257 2011 HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 161 VLLCDEATSALDPETTDQILDLLLDInKRLGLTIVLITHEMHVIRKICNRVAVMERG 217
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-261 |
1.17e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 90.47 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSliRLFNQlekptSGQITIANrviSAITGSELRKAR 81
Cdd:PTZ00265 1226 IVFKNEHTNDMTNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDS--TVFKN-----SGKILLDG---VDICDYNLKDLR 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHfNLLWSRTVRENIEFPLEIAGVDKAKRRKR---VDELIHlvGLEGRGDA----YPSQLSGGQKQRVGIARA 154
Cdd:PTZ00265 1296 NLFSIVSQE-PMLFNMSIYENIKFGKEDATREDVKRACKfaaIDEFIE--SLPNKYDTnvgpYGKSLSGGQKQRIAIARA 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 155 LANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHemhvirkicnRVAVMERG-KIVetgpvldVFRNPk 233
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH----------RIASIKRSdKIV-------VFNNP- 1434
|
250 260
....*....|....*....|....*...
gi 446524434 234 qDITKRFVQQLTDSEDTNETIESLIEKY 261
Cdd:PTZ00265 1435 -DRTGSFVQAHGTHEELLSVQDGVYKKY 1461
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-225 |
4.57e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 87.86 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 18 VTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSElrKARQEIGMIFQHFNLLWSR 97
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALENGISMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 98 TVRENI---EFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPE 174
Cdd:PRK10982 89 SVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446524434 175 TTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPV 225
Cdd:PRK10982 169 EVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPL 218
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-222 |
6.64e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 87.15 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 3 LLEnVKKIYKAKSGdVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLeKPT---SGQITIANRVI--SAITGSEl 77
Cdd:NF040905 1 ILE-MRGITKTFPG-VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCrfKDIRDSE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 78 rkaRQEIGMIFQHFNLLWSRTVRENIEFPLEIA--GV-DKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARA 154
Cdd:NF040905 77 ---ALGIVIIHQELALIPYLSIAENIFLGNERAkrGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 155 LANNPQVLLCDEATSALDPETTDQILDLLLDInKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVET 222
Cdd:NF040905 154 LSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-244 |
1.31e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.27 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELrkARQeIGMIFQHFNLLW 95
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV--ARR-IGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 SRTVRENI---EFPLEIAGVDKAKR-RKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSAL 171
Cdd:PRK10253 95 DITVQELVargRYPHQPLFTRWRKEdEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 172 DPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPvldvfrnPKQDITKRFVQQL 244
Cdd:PRK10253 175 DISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA-------PKEIVTAELIERI 240
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
31-199 |
1.76e-18 |
|
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: 82.41 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 31 GEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgsELRKARQEIGMIFQHFNLLWSR-TVRENIEFPLEI 109
Cdd:TIGR01189 26 GEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHENILYLGHLPGLKPElSALENLHFWAAI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 110 AGVDkakrRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKR 189
Cdd:TIGR01189 101 HGGA----QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLAR 176
|
170
....*....|
gi 446524434 190 LGLTIvLITH 199
Cdd:TIGR01189 177 GGIVL-LTTH 185
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-226 |
3.05e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.62 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSelRKA 80
Cdd:PRK11614 5 MLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA--KIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLLWSRTVRENiefpLEIAG--VDKAKRRKRVDELIHLVG-LEGRGDAYPSQLSGGQKQRVGIARALAN 157
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEEN----LAMGGffAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIV--ETGPVL 226
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVleDTGDAL 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
12-225 |
3.78e-18 |
|
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: 81.42 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 12 KAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLF--NQLEKPTSGQITIANRVISAITGSElrKARQEIGMIFQ 89
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE--RARLGIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 90 HfnllwsrtvreniefPLEIAGVdkakrrkRVDELIHLVGlEGrgdaypsqLSGGQKQRVGIARALANNPQVLLCDEATS 169
Cdd:cd03217 85 Y---------------PPEIPGV-------KNADFLRYVN-EG--------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 170 ALDPETTDQILDLLLDInKRLGLTIVLITHEMHVIRKI-CNRVAVMERGKIVETGPV 225
Cdd:cd03217 134 GLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-219 |
3.80e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 21 VDNANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLEKpTSGQITIANRVISAITG-----------SELRKARqeigmif 88
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKvLYGALPR-TSGYVTLDGHEVVTRSPqdglangivyiSEDRKRD------- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 89 qhfNLLWSRTVRENI------EFPLEIAGVDKAKRRKRVDELIHLVGLEGrgdayPSQ------LSGGQKQRVGIARALA 156
Cdd:PRK10762 340 ---GLVLGMSVKENMsltalrYFSRAGGSLKHADEQQAVSDFIRLFNIKT-----PSMeqaiglLSGGNQQKVAIARGLM 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524434 157 NNPQVLLCDEATSALDPETTDQILDLlldIN--KRLGLTIVLITHEMHVIRKICNRVAVMERGKI 219
Cdd:PRK10762 412 TRPKVLILDEPTRGVDVGAKKEIYQL---INqfKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-199 |
6.60e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.47 E-value: 6.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 21 VDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITianrvisaitgselRKARQEIGMIFQH--FNLLwsrT 98
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA--------------RPAGARVLFLPQRpyLPLG---T 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 99 VRENIEFPLEIAGVDKAkrrkRVDELIHLVGLE------GRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALD 172
Cdd:COG4178 442 LREALLYPATAEAFSDA----ELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170 180
....*....|....*....|....*...
gi 446524434 173 PETTDQILDLLLDinkRL-GLTIVLITH 199
Cdd:COG4178 518 EENEAALYQLLRE---ELpGTTVISVGH 542
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-199 |
7.81e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 7.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANrviSAITGSELRKARQEIGmifqHFNLLW 95
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLG----HRNAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 -SRTVRENIEFPLEIAGvdkaKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPE 174
Cdd:PRK13539 86 pALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180
....*....|....*....|....*
gi 446524434 175 TTDQILDLLLDINKRLGLtIVLITH 199
Cdd:PRK13539 162 AVALFAELIRAHLAQGGI-VIAATH 185
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-229 |
2.61e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.70 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 19 TAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQItianrvisAITGSELRKARQE--IGMIFQHFNLLWS 96
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI--------SILGQPTRQALQKnlVAYVPQSEEVDWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 97 rtvrenieFPLEIAGV--------------DKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVL 162
Cdd:PRK15056 93 --------FPVLVEDVvmmgryghmgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 163 LCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNrVAVMERGKIVETGPVLDVF 229
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTF 229
|
|
| NIL |
pfam09383 |
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ... |
265-337 |
2.94e-17 |
|
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins. This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.
Pssm-ID: 462781 [Multi-domain] Cd Length: 73 Bit Score: 75.18 E-value: 2.94e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 265 KVIRLQFIGEAVERPVLQRLMQRSDIEVSILQGNIAQTNNGSYGSLVVHLNGEETAIQQAIEGIHQDQVELEV 337
Cdd:pfam09383 1 RLVRLTFPGESADEPVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELPGDPEQIEAALAYLREQGVEVEV 73
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-251 |
1.52e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.84 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKAKSgDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRviSAITGSELRKAR 81
Cdd:PTZ00265 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS--HNLKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHfNLLWSRTVRENIEFPL--------------EIAGVDKAKRRKRV-------------------DELIHL- 127
Cdd:PTZ00265 460 SKIGVVSQD-PLLFSNSIKNNIKYSLyslkdlealsnyynEDGNDSQENKNKRNscrakcagdlndmsnttdsNELIEMr 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 128 -----------------VGLEGRGDAYP-----------SQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQI 179
Cdd:PTZ00265 539 knyqtikdsevvdvskkVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524434 180 LDLLLDINKRLGLTIVLITHEMHVIRkICNRVAVM---ERGKIVETGPVLDVFRNPKQDITKRFVQQLTDSEDTN 251
Cdd:PTZ00265 619 QKTINNLKGNENRITIIIAHRLSTIR-YANTIFVLsnrERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNN 692
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-199 |
2.31e-16 |
|
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: 75.65 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVkkIYKAKSGDVTaVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIAnrvisaitgselrkAR 81
Cdd:cd03223 1 IELENL--SLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP--------------EG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQH--FNLLwsrTVRENIefpleiagvdkakrrkrvdelihlvglegrgdAYPSQ--LSGGQKQRVGIARALAN 157
Cdd:cd03223 64 EDLLFLPQRpyLPLG---TLREQL--------------------------------IYPWDdvLSGGEQQRLAFARLLLH 108
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLldinKRLGLTIVLITH 199
Cdd:cd03223 109 KPKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-220 |
2.66e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.61 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVIsaITGSELRKARQEIGMIFQHfnllw 95
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLI--VARLQQDPPRNVEGTVYDF----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 srtVRENIEfplEIAGVDKA-----------------KRRKRVDELI-HLVG--LEGR-----------GDAYPSQLSGG 144
Cdd:PRK11147 87 ---VAEGIE---EQAEYLKRyhdishlvetdpseknlNELAKLQEQLdHHNLwqLENRinevlaqlgldPDAALSSLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524434 145 QKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKrlglTIVLITHEMHVIRKICNRVAVMERGKIV 220
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-199 |
3.51e-16 |
|
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: 75.99 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 26 LKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSeLRKARQEIGmifqHFNLLWSR-TVRENIE 104
Cdd:cd03231 21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYLG----HAPGIKTTlSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 105 FPLEIAGvdkakrRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLL 184
Cdd:cd03231 96 FWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|....*
gi 446524434 185 DINKRLGLtIVLITH 199
Cdd:cd03231 170 GHCARGGM-VVLTTH 183
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-224 |
6.87e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 78.60 E-value: 6.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 17 DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAItgsELRKARQEIGMIFQHfNLLWS 96
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQT-PFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 97 RTVRENIEF------PLEIagvDKAKRRKRV-DELIHL-------VGLEGrgdaypSQLSGGQKQRVGIARALANNPQVL 162
Cdd:PRK10789 403 DTVANNIALgrpdatQQEI---EHVARLASVhDDILRLpqgydteVGERG------VMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 163 LCDEATSALDPETTDQILDLLLDINKrlGLTIVLITHEMHVIRKiCNRVAVMERGKIVETGP 224
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGN 532
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
16-225 |
8.53e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 77.47 E-value: 8.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIrLFNQLEKPTSGQitianRVISAITGSELRKA-RQEIGMifqHFNLL 94
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR-----RPWRF*TWCANRRAlRRTIG*---HRPVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 95 WSR----TVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSA 170
Cdd:NF000106 95 *GRresfSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446524434 171 LDPETTDQILDLLLDInKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPV 225
Cdd:NF000106 175 LDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-219 |
8.88e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 8.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 23 NANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAI-TGSELRKA-------RQEIGMiFQHFNLL 94
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLARGlvylpedRQSSGL-YLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 95 WSRTVRENIEFPLEIagvDKAKRRKRVDELIHLVGLEGRGDAYPSQ-LSGGQKQRVGIARALANNPQVLLCDEATSALDP 173
Cdd:PRK15439 360 WNVCALTHNRRGFWI---KPARENAVLERYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446524434 174 ETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKI 219
Cdd:PRK15439 437 SARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
16-224 |
1.32e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.86 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIanrvisaiTGSELRKAR-------------Q 82
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEV--------LGGDMADARhrravcpriaympQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 83 EIGMifqhfNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVL 162
Cdd:NF033858 84 GLGK-----NLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 163 LCDEATSALDPETTDQILDLLLDINK-RLGLTIVLITHEM-------HVIrkicnrvaVMERGKIVETGP 224
Cdd:NF033858 159 ILDEPTTGVDPLSRRQFWELIDRIRAeRPGMSVLVATAYMeeaerfdWLV--------AMDAGRVLATGT 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-232 |
1.46e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.97 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 28 IEKGEIFGVIGYSGAGKSSLI-RLFNQLekPTSGQITIANRVISAITGSELRKAR----QE----IGM-IFQHFNLLWSr 97
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLaRMAGLL--PGSGSIQFAGQPLEAWSAAELARHRaylsQQqtppFAMpVFQYLTLHQP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 98 tvreniefpleiAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARAL-----ANNP--QVLLCDEATSA 170
Cdd:PRK03695 96 ------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524434 171 LDpeTTDQ-ILDLLLDINKRLGLTIVLITHEM-HVIRKiCNRVAVMERGKIVETGPVLDVFRNP 232
Cdd:PRK03695 164 LD--VAQQaALDRLLSELCQQGIAVVMSSHDLnHTLRH-ADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-230 |
1.52e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.88 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 25 NLKIEKGEIFGVIGYSGAGKSSLI-RLFNQLekPTSGQITIANRVISAITGSELRKARqeiGMIFQHFNLLWSRTVRENI 103
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLaRMAGLL--PGQGEILLNGRPLSDWSAAELARHR---AYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 104 EFPLEiAGVDKAKRRKRVDELIHLVGLEgrgDAYP---SQLSGGQKQRVGIARAL-----ANNP--QVLLCDEATSALDp 173
Cdd:COG4138 91 ALHQP-AGASSEAVEQLLAQLAEALGLE---DKLSrplTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSLD- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 174 eTTDQI-LDLLLDINKRLGLTIVLITHEM-HVIRKiCNRVAVMERGKIVETGPVLDVFR 230
Cdd:COG4138 166 -VAQQAaLDRLLRELCQQGITVVMSSHDLnHTLRH-ADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-207 |
2.15e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.68 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 22 DNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIanrvisaiTGSELRKARQEIgmifqHFNLLW------ 95
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLW--------QGEPIRRQRDEY-----HQDLLYlghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 ---SRTVRENIEFPLEIAGVdkAKRRKRVDELIHlVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALD 172
Cdd:PRK13538 85 iktELTALENLRFYQRLHGP--GDDEALWEALAQ-VGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524434 173 PETTDQILDLLLDINKRLGLtIVLITH-EMHVI----RKI 207
Cdd:PRK13538 162 KQGVARLEALLAQHAEQGGM-VILTTHqDLPVAsdkvRKL 200
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
10-247 |
2.82e-15 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 74.47 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 10 IYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQItianrvisaitgselrKARQEIGMIFQ 89
Cdd:PRK13546 29 IPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV----------------DRNGEVSVIAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 90 HFNLLWSRTVRENIEFPLEIAGVDKAKRRKRVDELIHLVGLeGRGDAYP-SQLSGGQKQRVGIARALANNPQVLLCDEAT 168
Cdd:PRK13546 93 SAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSEL-GEFIYQPvKKYSSGMRAKLGFSINITVNPDILVIDEAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 169 SALDPETTDQILDLLLDInKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDV----------FRNPKQDITK 238
Cdd:PRK13546 172 SVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVlpkyeaflndFKKKSKAEQK 250
|
....*....
gi 446524434 239 RFVQQLTDS 247
Cdd:PRK13546 251 EFRNKLDES 259
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-204 |
3.45e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.99 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQItianrvisaitgseLRKA 80
Cdd:PRK09544 4 LVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------------KRNG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQHFNLlwsrtvreNIEFPLEIA-------GVDKAK---RRKRVdELIHLVglegrgDAYPSQLSGGQKQRVG 150
Cdd:PRK09544 66 KLRIGYVPQKLYL--------DTTLPLTVNrflrlrpGTKKEDilpALKRV-QAGHLI------DAPMQKLSGGETQRVL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446524434 151 IARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVI 204
Cdd:PRK09544 131 LARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-223 |
3.49e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.30 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYKaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRkar 81
Cdd:PRK10790 341 IDIDNVSFAYR---DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLR--- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQHFNLLwSRTVRENIEFPLEI--AGVDKAKRRKRVDELIHLV--GLEGRGDAYPSQLSGGQKQRVGIARALAN 157
Cdd:PRK10790 415 QGVAMVQQDPVVL-ADTFLANVTLGRDIseEQVWQALETVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLLLDINKRlgLTIVLITHEMHVIRKiCNRVAVMERGKIVETG 223
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQG 556
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-223 |
7.94e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.54 E-value: 7.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 23 NANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLEKPTSGQITIANRVISAitgselrkarQEIGMIFqhfnllwSRTVRE 101
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTVAYV----------PQVSWIF-------NATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 102 NIEFPLEIAGvDKAKRRKRVDELIHLVGLEGRGDAYP-----SQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETT 176
Cdd:PLN03130 698 NILFGSPFDP-ERYERAIDVTALQHDLDLLPGGDLTEigergVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVG 776
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446524434 177 DQILDLLLDINKRlGLTIVLITHEMHVIRKIcNRVAVMERGKIVETG 223
Cdd:PLN03130 777 RQVFDKCIKDELR-GKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-230 |
1.34e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.94 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 21 VDNANLKIEKGEIFGVIGYSGAGKSSLIRLF-NQLEKPT-------SGQITIANRVISAITGSELRKARqeiGMIFQHFN 92
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLR---AVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 93 LLWSRTVRENI---EFP-LEIAGVDKAKRRKRVDELIHLVG---LEGRgDAypSQLSGGQKQRVGIARALAN-------- 157
Cdd:PRK13547 94 PAFAFSAREIVllgRYPhARRAGALTHRDGEIAWQALALAGataLVGR-DV--TTLSGGELARVQFARVLAQlwpphdaa 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524434 158 -NPQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFR 230
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-262 |
2.27e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.24 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 23 NANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLEKPTSGQITIANRVISAitgselrkarQEIGMIFqhfnllwSRTVRE 101
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVAYV----------PQVSWIF-------NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 102 NIEFpleiaGVDKakRRKRVDELIHLVGLEGRGDAYPSQ-----------LSGGQKQRVGIARALANNPQVLLCDEATSA 170
Cdd:PLN03232 698 NILF-----GSDF--ESERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 171 LDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKIcNRVAVMERGKIVETGPVLDVFRNpkQDITKRFVQ---QLTDS 247
Cdd:PLN03232 771 LDAHVAHQVFDSCMKDELK-GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS--GSLFKKLMEnagKMDAT 846
|
250
....*....|....*
gi 446524434 248 EDTNETIESLIEKYP 262
Cdd:PLN03232 847 QEVNTNDENILKLGP 861
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-202 |
2.55e-14 |
|
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: 71.21 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 17 DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLI-RLFNQLEKpTSGQITIANRVISAITGSELR-KARQEIGMIFQHFNLL 94
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNKNESEPSFEATRsRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 95 wSRTVRENIEFpleiagvDKAKRRKRVDELIHLVGLEGRGDAYPS-----------QLSGGQKQRVGIARALANNPQVLL 163
Cdd:cd03290 92 -NATVEENITF-------GSPFNKQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524434 164 CDEATSALDPETTDQ-----ILDLLLDiNKRlglTIVLITHEMH 202
Cdd:cd03290 164 LDDPFSALDIHLSDHlmqegILKFLQD-DKR---TLVLVTHKLQ 203
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-221 |
4.76e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 72.70 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYKAKSGDVTAVdnaNLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRvisAITGSELRKARQE 83
Cdd:PRK10522 325 LRNVTFAYQDNGFSVGPI---NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---PVTAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQHFNLLWSRTVRENieFPLEIAGVDKAKRRKrvdELIHLVGLEGrGDAYPSQLSGGQKQRVGIARALANNPQVLL 163
Cdd:PRK10522 399 FSAVFTDFHLFDQLLGPEG--KPANPALVEKWLERL---KMAHKLELED-GRISNLKLSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 164 CDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHVIRKiCNRVAVMERGKIVE 221
Cdd:PRK10522 473 LDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-221 |
5.57e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.09 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 32 EIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKARQeigmIFQHFNLLWSRTVRENIEfPLE--- 108
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLS----IIPQSPVLFSGTVRFNID-PFSehn 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 109 IAGVDKAKRRKRVDELI--HLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDI 186
Cdd:PLN03232 1338 DADLWEALERAHIKDVIdrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREE 1417
|
170 180 190
....*....|....*....|....*....|....*
gi 446524434 187 NKrlGLTIVLITHEMHVIRKiCNRVAVMERGKIVE 221
Cdd:PLN03232 1418 FK--SCTMLVIAHRLNTIID-CDKILVLSSGQVLE 1449
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-248 |
6.09e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.89 E-value: 6.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 27 KIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITgseLRKARQEIGMIFQHfNLLWSRTVRENIEFP 106
Cdd:PTZ00243 1332 RIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG---LRELRRQFSMIPQD-PVLFDGTVRQNVDPF 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 107 LEI------AGVDKAKRRKRV---DELIHLVGLEGrGDAYpsqlSGGQKQRVGIARA-LANNPQVLLCDEATSALDPETT 176
Cdd:PTZ00243 1408 LEAssaevwAALELVGLRERVaseSEGIDSRVLEG-GSNY----SVGQRQLMCMARAlLKKGSGFILMDEATANIDPALD 1482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 177 DQILDLLLDINKrlGLTIVLITHEMHVIRKiCNRVAVMERGKIVETGPVLDVFRNPkQDITKRFVQQLTDSE 248
Cdd:PTZ00243 1483 RQIQATVMSAFS--AYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGSPRELVMNR-QSIFHSMVEALGRSE 1550
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-221 |
7.56e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.85 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 27 KIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKArqeIGMIFQHfNLLWSRTVRENIEFP 106
Cdd:PLN03130 1261 EISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV---LGIIPQA-PVLFSGTVRFNLDPF 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 107 LEIAGVD--KAKRRKRVDELI--HLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETtdqilDL 182
Cdd:PLN03130 1337 NEHNDADlwESLERAHLKDVIrrNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT-----DA 1411
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524434 183 LldINKRL-----GLTIVLITHEMHVIRKiCNRVAVMERGKIVE 221
Cdd:PLN03130 1412 L--IQKTIreefkSCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-223 |
1.23e-13 |
|
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: 71.90 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 25 NLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITgseLRKARQEIGMIFQHfNLLWSRTVRENIE 104
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFKITIIPQD-PVLFSGSLRMNLD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 105 -----------FPLEIAGVdKAKRRKRVDELIHLVGLEGRgdaypsQLSGGQKQRVGIARALANNPQVLLCDEATSALDP 173
Cdd:TIGR00957 1382 pfsqysdeevwWALELAHL-KTFVSALPDKLDHECAEGGE------NLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524434 174 ETTDQILDLLLdiNKRLGLTIVLITHEMHVIRKIcNRVAVMERGKIVETG 223
Cdd:TIGR00957 1455 ETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFG 1501
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-220 |
3.38e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 24 ANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITI------ANRVISAITGS-----ELRKARQEIGMifqhfn 92
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdgkpidIRSPRDAIRAGimlcpEDRKAEGIIPV------ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 93 llwsRTVRENIefplEI--------AG--VDKAKRRKRVDELIHLVGLEGRGDAYP-SQLSGGQKQRVGIARALANNPQV 161
Cdd:PRK11288 346 ----HSVADNI----NIsarrhhlrAGclINNRWEAENADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIV 220
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-228 |
3.43e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 70.30 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 20 AVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITGSELRKARQEIgmifqhfnllwsrtv 99
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI--------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 100 rENIEFPLEIAGVDKAKRRKRVDELIHLVGLeGRGDAYPSQ-LSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQ 178
Cdd:PRK13545 104 -ENIELKGLMMGLTKEKIKEIIPEIIEFADI-GKFIYQPVKtYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524434 179 ILDLLLDInKRLGLTIVLITHEMHVIRKICNRVAVMERGKIVETGPVLDV 228
Cdd:PRK13545 182 CLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-212 |
4.02e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 69.96 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 5 ENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVisaitgselrkarqEI 84
Cdd:TIGR03719 326 ENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV--------------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 85 GMIFQ-HFNLLWSRTVRENIEFPLEIAGVDKAKRRKRvdelihlvglegrgdAYPS--------------QLSGGQKQRV 149
Cdd:TIGR03719 388 AYVDQsRDALDPNKTVWEEISGGLDIIKLGKREIPSR---------------AYVGrfnfkgsdqqkkvgQLSGGERNRV 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 150 GIARALANNPQVLLCDEATSALDPETTDQILDLLLDinkrLGLTIVLITHEmhviRKICNRVA 212
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLN----FAGCAVVISHD----RWFLDRIA 507
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
12-223 |
4.14e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.13 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 12 KAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLF--NQLEKPTSGQITIANRVISAITGSElrKARQEIGMIFQ 89
Cdd:CHL00131 14 HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPEE--RAHLGIFLAFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 90 hfnllwsrtvrenieFPLEIAGVD---------KAKRRKR-------------VDELIHLVGLEgrgdayPSQL------ 141
Cdd:CHL00131 92 ---------------YPIEIPGVSnadflrlayNSKRKFQglpeldplefleiINEKLKLVGMD------PSFLsrnvne 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 142 --SGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQI---LDLLLDINKrlglTIVLITHEMHVIRKIC-NRVAVME 215
Cdd:CHL00131 151 gfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIaegINKLMTSEN----SIILITHYQRLLDYIKpDYVHVMQ 226
|
....*...
gi 446524434 216 RGKIVETG 223
Cdd:CHL00131 227 NGKIIKTG 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-252 |
5.02e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.19 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 23 NANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLEKpTSGQItIANRVISAItgselrkARQEIGMifqhfnllwSRTVRE 101
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFEI-SEGRV-WAERSIAYV-------PQQAWIM---------NATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 102 NIEF--PLEIAGVDKAKRRKRVDELIHLV--GLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTD 177
Cdd:PTZ00243 740 NILFfdEEDAARLADAVRVSQLEADLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 178 QIL-DLLLDinkRL-GLTIVLITHEMHVIRKiCNRVAVMERGKIVETGPVLDVFRNPkqdITKRFVQQLTDSEDTNE 252
Cdd:PTZ00243 820 RVVeECFLG---ALaGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTS---LYATLAAELKENKDSKE 889
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-249 |
2.24e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.73 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 25 NLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLeKPTSGQITIANRVISAITGSELRKARQEIgmiFQHFN--LL------W 95
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARaLAGEL-PLLSGERQSQFSHITRLSFEQLQKLVSDE---WQRNNtdMLspgeddT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 96 SRTVRENIEfpleiAGVDKAKRRKRVDELIHLVGLEGRGDAYpsqLSGGQKQRVGIARALANNPQVLLCDEATSALDPET 175
Cdd:PRK10938 99 GRTTAEIIQ-----DEVKDPARCEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524434 176 TDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVETGpvldvfrnPKQDITKR-FVQQLTDSED 249
Cdd:PRK10938 171 RQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETG--------EREEILQQaLVAQLAHSEQ 236
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-199 |
2.29e-12 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 67.85 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 1 MILLENVKKIykAKSGDVTaVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIanrvisaitgselrKA 80
Cdd:TIGR00954 451 GIKFENIPLV--TPNGDVL-IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK--------------PA 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 81 RQEIGMIFQ--HFNLlwsRTVRENIEFPLeiaGVDKAKRRKRVD----------ELIHLVGLEGRGDA---YPSQLSGGQ 145
Cdd:TIGR00954 514 KGKLFYVPQrpYMTL---GTLRDQIIYPD---SSEDMKRRGLSDkdleqildnvQLTHILEREGGWSAvqdWMDVLSGGE 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446524434 146 KQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLldinKRLGLTIVLITH 199
Cdd:TIGR00954 588 KQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
35-218 |
2.60e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.65 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 35 GVIGYSGAGKSSLIRLFNQLEKPTSGQITIAnrviSAITgselrkarqeIGMIFQHFNLLWSRTVRENIE---------- 104
Cdd:TIGR03719 35 GVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ----PGIK----------VGYLPQEPQLDPTKTVRENVEegvaeikdal 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 105 ---------FPLEIAGVDK-AKRRKRVDELIHLVG---LEGR------------GDAYPSQLSGGQKQRVGIARALANNP 159
Cdd:TIGR03719 101 drfneisakYAEPDADFDKlAAEQAELQEIIDAADawdLDSQleiamdalrcppWDADVTKLSGGERRRVALCRLLLSKP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 160 QVLLCDEATSALDPETTDQILDLLldinKRLGLTIVLITHEMHVIRKICNRVAVMERGK 218
Cdd:TIGR03719 181 DMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHDRYFLDNVAGWILELDRGR 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-224 |
6.09e-12 |
|
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: 66.89 E-value: 6.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 16 GDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLEKpTSGQITIanrvisaiTGSELRKARQEigmifqhfnll 94
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHM--------KGSVAYVPQQA----------- 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 95 WSR--TVRENIEFpleiagvDKAKRRKRVDELIHLVGLEGRGDAYPS-----------QLSGGQKQRVGIARALANNPQV 161
Cdd:TIGR00957 709 WIQndSLRENILF-------GKALNEKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRL-GLTIVLITHEMHVIRKIcNRVAVMERGKIVETGP 224
Cdd:TIGR00957 782 YLFDDPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGS 844
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-219 |
6.58e-12 |
|
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: 66.39 E-value: 6.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 21 VDNANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLEKPTSGQITIANRVISaiTGSELRKARQEIGMI---FQHFNLLWS 96
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVD--IRNPAQAIRAGIAMVpedRKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 97 RTVRENIEFPL-----EIAGVDKAKRRKRVDELIHLVGLEGRGDAYP-SQLSGGQKQRVGIARALANNPQVLLCDEATSA 170
Cdd:TIGR02633 354 LGVGKNITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446524434 171 LDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKI 219
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-221 |
7.10e-12 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 66.36 E-value: 7.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 25 NLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITgselRKA-RQEIGMIFQHFNLlwsrtvreni 103
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN----REAyRQLFSAVFSDFHL---------- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 104 eFPlEIAGVDKAKRRKRVDELIHLVGLEG----RGDAYPS-QLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTD- 177
Cdd:COG4615 418 -FD-RLLGLDGEADPARARELLERLELDHkvsvEDGRFSTtDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRv 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524434 178 ---QILDLLldinKRLGLTIVLITHE---MHVirkiCNRVAVMERGKIVE 221
Cdd:COG4615 496 fytELLPEL----KARGKTVIAISHDdryFDL----ADRVLKMDYGKLVE 537
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-175 |
7.85e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.91 E-value: 7.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 5 ENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVisaitgselrkarqEI 84
Cdd:PRK11819 328 ENLSKSF----GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV--------------KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 85 GMIFQ-HFNLLWSRTVRENIEFPLEI-------------------AGVDKAKRrkrvdelihlVGlegrgdaypsQLSGG 144
Cdd:PRK11819 390 AYVDQsRDALDPNKTVWEEISGGLDIikvgnreipsrayvgrfnfKGGDQQKK----------VG----------VLSGG 449
|
170 180 190
....*....|....*....|....*....|.
gi 446524434 145 QKQRVGIARALANNPQVLLCDEATSALDPET 175
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-219 |
8.91e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.72 E-value: 8.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 21 VDNANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLEKPTSGQITIANRVISaiTGSELRKARQEIGMIFQ---HFNLLWS 96
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVK--IRNPQQAIAQGIAMVPEdrkRDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 97 RTVRENIEfpleIAGVDKAKRRKRVDELIHLVGLEGRGD------AYP----SQLSGGQKQRVGIARALANNPQVLLCDE 166
Cdd:PRK13549 356 MGVGKNIT----LAALDRFTGGSRIDDAAELKTILESIQrlkvktASPelaiARLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446524434 167 ATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKI 219
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-220 |
1.22e-11 |
|
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: 63.05 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 6 NVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLEKP--TSGQITIANrvisaITGSE-LRKAR 81
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKaLANRTEGNvsVEGDIHYNG-----IPYKEfAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGMIFQ---HFNLLwsrTVRENIEFPLEIagvdkakrrkrvdelihlvglegRGDAYPSQLSGGQKQRVGIARALANN 158
Cdd:cd03233 83 GEIIYVSEedvHFPTL---TVRETLDFALRC-----------------------KGNEFVRGISGGERKRVSIAEALVSR 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 159 PQVLLCDEATSALDPETTDQILDLLLDINKRLGLTIVLITHEMHV-IRKICNRVAVMERGKIV 220
Cdd:cd03233 137 ASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQI 199
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-215 |
4.99e-11 |
|
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: 62.04 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 28 IEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAitgselrkARQEIGMIFQhfnllwsRTVRENIEFPL 107
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY--------KPQYIKADYE-------GTVRDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 108 EIAGVDKAKRrkrvDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPE----TTDQILDLL 183
Cdd:cd03237 87 KDFYTHPYFK----TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASKVIRRFA 162
|
170 180 190
....*....|....*....|....*....|..
gi 446524434 184 LDINKrlglTIVLITHEMHVIRKICNRVAVME 215
Cdd:cd03237 163 ENNEK----TAFVVEHDIIMIDYLADRLIVFE 190
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-246 |
6.09e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 28 IEKGEIFGVIGYSGAGKSSLIRLF----NQLEKPTSGQITIanrviSAITGSELRKA-RQEIGMIFQ---HFNLLwsrTV 99
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITY-----DGITPEEIKKHyRGDVVYNAEtdvHFPHL---TV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 100 RENIEFP-------LEIAGVDKAKRRKRVDELIHLV-GLEGR-----GDAYPSQLSGGQKQRVGIARALANNPQVLLCDE 166
Cdd:TIGR00956 156 GETLDFAarcktpqNRPDGVSREEYAKHIADVYMATyGLSHTrntkvGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 167 ATSALDPETTDQILDLLLDINKRLGLT-IVLITHEMHVIRKICNRVAVMERGKIVETGP---VLDVFRN-----PKQDIT 237
Cdd:TIGR00956 236 ATRGLDSATALEFIRALKTSANILDTTpLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPadkAKQYFEKmgfkcPDRQTT 315
|
....*....
gi 446524434 238 KRFVQQLTD 246
Cdd:TIGR00956 316 ADFLTSLTS 324
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-206 |
7.31e-11 |
|
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: 62.18 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 23 NANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAitgselrkarqeigmifQHFNLLWSRTVREN 102
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFS-----------------SQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 103 IefpleIAGVDKAKRRKRvdELIHLVGLEGRGDAYPSQ-----------LSGGQKQRVGIARALANNPQVLLCDEATSAL 171
Cdd:cd03291 118 I-----IFGVSYDEYRYK--SVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190
....*....|....*....|....*....|....*...
gi 446524434 172 DPETTDQILD---LLLDINKrlglTIVLITHEMHVIRK 206
Cdd:cd03291 191 DVFTEKEIFEscvCKLMANK----TRILVTSKMEHLKK 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
12-219 |
1.08e-10 |
|
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: 61.41 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 12 KAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKpTSGQITIANRVISAITGSELRKArqeIGMIFQHF 91
Cdd:cd03289 11 KYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA---FGVIPQKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 92 nLLWSRTVRENiefpLEIAGVDKAKRRKRVDELihlVGLEGRGDAYPSQL-----------SGGQKQRVGIARALANNPQ 160
Cdd:cd03289 87 -FIFSGTFRKN----LDPYGKWSDEEIWKVAEE---VGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 161 VLLCDEATSALDPeTTDQILDLLLDiNKRLGLTIVLITHEMHVIRKiCNRVAVMERGKI 219
Cdd:cd03289 159 ILLLDEPSAHLDP-ITYQVIRKTLK-QAFADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-221 |
2.65e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 6 NVKKIYKAK---SGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAitGSELRKARQ 82
Cdd:PRK09700 261 AHETVFEVRnvtSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP--RSPLDAVKK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 83 EIGMIFQhfnllwSRtvRENIEFP-------------LEIAG-------VDKAKRRKRVDELIHLVGLEGRG-DAYPSQL 141
Cdd:PRK09700 339 GMAYITE------SR--RDNGFFPnfsiaqnmaisrsLKDGGykgamglFHEVDEQRTAENQRELLALKCHSvNQNITEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 142 SGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGKIVE 221
Cdd:PRK09700 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
12-183 |
4.24e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 12 KAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIrlfNQL-EKPTSGQITIANRVISaitGSELRKARQE-IGMIFQ 89
Cdd:TIGR00956 770 KIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLL---NVLaERVTTGVITGGDRLVN---GRPLDSSFQRsIGYVQQ 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 90 HFNLLWSRTVRENIEFPLEI---AGVDKAKRRKRVDELIHLVGLEGRGDAY----PSQLSGGQKQRVGIARALANNPQVL 162
Cdd:TIGR00956 844 QDLHLPTSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVvgvpGEGLNVEQRKRLTIGVELVAKPKLL 923
|
170 180
....*....|....*....|..
gi 446524434 163 L-CDEATSALDPETTDQILDLL 183
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLM 945
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
25-221 |
1.13e-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: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 25 NLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAITgseLRKARQEIGMIFQHfNLLWSRTVRENIE 104
Cdd:cd03288 41 KAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSRLSIILQD-PILFSGSIRFNLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 105 fPLEIAGVDKAKRRKRVDELIHLV-GLEGRGDAYPSQ----LSGGQKQRVGIARALANNPQVLLCDEATSALDpETTDQI 179
Cdd:cd03288 117 -PECKCTDDRLWEALEIAQLKNMVkSLPGGLDAVVTEggenFSVGQRQLFCLARAFVRKSSILIMDEATASID-MATENI 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446524434 180 LDLLLdINKRLGLTIVLITHEMHVIRKiCNRVAVMERGKIVE 221
Cdd:cd03288 195 LQKVV-MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVE 234
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-199 |
1.16e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 35 GVIGYSGAGKSSLIRLFNQLEKPTSGQITIAnrviSAITgselrkarqeIGMIFQHFNLLWSRTVRENIE---------- 104
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARPA----PGIK----------VGYLPQEPQLDPEKTVRENVEegvaevkaal 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 105 ---------FPLEIAGVDK-AKRRKRVDELIHLVG---LEGR------------GDAYPSQLSGGQKQRVGIARALANNP 159
Cdd:PRK11819 103 drfneiyaaYAEPDADFDAlAAEQGELQEIIDAADawdLDSQleiamdalrcppWDAKVTKLSGGERRRVALCRLLLEKP 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446524434 160 QVLLCDEATSALDPETTD---QILdllldinKRLGLTIVLITH 199
Cdd:PRK11819 183 DMLLLDEPTNHLDAESVAwleQFL-------HDYPGTVVAVTH 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-200 |
1.45e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 17 DVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISaitgSELRKARQEIGMIFQHFNLLWS 96
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTYQKQLCFVGHRSGINPY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 97 RTVRENIEFPLEIAGVDKAkrrkrVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETT 176
Cdd:PRK13540 89 LTLRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180
....*....|....*....|....
gi 446524434 177 DQILDlLLDINKRLGLTIVLITHE 200
Cdd:PRK13540 164 LTIIT-KIQEHRAKGGAVLLTSHQ 186
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-200 |
1.78e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.12 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 31 GEIFGVIGYSGAGKSSLIR-LFNQLEKPT-SGQITIANRVISaitgselRKARQEIGMIFQHFNLLWSRTVRENIEF--- 105
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNaLAGRIQGNNfTGTILANNRKPT-------KQILKRTGFVTQDDILYPHLTVRETLVFcsl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 106 ---PLEIAGVDKAKRRKRVDELIHLVGLEGR--GDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQIL 180
Cdd:PLN03211 167 lrlPKSLTKQEKILVAESVISELGLTKCENTiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180
....*....|....*....|
gi 446524434 181 DLLLDINKRlGLTIVLITHE 200
Cdd:PLN03211 247 LTLGSLAQK-GKTIVTSMHQ 265
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-172 |
2.13e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.64 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 29 EKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIA---NRVISAITGSELrkarqeigmiFQHFNLLWSRTVR----- 100
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEpswDEVLKRFRGTEL----------QDYFKKLANGEIKvahkp 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 101 ENIEF-PLEIAGV-----DKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALD 172
Cdd:COG1245 167 QYVDLiPKVFKGTvrellEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-199 |
2.31e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.78 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 25 NLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRviSAITGSELRKAR--QEIGMIFQHFNLLwsrtvrEN 102
Cdd:PRK13543 31 DFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK--TATRGDRSRFMAylGHLPGLKADLSTL------EN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 103 IEFpleIAGVDKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDqILDL 182
Cdd:PRK13543 103 LHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGIT-LVNR 178
|
170
....*....|....*..
gi 446524434 183 LLDINKRLGLTIVLITH 199
Cdd:PRK13543 179 MISAHLRGGGAALVTTH 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-206 |
2.34e-09 |
|
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: 58.77 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 18 VTAV-DNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAitgselrkarqeigmifQHFNLLWS 96
Cdd:TIGR01271 438 VTPVlKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFS-----------------PQTSWIMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 97 RTVRENIEFpleiaGVDKAKRRKRvdELIHLVGLEGRGDAYPSQ-----------LSGGQKQRVGIARALANNPQVLLCD 165
Cdd:TIGR01271 501 GTIKDNIIF-----GLSYDEYRYT--SVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLD 573
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446524434 166 EATSALDPETTDQILDLL---LDINKrlglTIVLITHEMHVIRK 206
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFESClckLMSNK----TRILVTSKLEHLKK 613
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-180 |
4.60e-09 |
|
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: 58.00 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 12 KAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKpTSGQITIANRVISAITgseLRKARQEIGMIFQHF 91
Cdd:TIGR01271 1226 KYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVT---LQTWRKAFGVIPQKV 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 92 nLLWSRTVRENIEfPLEiagvdkakrrKRVDELI----HLVGLEGRGDAYPSQL-----------SGGQKQRVGIARALA 156
Cdd:TIGR01271 1302 -FIFSGTFRKNLD-PYE----------QWSDEEIwkvaEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSIL 1369
|
170 180
....*....|....*....|....
gi 446524434 157 NNPQVLLCDEATSALDPeTTDQIL 180
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDP-VTLQII 1392
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
5-200 |
6.04e-09 |
|
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: 54.94 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 5 ENVKKIYKAKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQleKPTSGQITiANRVISaitGSELRKA-RQE 83
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVIT-GEILIN---GRPLDKNfQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 84 IGMIFQHFNLLWSRTVRENIEFpleiagvdkakrrkrvdelihlvglegrgDAYPSQLSGGQKQRVGIARALANNPQVLL 163
Cdd:cd03232 81 TGYVEQQDVHSPNLTVREALRF-----------------------------SALLRGLSVEQRKRLTIGVELAAKPSILF 131
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446524434 164 CDEATSALDPETTDQILDLLldinKRL---GLTIVLITHE 200
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFL----KKLadsGQAILCTIHQ 167
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-222 |
1.07e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 20 AVDNANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLEKpTSGQITIANRVIS------AITG-----SELRKARQEIGMI 87
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVEtLFGIREK-SAGTITLHGKKINnhnaneAINHgfalvTEERRSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 88 FQHFNLLWSrtvreNIEFPLEIAGVDKAKRRKRVDELIhlvgLEGRGDAYPSQ------LSGGQKQRVGIARALANNPQV 161
Cdd:PRK10982 342 DIGFNSLIS-----NIRNYKNKVGLLDNSRMKSDTQWV----IDSMRVKTPGHrtqigsLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524434 162 LLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIRKICNRVAVMERGK---IVET 222
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLvagIVDT 475
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-172 |
1.98e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 28 IEKGEIFGVIGYSGAGKSSLIRL--------FNQLEKPTSgqitiANRVISAITGSEL------------RKAR--QEIG 85
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIlsgelipnLGDYEEEPS-----WDEVLKRFRGTELqnyfkklyngeiKVVHkpQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 86 MIFQHFNllwsRTVRENIEfpleiagvdKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCD 165
Cdd:PRK13409 171 LIPKVFK----GKVRELLK---------KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
....*..
gi 446524434 166 EATSALD 172
Cdd:PRK13409 238 EPTSYLD 244
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-172 |
2.89e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.91 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 31 GEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIA---NRVISAITGSELRKARQEI-------GMIFQHFNLLwSRTVR 100
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPpdwDEILDEFRGSELQNYFTKLlegdvkvIVKPQYVDLI-PKAVK 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524434 101 ENIEFPLEiagvdKAKRRKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALD 172
Cdd:cd03236 105 GKVGELLK-----KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-251 |
2.90e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 13 AKSGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRVisaitgselrkarqEIGMIFQHfN 92
Cdd:PRK10636 320 AGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGI--------------KLGYFAQH-Q 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 93 LLWSRTVRENIEFPLEIAgvDKAKRRKRVDeliHLVGLEGRGDAYP---SQLSGGQKQRVGIARALANNPQVLLCDEATS 169
Cdd:PRK10636 385 LEFLRADESPLQHLARLA--PQELEQKLRD---YLGGFGFQGDKVTeetRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 170 ALDPETTDQILDLLLDINKRLgltiVLITHEMHVIRKICNRVAVMERGKIVETGPVLDVFRNPKQDITKRFVQQLTDSED 249
Cdd:PRK10636 460 HLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQENQTDEAPKE 535
|
..
gi 446524434 250 TN 251
Cdd:PRK10636 536 NN 537
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-205 |
3.24e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 38 GYSGAGKSSLIRLFNQLEKPTSGQITIANRVISAItgselrkARQEIGMIFQHFNLLWSRTVRENIEFPLEIagvdkAKR 117
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------AKPYCTYIGHNLGLKLEMTVFENLKFWSEI-----YNS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 118 RKRVDELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDqILDLLLDINKRLGLTIVLI 197
Cdd:PRK13541 101 AETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD-LLNNLIVMKANSGGIVLLS 179
|
....*...
gi 446524434 198 THEMHVIR 205
Cdd:PRK13541 180 SHLESSIK 187
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-219 |
1.37e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 23 NANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLEkPTSGQITIAN-----------------RVISA-ITG-SELRKARQ 82
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKiLGGDLE-PSAGNVSLDPnerlgklrqdqfafeefTVLDTvIMGhTELWEVKQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 83 EigmifqhfnllwsrtvRENI---------------EFPLEIAGVDKAKRRKRVDELIHLVGLEGRGDAYP-SQLSGGQK 146
Cdd:PRK15064 98 E----------------RDRIyalpemseedgmkvaDLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLmSEVAPGWK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446524434 147 QRVGIARALANNPQVLLCDEATSALDPETTDQILDLLldiNKRlGLTIVLITHEMHVIRKICNRVAVMERGKI 219
Cdd:PRK15064 162 LRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL---NER-NSTMIIISHDRHFLNSVCTHMADLDYGEL 230
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-206 |
9.38e-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: 47.75 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 30 KGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIanrvisaITGSELRkarqeigmifqhfnllwsrtvreniefplei 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDIL------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 110 agvdkakrrkrvdELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDL-----LL 184
Cdd:smart00382 43 -------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLL 109
|
170 180
....*....|....*....|..
gi 446524434 185 DINKRLGLTIVLITHEMHVIRK 206
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGP 131
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
139-205 |
2.02e-06 |
|
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: 47.32 E-value: 2.02e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446524434 139 SQLSGGQKQRVGIARALANNPQ--VLLCDEATSALDPETTDQILDLLLDInKRLGLTIVLITHEMHVIR 205
Cdd:cd03238 86 STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLS 153
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-205 |
2.28e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.02 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 23 NANLKIEKGEIFGVIGYSGAGKSSLI---------------------RLFNQLEKPTSGQITIANRVISAITGSELRKAR 81
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIEGLSPAIAIDQKTTSRNPR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 82 QEIGM---IFQHFNLLWSRtvreniefpleiAGVdkakrRKRVDELIHlVGLEG-RGDAYPSQLSGGQKQRVGIARALAN 157
Cdd:cd03270 93 STVGTvteIYDYLRLLFAR------------VGI-----RERLGFLVD-VGLGYlTLSRSAPTLSGGEAQRIRLATQIGS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446524434 158 NPQVLL--CDEATSALDPETTDQILDLLLDInKRLGLTIVLITHEMHVIR 205
Cdd:cd03270 155 GLTGVLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIR 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-220 |
2.44e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 21 VDNANLKIEKGEIFGVIGYSGAGKSSL-IRLFNQ-LEKPTSGQITIANRVIS------AITG-----SELRKarqeigmi 87
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRsYGRNISGTVFKDGKEVDvstvsdAIDAglayvTEDRK-------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 88 fqHFNLLWSRTVRENIEfpleIAGVDKAKRRKRVDELIHLVGLEGRGDAY----PS------QLSGGQKQRVGIARALAN 157
Cdd:NF040905 348 --GYGLNLIDDIKRNIT----LANLGKVSRRGVIDENEEIKVAEEYRKKMniktPSvfqkvgNLSGGNQQKVVLSKWLFT 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524434 158 NPQVLLCDEATSALDPETTDQILDLlldINK--RLGLTIVLITHEMHVIRKICNRVAVMERGKIV 220
Cdd:NF040905 422 DPDVLILDEPTRGIDVGAKYEIYTI---INElaAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
23-219 |
2.85e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 23 NANLKIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQItianrvisaitgseLRKARQEIGMIFQH----FNLLWSRT 98
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAKVRMAVFSQHhvdgLDLSSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 99 VRENIEFPleiaGVDKAKRRKRVDELihlvGLEGRGDAYPS-QLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTD 177
Cdd:PLN03073 593 LYMMRCFP----GVPEQKLRAHLGSF----GVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVE 664
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446524434 178 QILDLLLDINKrlglTIVLITHEMHVIRKICNRVAVMERGKI 219
Cdd:PLN03073 665 ALIQGLVLFQG----GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-174 |
6.23e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 28 IEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITIANRV------ISA---ITGSE-LRKARQEIGMifqhfNLLWSr 97
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKIsykpqyIKPdydGTVEDlLRSITDDLGS-----SYYKS- 435
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524434 98 tvreniefpleiagvdkakrrkrvdELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPE 174
Cdd:PRK13409 436 -------------------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-215 |
1.24e-05 |
|
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: 46.70 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 27 KIEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSGQITianrvisaitgSELRKAR--QEIGMIFqhfnllwSRTVRENIE 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-----------EDLKISYkpQYISPDY-------DGTVEEFLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 105 fpleiagvdkAKRRKRVD------ELIHLVGLEGRGDAYPSQLSGGQKQRVGIARALANNPQVLLCDEATSALDPE---- 174
Cdd:COG1245 424 ----------SANTDDFGssyyktEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrla 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446524434 175 TTDQIldllldinKRL----GLTIVLITHEMHVIRKICNRVAVME 215
Cdd:COG1245 494 VAKAI--------RRFaenrGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-224 |
2.32e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 139 SQLSGGQKQRVGIARALAN---NPQVLLCDEATSALDPETTDQILDLLLDINKrLGLTIVLITHEMHVIrKICNRVavme 215
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTH-QGHTVVIIEHNMHVV-KVADYV---- 881
|
....*....
gi 446524434 216 rgkiVETGP 224
Cdd:PRK00635 882 ----LELGP 886
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
98-172 |
2.56e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.99 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 98 TVRENIEF------PLEiagVDKAKRRKRVDELIHLVGLEGRGDA---YP--SQLSGGQKQRVGIARALANNPQVLLCDE 166
Cdd:PLN03140 969 TVRESLIYsaflrlPKE---VSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
....*.
gi 446524434 167 ATSALD 172
Cdd:PLN03140 1046 PTSGLD 1051
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
104-249 |
3.38e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.61 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 104 EFPLEIAGVDKAKRRKRVDELIhlvglegRGdaypsqLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLL 183
Cdd:PLN03140 313 DYTLKILGLDICKDTIVGDEMI-------RG------ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 184 LDINKRLGLTIVlitheMHVIR------KICNRVAVMERGKIVETGP---VLDV-----FRNPKQDITKRFVQQLTDSED 249
Cdd:PLN03140 380 QQIVHLTEATVL-----MSLLQpapetfDLFDDIILLSEGQIVYQGPrdhILEFfescgFKCPERKGTADFLQEVTSKKD 454
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-173 |
6.63e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 2 ILLENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIRLFNQlEKPT--SGQITIANRviSAITGSELRK 79
Cdd:PRK10938 261 IVLNNGVVSY----NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgySNDLTLFGR--RRGSGETIWD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 80 ARQEIGMIFQHFNLLW--SRTVRENI--EFPLEIaGVDKA---KRRKRVDELIHLVGLEGR-GDAYPSQLSGGQKQRVGI 151
Cdd:PRK10938 334 IKKHIGYVSSSLHLDYrvSTSVRNVIlsGFFDSI-GIYQAvsdRQQKLAQQWLDILGIDKRtADAPFHSLSWGQQRLALI 412
|
170 180
....*....|....*....|..
gi 446524434 152 ARALANNPQVLLCDEATSALDP 173
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDP 434
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
141-205 |
8.57e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 43.37 E-value: 8.57e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 141 LSGGQKQRVGIARAL---ANNPQVLLCDEATSALDPETTDQILDLLLDINKRlGLTIVLITHEMHVIR 205
Cdd:cd03271 170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTVVVIEHNLDVIK 236
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-205 |
2.65e-04 |
|
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: 42.69 E-value: 2.65e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446524434 141 LSGGQKQRVGIARAL---ANNPQVLLCDEATSALDPETTDQILDLLldinKRL---GLTIVLITHEMHVIR 205
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVL----QRLvdkGNTVVVIEHNLDVIK 896
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
33-199 |
4.57e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.76 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 33 IFGVIGYSGAGKSSLIR-----LFNQLEKPTSGQITIANRVISA--------ITGSELRKARQEiGMiFQHFNLLWSRTV 99
Cdd:COG0419 25 LNLIVGPNGAGKSTILEairyaLYGKARSRSKLRSDLINVGSEEasvelefeHGGKRYRIERRQ-GE-FAEFLEAKPSER 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 100 RENIEfplEIAGVDKAKR------------RKRVDELIHLVGLEGR------GDAYPSQLSGGQKQRVGIARALAnnpqv 161
Cdd:COG0419 103 KEALK---RLLGLEIYEElkerlkeleealESALEELAELQKLKQEilaqlsGLDPIETLSGGERLRLALADLLS----- 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 446524434 162 LLCDeaTSALDPETTDQILDLLLDinkrlgltIVLITH 199
Cdd:COG0419 175 LILD--FGSLDEERLERLLDALEE--------LAIITH 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
140-261 |
6.76e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 140 QLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDINKrlglTIVLITHEMHVIRKICNRVAVMERGKI 219
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSHAREFLNTVVTDILHLHGQKL 419
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446524434 220 VETGPVLDVFRNPKQDITKRFVQQLTDSEDTNETIESLIEKY 261
Cdd:PLN03073 420 VTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKF 461
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
140-199 |
1.21e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.88 E-value: 1.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524434 140 QLSGGQKQRVGIARALAN---NPQVLLC-DEATSALDPETTDQILDLLLDINKRLGLTIVlITH 199
Cdd:cd03227 77 QLSGGEKELSALALILALaslKPRPLYIlDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITH 139
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-215 |
1.30e-03 |
|
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: 39.09 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 28 IEKGEIFGVIGYSGAGKSSLIRLFNQLEKPTSgqitianrvisaitgselrkarqeigmifqhfnllwsrtvrENIEFPl 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNG-----------------------------------------DNDEWD- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 108 eiaGVDKAKRRKRVDelihlvglegrgdaypsqLSGGQKQRVGIARALANNPQVLLCDEATSALDPETTDQILDLLLDIN 187
Cdd:cd03222 60 ---GITPVYKPQYID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....*...
gi 446524434 188 KRLGLTIVLITHEMHVIRKICNRVAVME 215
Cdd:cd03222 119 EEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
139-183 |
5.07e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 35.67 E-value: 5.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446524434 139 SQLSGGQKQ-------------RVGIARALANNPQVLLCDEATSALDPETTDQILDLL 183
Cdd:pfam13558 31 GGLSGGEKQllaylplaaalaaQYGSAEGRPPAPRLVFLDEAFAKLDEENIRTALELL 88
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-62 |
5.17e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.72 E-value: 5.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524434 4 LENVKKIYkaksGDVTAVDNANLKIEKGEIFGVIGYSGAGKSSLIR-LFNQLEkPTSGQI 62
Cdd:PRK15064 322 VENLTKGF----DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRtLVGELE-PDSGTV 376
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
140-207 |
6.70e-03 |
|
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: 37.20 E-value: 6.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524434 140 QLSGGQKQ------RVGIARALANNPQVLLCDEATSALDPETTD-QILDLLLDINKRLGLTIVLITHEMHVIRKI 207
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| |
