|
Name |
Accession |
Description |
Interval |
E-value |
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-338 |
0e+00 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 505.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAQsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPV-TALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQ 240
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 241 LVSHTTPVELPDRF-----KKNNKGVLLKILFADDSVEQPILSDVAQQFQVSVNILHGNIEYINDRALGHIIAQISYRDD 315
Cdd:COG1135 240 FLPTVLNDELPEELlarlrEAAGGGRLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDDA 319
|
330 340
....*....|....*....|...
gi 504513067 316 paaeNLAAAIAYIRQNTFGVEVI 338
Cdd:COG1135 320 ----AIDAALAYLREQGVVVEVL 338
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-339 |
5.47e-157 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 443.09 E-value: 5.47e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAQSrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIH-ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQ 240
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 241 LVSHTTPVELPDRFKKN-------NKGVLLKILFADDSVEQPILSDVAQQFQVSVNILHGNIEYINDRALGHIIAQISYR 313
Cdd:PRK11153 240 FIQSTLHLDLPEDYLARlqaepttGSGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGD 319
|
330 340
....*....|....*....|....*.
gi 504513067 314 DDpaaeNLAAAIAYIRQNTFGVEVIN 339
Cdd:PRK11153 320 PG----DIQAAIAYLQEHGVKVEVLG 341
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-234 |
5.83e-130 |
|
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: 370.37 E-value: 5.83e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKtAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:cd03258 1 MIELKNVSKVFGDTG-GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQ 234
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
1-338 |
3.64e-104 |
|
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: 309.12 E-value: 3.64e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGkTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:TIGR02314 1 MIKLSNITKVFHQG-TKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:TIGR02314 80 ARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQ 240
Cdd:TIGR02314 160 KVLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 241 LVSHTTPVELPDRFKKNNKGV-------LLKILFADDSVEQPILSDVAQQFQVSVNILHGNIEYINDRALGHIIAQISYR 313
Cdd:TIGR02314 240 FIRSTLHLSIPEDYQERLQATpfadsvpMVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMHGT 319
|
330 340
....*....|....*....|....*
gi 504513067 314 DDpaaeNLAAAIAYIRQNTFGVEVI 338
Cdd:TIGR02314 320 QQ----DTQAAIAYLQEHNVKVEVL 340
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-243 |
8.05e-99 |
|
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: 301.05 E-value: 8.05e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQH----FNLMHTrnVYDNVAFSLRAAGK-SKADIAERVPEILALVGLQ-DKGTAYPAQLSGGQKQRVGIAR 154
Cdd:COG1123 340 LRRRVQMVFQDpyssLNPRMT--VGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 155 AIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQ 234
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
....*....
gi 504513067 235 HAYTKQLVS 243
Cdd:COG1123 498 HPYTRALLA 506
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-225 |
3.00e-94 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 279.24 E-value: 3.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAqsraVNNVNLTIQQGE-VFgIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELR 79
Cdd:COG2884 1 MIRFENVSKRYPGGREA----LSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 80 QHRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANH 159
Cdd:COG2884 76 YLRRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGE 225
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-223 |
4.21e-89 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 266.52 E-value: 4.21e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAQsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEV-TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HR-QRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANH 159
Cdd:COG1136 83 LRrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSvIKSICQRMAVMTGGNIVEE 223
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLRDGRIVSD 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-244 |
5.29e-89 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 266.47 E-value: 5.29e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpaGKTaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLIsNASGRELRQ 80
Cdd:COG1126 1 MIEIENLHKSF--GDL---EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVAFSLR-AAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANH 159
Cdd:COG1126 75 LRRKVGMVFQQFNLFPHLTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTK 239
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTR 233
|
....*
gi 504513067 240 QLVSH 244
Cdd:COG1126 234 AFLSK 238
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-243 |
5.77e-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: 266.92 E-value: 5.77e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTaQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTI-NLLQRP--TEGRVFLGDTLISNASGRE 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRG-VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPPgiTSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 78 LRQHR-QRIGMIFQH----FNLMHTrnVYDNVAFSLRAAGK-SKADIAERVPEILALVGLQDKGT---AYPAQLSGGQKQ 148
Cdd:COG0444 80 LRKIRgREIQMIFQDpmtsLNPVMT--VGDQIAEPLRIHGGlSKAEARERAIELLERVGLPDPERrldRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 149 RVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFT 228
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237
|
250
....*....|....*
gi 504513067 229 IFSAPQHAYTKQLVS 243
Cdd:COG0444 238 LFENPRHPYTRALLS 252
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-242 |
3.30e-84 |
|
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: 254.73 E-value: 3.30e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAQsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISnasGRELRQ 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRV-PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT---RRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQH----FNLMHTrnVYDNVAFSLRAAGKskADIAERVPEILALVGLqDKGTA--YPAQLSGGQKQRVGIAR 154
Cdd:COG1124 77 FRRRVQMVFQDpyasLHPRHT--VDRILAEPLRIHGL--PDREERIAELLEQVGL-PPSFLdrYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 155 AIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQ 234
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
....*...
gi 504513067 235 HAYTKQLV 242
Cdd:COG1124 232 HPYTRELL 239
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-253 |
4.53e-82 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 252.35 E-value: 4.53e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFP------AGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASG 75
Cdd:COG4608 8 LEVRDLKKHFPvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 76 RELRQHRQRIGMIFQH----FNLMHTrnVYDNVAFSLRAAG-KSKADIAERVPEILALVGL-QDKGTAYPAQLSGGQKQR 149
Cdd:COG4608 88 RELRPLRRRMQMVFQDpyasLNPRMT--VGDIIAEPLRIHGlASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 150 VGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTI 229
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDEL 245
|
250 260
....*....|....*....|....
gi 504513067 230 FSAPQHAYTKQLVShTTPVELPDR 253
Cdd:COG4608 246 YARPLHPYTQALLS-AVPVPDPER 268
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-224 |
5.13e-82 |
|
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: 248.74 E-value: 5.13e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpaGktaqSRAV-NNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELR 79
Cdd:COG1127 5 MIEVRNLTKSF--G----DRVVlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 80 QHRQRIGMIFQH---FNLMhtrNVYDNVAFSLRAAGK-SKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARA 155
Cdd:COG1127 79 ELRRRIGMLFQGgalFDSL---TVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 156 IANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-220 |
3.03e-81 |
|
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: 246.25 E-value: 3.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTaQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH 81
Cdd:cd03255 1 IELKNLSKTYGGGGE-KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 R-QRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:cd03255 80 RrRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSvIKSICQRMAVMTGGNI 220
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-224 |
1.50e-80 |
|
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: 244.72 E-value: 1.50e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAQsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSV-KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQH----FNLMHTrnVYDNVAFSLRAAGK--SKADIAERVPEILALVGLQDK-GTAYPAQLSGGQKQRVGIA 153
Cdd:cd03257 80 RRKEIQMVFQDpmssLNPRMT--IGEQIAEPLRIHGKlsKKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513067 154 RAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-237 |
4.25e-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: 242.70 E-value: 4.25e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNasgreLRQ 80
Cdd:COG3842 5 ALELENVSKRY-----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG-----LPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:COG3842 75 EKRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAY 237
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRF 231
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-221 |
4.26e-77 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 236.49 E-value: 4.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:COG3638 2 MLELRNLSKRYPGGTPA----LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVAF-------SLRAAGK--SKADIaERVPEILALVGLQDKGTAYPAQLSGGQKQRVG 151
Cdd:COG3638 78 LRRRIGMIFQQFNLVPRLSVLTNVLAgrlgrtsTWRSLLGlfPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 152 IARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIV 221
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-234 |
5.37e-77 |
|
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: 235.69 E-value: 5.37e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKtaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQh 81
Cdd:COG1122 1 IELENLSFSYPGGT----PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqRIGMIFQH-FNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:COG1122 76 --KVGLVFQNpDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQ 234
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-224 |
6.51e-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: 230.47 E-value: 6.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpagktaQSRAV-NNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:cd03261 1 IELRGLTKSF------GGRTVlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGK-SKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANH 159
Cdd:cd03261 75 LRRRMGMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-224 |
9.51e-75 |
|
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: 229.33 E-value: 9.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNasgreLRQH 81
Cdd:cd03259 1 LELKGLSKTY-----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-----VPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPE 161
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-243 |
6.74e-74 |
|
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: 237.28 E-value: 6.74e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGK------TAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTI-NLLqrPTEGRVFLGDTLISNAS 74
Cdd:COG4172 276 LEARDLKVWFPIKRglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALlRLI--PSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 75 GRELRQHRQRIGMIFQ----HFNLMHTrnVYDNVAFSLRA--AGKSKADIAERVPEILALVGLqDKGTA--YPAQLSGGQ 146
Cdd:COG4172 354 RRALRPLRRRMQVVFQdpfgSLSPRMT--VGQIIAEGLRVhgPGLSAAERRARVAEALEEVGL-DPAARhrYPHEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 147 KQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEV 226
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPT 510
|
250
....*....|....*..
gi 504513067 227 FTIFSAPQHAYTKQLVS 243
Cdd:COG4172 511 EQVFDAPQHPYTRALLA 527
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-223 |
3.98e-73 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 226.89 E-value: 3.98e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAQsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGdtlisnasGRELRQ 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGV-TALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD--------GKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHemSVIKSI--CQRMAVMTG--GNIVEE 223
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTH--DVDEAVflADRVVVLSArpGRIVEE 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-224 |
5.35e-73 |
|
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: 225.91 E-value: 5.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKtaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH 81
Cdd:cd03256 1 IEVENLSKTYPNGK----KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQHFNLMHTRNVYDNV---AFSLRAAGKS------KADIaERVPEILALVGLQDKGTAYPAQLSGGQKQRVGI 152
Cdd:cd03256 77 RRQIGMIFQQFNLIERLSVLENVlsgRLGRRSTWRSlfglfpKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513067 153 ARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDG 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-252 |
2.80e-72 |
|
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: 233.04 E-value: 2.80e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAQsRAVNNVNLTIQQGEVFGIVGTSGAGKS-TLLRTINLLQRP---TEGRVFLGDTLISNASGR 76
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTV-EAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 77 ELRQHR-QRIGMIFQH----FNLMHTrnVYDNVAFSLRA-AGKSKADIAERVPEILALVGLQD---KGTAYPAQLSGGQK 147
Cdd:COG4172 85 ELRRIRgNRIAMIFQEpmtsLNPLHT--IGKQIAEVLRLhRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 148 QRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVF 227
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTA 242
|
250 260
....*....|....*....|....*...
gi 504513067 228 TIFSAPQHAYTKQLVS---HTTPVELPD 252
Cdd:COG4172 243 ELFAAPQHPYTRKLLAaepRGDPRPVPP 270
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
21-220 |
6.02e-72 |
|
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: 222.40 E-value: 6.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 21 AVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLIsNASGRELRQHRQRIGMIFQHFNLMHTRNV 100
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQKVGMVFQQFNLFPHLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 101 YDNVAFSLRAA-GKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSAS 179
Cdd:cd03262 94 LENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504513067 180 ILALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGGNI 220
Cdd:cd03262 174 VLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-242 |
4.45e-70 |
|
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: 219.44 E-value: 4.45e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 15 KTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ-HRQRIGMIFQHFN 93
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElRRKKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 94 LMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALD 173
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513067 174 ----LETSASILALLKSinvrLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQLV 242
Cdd:cd03294 193 plirREMQDELLRLQAE----LQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-234 |
1.37e-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: 225.55 E-value: 1.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPT---EGRVFLGDTLISNASGRE 77
Cdd:COG1123 4 LLEVRDLSVRYPGGDV---PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 78 LRQhrqRIGMIFQhfNLMHTRN---VYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIAR 154
Cdd:COG1123 81 RGR---RIGMVFQ--DPMTQLNpvtVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 155 AIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQ 234
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-226 |
4.92e-69 |
|
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: 215.03 E-value: 4.92e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAQsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGdtlisnasGRELRQH 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAV-TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD--------GEPVTGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPE 161
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTG--GNIVEEGEV 226
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVEV 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-224 |
7.59e-69 |
|
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: 215.24 E-value: 7.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQA----LKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVaFSLRAAGK----------SKADIaERVPEILALVGLQDKGTAYPAQLSGGQKQRV 150
Cdd:TIGR02315 77 LRRRIGMIFQHYNLIERLTVLENV-LHGRLGYKptwrsllgrfSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513067 151 GIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDG 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-234 |
1.25e-67 |
|
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: 212.10 E-value: 1.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNasgreLRQH 81
Cdd:cd03300 1 IELENVSKFY-----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN-----LPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPE 161
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQ 234
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-205 |
3.43e-67 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 210.18 E-value: 3.43e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGktaqSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:TIGR02673 1 MIEFHNVSKAYPGG----VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:TIGR02673 77 LRRRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVI 205
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLN-KRGTTVIVATHDLSLV 200
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-218 |
2.25e-66 |
|
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: 206.65 E-value: 2.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLIsNASGRELRQH 81
Cdd:cd03229 1 LELKNVSKRY-----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL-TDLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQHFNLMHTRNVYDNVAFSlraagkskadiaervpeilalvglqdkgtaypaqLSGGQKQRVGIARAIANHPE 161
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGG 218
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-226 |
1.61e-65 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 206.45 E-value: 1.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpaGKTaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLIsnasGRELRQH 81
Cdd:COG1131 1 IEVRGLTKRY--GDK---TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPE 161
Cdd:COG1131 72 RRRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEV 226
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELA-AEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-242 |
3.92e-64 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 206.92 E-value: 3.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPagktaQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGD-TLISNASGRElrq 80
Cdd:COG1118 3 IEVRNISKRFG-----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrDLFTNLPPRE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 hRqRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:COG1118 75 -R-RVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQ 240
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVAR 232
|
..
gi 504513067 241 LV 242
Cdd:COG1118 233 FL 234
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-218 |
5.63e-64 |
|
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: 201.93 E-value: 5.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 3 RLENVSVDFPAGKTAqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQHr 82
Cdd:cd03225 1 ELKNLSFSYPDGARP---ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 83 qrIGMIFQHFN---LMHTrnVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANH 159
Cdd:cd03225 77 --VGLVFQNPDdqfFGPT--VEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGG 218
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-220 |
6.06e-64 |
|
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: 201.87 E-value: 6.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH 81
Cdd:cd03292 1 IEFINVTKTYPNGTAA----LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPE 161
Cdd:cd03292 77 RRKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNI 220
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-234 |
2.14e-63 |
|
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: 202.68 E-value: 2.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH 81
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQH-----FNlmhtRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDK-GTAYPAQLSGGQKQRVGIARA 155
Cdd:TIGR04521 81 RKKVGLVFQFpehqlFE----ETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 156 IANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQ 234
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-237 |
5.27e-63 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 203.77 E-value: 5.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpaGKTaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASgrelRQ 80
Cdd:COG3839 3 SLELENVSKSY--GGV---EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP----PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRqRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:COG3839 74 DR-NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHE----MsvikSICQRMAVMTGGNIVEEGEVFTIFSAPQHA 236
Cdd:COG3839 153 KVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaM----TLADRIAVMNDGRIQQVGTPEELYDRPANL 228
|
.
gi 504513067 237 Y 237
Cdd:COG3839 229 F 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-243 |
2.71e-62 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 198.82 E-value: 2.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLIS-----NASG 75
Cdd:PRK11264 3 AIEVKNLVKKF-HGQTV----LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtarslSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 76 RELRQHRQRIGMIFQHFNLMHTRNVYDNVAFS-LRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIAR 154
Cdd:PRK11264 78 GLIRQLRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 155 AIANHPEVLLCDEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQ 234
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
....*....
gi 504513067 235 HAYTKQLVS 243
Cdd:PRK11264 237 QPRTRQFLE 245
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-226 |
2.22e-61 |
|
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: 195.86 E-value: 2.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLL-----QRPTEGRVFLGDTLIsNASGR 76
Cdd:cd03260 1 IELRDLNVYY-----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDI-YDLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 77 ELRQHRQRIGMIFQHFNLMHTrNVYDNVAFSLRAAG-KSKADIAERVPEILALVGLQD--KGTAYPAQLSGGQKQRVGIA 153
Cdd:cd03260 75 DVLELRRRVGMVFQKPNPFPG-SIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513067 154 RAIANHPEVLLCDEPTSALDLETSASILALLKSINVRlgITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEV 226
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-242 |
8.87e-61 |
|
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: 194.83 E-value: 8.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQh 81
Cdd:cd03295 1 IEFENVTKRYGGGKKA----VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTA--YPAQLSGGQKQRVGIARAIANH 159
Cdd:cd03295 76 --KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFAdrYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTK 239
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
...
gi 504513067 240 QLV 242
Cdd:cd03295 234 EFV 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-244 |
9.92e-60 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 191.84 E-value: 9.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVfLGDTLISNASGRELRQ 80
Cdd:PRK09493 1 MIEFKNVSKHF-----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDL-IVDGLKVNDPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVAFS-LRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANH 159
Cdd:PRK09493 75 IRQEAGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTK 239
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQ 233
|
....*
gi 504513067 240 QLVSH 244
Cdd:PRK09493 234 EFLQH 238
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-243 |
4.68e-58 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 188.32 E-value: 4.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpaGKTaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLL------QRpTEGRVFLGDTLIsNASG 75
Cdd:COG1117 12 IEVRNLNVYY--GDK---QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipgAR-VEGEILLDGEDI-YDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 76 RELRQHRQRIGMIFQHFNL--MhtrNVYDNVAFSLRAAG-KSKADIAERVPEILALVG--------LQDKGTAypaqLSG 144
Cdd:COG1117 85 VDVVELRRRVGMVFQKPNPfpK---SIYDNVAYGLRLHGiKSKSELDEIVEESLRKAAlwdevkdrLKKSALG----LSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 145 GQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLgiTIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFG 235
|
250
....*....|....*....
gi 504513067 225 EVFTIFSAPQHAYTKQLVS 243
Cdd:COG1117 236 PTEQIFTNPKDKRTEDYIT 254
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-237 |
4.97e-58 |
|
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: 187.55 E-value: 4.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPagktaQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDtliSNASGRELRQh 81
Cdd:cd03296 3 IEVRNVSKRFG-----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVPVQE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQrIGMIFQHFNLMHTRNVYDNVAFSLR----AAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIA 157
Cdd:cd03296 74 RN-VGFVFQHYALFRHMTVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 158 NHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAY 237
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
25-244 |
5.16e-58 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 188.09 E-value: 5.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 25 VNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGD---TLISNASG-------RELRQHRQRIGMIFQHFNL 94
Cdd:COG4598 27 VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeiRLKPDRDGelvpadrRQLQRIRTRLGMVFQSFNL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 95 MHTRNVYDNVAFS-LRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALD 173
Cdd:COG4598 107 WSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513067 174 LETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQLVSH 244
Cdd:COG4598 187 PELVGEVLKVMRDL-AEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-263 |
4.74e-57 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 187.99 E-value: 4.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 20 RAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRV-FLGDTLIsNASGRELRQHRQRIGMIFQH--FNLMH 96
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLGKDLL-GMKDDEWRAVRSDIQMIFQDplASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 97 TRNVYDNVAFSLRA--AGKSKADIAERVPEILALVGL-QDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALD 173
Cdd:PRK15079 114 RMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 174 LETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQLVShttPVELPDR 253
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMS---AVPIPDP 270
|
250
....*....|
gi 504513067 254 FKKNNKGVLL 263
Cdd:PRK15079 271 DLERNKTIQL 280
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-223 |
1.48e-56 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 183.15 E-value: 1.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKtaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGR----QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:PRK10908 77 LRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEE 223
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-244 |
8.86e-56 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 181.75 E-value: 8.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDT---LISNASGREL 78
Cdd:COG4161 3 IQLKNINCFY-----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdFSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQHRQRIGMIFQHFNLMHTRNVYDN-VAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIA 157
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 158 NHPEVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVfTIFSAPQHAY 237
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEA 235
|
....*..
gi 504513067 238 TKQLVSH 244
Cdd:COG4161 236 FAHYLSH 242
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-244 |
6.13e-55 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 179.82 E-value: 6.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAgktaqSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDT---LISNASGREL 78
Cdd:PRK11124 3 IQLNGINCFYGA-----HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQHRQRIGMIFQHFNLMHTRNVYDN-VAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIA 157
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 158 NHPEVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVfTIFSAPQHAY 237
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQTEA 235
|
....*..
gi 504513067 238 TKQLVSH 244
Cdd:PRK11124 236 FKNYLSH 242
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-223 |
1.77e-54 |
|
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: 178.01 E-value: 1.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGkTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:COG4181 8 IIELRGLTKTVGTG-AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HR-QRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKAdiAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANH 159
Cdd:COG4181 87 LRaRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDA--RARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSiCQRMAVMTGGNIVEE 223
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-228 |
6.65e-54 |
|
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: 177.16 E-value: 6.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPagktaQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELrq 80
Cdd:COG1120 1 MLEAENLSVGYG-----GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 hRQRIGMIFQH----FNLmhtrNVYDNVAFSLRA-----AGKSKADIaERVPEILALVGLQDKGTAYPAQLSGGQKQRVG 151
Cdd:COG1120 74 -ARRIAYVPQEppapFGL----TVRELVALGRYPhlglfGRPSAEDR-EAVEEALERTGLEHLADRPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 152 IARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG---EVFT 228
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGppeEVLT 227
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-228 |
7.30e-54 |
|
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: 177.62 E-value: 7.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASgrELRQH 81
Cdd:TIGR04520 1 IEVENVSFSYPESEK---PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEE--NLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQhfnlmhtrN---------VYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGI 152
Cdd:TIGR04520 76 RKKVGMVFQ--------NpdnqfvgatVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 153 ARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMS-VIKSicQRMAVMTGGNIVEEG---EVFT 228
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEeAVLA--DRVIVMNKGKIVAEGtprEIFS 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-224 |
1.95e-53 |
|
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: 176.38 E-value: 1.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpaGKTaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRq 80
Cdd:COG0411 4 LLEVRGLTKRF--GGL---VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 hRQRIGMIFQHFNLMHTRNVYDNVA---------------FSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGG 145
Cdd:COG0411 78 -RLGIARTFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 146 QKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-200 |
1.98e-53 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 176.59 E-value: 1.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAQsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRElrq 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQ-PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 hrqriGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:COG4525 79 -----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISH 200
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-224 |
3.54e-53 |
|
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: 173.98 E-value: 3.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPaGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRElrqh 81
Cdd:cd03301 1 VELENVTKRFG-NVTA----LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPE 161
Cdd:cd03301 72 -RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-224 |
5.26e-52 |
|
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: 171.85 E-value: 5.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 20 RAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRqhRQRIGMIFQHFNLMHTRN 99
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--RLGIGRTFQIPRLFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 100 VYDNV----------AFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPT 169
Cdd:cd03219 92 VLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 170 SALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03219 172 AGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-224 |
1.85e-51 |
|
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: 169.78 E-value: 1.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 32 GEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNAS-GRELRQHRQRIGMIFQHFNLMHTRNVYDNVAFSLRa 110
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 111 aGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVR 190
Cdd:cd03297 102 -RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKN 180
|
170 180 190
....*....|....*....|....*....|....
gi 504513067 191 LGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03297 181 LNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-228 |
2.08e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 170.65 E-value: 2.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPagktaQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGdtlisnasGRELRQ 80
Cdd:COG1121 6 AIELENLTVSYG-----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLF--------GKPPRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLmhTRN----VYDNVAFSLRAAGK-----SKADiAERVPEILALVGLQDKGTAYPAQLSGGQKQRVG 151
Cdd:COG1121 73 ARRRIGYVPQRAEV--DWDfpitVRDVVLMGRYGRRGlfrrpSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 152 IARAIANHPEVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGnIVEEG---EVFT 228
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGppeEVLT 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-220 |
2.76e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 169.23 E-value: 2.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVdfpagKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQh 81
Cdd:COG4619 1 LELEGLSF-----RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqRIGMIFQHFNLMHTRnVYDNVAFSLRAAGKSKADiaERVPEILALVGLQDKGTAYPA-QLSGGQKQRVGIARAIANHP 160
Cdd:COG4619 75 --QVAYVPQEPALWGGT-VRDNLPFPFQLRERKFDR--ERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNI 220
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-237 |
8.14e-51 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 171.52 E-value: 8.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 37 IVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASgrelrQHRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKA 116
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP-----PHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 117 DIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIV 196
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504513067 197 LISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAY 237
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-256 |
1.39e-50 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 170.92 E-value: 1.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 15 KTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQHRQRIGMIFQhfNL 94
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQ--NP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 95 MHTRNVYDNVAFSLRA-----AGKSKADIAERVPEILALVGLQ-DKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEP 168
Cdd:PRK11308 102 YGSLNPRKKVGQILEEpllinTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 169 TSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQLVShTTPV 248
Cdd:PRK11308 182 VSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLS-ATPR 260
|
....*...
gi 504513067 249 ELPDRFKK 256
Cdd:PRK11308 261 LNPDDRRE 268
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-220 |
2.80e-50 |
|
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: 165.26 E-value: 2.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpaGKTaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLIsnasGRELRQH 81
Cdd:cd03230 1 IEVRNLSKRY--GKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQHFNLMHTRNVYDNVafslraagkskadiaervpeilalvglqdkgtaypaQLSGGQKQRVGIARAIANHPE 161
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNI 220
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-242 |
2.47e-49 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 168.97 E-value: 2.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGrelrQH 81
Cdd:PRK09452 15 VELRGISKSF-DGKEV----ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA----EN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQrIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPE 161
Cdd:PRK09452 86 RH-VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQL 241
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARF 244
|
.
gi 504513067 242 V 242
Cdd:PRK09452 245 I 245
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-236 |
4.54e-49 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 164.16 E-value: 4.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSV---DFPAgktaqsravnNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISnasgrE 77
Cdd:COG3840 1 MLRLDDLTYrygDFPL----------RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT-----A 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 78 LRQHRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIA 157
Cdd:COG3840 66 LPPAERPVSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 158 NHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHA 236
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-243 |
6.67e-49 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 164.76 E-value: 6.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 18 QSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGD---TLISNASG-------RELRQHRQRIGM 87
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtiNLVRDKDGqlkvadkNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 88 IFQHFNLMHTRNVYDNVAFS-LRAAGKSKADIAERVPEILALVGLQDKGTA-YPAQLSGGQKQRVGIARAIANHPEVLLC 165
Cdd:PRK10619 97 VFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513067 166 DEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQLVS 243
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-233 |
1.24e-48 |
|
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: 166.81 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGD-TLISNASGRELRQHRQRIGMIFQHFNLMHTRNVYD 102
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGeVLQDSARGIFLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 103 NVAFSLRAAGKSKAdiAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILA 182
Cdd:COG4148 97 NLLYGRKRAPRAER--RISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504513067 183 LLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAP 233
Cdd:COG4148 175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
23-221 |
1.87e-48 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 162.11 E-value: 1.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 23 NNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRV-FLGDTLiSNASGRELRQHRQRIGMIFQHFNLMHTRNVY 101
Cdd:TIGR02982 22 FDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLkVLGQEL-HGASKKQLVQLRRRIGYIFQAHNLLGFLTAR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 102 DNVAFSLR-AAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASI 180
Cdd:TIGR02982 101 QNVQMALElQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDV 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504513067 181 LALLKSINVRLGITIVLISHEmSVIKSICQRMAVMTGGNIV 221
Cdd:TIGR02982 181 VELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-243 |
2.67e-48 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 169.89 E-value: 2.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGK------TAQSRAVNNVNLTIQQGEVFGIVGTSGAGKST----LLRTINllqrpTEGRVFLGDTLI 70
Cdd:PRK15134 275 LLDVEQLQVAFPIRKgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 71 SNASGRELRQHRQRIGMIFQHFN--LMHTRNVYDNVAFSLRAAGK--SKADIAERVPEILALVGLqDKGTA--YPAQLSG 144
Cdd:PRK15134 350 HNLNRRQLLPVRHRIQVVFQDPNssLNPRLNVLQIIEEGLRVHQPtlSAAQREQQVIAVMEEVGL-DPETRhrYPAEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 145 GQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
250
....*....|....*....
gi 504513067 225 EVFTIFSAPQHAYTKQLVS 243
Cdd:PRK15134 509 DCERVFAAPQQEYTRQLLA 527
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
4.44e-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: 171.94 E-value: 4.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH 81
Cdd:COG2274 474 IELENVSFRYPGDSPP---VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqrIGMIFQHFNLMHtRNVYDNVAFslraaGKSKADIaERVPEILALVGLQDKGTAYP-----------AQLSGGQKQRV 150
Cdd:COG2274 551 ---IGVVLQDVFLFS-GTIRENITL-----GDPDATD-EEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513067 151 GIARAIANHPEVLLCDEPTSALDLETSASILALLKSInvRLGITIVLISHEMSVIKsICQRMAVMTGGNIVEEG 224
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-234 |
1.73e-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: 160.19 E-value: 1.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNasgreLRQHRQRIGMIFQHFNLMHTRNVYDN 103
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN-----LPPEKRDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 104 VAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILAL 183
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504513067 184 LKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQ 234
Cdd:cd03299 172 LKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-224 |
4.95e-47 |
|
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: 158.13 E-value: 4.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGktaqsRAVNNVNLTIQQGeVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNaSGRELRQH 81
Cdd:cd03264 1 LQLENLTKRYGKK-----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqrIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPE 161
Cdd:cd03264 74 ---IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 162 VLLCDEPTSALDLETSASILALLksinVRLGIT-IVLIS-HEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLL----SELGEDrIVILStHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-224 |
7.39e-47 |
|
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: 156.83 E-value: 7.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 3 RLENVSVDFPagktaQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQHr 82
Cdd:cd03214 1 EVENLSVGYG-----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 83 qrigmifqhfnlmhtrnvydnVAFslraagkskadiaerVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEV 162
Cdd:cd03214 75 ---------------------IAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513067 163 LLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-227 |
9.48e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 159.83 E-value: 9.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGReLRQH 81
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQH--FNLMHtRNVYDNVAFSLRAAGKSKADIAERVPEILALVGL-----QDKGtayPAQLSGGQKQRVGIAR 154
Cdd:PRK13637 82 RKKVGLVFQYpeYQLFE-ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyedyKDKS---PFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 155 AIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG---EVF 227
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGtprEVF 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-170 |
1.49e-46 |
|
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: 154.73 E-value: 1.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLIsnaSGRELRQHRQRIGMIFQHFNLMHTRNVY 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL---TDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513067 102 DNVAFSLRAAGKSKADIAERVPEILALVGLQDKG----TAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTS 170
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-242 |
2.15e-46 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 161.54 E-value: 2.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 21 AVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLgdtlisnaSGRELRQ---HRQRIGMIFQHFNLMHT 97
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML--------DGVDLSHvppYQRPINMMFQSYALFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 98 RNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETS 177
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 178 ASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQLV 242
Cdd:PRK11607 186 DRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-226 |
3.01e-46 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 157.93 E-value: 3.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 14 GKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQHRQRIGMIFQH-- 91
Cdd:PRK10419 20 GKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDsi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 92 --FNLMHTrnVYDNVAFSLR-AAGKSKADIAERVPEILALVGLQDK-GTAYPAQLSGGQKQRVGIARAIANHPEVLLCDE 167
Cdd:PRK10419 100 saVNPRKT--VREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 168 PTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEV 226
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPV 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-226 |
3.82e-46 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 156.94 E-value: 3.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpaGKtaqSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTlisnASGRELRQ 80
Cdd:COG4555 1 MIEVENLSKKY--GK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE----DVRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:COG4555 72 ARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEV 226
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSL 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-231 |
4.68e-46 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 157.87 E-value: 4.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPagkTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQh 81
Cdd:PRK13635 6 IRVEHISFRYP---DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqRIGMIFQH-FNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:PRK13635 82 --QVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSiCQRMAVMTGGNIVEEGEVFTIFS 231
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-211 |
1.24e-45 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 154.31 E-value: 1.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 4 LENVSvdfpagKTAQSRAV-NNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ-H 81
Cdd:TIGR03608 1 LKNIS------KKFGDKVIlDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKfR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPE 161
Cdd:TIGR03608 75 REKLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSvIKSICQR 211
Cdd:TIGR03608 155 LILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPE-VAKQADR 202
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-241 |
4.19e-45 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 156.83 E-value: 4.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKtAQSRAVNNVNLTIQQGEVFGIVGTSGAGKS-TLLRTINLLQRPteGRVfLGDTLISNasGREL- 78
Cdd:PRK11022 3 LLNVDKLSVHFGDES-APFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRV-MAEKLEFN--GQDLq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 ----RQHRQRIG----MIFQhfNLMHTRNVYDNVAFSLRAA-----GKSKADIAERVPEILALVGLQDKGT---AYPAQL 142
Cdd:PRK11022 77 riseKERRNLVGaevaMIFQ--DPMTSLNPCYTVGFQIMEAikvhqGGNKKTRRQRAIDLLNQVGIPDPASrldVYPHQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 143 SGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVE 222
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
250
....*....|....*....
gi 504513067 223 EGEVFTIFSAPQHAYTKQL 241
Cdd:PRK11022 235 TGKAHDIFRAPRHPYTQAL 253
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-218 |
4.34e-45 |
|
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: 151.77 E-value: 4.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKP---VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqrIGMIFQHFNLMHTrNVYDNVafslraagkskadiaervpeilalvglqdkgtaypaqLSGGQKQRVGIARAIANHPE 161
Cdd:cd03228 78 ---IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSInvRLGITIVLISHEMSVIKsICQRMAVMTGG 218
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-223 |
9.10e-45 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 153.05 E-value: 9.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 18 QSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRV-FLGDTL--ISNASGRELRQHRqrIGMIFQHFNL 94
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDViFNGQPMskLSSAAKAELRNQK--LGFIYQFHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 95 MHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDL 174
Cdd:PRK11629 99 LPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504513067 175 ETSASILALLKSINVRLGITIVLISHEMSVIKSIcQRMAVMTGGNIVEE 223
Cdd:PRK11629 179 RNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
18-224 |
1.57e-44 |
|
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: 152.14 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 18 QSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISnasgRELRQHRQRIGMIFQHFNLMHT 97
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRRRIGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 98 RNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETS 177
Cdd:cd03265 88 LTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504513067 178 ASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03265 168 AHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-224 |
2.44e-44 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 155.63 E-value: 2.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpaGKTaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRElrqh 81
Cdd:PRK10851 3 IEIANIKKSF--GRT---QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rQRIGMIFQHFNLMHTRNVYDNVAFSL----RAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIA 157
Cdd:PRK10851 74 -RKVGFVFQHYALFRHMTVFDNIAFGLtvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 158 NHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-220 |
2.88e-44 |
|
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: 151.15 E-value: 2.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 3 RLENVSVDFPagktaQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLgdtlisnaSGRELRQHR 82
Cdd:cd03235 1 EVEDLTVSYG-----GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV--------FGKPLEKER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 83 QRIGMIFQHFNLMHTR--NVYDNVAFSLRAAGK-----SKADiAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARA 155
Cdd:cd03235 68 KRIGYVPQRRSIDRDFpiSVRDVVLMGLYGHKGlfrrlSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 156 IANHPEVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNI 220
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-224 |
4.66e-44 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 159.17 E-value: 4.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLlrtINLLQR---PTEGRVFLGDTLISNASGREL 78
Cdd:COG1132 340 IEFENVSFSYPGDRPV----LKDISLTIPPGETVALVGPSGSGKSTL---VNLLLRfydPTSGRILIDGVDIRDLTLESL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQHrqrIGMIFQHFNLMHtRNVYDNVAFslraaGKSKADIAErVPEILALVGLQDKGTAYP-----------AQLSGGQK 147
Cdd:COG1132 413 RRQ---IGVVPQDTFLFS-GTIRENIRY-----GRPDATDEE-VEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 148 QRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKsiNVRLGITIVLISHEMSVIKSiCQRMAVMTGGNIVEEG 224
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALE--RLMKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
21-244 |
7.12e-44 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 151.53 E-value: 7.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 21 AVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASgrelRQHR-QRIGMIFQHFNlmHTRN 99
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD----YKYRcKHIRMIFQDPN--TSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 100 VYDNVAFSLRAAGK-----SKADIAERVPEILALVGL-QDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALD 173
Cdd:COG4167 102 PRLNIGQILEEPLRlntdlTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513067 174 LETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQLV-SH 244
Cdd:COG4167 182 MSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHEVTKRLIeSH 253
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-273 |
8.62e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 152.16 E-value: 8.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAQSR-AVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASgrELR 79
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTEKlALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE--NLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 80 QHRQRIGMIFQH-FNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIAN 158
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 159 HPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEM-SVIKSicQRMAVMTGGNIVEEGEVFTIFSapQHAY 237
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMeEAVEA--DRIIVMDSGKVVMEGTPKEIFK--EVEM 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 504513067 238 TKQL---VSHTTpvELPDRFKKNNKGVLLKILFADDSVE 273
Cdd:PRK13633 238 MKKIgldVPQVT--ELAYELKKEGVDIPSDILTIDEMVN 274
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
15-239 |
2.06e-43 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 154.04 E-value: 2.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 15 KTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ-HRQRIGMIFQHFN 93
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvRRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 94 LMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALD 173
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 174 LETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTK 239
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-241 |
7.81e-43 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 155.25 E-value: 7.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 4 LENVSVDFPAGKTaQSRAVNNVNLTIQQGEVFGIVGTSGAGKS-TLLRTINLLQRP----TEGRV-FLGDTLIsNASGRE 77
Cdd:PRK15134 8 IENLSVAFRQQQT-VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIrFHGESLL-HASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 78 LRQHR-QRIGMIFQH----FNLMHT--RNVYDnvAFSLRAAGKSKADIAERVpEILALVGLQDKG---TAYPAQLSGGQK 147
Cdd:PRK15134 86 LRGVRgNKIAMIFQEpmvsLNPLHTleKQLYE--VLSLHRGMRREAARGEIL-NCLDRVGIRQAAkrlTDYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 148 QRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVF 227
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
250
....*....|....
gi 504513067 228 TIFSAPQHAYTKQL 241
Cdd:PRK15134 243 TLFSAPTHPYTQKL 256
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
15-224 |
1.42e-42 |
|
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: 146.88 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 15 KTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISnasgRELRQHRQRIGMIFQHFNL 94
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAARQSLGYCPQFDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 95 MHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDL 174
Cdd:cd03263 87 FDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504513067 175 ETSASILALLKSinVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03263 167 ASRRAIWDLILE--VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-218 |
1.44e-42 |
|
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: 144.69 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 3 RLENVSVDFPAGKtaqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQhr 82
Cdd:cd00267 1 EIENLSFRYGGRT-----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 83 qRIGMIFQhfnlmhtrnvydnvafslraagkskadiaervpeilalvglqdkgtaypaqLSGGQKQRVGIARAIANHPEV 162
Cdd:cd00267 74 -RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 163 LLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGG 218
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
2-247 |
4.15e-42 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 148.90 E-value: 4.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRP----TEGRVFLGDTLISNASGRE 77
Cdd:COG4170 6 IRNLTIEIDTPQGRV---KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 78 LRQ-HRQRIGMIFQHFN--LMHTRNVYDNVAFSL---RAAGK---SKADIAERVPEILALVGLQDKG---TAYPAQLSGG 145
Cdd:COG4170 83 RRKiIGREIAMIFQEPSscLDPSAKIGDQLIEAIpswTFKGKwwqRFKWRKKRAIELLHRVGIKDHKdimNSYPHELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 146 QKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGE 225
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGP 242
|
250 260
....*....|....*....|..
gi 504513067 226 VFTIFSAPQHAYTKQLVsHTTP 247
Cdd:COG4170 243 TEQILKSPHHPYTKALL-RSMP 263
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-224 |
4.54e-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: 153.38 E-value: 4.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH 81
Cdd:COG4988 337 IELEDVSFSYPGGRPA----LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqrIGMIFQHFNLMHTrNVYDNVAFslraaGKSKADIAErVPEILALVGLQD------KGTAYP-----AQLSGGQKQRV 150
Cdd:COG4988 413 ---IAWVPQNPYLFAG-TIRENLRL-----GRPDASDEE-LEAALEAAGLDEfvaalpDGLDTPlgeggRGLSGGQAQRL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513067 151 GIARAIANHPEVLLCDEPTSALDLETSASILALLKSInvRLGITIVLISHEMSVIKsICQRMAVMTGGNIVEEG 224
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHRLALLA-QADRILVLDDGRIVEQG 553
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-241 |
1.03e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 146.70 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNA-SGRELRQ 80
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQhF--NLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGL-QDKGTAYPAQLSGGQKQRVGIARAIA 157
Cdd:PRK13634 83 LRKKVGIVFQ-FpeHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 158 NHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAY 237
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELE 241
|
....
gi 504513067 238 TKQL 241
Cdd:PRK13634 242 AIGL 245
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-241 |
1.17e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 146.43 E-value: 1.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNAS-GRELRQ 80
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSkNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQhF--NLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGL-QDKGTAYPAQLSGGQKQRVGIARAIA 157
Cdd:PRK13649 83 IRKKVGLVFQ-FpeSQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 158 NHPEVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAY 237
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFLE 240
|
....
gi 504513067 238 TKQL 241
Cdd:PRK13649 241 EKQL 244
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-233 |
2.09e-41 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 147.56 E-value: 2.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 4 LENVSVDFpaGKtaqSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASgrelRQHRQ 83
Cdd:PRK11432 9 LKNITKRF--GS---NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS----IQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 84 rIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVL 163
Cdd:PRK11432 80 -ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 164 LCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAP 233
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-202 |
3.08e-41 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 144.46 E-value: 3.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPaGKtaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRElrq 80
Cdd:PRK11248 1 MLQISHLYADYG-GK----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 hrqriGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:PRK11248 73 -----GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEM 202
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-234 |
4.63e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 144.84 E-value: 4.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGktaqSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFL-GDTLISNASGreLR 79
Cdd:PRK13639 1 ILETRDLKYSYPDG----TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIKYDKKS--LL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 80 QHRQRIGMIFQHF-NLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIAN 158
Cdd:PRK13639 75 EVRKTVGIVFQNPdDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 159 HPEVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQ 234
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-224 |
1.12e-40 |
|
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: 141.96 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH 81
Cdd:cd03245 3 IEFRNVSFSYPNQEIP---ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqrIGMIFQHFNLMHTrNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYP-----AQLSGGQKQRVGIARAI 156
Cdd:cd03245 80 ---IGYVPQDVTLFYG-TLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQigergRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513067 157 ANHPEVLLCDEPTSALDLETSASILALLKsiNVRLGITIVLISHEMSVIkSICQRMAVMTGGNIVEEG 224
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLR--QLLGDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-243 |
2.06e-40 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 142.53 E-value: 2.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDfpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKS-TLLRTINLLQ---RPTEGRVFLGDTLISNASGRE 77
Cdd:PRK10418 5 IELRNIALQ------AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKPVAPCALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 78 lrqhrQRIGMIFQH----FNLMHTrnVYDNVAFSLRAAGKSKADiaERVPEILALVGLQDKGT---AYPAQLSGGQKQRV 150
Cdd:PRK10418 79 -----RKIATIMQNprsaFNPLHT--MHTHARETCLALGKPADD--ATLTAALEAVGLENAARvlkLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 151 GIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIF 230
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
250
....*....|...
gi 504513067 231 SAPQHAYTKQLVS 243
Cdd:PRK10418 230 NAPKHAVTRSLVS 242
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-243 |
4.67e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 141.20 E-value: 4.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTIN-LLQRPTEGRVfLGDTLISNAS--GREL 78
Cdd:PRK14247 4 IEIRDLKVSF-----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNrLIELYPEARV-SGEVYLDGQDifKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQHRQRIGMIFQHFNLMHTRNVYDNVAFSLR--AAGKSKADIAERVPEILALVGL----QDKGTAYPAQLSGGQKQRVGI 152
Cdd:PRK14247 78 IELRRRVQMVFQIPNPIPNLSIFENVALGLKlnRLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 153 ARAIANHPEVLLCDEPTSALDLETSASILALLksINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSA 232
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLF--LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
250
....*....|.
gi 504513067 233 PQHAYTKQLVS 243
Cdd:PRK14247 236 PRHELTEKYVT 246
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-224 |
7.24e-40 |
|
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: 147.61 E-value: 7.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLrtiNLLQR---PTEGRVFLGDTLISNASGREL 78
Cdd:COG4987 334 LELEDVSFRYPGAGRP---VLDGLSLTLPPGERVAIVGPSGSGKSTLL---ALLLRfldPQSGSITLGGVDLRDLDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQHrqrIGMIFQHFNLMHTrNVYDNVAFslraaGKSKADIAErVPEILALVGLQDKGTAYP-----------AQLSGGQK 147
Cdd:COG4987 408 RRR---IAVVPQRPHLFDT-TLRENLRL-----ARPDATDEE-LWAALERVGLGDWLAALPdgldtwlgeggRRLSGGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 148 QRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKsiNVRLGITIVLISHEMSVIkSICQRMAVMTGGNIVEEG 224
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLL--EALAGRTVLLITHRLAGL-ERMDRILVLEDGRIVEQG 551
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-257 |
9.85e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 141.28 E-value: 9.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGktaqSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDtlISNASGRELRQ 80
Cdd:PRK13644 1 MIRLENVSYSYPDG----TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHT-RNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANH 159
Cdd:PRK13644 75 IRKLVGIVFQNPETQFVgRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKsICQRMAVMTGGNIVEEGEVFTIFSAPqhayTK 239
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVLSDV----SL 228
|
250 260
....*....|....*....|
gi 504513067 240 QLVSHTTP--VELPDRFKKN 257
Cdd:PRK13644 229 QTLGLTPPslIELAENLKMH 248
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-233 |
1.22e-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: 142.94 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 25 VNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFL-GDTLISNASGRELRQHRQRIGMIFQHFNLMHTRNVYDN 103
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLnGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 104 VAFSL-RAAGKSKADIAERVPEILALVGLQDKgtaYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILA 182
Cdd:TIGR02142 96 LRYGMkRARPSERRISFERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504513067 183 LLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAP 233
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-221 |
1.24e-39 |
|
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: 138.93 E-value: 1.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 3 RLENVSVDFPAGKtaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNasgrelRQHR 82
Cdd:cd03226 1 RIENISFSYKKGT----EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 83 QRIGMIFQH--FNLMhTRNVYDNVAFSLRAAGKSKADIAErvpeILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:cd03226 71 KSIGYVMQDvdYQLF-TDSVREELLLGLKELDAGNEQAET----VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIV 221
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-270 |
1.41e-39 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 147.31 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 16 TAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQHRQRIGMIFQ--HFN 93
Cdd:PRK10261 334 TREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQdpYAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 94 LMHTRNVYDNVAFSLRAAGKSKADIA-ERVPEILALVGLQ-DKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSA 171
Cdd:PRK10261 414 LDPRQTVGDSIMEPLRVHGLLPGKAAaARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 172 LDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQLVShTTPVELP 251
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMA-AVPVADP 572
|
250
....*....|....*....
gi 504513067 252 DRFKKNnkgvllKILFADD 270
Cdd:PRK10261 573 SRQRPQ------RVLLSDD 585
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
1.90e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 140.75 E-value: 1.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGktaqSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLIsNASGRELRQ 80
Cdd:PRK13636 5 ILKVEELNYNYSDG----THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQH-FNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVG---LQDKGTAYpaqLSGGQKQRVGIARAI 156
Cdd:PRK13636 80 LRESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGiehLKDKPTHC---LSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 157 ANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFS 231
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-224 |
3.36e-39 |
|
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: 138.83 E-value: 3.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAQsrAVNNVNLTIQQGEVFGIVGTSGAGKSTllrTINLLQR---PTEGRVFLGDTLISNASgreL 78
Cdd:cd03249 1 IEFKNVSFRYPSRPDVP--ILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERfydPTSGEILLDGVDIRDLN---L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQHRQRIGMIFQHFNLMHTrNVYDNVAFSLRAAGKSKADIAERVPEILA-----------LVGlqDKGTaypaQLSGGQK 147
Cdd:cd03249 73 RWLRSQIGLVSQEPVLFDG-TIAENIRYGKPDATDEEVEEAAKKANIHDfimslpdgydtLVG--ERGS----QLSGGQK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 148 QRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKsiNVRLGITIVLISHEMSVIKSiCQRMAVMTGGNIVEEG 224
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLVQEALD--RAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQG 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-235 |
5.98e-39 |
|
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: 137.98 E-value: 5.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLgdtlisnaSGRELRQHRQRIGMIFQHFNLMHTRNVY 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL--------EGKQITEPGPDRMVVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 102 DNVAFSLRAAGK--SKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSAS 179
Cdd:TIGR01184 73 ENIALAVDRVLPdlSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 180 ILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTI-FSAPQH 235
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-226 |
7.33e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 143.62 E-value: 7.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAgktaqSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:COG1129 4 LLEMRGISKSFGG-----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HrqRIGMIFQHFNLMHTRNVYDNVAFS--LRAAGK-SKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIA 157
Cdd:COG1129 79 A--GIAIIHQELNLVPNLSVAENIFLGrePRRGGLiDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513067 158 NHPEVLLCDEPTSALDLETSASILALLKsinvRL---GITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEV 226
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIR----RLkaqGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPV 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
15-226 |
2.28e-38 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 137.12 E-value: 2.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 15 KTAQSRAV-NNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNAsgrelrqhRQRIGMIFQHFN 93
Cdd:PRK11247 20 KRYGERTVlNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA--------REDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 94 LMHTRNVYDNVAFSLRAAGKSKADiaervpEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALD 173
Cdd:PRK11247 92 LLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504513067 174 LETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAvmtggnIVEEGEV 226
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVL------LIEEGKI 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-231 |
2.77e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 137.60 E-value: 2.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNAS-GRELRQ 80
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQhF--NLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGL-QDKGTAYPAQLSGGQKQRVGIARAIA 157
Cdd:PRK13646 83 VRKRIGMVFQ-FpeSQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513067 158 NHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFS 231
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-201 |
4.26e-38 |
|
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: 134.91 E-value: 4.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpagktaQSRAV-NNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASgrelR 79
Cdd:COG4133 2 MLEAENLSCRR------GERLLfSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR----E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 80 QHRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADiaERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANH 159
Cdd:COG4133 72 DYRRRLAYLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSiNVRLGITIVLISHE 201
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-220 |
1.16e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 136.01 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSvdFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:PRK13650 4 IIEVKNLT--FKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HrqrIGMIFQH-FNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANH 159
Cdd:PRK13650 82 K---IGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIkSICQRMAVMTGGNI 220
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-220 |
1.20e-37 |
|
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: 132.73 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAQsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPV---LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqrIGMIFQHFNLmhtrnvydnvaFSlraagkskADIAERVpeilalvglqdkgtaypaqLSGGQKQRVGIARAIANHPE 161
Cdd:cd03246 78 ---VGYLPQDDEL-----------FS--------GSIAENI-------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSiCQRMAVMTGGNI 220
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-286 |
1.52e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 136.01 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGdtlisnasGREL-R 79
Cdd:COG4152 1 MLELKGLTKRF-GDKTA----VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD--------GEPLdP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 80 QHRQRIG-----------MifqhfnlmhtrNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQ 148
Cdd:COG4152 68 EDRRRIGylpeerglypkM-----------KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 149 RVGIARAIANHPEVLLCDEPTSALDletsasilallkSINVRL-----------GITIVLISHEMSVIKSICQRMAVMTG 217
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLD------------PVNVELlkdvirelaakGTTVIFSSHQMELVEELCDRIVIINK 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 218 GNIVEEGEVFTIFSapQHAYTK-QLVSHTTPVELPDRF-----KKNNKGVLLKIlfADDSVEQPILSDVAQQFQV 286
Cdd:COG4152 205 GRKVLSGSVDEIRR--QFGRNTlRLEADGDAGWLRALPgvtvvEEDGDGAELKL--EDGADAQELLRALLARGPV 275
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
20-224 |
1.82e-37 |
|
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: 133.11 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 20 RAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRV-FLGDTLISNASGrelrqhRQRIGMIFQHFNLMHTR 98
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItFDGKSYQKNIEA------LRRIGALIEAPGFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 99 NVYDNVAFSLRAAGKSKadiaERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSA 178
Cdd:cd03268 88 TARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504513067 179 SILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03268 164 ELRELILSLR-DQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-234 |
1.96e-37 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 137.47 E-value: 1.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpaGKTAQSRavnNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISnasgrELRQH 81
Cdd:PRK11000 4 VTLRNVTKAY--GDVVISK---DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-----DVPPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERV---PEILALVGLQDKgtaYPAQLSGGQKQRVGIARAIAN 158
Cdd:PRK11000 74 ERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVnqvAEVLQLAHLLDR---KPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 159 HPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQ 234
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-243 |
2.38e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 134.20 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 18 QSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTIN-LLQRPTEGRVfLGDTLISnasGRELRQH-------RQRIGMIF 89
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrLLELNEEARV-EGEVRLF---GRNIYSPdvdpievRREVGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 90 QHFNLMHTRNVYDNVAFSLRAAG--KSKADIAERVPEILALVGL----QDKGTAYPAQLSGGQKQRVGIARAIANHPEVL 163
Cdd:PRK14267 92 QYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 164 LCDEPTSALDLETSASILALLksINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQLVS 243
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELL--FELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVT 249
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-241 |
2.73e-37 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 136.39 E-value: 2.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 21 AVNNVNLTIQQGEVFGIVGTSGAGKS-TLLRTINLLQRptEGRV-----FLGDTLIsNASGRELRQHR-QRIGMIFQhfN 93
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAA--NGRIggsatFNGREIL-NLPEKELNKLRaEQISMIFQ--D 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 94 LMHTRNVYDNVAFSLRAA-----GKSKADIAERVPEILALVGLQD---KGTAYPAQLSGGQKQRVGIARAIANHPEVLLC 165
Cdd:PRK09473 106 PMTSLNPYMRVGEQLMEVlmlhkGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 166 DEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQL 241
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGL 261
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-224 |
4.34e-37 |
|
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: 132.56 E-value: 4.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 18 QSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRqhRQRIGMIFQHFNLMHT 97
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--RAGIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 98 RNVYDNvafsLRAAG--KSKADIAERVPEILALV-GLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDL 174
Cdd:cd03224 90 LTVEEN----LLLGAyaRRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504513067 175 ETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03224 166 KIVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-220 |
5.64e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 136.13 E-value: 5.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGktaqSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRElrq 80
Cdd:PRK11650 3 GLKLQAVRKSYDGK----TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 hrqR-IGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPE---ILALVGLQDKGtayPAQLSGGQKQRVGIARAI 156
Cdd:PRK11650 76 ---RdIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEaarILELEPLLDRK---PRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513067 157 ANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNI 220
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-218 |
5.76e-37 |
|
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: 132.56 E-value: 5.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFP----AGKTAQsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFL----GDTLISN 72
Cdd:COG4778 4 LLEVENLSKTFTlhlqGGKRLP--VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 73 ASGRE---LRqhRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDK-GTAYPAQLSGGQKQ 148
Cdd:COG4778 82 ASPREilaLR--RRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 149 RVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGG 218
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-228 |
1.09e-36 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 132.55 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVdfpagKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:COG4559 1 MLEAENLSV-----RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HR----QRIGMIFqHFnlmhtrNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQD-KGTAYPaQLSGGQKQRVGIARA 155
Cdd:COG4559 76 RRavlpQHSSLAF-PF------TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHlAGRSYQ-TLSGGEQQRVQLARV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 156 IA-------NHPEVLLCDEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG---E 225
Cdd:COG4559 148 LAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGtpeE 226
|
...
gi 504513067 226 VFT 228
Cdd:COG4559 227 VLT 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-221 |
1.30e-36 |
|
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: 129.47 E-value: 1.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKtaqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH 81
Cdd:cd03216 1 LELRGITKRFGGVK-----ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RqrIGMIFQhfnlmhtrnvydnvafslraagkskadiaervpeilalvglqdkgtaypaqLSGGQKQRVGIARAIANHPE 161
Cdd:cd03216 76 G--IAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGGNIV 221
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-231 |
1.98e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 132.82 E-value: 1.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGR--ELR 79
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 80 QHRQRIGMIFQ--HFNLMHtRNVYDNVAFSLRAAGKSKADIAERVPEILALVGL-QDKGTAYPAQLSGGQKQRVGIARAI 156
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQ-ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 157 ANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFS 231
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-224 |
2.85e-36 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 138.46 E-value: 2.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH 81
Cdd:TIGR03375 464 IEFRNVSFAYPGQETP---ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRN 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqrIGMIFQHFNLMHTrNVYDNVAFSLRAAGKskadiaERVPEILALVGLQD------KGTAYP-----AQLSGGQKQRV 150
Cdd:TIGR03375 541 ---IGYVPQDPRLFYG-TLRDNIALGAPYADD------EEILRAAELAGVTEfvrrhpDGLDMQigergRSLSGGQRQAV 610
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513067 151 GIARAIANHPEVLLCDEPTSALDLETSASILALLKSinVRLGITIVLISHEMSVIKsICQRMAVMTGGNIVEEG 224
Cdd:TIGR03375 611 ALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKR--WLAGKTLVLVTHRTSLLD-LVDRIIVMDNGRIVADG 681
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-230 |
4.10e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 132.16 E-value: 4.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASG-RELR 79
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 80 QHRQRIGMIFQH-FNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDK-GTAYPAQLSGGQKQRVGIARAIA 157
Cdd:PRK13643 81 PVRKKVGVVFQFpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513067 158 NHPEVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIF 230
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-226 |
4.57e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 136.31 E-value: 4.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAgktaqSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGdtlisnasGRELRQ 80
Cdd:COG3845 5 ALELRGITKRFGG-----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID--------GKPVRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 H------RQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGK---SKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVG 151
Cdd:COG3845 72 RsprdaiALGIGMVHQHFMLVPNLTVAENIVLGLEPTKGgrlDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 152 IARAIANHPEVLLCDEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEV 226
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDT 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-233 |
4.66e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 131.46 E-value: 4.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 16 TAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQHrqrIGMIFQHFN-L 94
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF---VGLVFQNPDdQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 95 MHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDL 174
Cdd:PRK13652 91 IFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 175 ETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAP 233
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-200 |
4.93e-36 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 129.52 E-value: 4.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVdfpagKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTIN-LLQRP--TEGRVFLGDTLISnasgrE 77
Cdd:COG4136 1 MLSLENLTI-----TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLT-----A 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 78 LRQHRQRIGMIFQ------HFNlmhtrnVYDNVAFSLrAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVG 151
Cdd:COG4136 71 LPAEQRRIGILFQddllfpHLS------VGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504513067 152 IARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISH 200
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-243 |
5.26e-36 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 130.67 E-value: 5.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 18 QSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLL-----QRPTEGRV-FLGDTLIS-NASGRELRQHrqrIGMIFQ 90
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIvYNGHNIYSpRTDTVDLRKE---IGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 91 HFNLMhTRNVYDNVAFSLRAAG-KSKADIAERVPEilALVG------LQDKGTAYPAQLSGGQKQRVGIARAIANHPEVL 163
Cdd:PRK14239 94 QPNPF-PMSIYENVVYGLRLKGiKDKQVLDEAVEK--SLKGasiwdeVKDRLHDSALGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 164 LCDEPTSALDLETSASILALLksINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQLVS 243
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETL--LGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYIS 248
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-243 |
6.27e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 131.37 E-value: 6.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 6 NVSVDFpAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNAS---GRELRQHR 82
Cdd:PRK14271 26 NLTLGF-AGKTV----LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSifnYRDVLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 83 QRIGMIFQHFNLMhTRNVYDNVAFSLRA----AGKSKADIAE-RVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIA 157
Cdd:PRK14271 101 RRVGMLFQRPNPF-PMSIMDNVLAGVRAhklvPRKEFRGVAQaRLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 158 NHPEVLLCDEPTSALDLETSASILALLKSINVRLgiTIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAY 237
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAE 257
|
....*.
gi 504513067 238 TKQLVS 243
Cdd:PRK14271 258 TARYVA 263
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-204 |
1.19e-35 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 136.78 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTaQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:PRK10535 4 LLELKDIRRSYPSGEE-QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 -HRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANH 159
Cdd:PRK10535 83 lRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSV 204
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQV 206
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-232 |
1.33e-35 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 129.43 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAQSR-----------------AVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRV 63
Cdd:COG1134 4 MIEVENVSKSYRLYHEPSRSlkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 64 flgdtlisnasgrelrQHRQRIGMIFQH---FNLMHTrnVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDK-----G 135
Cdd:COG1134 84 ----------------EVNGRVSALLELgagFHPELT--GRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFidqpvK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 136 TaYpaqlSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAVM 215
Cdd:COG1134 146 T-Y----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWL 219
|
250
....*....|....*..
gi 504513067 216 TGGNIVEEGEVFTIFSA 232
Cdd:COG1134 220 EKGRLVMDGDPEEVIAA 236
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-224 |
2.52e-35 |
|
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: 128.50 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRtinLLQR---PTEGRVflgdtLISNASGREL 78
Cdd:cd03253 1 IEFENVTFAYDPGRPV----LKDVSFTIPAGKKVAIVGPSGSGKSTILR---LLFRfydVSSGSI-----LIDGQDIREV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQH--RQRIGMIFQHFNLMHTrNVYDNVAFS--------LRAAGKsKADIAERvpeILAL-------VGlqDKGTaypaQ 141
Cdd:cd03253 69 TLDslRRAIGVVPQDTVLFND-TIGYNIRYGrpdatdeeVIEAAK-AAQIHDK---IMRFpdgydtiVG--ERGL----K 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 142 LSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSinVRLGITIVLISHEMSVIKSiCQRMAVMTGGNIV 221
Cdd:cd03253 138 LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRD--VSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
...
gi 504513067 222 EEG 224
Cdd:cd03253 215 ERG 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-228 |
3.34e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 128.74 E-value: 3.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVdfpagKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:PRK13548 2 MLEARNLSV-----RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRqriGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQD-KGTAYPaQLSGGQKQRVGIARAIA-- 157
Cdd:PRK13548 77 RR---AVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHlAGRDYP-QLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513067 158 ----NHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG---EVFT 228
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGtpaEVLT 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
4.54e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 128.72 E-value: 4.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpagKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:PRK13648 7 IIVFKNVSFQY---QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HrqrIGMIFQH-FNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANH 159
Cdd:PRK13648 84 H---IGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSiCQRMAVMTGGNIVEEGEVFTIFS 231
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-242 |
1.04e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 127.47 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLL------QRPTEGRVFLGDTLISNASGRELRQHrqrIGMIFQHFNLM 95
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKLRKE---VGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 96 HTRNVYDNVAFSLRAAG-KSKADIAERVPEILALVGL----QDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTS 170
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513067 171 ALDLETSASILALLKSINVRlgITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQLV 242
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-225 |
1.09e-34 |
|
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: 132.62 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVF--LGDTLISNASGREL 78
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQHR--QRIGMIFQHFNLMHTRNVYDNV--AFSLRAA---GKSKADIaervpeILALVGLQDKGTA-----YPAQLSGGQ 146
Cdd:TIGR03269 359 GRGRakRYIGILHQEYDLYPHRTVLDNLteAIGLELPdelARMKAVI------TLKMVGFDEEKAEeildkYPDELSEGE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 147 KQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGE 225
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-224 |
1.50e-34 |
|
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: 126.45 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 21 AVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRqhRQrIGMIFQHfNLMHTRNV 100
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLR--RQ-VGVVLQE-NVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 101 YDNVAFSLRAAGKskadiaERVPEILALVGLQDKGTAYP-----------AQLSGGQKQRVGIARAIANHPEVLLCDEPT 169
Cdd:cd03252 93 RDNIALADPGMSM------ERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 170 SALDLETSASILALLKSINVrlGITIVLISHEMSVIKSiCQRMAVMTGGNIVEEG 224
Cdd:cd03252 167 SALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-224 |
1.88e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 128.00 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASgrelRQHRQRIGMIFQHFNLMHTRNVY 101
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA----RHARQRVGVVPQFDNLDPDFTVR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 102 DNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASIL 181
Cdd:PRK13537 99 ENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMW 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504513067 182 ALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:PRK13537 179 ERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-230 |
2.21e-34 |
|
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: 131.85 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpAGKtaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLlrtINLLQ-----RPTEGRVFL----------- 65
Cdd:TIGR03269 1 IEVKNLTKKF-DGK----EVLKNISFTIEEGEVLGILGRSGAGKSVL---MHVLRgmdqyEPTSGRIIYhvalcekcgyv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 66 -------------GDTLIS------NASGRELRQHRQRIGMIFQH-FNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEI 125
Cdd:TIGR03269 73 erpskvgepcpvcGGTLEPeevdfwNLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 126 LALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVI 205
Cdd:TIGR03269 153 IEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVI 232
|
250 260
....*....|....*....|....*...
gi 504513067 206 KSICQRMAVMTGGNIVEEG---EVFTIF 230
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKEEGtpdEVVAVF 260
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
24-243 |
2.25e-34 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 126.58 E-value: 2.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQHRQRIgmifqhfnLMHTR--NVY 101
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRR--------LLRTEwgFVH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 102 DNVAFSLRAAGKSKADIAERvpeiLALVG------LQDKGTAY--------------PAQLSGGQKQRVGIARAIANHPE 161
Cdd:PRK11701 96 QHPRDGLRMQVSAGGNIGER----LMAVGarhygdIRATAGDWlerveidaariddlPTTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQL 241
Cdd:PRK11701 172 LVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLL 251
|
..
gi 504513067 242 VS 243
Cdd:PRK11701 252 VS 253
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-243 |
3.69e-34 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 132.29 E-value: 3.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAgKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKS----TLLRTIN-----------LLQRPTEGRVFL 65
Cdd:PRK10261 12 VLAVENLNIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEqagglvqcdkmLLRRRSRQVIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 66 GDTliSNASGRELRQhrQRIGMIFQH--FNLMHTRNVYDNVAFSLR---AAGKSKAdIAE--------RVPEILALVGlq 132
Cdd:PRK10261 91 SEQ--SAAQMRHVRG--ADMAMIFQEpmTSLNPVFTVGEQIAESIRlhqGASREEA-MVEakrmldqvRIPEAQTILS-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 133 dkgtAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRM 212
Cdd:PRK10261 164 ----RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRV 239
|
250 260 270
....*....|....*....|....*....|.
gi 504513067 213 AVMTGGNIVEEGEVFTIFSAPQHAYTKQLVS 243
Cdd:PRK10261 240 LVMYQGEAVETGSVEQIFHAPQHPYTRALLA 270
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-224 |
4.14e-34 |
|
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: 125.04 E-value: 4.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLlrtINLLQR---PTEGRVFLGDTLISNASGREL 78
Cdd:cd03251 1 VEFKNVTFRYPGDGPP---VLRDISLDIPAGETVALVGPSGSGKSTL---VNLIPRfydVDSGRILIDGHDVRDYTLASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQHrqrIGMIFQHFNLMHTrNVYDNVAFSLRAAGKskadiaERVPEILALVGLQDKGTAYP-----------AQLSGGQK 147
Cdd:cd03251 75 RRQ---IGLVSQDVFLFND-TVAENIAYGRPGATR------EEVEEAARAANAHEFIMELPegydtvigergVKLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 148 QRVGIARAIANHPEVLLCDEPTSALDLET----SASILALLKsinvrlGITIVLISHEMSVIKSIcQRMAVMTGGNIVEE 223
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESerlvQAALERLMK------NRTTFVIAHRLSTIENA-DRIVVLEDGKIVER 217
|
.
gi 504513067 224 G 224
Cdd:cd03251 218 G 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-223 |
5.30e-34 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 124.89 E-value: 5.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 25 VNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFL-GDTLIS-NASGR-ELRQhrQRIGMIFQHFNLMHTRNVY 101
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvGQPLHQmDEEARaKLRA--KHVGFVFQSFMLIPTLNAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 102 DNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASIL 181
Cdd:PRK10584 107 ENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504513067 182 ALLKSINVRLGITIVLISHEmSVIKSICQRMAVMTGGNIVEE 223
Cdd:PRK10584 187 DLLFSLNREHGTTLILVTHD-LQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-243 |
1.27e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 124.89 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQR--PT---EGRVFLGDTLIsNASGR 76
Cdd:PRK14243 11 LRTENLNVYY-----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNL-YAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 77 ELRQHRQRIGMIFQHFNLMhTRNVYDNVAFSLRAAGkSKADIAERVPEILALVGL----QDKGTAYPAQLSGGQKQRVGI 152
Cdd:PRK14243 85 DPVEVRRRIGMVFQKPNPF-PKSIYDNIAYGARING-YKGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 153 ARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLgiTIVLISHEMSViksiCQRMAVMTG-------------GN 219
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQ----AARVSDMTAffnveltegggryGY 236
|
250 260
....*....|....*....|....
gi 504513067 220 IVEEGEVFTIFSAPQHAYTKQLVS 243
Cdd:PRK14243 237 LVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-224 |
2.60e-33 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 123.97 E-value: 2.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLL---QRPTEGRV-FLGDTLISNAS-G 75
Cdd:PRK09984 4 IIRVEKLAKTF-----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIeLLGRTVQREGRlA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 76 RELRQHRQRIGMIFQHFNLMHTRNVYDNV---AFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQ-----LSGGQK 147
Cdd:PRK09984 79 RDIRKSRANTGYIFQQFNLVNRLSVLENVligALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHqrvstLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 148 QRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-224 |
3.43e-33 |
|
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: 122.22 E-value: 3.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 27 LTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLG--DTLISNASGRElrqhrqrIGMIFQHFNLMHTRNVYDNV 104
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvDVTAAPPADRP-------VSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 105 AFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALL 184
Cdd:cd03298 92 GLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504513067 185 KSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-224 |
3.49e-33 |
|
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: 122.48 E-value: 3.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDF-PAGKTAQsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVflgdTLISNASGRELR 79
Cdd:cd03266 1 MITADALTKRFrDVKKTVQ--AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA----TVDGFDVVKEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 80 QHRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANH 159
Cdd:cd03266 75 EARRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLR-ALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
4.92e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 123.56 E-value: 4.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPagkTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:PRK13632 7 MIKVENVSFSYP---NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HrqrIGMIFQH-FNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANH 159
Cdd:PRK13632 84 K---IGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMS-VIKsiCQRMAVMTGGNIVEEGEVFTIF 230
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDeAIL--ADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-242 |
7.02e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 122.84 E-value: 7.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTaqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQR-----PTEGRV-FLGDTLISNASg 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKI-----LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVeFFNQNIYERRV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 76 rELRQHRQRIGMIFQHFNLMhTRNVYDNVAFSLRAAG-KSKADIAERVPEILALVGLQD----KGTAYPAQLSGGQKQRV 150
Cdd:PRK14258 82 -NLNRLRRQVSMVHPKPNLF-PMSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDeikhKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 151 GIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTG-----GNIVEEGE 225
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGL 239
|
250
....*....|....*..
gi 504513067 226 VFTIFSAPQHAYTKQLV 242
Cdd:PRK14258 240 TKKIFNSPHDSRTREYV 256
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-224 |
8.36e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 124.56 E-value: 8.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 4 LENVSVDFpAG--KTAQSRA-VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVflgdTLISNASGRELRQ 80
Cdd:PRK13536 37 MSTVAIDL-AGvsKSYGDKAvVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI----TVLGVPVPARARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:PRK13536 112 ARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-224 |
1.11e-32 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 122.57 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQHRQRIGMIFQHFNLMHTRNVYDN 103
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 104 VAFSLRAAGKSKADIAER-VPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILA 182
Cdd:PRK11831 105 VAYPLREHTQLPAPLLHStVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504513067 183 LLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:PRK11831 185 LISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHG 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
1.29e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 123.27 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRV------------------ 63
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 64 FLGDTLISNASGRELRQH---RQRIGMIFQ--HFNLMHTrNVYDNVAFSLRAAGKSKADIAERVPEILALVGL-QDKGTA 137
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIkeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 138 YPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTG 217
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250
....*....|....
gi 504513067 218 GNIVEEGEVFTIFS 231
Cdd:PRK13651 241 GKIIKDGDTYDILS 254
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-234 |
1.31e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 122.63 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRV-FLGDTLISNASGRELRQ 80
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItIAGYHITPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQhF--NLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGL-QDKGTAYPAQLSGGQKQRVGIARAIA 157
Cdd:PRK13641 83 LRKKVSLVFQ-FpeAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 158 NHPEVLLCDEPTSALDLETSASILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQ 234
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-224 |
2.81e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 120.61 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 4 LENVSVDFPAGKtaqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGdtlisnasGRELRQH-- 81
Cdd:COG4674 13 VEDLTVSFDGFK-----ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFG--------GTDLTGLde 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 ----RQRIGMIFQH---FNlMHTrnVYDNVAFSLRA--------AGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQ 146
Cdd:COG4674 80 heiaRLGIGRKFQKptvFE-ELT--VFENLELALKGdrgvfaslFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 147 KQRVGIARAIANHPEVLLCDEPTSAL-DLETSASIlALLKSINVRLgiTIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:COG4674 157 KQWLEIGMLLAQDPKLLLLDEPVAGMtDAETERTA-ELLKSLAGKH--SVVVVEHDMEFVRQIARKVTVLHQGSVLAEG 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-228 |
3.06e-32 |
|
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: 120.57 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVF--LGDTLisnasGRE- 77
Cdd:COG1119 3 LLELRNVTVRR-GGKTI----LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlFGERR-----GGEd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 78 LRQHRQRIGMI--FQHFNLMHTRNVYDNV--AF--SLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVG 151
Cdd:COG1119 73 VWELRKRIGLVspALQLRFPRDETVLDVVlsGFfdSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 152 IARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG---EVFT 228
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGpkeEVLT 232
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-224 |
1.67e-31 |
|
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: 118.02 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAQSR-----------------AVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRV- 63
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSlkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 64 ---------FLGDTLISNASGRElrqhrqrigmifqhfnlmhtrnvydNVAFSLRAAGKSKADIAERVPEILALVGLQDK 134
Cdd:cd03220 81 vrgrvssllGLGGGFNPELTGRE-------------------------NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 135 GTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAV 214
Cdd:cd03220 136 IDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALV 214
|
250
....*....|
gi 504513067 215 MTGGNIVEEG 224
Cdd:cd03220 215 LEKGKIRFDG 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
1.80e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.46 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGktaqSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQh 81
Cdd:PRK13647 5 IEVEDLHFRYKDG----TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqRIGMIFQH-FNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:PRK13647 80 --KVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEV 226
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-225 |
2.10e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 118.15 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 26 NLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLgdtliSNASGRELRQHRQRIGMIFQHFNLMHTRNVYDNVA 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL-----NGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 106 FSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLK 185
Cdd:PRK10771 94 LGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504513067 186 SINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGE 225
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-224 |
6.96e-31 |
|
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: 115.84 E-value: 6.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNAsgrelrqH 81
Cdd:cd03269 1 LEVENVTKRF-----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA-------A 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPE 161
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 162 VLLCDEPTSALDletSASILALLKSIN--VRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03269 149 LLILDEPFSGLD---PVNVELLKDVIRelARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-243 |
8.86e-31 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 117.20 E-value: 8.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 21 AVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNAsgrELRQHRQRIGMIFQ--HFNLMHTR 98
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG---DYSYRSQRIRMIFQdpSTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 99 NVYDNVAFSLRAAGK-SKADIAERVPEILALVGL-QDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLET 176
Cdd:PRK15112 105 RISQILDFPLRLNTDlEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 177 SASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKQLVS 243
Cdd:PRK15112 185 RSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIA 251
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-224 |
9.83e-31 |
|
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: 116.23 E-value: 9.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPagktaQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRq 80
Cdd:COG0410 3 MLEVENLHAGYG-----GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 hRQRIGM------IFQHFnlmhtrNVYDNvafsLRAAG---KSKADIAERVPEILAL--VgLQDKGTAYPAQLSGGQKQR 149
Cdd:COG0410 77 -RLGIGYvpegrrIFPSL------TVEEN----LLLGAyarRDRAEVRADLERVYELfpR-LKERRRQRAGTLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 150 VGIARAIANHPEVLLCDEPTSALdletsA-----SILALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGL-----ApliveEIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEG 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-234 |
2.68e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 116.35 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 4 LENVSVDFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFL-GDTLisnaSGRELRQHR 82
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELL----TAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 83 QRIGMIFQH-FNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPE 161
Cdd:PRK13642 81 RKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSiCQRMAVMTGGNIVEEGEVFTIFSAPQ 234
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-225 |
3.64e-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: 120.24 E-value: 3.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH 81
Cdd:COG4618 331 LSVENLTVVPPGSKRP---ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqrIGMIFQHFNLMH-TrnVYDNVA-FS-------LRAAgkSKADIAERvpeILAL-------VGlqDKGTAypaqLSGG 145
Cdd:COG4618 408 ---IGYLPQDVELFDgT--IAENIArFGdadpekvVAAA--KLAGVHEM---ILRLpdgydtrIG--EGGAR----LSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 146 QKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIkSICQRMAVMTGGNIVEEGE 225
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLL-AAVDKLLVLRDGRVQAFGP 549
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-224 |
4.62e-30 |
|
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: 114.35 E-value: 4.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 10 DFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDtlisNASGRELRQHRQRIGMIF 89
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKKFLRRIGVVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 90 -QHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEP 168
Cdd:cd03267 101 gQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 169 TSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-205 |
4.78e-30 |
|
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: 119.70 E-value: 4.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPaGKTAqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQh 81
Cdd:TIGR02857 322 LEFSGVSVAYP-GRRP---ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqRIGMIFQHFNLMHTrNVYDNVAFSLRAAgkSKADIAErvpeILALVGLQDKGTAYP-----------AQLSGGQKQRV 150
Cdd:TIGR02857 397 --QIAWVPQHPFLFAG-TIAENIRLARPDA--SDAEIRE----ALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRL 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 151 GIARAIANHPEVLLCDEPTSALDLETSASILALLKSInvRLGITIVLISHEMSVI 205
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALA 520
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-234 |
9.08e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 114.90 E-value: 9.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEgrvfLGDTLIsNASGRELRQH 81
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP---ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD----NPNSKI-TVDGITLTAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 -----RQRIGMIFQH-FNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARA 155
Cdd:PRK13640 78 tvwdiREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 156 IANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSViKSICQRMAVMTGGNIVEEGEVFTIFSAPQ 234
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-220 |
9.60e-30 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 113.03 E-value: 9.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 26 NLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTlisnaSGRELRQHRQRIGMIFQHFNLMHTRNVYDNVA 105
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ-----SHTGLAPYQRPVSMLFQENNLFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 106 FSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLK 185
Cdd:TIGR01277 93 LGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*
gi 504513067 186 SINVRLGITIVLISHEMSVIKSICQRMAVMTGGNI 220
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-224 |
9.77e-30 |
|
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: 113.52 E-value: 9.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 3 RLENVSVDFPaGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINllQRPTEGRVFLGDTLIsNASGRELRQHR 82
Cdd:cd03234 5 PWWDVGLKAK-NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIS--GRVEGGGTTSGQILF-NGQPRKPDQFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 83 QRIGMIFQHFNLMHTRNVYDNVAFSLRAAG---KSKADIAERVP-EILALVGLQDKGTAYPAQLSGGQKQRVGIARAIAN 158
Cdd:cd03234 81 KCVAYVRQDDILLPGLTVRETLTYTAILRLprkSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 159 HPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-226 |
1.04e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 114.02 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:COG4604 1 MIEIKNVSKRY-----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 H----RQRigmifQHFNLMHTrnVYDNVAFSlR---AAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIA 153
Cdd:COG4604 76 RlailRQE-----NHINSRLT--VRELVAFG-RfpySKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513067 154 RAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEV 226
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-224 |
1.43e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 118.91 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPaGKtaqSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLlrtINLLQR---PTEGRVFLGDTLISNASGREL 78
Cdd:PRK13657 335 VEFDDVSFSYD-NS---RQGVEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRvfdPQSGRILIDGTDIRTVTRASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQHrqrIGMIFQHFNLMHtRNVYDNV---------AFSLRAAGKSKA-DIAERVPEIL-ALVGlqDKGTaypaQLSGGQK 147
Cdd:PRK13657 408 RRN---IAVVFQDAGLFN-RSIEDNIrvgrpdatdEEMRAAAERAQAhDFIERKPDGYdTVVG--ERGR----QLSGGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 148 QRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKsiNVRLGITIVLISHEMSVIKSiCQRMAVMTGGNIVEEG 224
Cdd:PRK13657 478 QRLAIARALLKDPPILILDEATSALDVETEAKVKAALD--ELMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-221 |
1.74e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 113.64 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNasgreLRQ 80
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-----LPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HR--QRIGMIFQhfN-LMHT---RNVYDNVA--------FSLRaAGKSKADIaERVPEILALV--GLQDKGTAYPAQLSG 144
Cdd:COG1101 76 YKraKYIGRVFQ--DpMMGTapsMTIEENLAlayrrgkrRGLR-RGLTKKRR-ELFRELLATLglGLENRLDTKVGLLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 145 GQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIV 221
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-251 |
1.96e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 113.95 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 25 VNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFL-GDTLisNASGRELRQHRQRIGMIFQHFN--LMHTrNVY 101
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWqGKPL--DYSKRGLLALRQQVATVFQDPEqqIFYT-DID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 102 DNVAFSLRAAGKSKADIAERVPEILALVGLQdKGTAYPAQ-LSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASI 180
Cdd:PRK13638 97 SDIAFSLRNLGVPEAEITRRVDEALTLVDAQ-HFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 181 LALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGGNIV---EEGEVFTIFSAPQHAYTKQ--LVSHTTPVELP 251
Cdd:PRK13638 176 IAIIRRI-VAQGNHVIISSHDIDLIYEISDAVYVLRQGQILthgAPGEVFACTEAMEQAGLTQpwLVKLHTQLGLP 250
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-251 |
2.80e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 114.56 E-value: 2.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 H-------------RQRIGMIFQ--HFNLMHTrNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDkgtAY----PAQ 141
Cdd:PRK13631 101 TnpyskkiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDD---SYlersPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 142 LSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIV 221
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
250 260 270
....*....|....*....|....*....|
gi 504513067 222 EEGEVFTIFsapqhayTKQLVSHTTPVELP 251
Cdd:PRK13631 256 KTGTPYEIF-------TDQHIINSTSIQVP 278
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-242 |
3.37e-29 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 114.51 E-value: 3.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpagKTAQS--RAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTI------NLlqRPTEGRVFLGDTLISN 72
Cdd:PRK15093 3 LLDIRNLTIEF---KTSDGwvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdNW--RVTADRMRFDDIDLLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 73 ASGRELRQH-RQRIGMIFQHFN--LMHTRNVYDNVAFSLRA---AGKSKADI---AERVPEILALVGLQDKGTA---YPA 140
Cdd:PRK15093 78 LSPRERRKLvGHNVSMIFQEPQscLDPSERVGRQLMQNIPGwtyKGRWWQRFgwrKRRAIELLHRVGIKDHKDAmrsFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 141 QLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNI 220
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
250 260
....*....|....*....|..
gi 504513067 221 VEEGEVFTIFSAPQHAYTKQLV 242
Cdd:PRK15093 238 VETAPSKELVTTPHHPYTQALI 259
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-310 |
6.07e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 113.64 E-value: 6.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 20 RAVNNVNLTIQQGEVFGIVGTSGAGKSTllrTINLLQ---RPTEGRV-FLGdtLISNasgRELRQHRQRIGMIF-Qhfnl 94
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKST---TIKMLTgilVPTSGEVrVLG--YVPF---KRRKEFARRIGVVFgQ---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 95 mhtRN-------VYDNvaFSLRAA--GKSKADIAERVPEILALVGLQDK-GTayPA-QLSGGQKQRVGIARAIANHPEVL 163
Cdd:COG4586 104 ---RSqlwwdlpAIDS--FRLLKAiyRIPDAEYKKRLDELVELLDLGELlDT--PVrQLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 164 LCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSapQHAYTKQLV- 242
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKE--RFGPYKTIVl 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513067 243 ---SHTTPVELPDRFK-KNNKGVLLKILFADDSVEQPILSDVAQQFQVSvnilhgNIEyINDRALGHIIAQI 310
Cdd:COG4586 255 elaEPVPPLELPRGGEvIEREGNRVRLEVDPRESLAEVLARLLARYPVR------DLT-IEEPPIEEVIRRI 319
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-224 |
9.51e-29 |
|
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: 116.35 E-value: 9.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAgktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLlrtINLLQR---PTEGRVFLGDTLISNASGREL 78
Cdd:TIGR02203 331 VEFRNVTFRYPG---RDRPALDSISLVIEPGETVALVGRSGSGKSTL---VNLIPRfyePDSGQILLDGHDLADYTLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQHrqrIGMIFQHFNLMHTrNVYDNVAFSlRAAGKSKADI--AERVPEILALVGLQDKGTAYP-----AQLSGGQKQRVG 151
Cdd:TIGR02203 405 RRQ---VALVSQDVVLFND-TIANNIAYG-RTEQADRAEIerALAAAYAQDFVDKLPLGLDTPigengVLLSGGQRQRLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513067 152 IARAIANHPEVLLCDEPTSALDLETSASILALLKSinVRLGITIVLISHEMSVIKSiCQRMAVMTGGNIVEEG 224
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALER--LMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
20-224 |
1.43e-28 |
|
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: 110.33 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 20 RAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNasgreLRQH-RQRIGMIF--QHFNLMH 96
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK-----LPMHkRARLGIGYlpQEASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 97 TRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLET 176
Cdd:cd03218 89 KLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504513067 177 SASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03218 169 VQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEG 215
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
21-226 |
2.00e-28 |
|
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: 109.80 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 21 AVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLgdtlisnaSGREL-RQHRQRIGMIFQHFNLMHTRN 99
Cdd:TIGR03740 15 AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIF--------DGHPWtRKDLHKIGSLIESPPLYENLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 100 VYDNVAFSLRAAGKSKAdiaeRVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSAS 179
Cdd:TIGR03740 87 ARENLKVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504513067 180 ILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEV 226
Cdd:TIGR03740 163 LRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLGYQGKI 208
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-234 |
3.99e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 111.89 E-value: 3.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGD-TLISNASGRELRQHRQRIGMIFQHFNLMHTRNVYD 102
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 103 NVAFSLRAAGKSKADiaervpEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILA 182
Cdd:PRK11144 96 NLRYGMAKSMVAQFD------KIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504513067 183 LLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFSAPQ 234
Cdd:PRK11144 170 YLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-224 |
4.52e-28 |
|
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: 114.53 E-value: 4.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSvdFpaGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRtinLLQR---PTEGRVFLGDTLIsnasgREL 78
Cdd:COG5265 358 VRFENVS--F--GYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLAR---LLFRfydVTSGRILIDGQDI-----RDV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQH--RQRIGMIFQH---FNlmhtRNVYDNVAFSlrAAGKSKADIAE--RVPEILALV-GLQDKgtaYPAQ-------LS 143
Cdd:COG5265 426 TQAslRAAIGIVPQDtvlFN----DTIAYNIAYG--RPDASEEEVEAaaRAAQIHDFIeSLPDG---YDTRvgerglkLS 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 144 GGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSinVRLGITIVLISHEMSVIKSiCQRMAVMTGGNIVEE 223
Cdd:COG5265 497 GGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALRE--VARGRTTLVIAHRLSTIVD-ADEILVLEAGRIVER 573
|
.
gi 504513067 224 G 224
Cdd:COG5265 574 G 574
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-220 |
6.38e-28 |
|
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: 107.13 E-value: 6.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 3 RLENVSVDfpagktaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH- 81
Cdd:cd03215 6 EVRGLSVK---------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 -------RQRIGmifqhfnLMHTRNVYDNVAFslraagkskadiaervpeilalvglqdkgtayPAQLSGGQKQRVGIAR 154
Cdd:cd03215 77 iayvpedRKREG-------LVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLAR 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 155 AIANHPEVLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNI 220
Cdd:cd03215 118 WLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-225 |
1.29e-27 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 108.72 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 3 RLENVSVDFPaGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLI----SNASGREL 78
Cdd:PRK10575 13 ALRNVSFRVP-GRTL----LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsSKAFARKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 ----RQHRQRIGMifqhfnlmhtrNVYDNVAFSLR----AAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRV 150
Cdd:PRK10575 88 aylpQQLPAAEGM-----------TVRELVAIGRYpwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 151 GIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGE 225
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-228 |
1.37e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.56 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpaGKTaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:PRK11231 2 TLRTENLTVGY--GTK---RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HrqrIGMIFQHFNLMHTRNVYDNVAF------SL--RAAGKSKAdIAERVPEILALVGLQDKGTAypaQLSGGQKQRVGI 152
Cdd:PRK11231 77 R---LALLPQHHLTPEGITVRELVAYgrspwlSLwgRLSAEDNA-RVNQAMEQTRINHLADRRLT---DLSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 153 ARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG---EVFT 228
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGtpeEVMT 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-224 |
1.79e-27 |
|
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: 107.31 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLlrtINLLQR---PTEGRVFLGDTLISNASGREL 78
Cdd:cd03254 3 IEFENVNFSYDEKKPV----LKDINFSIKPGETVAIVGPTGAGKTTL---INLLMRfydPQKGQILIDGIDIRDISRKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 rqhRQRIGMIFQHFNLMhTRNVYDNVAFslraaGKSKADiAERVPEILALVGLQDKGTAYP-----------AQLSGGQK 147
Cdd:cd03254 76 ---RSMIGVVLQDTFLF-SGTIMENIRL-----GRPNAT-DEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGER 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 148 QRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVrlGITIVLISHEMSVIKSICQRMaVMTGGNIVEEG 224
Cdd:cd03254 146 QLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKIL-VLDDGKIIEEG 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-224 |
7.53e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.07 E-value: 7.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAgktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLrtiNLLQR---PTEGRVFLGDTLISNASGREL 78
Cdd:PRK11160 339 LTLNNVSFTYPD---QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL---QLLTRawdPQQGEILLNGQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQH----RQRIgMIFQHfnlmhtrNVYDNvafsLRAAGKSKADiaERVPEILALVGL-----QDKGTAypA-------QL 142
Cdd:PRK11160 413 RQAisvvSQRV-HLFSA-------TLRDN----LLLAAPNASD--EALIEVLQQVGLeklleDDKGLN--AwlgeggrQL 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 143 SGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSinVRLGITIVLISHEMSVIKSIcQRMAVMTGGNIVE 222
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE--HAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIE 553
|
..
gi 504513067 223 EG 224
Cdd:PRK11160 554 QG 555
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-200 |
1.41e-26 |
|
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: 109.76 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGktaqSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQh 81
Cdd:TIGR02868 335 LELRDLSAGYPGA----PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqRIGMIFQHFNLMHTrNVYDNVAFS------------LRAAGKskADIAERVPEilalvGLQDKGTAYPAQLSGGQKQR 149
Cdd:TIGR02868 410 --RVSVCAQDAHLFDT-TVRENLRLArpdatdeelwaaLERVGL--ADWLRALPD-----GLDTVLGEGGARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504513067 150 VGIARAIANHPEVLLCDEPTSALDLETSASILALLKSinVRLGITIVLISH 200
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLA--ALSGRTVVLITH 528
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-228 |
1.97e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 108.39 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELrq 80
Cdd:PRK09536 3 MIDVSDLSVEF-----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 hRQRIGMIFQHFNLMHTRNVYDNVAFSL-----RAAGKSKADIAErVPEILALVGLqdkgTAYPAQ----LSGGQKQRVG 151
Cdd:PRK09536 76 -SRRVASVPQDTSLSFEFDVRQVVEMGRtphrsRFDTWTETDRAA-VERAMERTGV----AQFADRpvtsLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 152 IARAIANHPEVLLCDEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG---EVFT 228
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGppaDVLT 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-218 |
3.83e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 104.69 E-value: 3.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 21 AVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGrelrQHRQRIGMI--FQHFNLMHTR 98
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG----HQIARMGVVrtFQHVRLFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 99 NVYDN--VA-------------FSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVL 163
Cdd:PRK11300 96 TVIENllVAqhqqlktglfsglLKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 164 LCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGG 218
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-225 |
5.87e-26 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 108.20 E-value: 5.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLgdtlisnaSGRELRQH 81
Cdd:TIGR01842 317 LSVENVTIVPPGGKK---PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRL--------DGADLKQW 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQR-----IGMIFQHFNLMhtrnvydnvafslraAGKSKADIA--------ERVPEILALVGLQDKGTAYP--------- 139
Cdd:TIGR01842 386 DREtfgkhIGYLPQDVELF---------------PGTVAENIArfgenadpEKIIEAAKLAGVHELILRLPdgydtvigp 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 140 --AQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSIcQRMAVMTG 217
Cdd:TIGR01842 451 ggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCV-DKILVLQD 528
|
....*...
gi 504513067 218 GNIVEEGE 225
Cdd:TIGR01842 529 GRIARFGE 536
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-223 |
2.70e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.88 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 3 RLENVSVDFPAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH- 81
Cdd:COG3845 259 EVENLSVRDDRGVPA----LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 -------RQRIGMIfQHFNLMHtrNV----YDNVAFS-----LRAAGKSKAD--IAE---RVPEILALVGLqdkgtaypa 140
Cdd:COG3845 335 vayipedRLGRGLV-PDMSVAE--NLilgrYRRPPFSrggflDRKAIRAFAEelIEEfdvRTPGPDTPARS--------- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 141 qLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLksinVRL---GITIVLISHEMSVIKSICQRMAVMTG 217
Cdd:COG3845 403 -LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRL----LELrdaGAAVLLISEDLDEILALSDRIAVMYE 477
|
....*.
gi 504513067 218 GNIVEE 223
Cdd:COG3845 478 GRIVGE 483
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-242 |
3.96e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 106.34 E-value: 3.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPagkTAQSRAV-NNVNLTIQQGEVFGIVGTSGAGKSTLlrtINLLQR---PTEGRVFLgdtlisnaSGRE 77
Cdd:TIGR00958 479 IEFQDVSFSYP---NRPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTV---AALLQNlyqPTGGQVLL--------DGVP 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 78 LRQ------HRQrIGMIFQHFNLMhTRNVYDNVAFSLR---------AAGKSKAD--IAERVPEILALVGlqDKGTaypa 140
Cdd:TIGR00958 545 LVQydhhylHRQ-VALVGQEPVLF-SGSVRENIAYGLTdtpdeeimaAAKAANAHdfIMEFPNGYDTEVG--EKGS---- 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 141 QLSGGQKQRVGIARAIANHPEVLLCDEPTSALDletsASILALLKSINVRLGITIVLISHEMSVIKSiCQRMAVMTGGNI 220
Cdd:TIGR00958 617 QLSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
250 260
....*....|....*....|..
gi 504513067 221 VEEGEvFTIFSAPQHAYtKQLV 242
Cdd:TIGR00958 692 VEMGT-HKQLMEDQGCY-KHLV 711
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-220 |
4.18e-25 |
|
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: 101.01 E-value: 4.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPagKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLlrtINLLQR---PTEGRVFLGDTLISNASGREL 78
Cdd:cd03248 12 VKFQNVTFAYP--TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTV---VALLENfyqPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 rqHRQrIGMIFQHFNLMhTRNVYDNVAFSL---------RAAGKSKAD--IAERVPEILALVGlqDKGtaypAQLSGGQK 147
Cdd:cd03248 87 --HSK-VSLVGQEPVLF-ARSLQDNIAYGLqscsfecvkEAAQKAHAHsfISELASGYDTEVG--EKG----SQLSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513067 148 QRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLgiTIVLISHEMSVIKSiCQRMAVMTGGNI 220
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
20-224 |
5.03e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.87 E-value: 5.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 20 RAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNasgreLRQH-RQRIGM--------IFQ 90
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH-----LPMHkRARLGIgylpqeasIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 91 hfNLmhtrNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQD--KGTAYpaQLSGGQKQRVGIARAIANHPEVLLCDEP 168
Cdd:COG1137 92 --KL----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHlrKSKAY--SLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 169 TSALDLETSASILALLKSINVRlGITiVLIS-HEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:COG1137 164 FAGVDPIAVADIQKIIRHLKER-GIG-VLITdHNVRETLGICDRAYIISEGKVLAEG 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-206 |
2.11e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 103.73 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVflgdtlisnasgrelrq 80
Cdd:COG4178 362 ALALEDLTLRTPDGRPL----LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI----------------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 hrqrigmifqhfnlmhTRNVYDNVAF----------SLRAA---GKSKADIA-ERVPEILALVGLQ------DKGTAYPA 140
Cdd:COG4178 421 ----------------ARPAGARVLFlpqrpylplgTLREAllyPATAEAFSdAELREALEAVGLGhlaerlDEEADWDQ 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 141 QLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSinvRL-GITIVLISHEMSVIK 206
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE---ELpGTTVISVGHRSTLAA 548
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
18-224 |
2.68e-24 |
|
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: 98.75 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 18 QSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGrelrQHRQRIG--------MIF 89
Cdd:TIGR03410 12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPP----HERARAGiayvpqgrEIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 90 QHFNlmhtrnVYDNVAFSLRAAGKSKADIAERVPEIL-ALVGLQD-KGtaypAQLSGGQKQRVGIARAIANHPEVLLCDE 167
Cdd:TIGR03410 88 PRLT------VEENLLTGLAALPRRSRKIPDEIYELFpVLKEMLGrRG----GDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 168 PTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASG 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-207 |
3.08e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.69 E-value: 3.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 21 AVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVflgdtlisnasgreLRQHRQRIGMIFQHFNLMHT--R 98
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV--------------RRAGGARVAYVPQRSEVPDSlpL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 99 NVYDNVAFSL----RAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDL 174
Cdd:NF040873 73 TVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|...
gi 504513067 175 ETSASILALLKSInVRLGITIVLISHEMSVIKS 207
Cdd:NF040873 153 ESRERIIALLAEE-HARGATVVVVTHDLELVRR 184
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-224 |
3.11e-24 |
|
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: 98.33 E-value: 3.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASgreLRQH 81
Cdd:cd03244 3 IEFKNVSLRYRPNLPP---VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQhfnlmhtrnvyDNVAFS--LRA---AGKSKADiaERVPEILALVGLQDKGTAYP-----------AQLSGG 145
Cdd:cd03244 77 RSRISIIPQ-----------DPVLFSgtIRSnldPFGEYSD--EELWQALERVGLKEFVESLPggldtvveeggENLSVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 146 QKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSinVRLGITIVLISHEMSVIKSiCQRMAVMTGGNIVEEG 224
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-205 |
8.40e-24 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 98.26 E-value: 8.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVflgdtlisnasgreLRQ 80
Cdd:PRK09544 4 LVSLENVSVSF-----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------------KRN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVAFSLRAaGKSKADIAERVPEILALVGLQdkgtaYPAQ-LSGGQKQRVGIARAIANH 159
Cdd:PRK09544 65 GKLRIGYVPQKLYLDTTLPLTVNRFLRLRP-GTKKEDILPALKRVQAGHLID-----APMQkLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVI 205
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
22-224 |
1.21e-23 |
|
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: 96.08 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTIN--LLQRPTEGRVFLgdtlisNASGRELRQHRQRIGMIFQHFNLMHTRN 99
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLI------NGRPLDKRSFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 100 VYDNVAFSLRAAGkskadiaervpeilalvglqdkgtaypaqLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSAS 179
Cdd:cd03213 99 VRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504513067 180 ILALLKSInVRLGITIVLISHEMS-VIKSICQRMAVMTGGNIVEEG 224
Cdd:cd03213 150 VMSLLRRL-ADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-244 |
2.08e-23 |
|
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: 100.97 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 19 SRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQHRQRI--------GMIFQ 90
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLpqepyifsGSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 91 HFNLMHTRNV-YDNVAFSLRAAgKSKADIaERVPEilalvGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPT 169
Cdd:TIGR01193 567 NLLLGAKENVsQDEIWAACEIA-EIKDDI-ENMPL-----GYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 170 SALDLETSASILALLKSINVRlgiTIVLISHEMSVIKSIcQRMAVMTGGNIVEEGEVFTIFSapQHAYTKQLVSH 244
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLD--RNGFYASLIHN 708
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-206 |
2.52e-23 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 96.18 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 18 QSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTI--NLLQRPTEGRVFLGDtlisNASGRElrqhrqrigmifqhfnlm 95
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPD----NQFGRE------------------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 96 htRNVYDNVAfslraagkSKADIAERVpEILALVGLQDkgtAY-----PAQLSGGQKQRVGIARAIANHPEVLLCDEPTS 170
Cdd:COG2401 100 --ASLIDAIG--------RKGDFKDAV-ELLNAVGLSD---AVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 504513067 171 ALDLETSASILALLKSINVRLGITIVLISHEMSVIK 206
Cdd:COG2401 166 HLDRQTAKRVARNLQKLARRAGITLVVATHHYDVID 201
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-218 |
3.52e-23 |
|
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: 95.23 E-value: 3.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTI--NLlqRPTEGRVFLGDTL--------IS 71
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgEL--EKLSGSVSVPGSIayvsqepwIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 72 NASGRElrqhrqriGMIF-QHFNlmHTRnvYDNVafsLRAAGKSKaDIaERVPE-ILALVGlqDKGTAypaqLSGGQKQR 149
Cdd:cd03250 79 NGTIRE--------NILFgKPFD--EER--YEKV---IKACALEP-DL-EILPDgDLTEIG--EKGIN----LSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513067 150 VGIARAIANHPEVLLCDEPTSALDLETSASIL--ALLKsiNVRLGITIVLISHEMSVIKSiCQRMAVMTGG 218
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIFenCILG--LLLNNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-223 |
4.78e-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: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 3 RLENVSVDfpagktaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH- 81
Cdd:COG1129 258 EVEGLSVG---------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAg 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 -------RQRIGmifqhfnLMHTRNVYDNVAF-SLRAAGK----SKADIAERVPEILALVGLQdkgTAYPAQ----LSGG 145
Cdd:COG1129 329 iayvpedRKGEG-------LVLDLSIRENITLaSLDRLSRggllDRRRERALAEEYIKRLRIK---TPSPEQpvgnLSGG 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513067 146 QKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEE 223
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMREGRIVGE 475
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-200 |
7.19e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.98 E-value: 7.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 4 LENVSVDFPAgktaqsRAV-NNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFlgdtlisnasgrelRQHR 82
Cdd:COG0488 1 LENLSKSFGG------RPLlDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS--------------IPKG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 83 QRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAE--------------------------------RVPEILALVG 130
Cdd:COG0488 61 LRIGYLPQEPPLDDDLTVLDTVLDGDAELRALEAELEEleaklaepdedlerlaelqeefealggweaeaRAEEILSGLG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513067 131 L-QDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLEtsaSILAL---LKSINvrlgITIVLISH 200
Cdd:COG0488 141 FpEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE---SIEWLeefLKNYP----GTVLVVSH 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
24-242 |
8.66e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 95.82 E-value: 8.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQhrqRIGMIFQHFNLMHTRNVYDN 103
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR---RIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 104 VA---------FSlraagKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDL 174
Cdd:PRK10253 102 VArgryphqplFT-----RWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513067 175 ETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGevftifsAPQHAYTKQLV 242
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELI 237
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-261 |
1.60e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 97.93 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAgktaqSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ 80
Cdd:PRK09700 5 YISMAGIGKSFGP-----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 hrQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGK-------SKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIA 153
Cdd:PRK09700 80 --LGIGIIYQELSVIDELTVLENLYIGRHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 154 RAIANHPEVLLCDEPTSALdleTSASILALLKSINvRL---GITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVftif 230
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMN-QLrkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMV---- 229
|
250 260 270
....*....|....*....|....*....|.
gi 504513067 231 sapQHAYTKQLVSHTTPVELPDRFKKNNKGV 261
Cdd:PRK09700 230 ---SDVSNDDIVRLMVGRELQNRFNAMKENV 257
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
2-200 |
2.16e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 94.14 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDfpagktaqSRaVNNVNLTIQQGEVFGIVGTSGAGKSTLL-RTINLLqrPTEGRVFLGDTLISNASGRELRQ 80
Cdd:COG4138 1 LQLNDVAVA--------GR-LGPISAQVNAGELIHLIGPNGAGKSTLLaRMAGLL--PGQGEILLNGRPLSDWSAAELAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRqriGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAErVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIAN-H 159
Cdd:COG4138 70 HR---AYLSQQQSPPFAMPVFQYLALHQPAGASSEAVEQL-LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvW 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504513067 160 PEV------LLCDEPTSALDLETSASILALLKSInVRLGITIVLISH 200
Cdd:COG4138 146 PTInpegqlLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSH 191
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-224 |
2.35e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 92.38 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAgktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGrelrQH 81
Cdd:cd03247 1 LSINNVSFSYPE---QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK----AL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQHFNLMHTrNVYDNVAfslraagkskadiaervpeilalvglqdkgtaypAQLSGGQKQRVGIARAIANHPE 161
Cdd:cd03247 74 SSLISVLNQRPYLFDT-TLRNNLG----------------------------------RRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSinVRLGITIVLISHEMSVIKSIcQRMAVMTGGNIVEEG 224
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFE--VLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
9-206 |
3.41e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.24 E-value: 3.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 9 VDFPAGKTaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGrelRQHRQRIGMI 88
Cdd:PRK10247 13 VGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP---EIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 89 FQHFNLMhTRNVYDNVAFSLRAagKSKADIAERVPEILALVGLQDKGTAYP-AQLSGGQKQRVGIARAIANHPEVLLCDE 167
Cdd:PRK10247 87 AQTPTLF-GDTVYDNLIFPWQI--RNQQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 504513067 168 PTSALDLETSASILALLKSINVRLGITIVLISHEMSVIK 206
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEIN 202
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-236 |
3.81e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 97.43 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 18 QSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTinLLQRPTEGRVFLGDTLIsNASGRELRQHRQRIGMIFQHFNLMHT 97
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNA--LAFRSPKGVKGSGSVLL-NGMPIDAKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 98 RNVYDNVAFS--LR-AAGKSKADIAERVPEILALVGL---QDKGTAYPAQ---LSGGQKQRVGIARAIANHPEVLLCDEP 168
Cdd:TIGR00955 114 LTVREHLMFQahLRmPRRVTKKEKRERVDEVLQALGLrkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513067 169 TSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGevftifsAPQHA 236
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG-------SPDQA 254
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-202 |
5.68e-22 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 93.07 E-value: 5.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 25 VNLTIQQGEVFGIVGTSGAGKSTLL-RTINLLqrPTEGRVFLGDTLISNASGRELRQHR----QRIGMIFqhfnLMHtrn 99
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLaRMAGLL--PGSGSIQFAGQPLEAWSAAELARHRaylsQQQTPPF----AMP--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 100 VYDNVAFSLrAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAI-----ANHPE--VLLCDEPTSAL 172
Cdd:PRK03695 86 VFQYLTLHQ-PDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSL 164
|
170 180 190
....*....|....*....|....*....|
gi 504513067 173 DLETSASILALLKSInVRLGITIVLISHEM 202
Cdd:PRK03695 165 DVAQQAALDRLLSEL-CQQGIAVVMSSHDL 193
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-222 |
9.78e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 9.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPaGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLisnasgrelrq 80
Cdd:COG0488 315 VLELEGLSKSYG-DKTL----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 hrqRIGMIFQHF-NLMHTRNVYDNVafslraagkskADIAERVPE--ILALVGL----QDKGTAYPAQLSGGQKQRVGIA 153
Cdd:COG0488 379 ---KIGYFDQHQeELDPDKTVLDEL-----------RDGAPGGTEqeVRGYLGRflfsGDDAFKPVGVLSGGEKARLALA 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 154 RAIANHPEVLLCDEPTSALDLETSASILALLKSINvrlGiTIVLISHEMSVIKSICQRMAVMTGGNIVE 222
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-224 |
1.25e-21 |
|
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: 96.24 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 12 PAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNasgrELRQHRQRIGMIFQH 91
Cdd:TIGR01257 940 PSGRPA----VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQSLGMCPQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 92 FNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSA 171
Cdd:TIGR01257 1012 NILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504513067 172 LDLETSASILALLksINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:TIGR01257 1092 VDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-218 |
1.32e-21 |
|
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: 89.04 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTaqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLisnasgrelrqh 81
Cdd:cd03221 1 IELENLSKTYGGKLL-----LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqRIGmifqhfnlmhtrnvydnvafslraagkskadiaervpeilalvglqdkgtaYPAQLSGGQKQRVGIARAIANHPE 161
Cdd:cd03221 64 --KIG---------------------------------------------------YFEQLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 162 VLLCDEPTSALDLETSASILALLKSINvrlgITIVLISHEMSVIKSICQRMAVMTGG 218
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEYP----GTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-200 |
4.37e-21 |
|
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: 89.47 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 25 VNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVflgdtLISNASGRELRQHRQRIGMIFQHFNLMHTR-NVYDN 103
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV-----LLNGGPLDFQRDSIARGLLYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 104 VAFsLRAAGKSkadiaERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILAL 183
Cdd:cd03231 94 LRF-WHADHSD-----EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|....*..
gi 504513067 184 LKSINVRLGItIVLISH 200
Cdd:cd03231 168 MAGHCARGGM-VVLTTH 183
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-200 |
4.87e-21 |
|
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: 89.34 E-value: 4.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 20 RAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISnasgrELRQHRQRIGMIFQHFNLMHTR- 98
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHENILYLGHLPGLKPEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 99 NVYDNVAFSLRAAGKSKADIAErvpeILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSA 178
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTIED----ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|..
gi 504513067 179 SILALLKSINVRLGITIvLISH 200
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVL-LTTH 185
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-224 |
8.39e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 93.37 E-value: 8.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKtaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLrtiNLLQrpteGrvFL---GDTLISnasGREL 78
Cdd:PRK11174 350 IEAEDLEILSPDGK----TLAGPLNFTLPAGQRIALVGPSGAGKTSLL---NALL----G--FLpyqGSLKIN---GIEL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 R-----QHRQRIGMIFQHFNLMHTrNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYP-----AQLSGGQKQ 148
Cdd:PRK11174 414 ReldpeSWRKHLSWVGQNPQLPHG-TLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPigdqaAGLSVGQAQ 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 149 RVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSInvRLGITIVLISHEMSVIKSiCQRMAVMTGGNIVEEG 224
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA--SRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-173 |
2.76e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 92.11 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 21 AVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFL-GDTLisNASGRELRQhrqRIGMIFQHFNLMHTRN 99
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfGQPV--DAGDIATRR---RVGYMSQAFSLYGELT 355
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513067 100 VYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALD 173
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
24-184 |
5.13e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.47 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDtlisnaSGRELRQHRQRIGMIfQHFNLMH-TRNVYD 102
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG------GDIDDPDVAEACHYL-GHRNAMKpALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 103 NVAFSLRAAGKSKADIAervpEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILA 182
Cdd:PRK13539 93 NLEFWAAFLGGEELDIA----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE 168
|
..
gi 504513067 183 LL 184
Cdd:PRK13539 169 LI 170
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-224 |
5.98e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.46 E-value: 5.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPagkTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLlrtINLLQR---PTEGRVFLgdtlisnaSGREL 78
Cdd:PRK11176 342 IEFRNVTFTYP---GKEVPALRNINFKIPAGKTVALVGRSGSGKSTI---ANLLTRfydIDEGEILL--------DGHDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQH-----RQRIGMIFQHFNLMHTrNVYDNVAFslrAAGK--SKADI--AERVPEILALVGLQDKG--TAYP---AQLSG 144
Cdd:PRK11176 408 RDYtlaslRNQVALVSQNVHLFND-TIANNIAY---ARTEqySREQIeeAARMAYAMDFINKMDNGldTVIGengVLLSG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 145 GQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSInvRLGITIVLISHEMSVIKSiCQRMAVMTGGNIVEEG 224
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-248 |
3.79e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.18 E-value: 3.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 25 VNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASgrELRQHRQRIGMIFQHFNLMHTRNVYDNV 104
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT--PAKAHQLGIYLVPQEPLLFPNLSVKENI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 105 AFSLRAagksKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALdleTSASILALL 184
Cdd:PRK15439 108 LFGLPK----RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL---TPAETERLF 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 185 KSIN--VRLGITIVLISHEMSVIKSICQRMAVMTGGNIVeegevftiFSAPQHAYTK-QLVSHTTPV 248
Cdd:PRK15439 181 SRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA--------LSGKTADLSTdDIIQAITPA 239
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-206 |
1.84e-18 |
|
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: 81.43 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINllqrptegrvflgdtlisnasgrELRQH 81
Cdd:cd03223 1 IELENLSLATPDGRVL----LKDLSFEIKPGDRLLITGPSGTGKSSLFRALA-----------------------GLWPW 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQ-RIGMifqhfnlmHTRNvydNVAF----------SLRaagkskadiaervpEILAlvglqdkgtaYP--AQLSGGQKQ 148
Cdd:cd03223 54 GSgRIGM--------PEGE---DLLFlpqrpylplgTLR--------------EQLI----------YPwdDVLSGGEQQ 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504513067 149 RVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSinvrLGITIVLISHEMSVIK 206
Cdd:cd03223 99 RLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE----LGITVISVGHRPSLWK 152
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-224 |
2.35e-18 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 82.07 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGktaQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNAsgrELRQH 81
Cdd:cd03369 7 IEVENLSVRYAPD---LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQhfnlmhtrnvyDNVAFSlrAAGKSKADIAERVP--EILALVGLQDKGTaypaQLSGGQKQRVGIARAIANH 159
Cdd:cd03369 81 RSSLTIIPQ-----------DPTLFS--GTIRSNLDPFDEYSdeEIYGALRVSEGGL----NLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 160 PEVLLCDEPTSALDLETSASIlalLKSINVRL-GITIVLISHEMSVIKSiCQRMAVMTGGNIVEEG 224
Cdd:cd03369 144 PRVLVLDEATASIDYATDALI---QKTIREEFtNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-232 |
2.35e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.39 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVflgdTLISNASGRELRQH 81
Cdd:PRK15056 7 IVVNDVTVTWRNGHTA----LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI----SILGQPTRQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RqrIGMIFQHFNL------------MHTRnvYDNVAFSLRAagksKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQR 149
Cdd:PRK15056 79 L--VAYVPQSEEVdwsfpvlvedvvMMGR--YGHMGWLRRA----KKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 150 VGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQrMAVMTGGNIVEEGEVFTI 229
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETT 228
|
...
gi 504513067 230 FSA 232
Cdd:PRK15056 229 FTA 231
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-281 |
2.42e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 85.55 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 4 LENVSVDFPAGKtaqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQHrq 83
Cdd:PRK10982 1 MSNISKSFPGVK-----ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALEN-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 84 RIGMIFQHFNLMHTRNVYDNV---AFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHP 160
Cdd:PRK10982 74 GISMVHQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVftifsapQHAYTKQ 240
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPL-------AGLTMDK 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 504513067 241 LVSHTTPVELPDRF-KKNN--KGVLLKILFAdDSVEQPILSDVA 281
Cdd:PRK10982 226 IIAMMVGRSLTQRFpDKENkpGEVILEVRNL-TSLRQPSIRDVS 268
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-222 |
3.38e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.35 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 3 RLENVSVDFPAgktaqSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGdtlisnasGRELRQHR 82
Cdd:PRK11288 6 SFDGIGKTFPG-----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID--------GQEMRFAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 83 QR------IGMIFQHFNLMHTRNVYDNV---AFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIA 153
Cdd:PRK11288 73 TTaalaagVAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513067 154 RAIANHPEVLLCDEPTSALdletSASILALLKSINVRL---GITIVLISHEMSVIKSICQRMAVMTGGNIVE 222
Cdd:PRK11288 153 KALARNARVIAFDEPTSSL----SAREIEQLFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-206 |
4.42e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.47 E-value: 4.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAQsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTliSNASGRELRQH 81
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVE--IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS--HNLKDINLKWW 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQHfNLMHTRNVYDNVAFSLRA--------------AGKSKADIAER-------------------------- 121
Cdd:PTZ00265 459 RSKIGVVSQD-PLLFSNSIKNNIKYSLYSlkdlealsnyynedGNDSQENKNKRnscrakcagdlndmsnttdsneliem 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 122 -----------VPEILALVGLQDKGTAYP-----------AQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDletSAS 179
Cdd:PTZ00265 538 rknyqtikdseVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD---NKS 614
|
250 260 270
....*....|....*....|....*....|.
gi 504513067 180 ILALLKSINVRLG----ITIVlISHEMSVIK 206
Cdd:PTZ00265 615 EYLVQKTINNLKGnenrITII-IAHRLSTIR 644
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-224 |
7.37e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.48 E-value: 7.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 20 RAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRElrQHRQRIGMIFQHFNLMHTRN 99
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 100 VYDNVAFSLRA----AGKSKADIAERVPEILALVGLQDkgtAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLE 175
Cdd:PRK10895 95 VYDNLMAVLQIrddlSAEQREDRANELMEEFHIEHLRD---SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504513067 176 TSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIVEEG 224
Cdd:PRK10895 172 SVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHG 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-223 |
1.18e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRE--------LRQHRQRIGMifqHFNLM 95
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlarglvyLPEDRQSSGL---YLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 96 HTRNV----YDNVAFSLRAAGKSKadIAERVPEILalvGLQDKGTAYPAQ-LSGGQKQRVGIARAIANHPEVLLCDEPTS 170
Cdd:PRK15439 358 LAWNVcaltHNRRGFWIKPARENA--VLERYRRAL---NIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504513067 171 ALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIVEE 223
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGA 484
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-205 |
3.81e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.69 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGdtlisnasGRELRQHRQRIgmifqHFNLM---HTRNV 100
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ--------GEPIRRQRDEY-----HQDLLylgHQPGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 101 YD------NVAFSLRAAGKSKADiaeRVPEILALVGLQDKGTAYPAQLSGGQKQRVGIAR-AIANHPEVLLcDEPTSALD 173
Cdd:PRK13538 86 KTeltaleNLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARlWLTRAPLWIL-DEPFTAID 161
|
170 180 190
....*....|....*....|....*....|...
gi 504513067 174 LETSASILALLKSiNVRLGITIVLISH-EMSVI 205
Cdd:PRK13538 162 KQGVARLEALLAQ-HAEQGGMVILTTHqDLPVA 193
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-249 |
5.43e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.75 E-value: 5.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASgrELRQHRQRIGMI---------FQHF 92
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS--PLDAVKKGMAYItesrrdngfFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 93 NLmhTRNVydNVAFSLRAAG----------KSKADIAERVPEILAL--VGLQDKGTaypaQLSGGQKQRVGIARAIANHP 160
Cdd:PRK09700 357 SI--AQNM--AISRSLKDGGykgamglfheVDEQRTAENQRELLALkcHSVNQNIT----ELSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTggniveEGEVFTIFSAPQHAYTKQ 240
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFC------EGRLTQILTNRDDMSEEE 501
|
....*....
gi 504513067 241 LVSHTTPVE 249
Cdd:PRK09700 502 IMAWALPQE 510
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-218 |
1.95e-16 |
|
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: 79.87 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 20 RAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLL--QRPTEGRVFLGDTLISNASGRElrQHRQRIGMIFQHFNLMHT 97
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRD--TERAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 98 RNVYDNV----AFSLRAAGKSKADIAERVPEILALVGLQDKGTAYP-AQLSGGQKQRVGIARAIANHPEVLLCDEPTSAL 172
Cdd:TIGR02633 93 LSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504513067 173 DLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGG 218
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-173 |
2.06e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.17 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpaGKTaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGR--VFLGDtlISNASGRELR 79
Cdd:NF033858 2 ARLEGVSHRY--GKT---VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRveVLGGD--MADARHRRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 80 QHR-----QRIGMifqhfNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQ---DKgtayPA-QLSGGQKQRV 150
Cdd:NF033858 75 CPRiaympQGLGK-----NLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLApfaDR----PAgKLSGGMKQKL 145
|
170 180
....*....|....*....|...
gi 504513067 151 GIARAIANHPEVLLCDEPTSALD 173
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVD 168
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-200 |
2.77e-16 |
|
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: 79.46 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASgreLRQH 81
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN---REAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 RQRIGMIFQHFNLmhtrnvydnvaFSlRAAGKSKADIAERVPEILALVGLQDKgTAYPA------QLSGGQKQRVGIARA 155
Cdd:COG4615 405 RQLFSAVFSDFHL-----------FD-RLLGLDGEADPARARELLERLELDHK-VSVEDgrfsttDLSQGQRKRLALLVA 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504513067 156 IANHPEVLLCDEptsaldletSAS-------------ILALLKsinvRLGITIVLISH 200
Cdd:COG4615 472 LLEDRPILVFDE---------WAAdqdpefrrvfyteLLPELK----ARGKTVIAISH 516
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-237 |
2.84e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.84 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpaGKTaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNasGRELRQ 80
Cdd:PRK11614 5 MLSFDKVSAHY--GKI---QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD--WQTAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAgkSKADIAERVPEILALVG-LQDKGTAYPAQLSGGQKQRVGIARAIANH 159
Cdd:PRK11614 78 MREAVAIVPEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIVEE--GEVFTIFSAPQHAY 237
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEdtGDALLANEAVRSAY 234
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-224 |
1.32e-15 |
|
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: 74.10 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTI--NLLQRPTEGRVFLGDTLISNASGRElrqhRQR--IGMIFQH------ 91
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE----RARlgIFLAFQYppeipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 92 -FNLMHTRNVydNVAFslraagkskadiaervpeilalvglqdkgtaypaqlSGGQKQRVGIARAIANHPEVLLCDEPTS 170
Cdd:cd03217 92 vKNADFLRYV--NEGF------------------------------------SGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 171 ALDLEtsaSILALLKSIN--VRLGITIVLISHEMSVIKSI-CQRMAVMTGGNIVEEG 224
Cdd:cd03217 134 GLDID---ALRLVAEVINklREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-201 |
1.34e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 77.70 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAgktaQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH 81
Cdd:PRK10522 323 LELRNVTFAYQD----NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 82 rqrIGMIFQHFNLmhtrnvYDNVafsLRAAGKSKADiaERVPEILALVGLQDK-----GTAYPAQLSGGQKQRVGIARAI 156
Cdd:PRK10522 399 ---FSAVFTDFHL------FDQL---LGPEGKPANP--ALVEKWLERLKMAHKleledGRISNLKLSKGQKKRLALLLAL 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504513067 157 ANHPEVLLCDEPTSALD----LETSASILALLKSinvrLGITIVLISHE 201
Cdd:PRK10522 465 AEERDILLLDEWAADQDphfrREFYQVLLPLLQE----MGKTIFAISHD 509
|
|
| NIL |
smart00930 |
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ... |
260-338 |
1.62e-15 |
|
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: 70.62 E-value: 1.62e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 260 GVLLKILFADDSVEQPILSDVAQQFQVSVNILHGNIEYINDRALGHIIAQISYRDDpaaeNLAAAIAYIRQNTFGVEVI 338
Cdd:smart00930 2 GRLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGDEE----DIEAALAYLREQGVEVEVL 76
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-225 |
1.84e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 77.06 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 17 AQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLrtiNLLQRP---TEGRVFLGDTLISNAsgrELRQHRQRIGMIFQHFN 93
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLL---SLIQRHfdvSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 94 LMhTRNVYDNVAFSLRAAGKSKADIAERVP----EILAL-VGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEP 168
Cdd:PRK10789 400 LF-SDTVANNIALGRPDATQQEIEHVARLAsvhdDILRLpQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 169 TSALDLETSASILALLKSInvRLGITIVLISHEMSVIKSiCQRMAVMTGGNIVEEGE 225
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQW--GEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGN 532
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-218 |
3.86e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.12 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 20 RAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRtinLLQRPTEGRVFLGDTLISnasGRELRQH------RQRIGMIFQHFN 93
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMK---VLSGVYPHGTYEGEIIFE---GEELQASnirdteRAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 94 LMHTRNVYDNVaF---SLRAAGKSKAD-IAERVPEILALVGLqDKGTAYP-AQLSGGQKQRVGIARAIANHPEVLLCDEP 168
Cdd:PRK13549 93 LVKELSVLENI-FlgnEITPGGIMDYDaMYLRAQKLLAQLKL-DINPATPvGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504513067 169 TSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGG 218
Cdd:PRK13549 171 TASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-211 |
4.84e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.14 E-value: 4.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRV-FLGDTLISnasgrELRQHRQRigmifqhfnlMHTRNVYD 102
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiYEQDLIVA-----RLQQDPPR----------NVEGTVYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 103 NVAFSLRAAGK----------------SKADIAE------------------RVPEILALVGLQdkGTAYPAQLSGGQKQ 148
Cdd:PRK11147 86 FVAEGIEEQAEylkryhdishlvetdpSEKNLNElaklqeqldhhnlwqlenRINEVLAQLGLD--PDAALSSLSGGWLR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513067 149 RVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINvrlGiTIVLISHEMSVIKSICQR 211
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ---G-SIIFISHDRSFIRNMATR 222
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-226 |
7.91e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.04 E-value: 7.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKtaqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTIN-LLQRPTEGRVFLGDTLisNASGRELR 79
Cdd:PRK10762 4 LLQLKGIDKAFPGVK-----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTgIYTRDAGSILYLGKEV--TFNGPKSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 80 QhRQRIGMIFQHFNLMHTRNVYDNV----AFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARA 155
Cdd:PRK10762 77 Q-EAGIGIIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 156 IANHPEVLLCDEPTSAL-DLETSasilALLKSINvRL---GITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEV 226
Cdd:PRK10762 156 LSFESKVIIMDEPTDALtDTETE----SLFRVIR-ELksqGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREV 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-226 |
1.54e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.18 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 25 VNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFL-GDTLISNASGRELRQ-------HRQRIGMIfqhfnlmH 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdGKPIDIRSPRDAIRAgimlcpeDRKAEGII-------P 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 97 TRNVYDNVAFSLRAA---------GKSKADIAERVPEILALvglqdkGTAYPAQ----LSGGQKQRVGIARAIANHPEVL 163
Cdd:PRK11288 345 VHSVADNINISARRHhlragclinNRWEAENADRFIRSLNI------KTPSREQlimnLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513067 164 LCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIVeeGEV 226
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA--GEL 478
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-224 |
2.20e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.98 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKtaqsRAVNNVNLTIQQGEVFGIVGTSGAGKSTLlrtINLLQ---RPTEGRVFLGDTLISNASGREL 78
Cdd:PRK10790 341 IDIDNVSFAYRDDN----LVLQNINLSVPSRGFVALVGHTGSGKSTL---ASLLMgyyPLTEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQHrqrIGMIFQHFNLMhTRNVYDNVAFslraaGKskaDIAE-RVPEILALVGLQDKGTAYPA-----------QLSGGQ 146
Cdd:PRK10790 414 RQG---VAMVQQDPVVL-ADTFLANVTL-----GR---DISEeQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513067 147 KQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSInvRLGITIVLISHEMSVIKSiCQRMAVMTGGNIVEEG 224
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQG 556
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-205 |
3.02e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.99 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 15 KTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTinLLQRPTEGRVFLGDTLISnasGRELRQHRQR-IGMIFQHFN 93
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNV--LAERVTTGVITGGDRLVN---GRPLDSSFQRsIGYVQQQDL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 94 LMHTRNVYDNVAFS--LRAAG----KSKADIAERVPEIL-------ALVGLQDKGtaypaqLSGGQKQRVGIARAIANHP 160
Cdd:TIGR00956 847 HLPTSTVRESLRFSayLRQPKsvskSEKMEYVEEVIKLLemesyadAVVGVPGEG------LNVEQRKRLTIGVELVAKP 920
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504513067 161 EVLL-CDEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVI 205
Cdd:TIGR00956 921 KLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPSAI 965
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-222 |
3.24e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.29 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 20 RAVNNVNLTIQQGEVFGIVGTSGAGKSTLLrtiNLLQ--RPT---EGR-VFLGDTlisnASGRELRQHRQR-IGMIFQHF 92
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLM---KVLSgvYPHgsyEGEiLFDGEV----CRFKDIRDSEALgIVIIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 93 NLMHTRNVYDNVAFSLRAAGKSKADIAE---RVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPT 169
Cdd:NF040905 88 ALIPYLSIAENIFLGNERAKRGVIDWNEtnrRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504513067 170 SALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIVE 222
Cdd:NF040905 168 AALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-202 |
6.76e-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: 70.05 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELR-QHRQRIGMIFQHFNLMHTrNV 100
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsRNRYSVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 101 YDNVAFSL---RAAGKSKADIAERVPEI-LALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLET 176
Cdd:cd03290 96 EENITFGSpfnKQRYKAVTDACSLQPDIdLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190
....*....|....*....|....*....|.
gi 504513067 177 S-----ASILALLKSiNVRlgiTIVLISHEM 202
Cdd:cd03290 176 SdhlmqEGILKFLQD-DKR---TLVLVTHKL 202
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-218 |
7.87e-14 |
|
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: 72.74 E-value: 7.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAgktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFL-GDTLISNASgrelr 79
Cdd:TIGR01257 1937 ILRLNELTKVYSG---TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSILTNIS----- 2008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 80 QHRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANH 159
Cdd:TIGR01257 2009 DVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 160 PEVLLCDEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGG 218
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-234 |
1.22e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.57 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRE--------LRQHRQRIGMIF---- 89
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDRKRDGLVLgmsv 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 90 -QHFNLMHTRNvYDNVAFSLRAAGKSKA--DIAE----RVPEILALVGLqdkgtaypaqLSGGQKQRVGIARAIANHPEV 162
Cdd:PRK10762 348 kENMSLTALRY-FSRAGGSLKHADEQQAvsDFIRlfniKTPSMEQAIGL----------LSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513067 163 LLCDEPTSALDLETSASILALlksINV--RLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEgevFTIFSAPQ 234
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQL---INQfkAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGE---FTREQATQ 484
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-203 |
1.56e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.45 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 15 KTAQSRAV-NNVNLTIQQGEVFGIVGTSGAGKSTLLrtiNLLQRPTEGRVFLGDTLISNasGRELRQHRQRIGMIFQHFN 93
Cdd:PLN03211 76 RQIQERTIlNGVTGMASPGEILAVLGPSGSGKSTLL---NALAGRIQGNNFTGTILANN--RKPTKQILKRTGFVTQDDI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 94 LMHTRNVYDNVAF-SLRAAGKS-----KADIAERVPEILALVGLQDK--GTAYPAQLSGGQKQRVGIARAIANHPEVLLC 165
Cdd:PLN03211 151 LYPHLTVRETLVFcSLLRLPKSltkqeKILVAESVISELGLTKCENTiiGNSFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190
....*....|....*....|....*....|....*...
gi 504513067 166 DEPTSALDLETSASILALLKSINVRlGITIVLISHEMS 203
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPS 267
|
|
| NIL |
pfam09383 |
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ... |
261-337 |
1.78e-13 |
|
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: 64.78 E-value: 1.78e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 261 VLLKILFADDSVEQPILSDVAQQFQVSVNILHGNIEYINDRALGHIIAQISYRDDpaaeNLAAAIAYIRQNTFGVEV 337
Cdd:pfam09383 1 RLVRLTFPGESADEPVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELPGDPE----QIEAALAYLREQGVEVEV 73
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-224 |
1.97e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.94 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 23 NNVNLTIQQGEVFGIVGTSGAGKSTLLRTI--NLLQRPTEGRVFLGDTLISNASGRElrqhRQR--IGMIFQH------- 91
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDE----RARagIFLAFQYpveipgv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 92 --FNLMHTrnvydnvafSLRAAGKSKADIAE---RVPEILALVGLQDK--------GtaypaqLSGGQKQRVGIARAIAN 158
Cdd:COG0396 93 svSNFLRT---------ALNARRGEELSAREflkLLKEKMKELGLDEDfldryvneG------FSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 159 HPEVLLCDEPTSALDLEtSASILAllKSINvRL---GITIVLISHEMSVIKSI-CQRMAVMTGGNIVEEG 224
Cdd:COG0396 158 EPKLAILDETDSGLDID-ALRIVA--EGVN-KLrspDRGILIITHYQRILDYIkPDFVHVLVDGRIVKSG 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-201 |
4.81e-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: 69.58 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLisnasgrelrqhrqRIGMIFQ-HFNLMHTRNV 100
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV--------------KLAYVDQsRDALDPNKTV 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 101 YDNVAFSLRAAGKSKADIAERvpeilALVGL-------QDKgtaYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALD 173
Cdd:TIGR03719 404 WEEISGGLDIIKLGKREIPSR-----AYVGRfnfkgsdQQK---KVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
170 180
....*....|....*....|....*...
gi 504513067 174 LETsasILALLKSINVRLGITIVlISHE 201
Cdd:TIGR03719 476 VET---LRALEEALLNFAGCAVV-ISHD 499
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-226 |
6.53e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 69.53 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 21 AVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFL--GDTLISNASGrelrQHRQRIGMifqhfnlmhtr 98
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkgSAALIAISSG----LNGQLTGI----------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 99 nvyDNVAFSLRAAGKSKADIAERVPEILALVGLqDKGTAYPAQ-LSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETS 177
Cdd:PRK13545 104 ---ENIELKGLMMGLTKEKIKEIIPEIIEFADI-GKFIYQPVKtYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504513067 178 ASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEV 226
Cdd:PRK13545 180 KKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDI 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-220 |
6.87e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.08 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKtaQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTI-NLLQRPTEGRVFL-GDTLISNASGREL 78
Cdd:TIGR02633 257 ILEARNLTCWDVINP--HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFInGKPVDIRNPAQAI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQ-------HRQRIGMIFQhfnlmhtRNVYDNVAFSL--RAAGKSKADIAERVPEILALVGLQDKGTAYP----AQLSGG 145
Cdd:TIGR02633 335 RAgiamvpeDRKRHGIVPI-------LGVGKNITLSVlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 146 QKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGGNI 220
Cdd:TIGR02633 408 NQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQL-AQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
3-226 |
7.44e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 67.53 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 3 RLENVSVDFPAGKTAQsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGrvflgdtlisnasgrELRQHR 82
Cdd:PRK13546 23 RMKDALIPKHKNKTFF--ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG---------------KVDRNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 83 QrIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEV 162
Cdd:PRK13546 86 E-VSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513067 163 LLCDEPTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEV 226
Cdd:PRK13546 165 LVIDEALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGEL 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-220 |
1.08e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 20 RAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTI-NLLQRPTEGRVFL-GDTLISNASGRELRQH-------RQRIGMIfq 90
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIdGKPVKIRNPQQAIAQGiamvpedRKRDGIV-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 91 hfNLMhtrNVYDNVAFSL--RAAGKSKADIAERVPEILALVGLQDKGTAYP----AQLSGGQKQRVGIARAIANHPEVLL 164
Cdd:PRK13549 354 --PVM---GVGKNITLAAldRFTGGSRIDDAAELKTILESIQRLKVKTASPelaiARLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 165 CDEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGGNI 220
Cdd:PRK13549 429 LDEPTRGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
17-226 |
2.23e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 67.07 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 17 AQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISN--ASGRELRQHRQ-RIGMifqhfn 93
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANrrALRRTIG*HRPvR*GR------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 94 lMHTRNVYDNVAFSLRAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALD 173
Cdd:NF000106 98 -RESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504513067 174 LETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEV 226
Cdd:NF000106 177 PRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-206 |
2.53e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 23 NNVNLTIQQGEVFGIVGTSGAGKSTLLRTINllqrpteGRVFLGDTLISNASGRELRQHRQRIGMIFQHFNLmhtrNVYD 102
Cdd:PTZ00265 1246 EEQNVGMKNVNEFSLTKEGGSGEDSTVFKNS-------GKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNM----SIYE 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 103 NVAFSLRAAGKSKADIAERVPEILALV-GLQDKGTA----YPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETS 177
Cdd:PTZ00265 1315 NIKFGKEDATREDVKRACKFAAIDEFIeSLPNKYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1394
|
170 180
....*....|....*....|....*....
gi 504513067 178 ASILALLKSINVRLGITIVLISHEMSVIK 206
Cdd:PTZ00265 1395 KLIEKTIVDIKDKADKTIITIAHRIASIK 1423
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-201 |
2.86e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 4 LENVSVDFPaGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLR-TINLLQrPTEGRVFLGDTLisnasgrELR--- 79
Cdd:PRK11147 322 MENVNYQID-GKQL----VKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQ-ADSGRIHCGTKL-------EVAyfd 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 80 QHRQrigmifqhfNLMHTRNVYDNVafslrAAGKSKADIAERVPEILALvgLQD-----KGTAYPAQ-LSGGQKQRVGIA 153
Cdd:PRK11147 389 QHRA---------ELDPEKTVMDNL-----AEGKQEVMVNGRPRHVLGY--LQDflfhpKRAMTPVKaLSGGERNRLLLA 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504513067 154 RAIANHPEVLLCDEPTSALDLETsasiLALLKSINVRLGITIVLISHE 201
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLDVET----LELLEELLDSYQGTVLLVSHD 496
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
17-316 |
1.18e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.42 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 17 AQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASgreLRQHRQRIGMIFQhfnlmh 96
Cdd:PRK10938 14 SDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS---FEQLQKLVSDEWQ------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 97 tRNVYDNVAFSLRAAGKSKADI-------AERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPT 169
Cdd:PRK10938 85 -RNNTDMLSPGEDDTGRTTAEIiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 170 SALDLETSASILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEVFTIFS---APQHAYTKQLVShtt 246
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQqalVAQLAHSEQLEG--- 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 247 pVELPDrfkknnkgvllkilfADDSVEQPILSDVAQQFQvsvnILHGNIEYiNDRAlghIIAQISYRDDP 316
Cdd:PRK10938 240 -VQLPE---------------PDEPSARHALPANEPRIV----LNNGVVSY-NDRP---ILHNLSWQVNP 285
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-206 |
1.27e-11 |
|
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: 65.54 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTIN--------LLQRPTEGRVFLgdtlISN 72
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVL----IESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFY----VPQ 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 73 ASGRELRQHRQRIgmifqhfnlmhtrnVYDNVAFSLRAAGKSKADIAErvpeILALVGLQD---KGTAYPA------QLS 143
Cdd:TIGR00954 523 RPYMTLGTLRDQI--------------IYPDSSEDMKRRGLSDKDLEQ----ILDNVQLTHileREGGWSAvqdwmdVLS 584
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513067 144 GGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKsinvRLGITIVLISHEMSVIK 206
Cdd:TIGR00954 585 GGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCR----EFGITLFSVSHRKSLWK 643
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-224 |
2.61e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.97 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLgDTLisNASGRELRQHRQRIGMIFQhfnlmhtrnvyDN 103
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII-DGL--NIAKIGLHDLRFKITIIPQ-----------DP 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 104 VAFS--LRAAGKSKADIA-ERVPEILALVGLQDKGTAYPAQL-----------SGGQKQRVGIARAIANHPEVLLCDEPT 169
Cdd:TIGR00957 1370 VLFSgsLRMNLDPFSQYSdEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 170 SALDLETSASILAllkSINVRL-GITIVLISHEMSVIKSIcQRMAVMTGGNIVEEG 224
Cdd:TIGR00957 1450 AAVDLETDNLIQS---TIRTQFeDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFG 1501
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
5-203 |
2.71e-11 |
|
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: 61.88 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 5 ENVSVDFPaGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTinLLQRPTEGrVFLGDTLIsnaSGRELRQHRQR 84
Cdd:cd03232 7 KNLNYTVP-VKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDV--LAGRKTAG-VITGEILI---NGRPLDKNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 85 IGMIFQHFNLmHTRN--VYDNVAFS--LRAagkskadiaervpeilalvglqdkgtaypaqLSGGQKQRVGIARAIANHP 160
Cdd:cd03232 80 STGYVEQQDV-HSPNltVREALRFSalLRG-------------------------------LSVEQRKRLTIGVELAAKP 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSInVRLGITIVLISHEMS 203
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKL-ADSGQAILCTIHQPS 169
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-225 |
3.53e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 21 AVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQH--------RQRIGmIFQH- 91
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHgfalvteeRRSTG-IYAYl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 92 ---FN-LMHTRNVYDNvAFSLRAAGKSKADI-----AERV--PEILALVGlqdkgtaypaQLSGGQKQRVGIARAIANHP 160
Cdd:PRK10982 342 digFNsLISNIRNYKN-KVGLLDNSRMKSDTqwvidSMRVktPGHRTQIG----------SLSGGNQQKVIIGRWLLTQP 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIKSICQRMAVMTGG---NIVEEGE 225
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNGlvaGIVDTKT 477
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-201 |
4.28e-11 |
|
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: 63.80 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLisnasgrelrqhrqRIGMIFQHFNLMHTRNVYDN 103
Cdd:TIGR03719 23 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI--------------KVGYLPQEPQLDPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 104 VAFSLRaagkSKADIAERVPEILALVG---------------LQDK------------------------GTAYPAQLSG 144
Cdd:TIGR03719 89 VEEGVA----EIKDALDRFNEISAKYAepdadfdklaaeqaeLQEIidaadawdldsqleiamdalrcppWDADVTKLSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 145 GQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKsinvRLGITIVLISHE 201
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ----EYPGTVVAVTHD 217
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-243 |
5.54e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 63.73 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFPAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFlgdtlisnasgrelRQ 80
Cdd:PLN03073 508 IISFSDASFGYPGGPLL----FKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF--------------RS 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 HRQRIGMIFQH----FNLMHTRNVYDNVAFSLRAAGKSKADIAErvpeiLALVG---LQDKGTaypaqLSGGQKQRVGIA 153
Cdd:PLN03073 570 AKVRMAVFSQHhvdgLDLSSNPLLYMMRCFPGVPEQKLRAHLGS-----FGVTGnlaLQPMYT-----LSGGQKSRVAFA 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 154 RAIANHPEVLLCDEPTSALDLEtsaSILALLKSINVRLGiTIVLISHEMSVIKSICQRMAVMTGGNIveegevfTIFSAP 233
Cdd:PLN03073 640 KITFKKPHILLLDEPSNHLDLD---AVEALIQGLVLFQG-GVLMVSHDEHLISGSVDELWVVSEGKV-------TPFHGT 708
|
250
....*....|
gi 504513067 234 QHAYTKQLVS 243
Cdd:PLN03073 709 FHDYKKTLQS 718
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-224 |
6.80e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.81 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTL--------ISNASGRElrqhrqriGMIFQH-F 92
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVayvpqqawIQNDSLRE--------NILFGKaL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 93 NLMHTRNVYDNVAFslraagkskadiaerVPEILALVG-----LQDKGTaypaQLSGGQKQRVGIARAIANHPEVLLCDE 167
Cdd:TIGR00957 726 NEKYYQQVLEACAL---------------LPDLEILPSgdrteIGEKGV----NLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504513067 168 PTSALDLETSASILA-LLKSINVRLGITIVLISHEMSVIKSIcQRMAVMTGGNIVEEG 224
Cdd:TIGR00957 787 PLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-233 |
8.75e-11 |
|
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: 61.23 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 32 GEVFGIVGTSGAGKSTLLRTINLLQRPTEGRvFLG----DTLISNASGRELRQHRQRI-------GMIFQHFNLMhTRNV 100
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDppdwDEILDEFRGSELQNYFTKLlegdvkvIVKPQYVDLI-PKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 101 YDNVAFSLRAagKSKADIAERVPEILALVGLQDKGTAypaQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASI 180
Cdd:cd03236 104 KGKVGELLKK--KDERGKLDELVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504513067 181 LALLKSINvRLGITIVLISHEMSVIKSICQRMAVMTGgniveEGEVFTIFSAP 233
Cdd:cd03236 179 ARLIRELA-EDDNYVLVVEHDLAVLDYLSDYIHCLYG-----EPGAYGVVTLP 225
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
22-221 |
1.22e-10 |
|
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: 59.97 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLlQRPTEGRVfLGDTLISNASGRE-LRQHRQRIGMIFQHFNLMHTRNV 100
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN-RTEGNVSV-EGDIHYNGIPYKEfAEKYPGEIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 101 YDNVAFSLRAagkskadiaervpeilalvglqdKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASI 180
Cdd:cd03233 101 RETLDFALRC-----------------------KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504513067 181 LALLKSINVRLGITIVLISHEMSV-IKSICQRMAVMTGGNIV 221
Cdd:cd03233 158 LKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQI 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-181 |
4.42e-10 |
|
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: 61.08 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVflgdtlisnasgrelrQHRQRIGMIFQhFNLMHTRNVYDN 103
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----------------KHSGRISFSPQ-TSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 104 VAF----------SLRAAGKSKADIAeRVPEILALVgLQDKGTAypaqLSGGQKQRVGIARAIANHPEVLLCDEPTSALD 173
Cdd:TIGR01271 507 IIFglsydeyrytSVIKACQLEEDIA-LFPEKDKTV-LGEGGIT----LSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
....*...
gi 504513067 174 LETSASIL 181
Cdd:TIGR01271 581 VVTEKEIF 588
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-214 |
5.35e-10 |
|
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: 57.00 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 31 QGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDtlisnasgrelrqhrqrigmifqhfnlmhtrnvydnvafslra 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 111 agkskadiAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILAL-----LK 185
Cdd:smart00382 38 --------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLL 109
|
170 180
....*....|....*....|....*....
gi 504513067 186 SINVRLGITIVLISHEMSVIKSICQRMAV 214
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-222 |
5.77e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.91 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 25 VNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQhrqRIGMIFQ---------HFNL- 94
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK---VLGIIPQapvlfsgtvRFNLd 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 95 -MHTRNVYDNVAFSLRAAGKskaDIAERVPeilalVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALD 173
Cdd:PLN03130 1335 pFNEHNDADLWESLERAHLK---DVIRRNS-----LGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504513067 174 LETSASIlalLKSINVRL-GITIVLISHEMSVIKSiCQRMAVMTGGNIVE 222
Cdd:PLN03130 1407 VRTDALI---QKTIREEFkSCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
29-175 |
7.30e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.94 E-value: 7.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 29 IQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASgrelrqhRQRIGMIFQHF-NLMHTRNVYDNVAFS 107
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLpGLKADLSTLENLHFL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 108 LRAAGKSkadiAERVP-EILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLE 175
Cdd:PRK13543 107 CGLHGRR----AKQMPgSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-180 |
8.51e-10 |
|
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: 58.71 E-value: 8.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVflgdtlisnasgrelrQHRQRIGMIFQhFNLMHTRNVYDN 103
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----------------KHSGRISFSSQ-FSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 104 VAFSLRAAgkskadiAERVPEILALVGLQDKGTAYPAQ-----------LSGGQKQRVGIARAIANHPEVLLCDEPTSAL 172
Cdd:cd03291 118 IIFGVSYD-------EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
....*...
gi 504513067 173 DLETSASI 180
Cdd:cd03291 191 DVFTEKEI 198
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-234 |
9.16e-10 |
|
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: 58.19 E-value: 9.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 28 TIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGrvflgDTLISNASgrelrqhrqrIGMIFQHFNLMHTRNVYDNVAFS 107
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-----DIEIELDT----------VSYKPQYIKADYEGTVRDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 108 LRAAGKS---KADIAErvPeiLALVGLQDKGTAypaQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALL 184
Cdd:cd03237 86 TKDFYTHpyfKTEIAK--P--LQIEQILDREVP---ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504513067 185 KSINVRLGITIVLISHEMSVIKSICQRMavmtggnIVEEGE--VFTIFSAPQ 234
Cdd:cd03237 159 RRFAENNEKTAFVVEHDIIMIDYLADRL-------IVFEGEpsVNGVANPPQ 203
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
22-226 |
1.04e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.11 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTInlLQRP----TEGRVFLGDTLISNASGrELRQHRQrigmIFQHFNLMHT 97
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHPaykiLEGDILFKGESILDLEP-EERAHLG----IFLAFQYPIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 98 RNVYDNVAFsLRAA--------GKSKAD---IAERVPEILALVGLQ--------DKGtaypaqLSGGQKQRVGIARAIAN 158
Cdd:CHL00131 96 IPGVSNADF-LRLAynskrkfqGLPELDpleFLEIINEKLKLVGMDpsflsrnvNEG------FSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513067 159 HPEVLLCDEPTSALDLETSASIlalLKSIN--VRLGITIVLISHEMSVIKSIC-QRMAVMTGGNIVEEGEV 226
Cdd:CHL00131 169 DSELAILDETDSGLDIDALKII---AEGINklMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDA 236
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-226 |
1.29e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.03 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTI--NLLQRPTEGRVFLGDTLISNASGRELRQH--------RQRIGMIFQ- 90
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDGKEVDVSTVSDAIDAglayvtedRKGYGLNLId 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 91 ---------HFNLMHTRNVYDNVAfSLRAAGKSKADIAERVPEILALVGlqdkgtaypaQLSGGQKQRVGIARAIANHPE 161
Cdd:NF040905 356 dikrnitlaNLGKVSRRGVIDENE-EIKVAEEYRKKMNIKTPSVFQKVG----------NLSGGNQQKVVLSKWLFTDPD 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 162 VLLCDEPTSALDLETSASILALlksIN--VRLGITIVLISHEMSVIKSICQRMAVMTGGNIVeeGEV 226
Cdd:NF040905 425 VLILDEPTRGIDVGAKYEIYTI---INelAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT--GEL 486
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-201 |
1.41e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRQ-----HRQRIGMifqhfNLMH 96
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQlcfvgHRSGINP-----YLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 97 TRNVYDNVAFSLRAAGkskadIAERVpEILALVGLQDkgtaYP-AQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDle 175
Cdd:PRK13540 92 RENCLYDIHFSPGAVG-----ITELC-RLFSLEHLID----YPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD-- 159
|
170 180
....*....|....*....|....*...
gi 504513067 176 tSASILALLKSINV--RLGITIVLISHE 201
Cdd:PRK13540 160 -ELSLLTIITKIQEhrAKGGAVLLTSHQ 186
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-250 |
1.63e-09 |
|
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: 57.94 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFPAGKTAqsrAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRT-INLLQrpTEGrvflgDTLISNASGRE--L 78
Cdd:cd03289 3 MTVKDLTAKYTEGGNA---VLENISFSISPGQRVGLLGRTGSGKSTLLSAfLRLLN--TEG-----DIQIDGVSWNSvpL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 79 RQHRQRIGMIFQHFnLMHTRNVYDNvafsLRAAGKSKADIAERVPEilaLVGLQDKGTAYPAQL-----------SGGQK 147
Cdd:cd03289 73 QKWRKAFGVIPQKV-FIFSGTFRKN----LDPYGKWSDEEIWKVAE---EVGLKSVIEQFPGQLdfvlvdggcvlSHGHK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 148 QRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKsiNVRLGITIVLISHEMSVIKSiCQRMAVMTGGNIVEEGEVF 227
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQ 221
|
250 260
....*....|....*....|...
gi 504513067 228 TIFSapQHAYTKQLVSHTTPVEL 250
Cdd:cd03289 222 KLLN--EKSHFKQAISPSDRLKL 242
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-224 |
2.12e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTI--NLLQRPTEGRVFLGD-------TLISNASGRE-----LRQHRQRIGM 87
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMlgELSHAETSSVVIRGSvayvpqvSWIFNATVREnilfgSDFESERYWR 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 88 IFQHFNLMHTRNVYdnvafslraAGKSKADIAERVPEIlalvglqdkgtaypaqlSGGQKQRVGIARAIANHPEVLLCDE 167
Cdd:PLN03232 713 AIDVTALQHDLDLL---------PGRDLTEIGERGVNI-----------------SGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 168 PTSALDLETSASILALLKSINVRlGITIVLISHEMSVIKSIcQRMAVMTGGNIVEEG 224
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMKDELK-GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEG 821
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-258 |
2.40e-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: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 10 DFPAGKTAQSRAV-NNVNLTIQQGEVFGIVGTSGAGKSTLLRTInLLQRPTEGRVFLGDTLISNASgreLRQHRQRIGMI 88
Cdd:TIGR01271 1222 GLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL-LRLLSTEGEIQIDGVSWNSVT---LQTWRKAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 89 FQH---FNLMHTRNVYDNVAFSLRAAGKSKADIA-----ERVPEILALVgLQDKGTAypaqLSGGQKQRVGIARAIANHP 160
Cdd:TIGR01271 1298 PQKvfiFSGTFRKNLDPYEQWSDEEIWKVAEEVGlksviEQFPDKLDFV-LVDGGYV----LSNGHKQLMCLARSILSKA 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 161 EVLLCDEPTSALDLETSASILALLKsiNVRLGITIVLISHEMSVIKSiCQRMAVMTGGNIVEEGEVFTIFSAPQHayTKQ 240
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLK--QSFSNCTVILSEHRVEALLE-CQQFLVIEGSSVKQYDSIQKLLNETSL--FKQ 1447
|
250
....*....|....*...
gi 504513067 241 LVSHTTPVELPDRFKKNN 258
Cdd:TIGR01271 1448 AMSAADRLKLFPLHRRNS 1465
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-226 |
2.47e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.14 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 20 RAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTI-NLLQRP--TEGRVFLGDTLISnasGRELRQhrqrigmiFQHFNLMH 96
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGgaPRGARVTGDVTLN---GEPLAA--------IDAPRLAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 97 TRNVYDNVA-----FSL------------RAAGKSKADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIAN- 158
Cdd:PRK13547 84 LRAVLPQAAqpafaFSAreivllgryphaRRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 159 --------HPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGGNIVEEGEV 226
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
22-176 |
2.95e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLisnasgrelrqhrqRIGMIFQ-HFNLMHTRNV 100
Cdd:PRK11819 340 IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV--------------KLAYVDQsRDALDPNKTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 101 YDNVAFSLraagkskadiaervpEILALVGLQDKGTAYPA--------------QLSGGQKQRVGIARAIANHPEVLLCD 166
Cdd:PRK11819 406 WEEISGGL---------------DIIKVGNREIPSRAYVGrfnfkggdqqkkvgVLSGGERNRLHLAKTLKQGGNVLLLD 470
|
170
....*....|
gi 504513067 167 EPTSALDLET 176
Cdd:PRK11819 471 EPTNDLDVET 480
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
18-207 |
3.03e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.03 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 18 QSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNAsgrelrqHRQRIGMIFQHFNLMHT 97
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------AKPYCTYIGHNLGLKLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 98 RNVYDNVAFSLRAagkskADIAERVPEILALVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETS 177
Cdd:PRK13541 85 MTVFENLKFWSEI-----YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
170 180 190
....*....|....*....|....*....|
gi 504513067 178 AsILALLKSINVRLGITIVLISHEMSVIKS 207
Cdd:PRK13541 160 D-LLNNLIVMKANSGGIVLLSSHLESSIKS 188
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-178 |
3.43e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLisnasgrelrqhrqRIGMIFQHFNLMHTRNVYDN 103
Cdd:PRK11819 25 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGI--------------KVGYLPQEPQLDPEKTVREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 104 VafslRAAGKSKADIAERVPEILALVG---------------LQDK------------------------GTAYPAQLSG 144
Cdd:PRK11819 91 V----EEGVAEVKAALDRFNEIYAAYAepdadfdalaaeqgeLQEIidaadawdldsqleiamdalrcppWDAKVTKLSG 166
|
170 180 190
....*....|....*....|....*....|....
gi 504513067 145 GQKQRVGIARAIANHPEVLLCDEPTSALDLETSA 178
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-217 |
3.78e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 28 TIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTL------ISNASGRELRQH-RQRIGMIFQhfnlmhtrnv 100
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKIsykpqyISPDYDGTVEEFlRSANTDDFG---------- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 101 ydnvafslraAGKSKADIAERvpeiLALVGLQDKgtaYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASI 180
Cdd:COG1245 432 ----------SSYYKTEIIKP----LGLEKLLDK---NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494
|
170 180 190
....*....|....*....|....*....|....*..
gi 504513067 181 LALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTG 217
Cdd:COG1245 495 AKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-247 |
6.05e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 33 EVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLISNASGRELRqhrqRIGMIFQHFNLMHTRNVYDNV-AFSLRA- 110
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLR----RVLSIIPQSPVLFSGTVRFNIdPFSEHNd 1338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 111 AGKSKA-------DIAERVPeilalVGLQDKGTAYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASIlal 183
Cdd:PLN03232 1339 ADLWEAlerahikDVIDRNP-----FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI--- 1410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513067 184 LKSINVRL-GITIVLISHEMSVIKSiCQRMAVMTGGNIVEEGEVFTIFSAPQHAYTKqLVSHTTP 247
Cdd:PLN03232 1411 QRTIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFR-MVHSTGP 1473
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-173 |
7.11e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.48 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLgdtlisnasgrelrqhRQRIGMIFQHFNLMHTrNVYDN 103
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA----------------ERSIAYVPQQAWIMNA-TVRGN 740
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513067 104 VAFSLRAAGKSKADiAERVPEILALV-----GLQ----DKGTaypaQLSGGQKQRVGIARAIANHPEVLLCDEPTSALD 173
Cdd:PTZ00243 741 ILFFDEEDAARLAD-AVRVSQLEADLaqlggGLEteigEKGV----NLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-207 |
1.28e-08 |
|
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: 53.87 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 17 AQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTInllqRPTEGRVFLGDTLisnasgrelrqhrqrigmifqhfnlmh 96
Cdd:cd03238 6 ANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG----LYASGKARLISFL--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 97 TRNVYDNVAFslraagkskadiaervpeILALVGLQDKGTAY-----PAQ-LSGGQKQRVGIARAIANHPE--VLLCDEP 168
Cdd:cd03238 55 PKFSRNKLIF------------------IDQLQFLIDVGLGYltlgqKLStLSGGELQRVKLASELFSEPPgtLFILDEP 116
|
170 180 190
....*....|....*....|....*....|....*....
gi 504513067 169 TSALDLETSASILALLKSInVRLGITIVLISHEMSVIKS 207
Cdd:cd03238 117 STGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSS 154
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
24-207 |
3.31e-08 |
|
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: 53.77 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 24 NVNLTIQQGEVFGIVGTSGAGKSTLLrtINLLQRPTEGRVFLGDTLISNASGRELRQHRQRIGMIFQH------------ 91
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLI--NDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSpigrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 92 ----FNLMhtRNV---------YDNVAFSLRAAGKSKADIA-----------ERVPEILA-LVGLQDKGTAY-----PA- 140
Cdd:cd03271 91 ytgvFDEI--RELfcevckgkrYNRETLEVRYKGKSIADVLdmtveealeffENIPKIARkLQTLCDVGLGYiklgqPAt 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 141 QLSGGQKQRVGIARAI---ANHPEVLLCDEPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIKS 207
Cdd:cd03271 169 TLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHNLDVIKC 237
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-207 |
1.96e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 1 MIRLENVSVDFpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGDTLisnasgrelrq 80
Cdd:PRK10636 312 LLKMEKVSAGY-----GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGI----------- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 81 hrqRIGMIFQHfnlmhtrnvydNVAFsLRA---AGKSKADIAERVPE-----ILALVGLQ-DKGTAYPAQLSGGQKQRVG 151
Cdd:PRK10636 376 ---KLGYFAQH-----------QLEF-LRAdesPLQHLARLAPQELEqklrdYLGGFGFQgDKVTEETRRFSGGEKARLV 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 152 IARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLgitiVLISHEMSVIKS 207
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRS 492
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
124-207 |
1.98e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.71 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 124 EILALVGLQDKGTAYPA-QLSGGQKQRVGIARAI---ANHPEVLLCDEPTSALDLETSASILALLKSInVRLGITIVLIS 199
Cdd:TIGR00630 811 QTLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIE 889
|
....*...
gi 504513067 200 HEMSVIKS 207
Cdd:TIGR00630 890 HNLDVIKT 897
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-224 |
2.01e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 16 TAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTInLLQRPTegrvfLGDTlisNASGRELRQHRQRIGMIFQhfnlm 95
Cdd:PLN03130 627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM-LGELPP-----RSDA---SVVIRGTVAYVPQVSWIFN----- 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 96 htRNVYDNVAFSlraagkSKADiAERVPEILALVGLQDKGTAYPA-----------QLSGGQKQRVGIARAIANHPEVLL 164
Cdd:PLN03130 693 --ATVRDNILFG------SPFD-PERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYI 763
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513067 165 CDEPTSALDLETSASILAllKSINVRL-GITIVLISHEMSVIKSIcQRMAVMTGGNIVEEG 224
Cdd:PLN03130 764 FDDPLSALDAHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-217 |
2.40e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 28 TIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLgDTLISNASgrelrqhrQRIgmifqhfnlmhtRNVYD-NVAF 106
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKISYKP--------QYI------------KPDYDgTVED 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 107 SLRAAGKS------KADIAERvpeiLALVGLQDKgtaYPAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASI 180
Cdd:PRK13409 420 LLRSITDDlgssyyKSEIIKP----LQLERLLDK---NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 492
|
170 180 190
....*....|....*....|....*....|....*..
gi 504513067 181 LALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTG 217
Cdd:PRK13409 493 AKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-222 |
3.87e-07 |
|
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: 50.68 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpagKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTL----LRTINLLqrptEGRVFLGDTLISNASgre 77
Cdd:cd03288 20 IKIHDLCVRY---ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLP--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 78 LRQHRQRIGMIFQHFNLMHtrnvyDNVAFSLRAAGKSKADiaeRVPEILALVGLQDKGTAYPAQL-----------SGGQ 146
Cdd:cd03288 90 LHTLRSRLSIILQDPILFS-----GSIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513067 147 KQRVGIARAIANHPEVLLCDEPTSALDLETSaSIL--ALLKSINVRlgiTIVLISHEMSVIKSICQRMaVMTGGNIVE 222
Cdd:cd03288 162 RQLFCLARAFVRKSSILIMDEATASIDMATE-NILqkVVMTAFADR---TVVTIAHRVSTILDADLVL-VLSRGILVE 234
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-220 |
4.20e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 5 ENVSVDFpagktaqsravnnvnltiQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLGdtliSNASGRELRQHR-- 82
Cdd:PRK15064 18 ENISVKF------------------GGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD----PNERLGKLRQDQfa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 83 ---QRI--GMIFQHFNL---MHTRN-VYDNVAFS----LRAAgKSKADIAE--------RVPEILALVGL---QDKGTAy 138
Cdd:PRK15064 76 feeFTVldTVIMGHTELwevKQERDrIYALPEMSeedgMKVA-DLEVKFAEmdgytaeaRAGELLLGVGIpeeQHYGLM- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 139 pAQLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETsasILALLKSINVRlGITIVLISHEMSVIKSICQRMAVMTGG 218
Cdd:PRK15064 154 -SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT---IRWLEDVLNER-NSTMIIISHDRHFLNSVCTHMADLDYG 228
|
..
gi 504513067 219 NI 220
Cdd:PRK15064 229 EL 230
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
6-204 |
5.54e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 6 NVSVDFPAGKTAQSRAVNNVNL------TIQQGEVFGIVGTSGAGKSTLLRTinLLQRPTEGRVfLGDTLIsnaSGRELR 79
Cdd:PLN03140 874 NYFVDMPAEMKEQGVTEDRLQLlrevtgAFRPGVLTALMGVSGAGKTTLMDV--LAGRKTGGYI-EGDIRI---SGFPKK 947
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 80 QHR-QRI-GMIFQhfNLMHTRNVY--DNVAFS--LR----AAGKSKADIAERVPEILALVGLQDKGTAYPA--QLSGGQK 147
Cdd:PLN03140 948 QETfARIsGYCEQ--NDIHSPQVTvrESLIYSafLRlpkeVSKEEKMMFVDEVMELVELDNLKDAIVGLPGvtGLSTEQR 1025
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 148 QRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSiNVRLGITIVLISHEMSV 204
Cdd:PLN03140 1026 KRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSI 1081
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-173 |
6.30e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpagktAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTINllqrptegrvflGD---------TLISN 72
Cdd:PRK10938 261 IVLNNGVVSY-----NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT------------GDhpqgysndlTLFGR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 73 --ASGRELRQHRQRIGMIFQHFNLMH-----TRNV-----------YDNVAFSLRaagkSKADiaervpEILALVGLQDK 134
Cdd:PRK10938 324 rrGSGETIWDIKKHIGYVSSSLHLDYrvstsVRNVilsgffdsigiYQAVSDRQQ----KLAQ------QWLDILGIDKR 393
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504513067 135 GTAYPAQ-LSGGQKQRVGIARAIANHPEVLLCDEPTSALD 173
Cdd:PRK10938 394 TADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-200 |
9.99e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 9.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 2 IRLENVSVDFpAGKTAqsraVNNVNLTIQQGEVFGIVGTSGAGKSTLLR-----TINLLQRP-----TEGRVFLGDTLIS 71
Cdd:PLN03073 178 IHMENFSISV-GGRDL----IVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGIPKNcqilhVEQEVVGDDTTAL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 72 NASgreLRQHRQRIGMIFQHFNLMHTRNVYDNVAFSLRAAGKSKAD-----IAERVPEILALVGLQDkgtAYPA------ 140
Cdd:PLN03073 253 QCV---LNTDIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGvdkdaVSQRLEEIYKRLELID---AYTAearaas 326
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513067 141 -----------------QLSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETsasiLALLKSINVRLGITIVLISH 200
Cdd:PLN03073 327 ilaglsftpemqvkatkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA----VLWLETYLLKWPKTFIVVSH 399
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-173 |
1.06e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.17 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 28 TIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLG---DTLISNASGRELrqhrqrigmiFQHFnlmhtRNVYDNv 104
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEpswDEVLKRFRGTEL----------QDYF-----KKLANG- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 105 afSLRAAGK-------------------SKAD---IAERVPEILALVGLQDKGTAypaQLSGGQKQRVGIARAIANHPEV 162
Cdd:COG1245 159 --EIKVAHKpqyvdlipkvfkgtvrellEKVDergKLDELAEKLGLENILDRDIS---ELSGGELQRVAIAAALLRDADF 233
|
170
....*....|.
gi 504513067 163 LLCDEPTSALD 173
Cdd:COG1245 234 YFFDEPSSYLD 244
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
22-201 |
1.48e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTIN--------------------------LLQRPTEGRVFLGDtlisnasg 75
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKneisadggsytfpgnwqlawvnqetpALPQPALEYVIDGD-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 76 RELRQHRQRIgmifQHFNlmhTRNvyDNVAFSLrAAGKSKA----DIAERVPEILALVGLQDKGTAYPAQ-LSGGQKQRV 150
Cdd:PRK10636 89 REYRQLEAQL----HDAN---ERN--DGHAIAT-IHGKLDAidawTIRSRAASLLHGLGFSNEQLERPVSdFSGGWRMRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504513067 151 GIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVrlgiTIVLISHE 201
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHD 205
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
142-234 |
1.52e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.95 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 142 LSGGQKQRVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSINVRLGITIVLISHEMSVIKSICQRMAVMTGgniv 221
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG---- 147
|
90
....*....|...
gi 504513067 222 eEGEVFTIFSAPQ 234
Cdd:cd03222 148 -EPGVYGIASQPK 159
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-199 |
1.81e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 11 FPAGKTAQSRAVNNVNLTIQQGEVFGIVGTSGAGKSTLLRTI--NLLQ--RPTEGRVFLgdtliSNASGRELRQHRqRIG 86
Cdd:TIGR00956 66 KKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasNTDGfhIGVEGVITY-----DGITPEEIKKHY-RGD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 87 MIFQ-----HFNLMhtrNVYDNVAFS-------LRAAGKSKADIAERVPE-ILALVGLQDK-----GTAYPAQLSGGQKQ 148
Cdd:TIGR00956 140 VVYNaetdvHFPHL---TVGETLDFAarcktpqNRPDGVSREEYAKHIADvYMATYGLSHTrntkvGNDFVRGVSGGERK 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504513067 149 RVGIARAIANHPEVLLCDEPTSALDLETSASILALLKSInVRLGITIVLIS 199
Cdd:TIGR00956 217 RVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTS-ANILDTTPLVA 266
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-221 |
2.26e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 23 NNVNLTIQQGEVFGIVGTSGAGKSTLLRT-INLLQrPTEGRVFLGDtlisNASgrelrqhrqrIGMIFQ-H--------- 91
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTlVGELE-PDSGTVKWSE----NAN----------IGYYAQdHaydfendlt 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 92 -FNLMHT-RNVYDNVAfSLRAA-GK---SKADIAERVpeilalvglqdkgtaypAQLSGGQKQRVGIARAIANHPEVLLC 165
Cdd:PRK15064 401 lFDWMSQwRQEGDDEQ-AVRGTlGRllfSQDDIKKSV-----------------KVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513067 166 DEPTSALDLEtsaSILALLKSINVRLGiTIVLISHEMSVIKSICQRMAVMTGGNIV 221
Cdd:PRK15064 463 DEPTNHMDME---SIESLNMALEKYEG-TLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-224 |
4.73e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 22 VNNVNLTIQQGEVFGIVGTSGAGKSTLLRTinlLQRPTEgrvFLGDTLISNasGRE-----LRQHRQRIGMIFQHFNLMH 96
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLT---FMRMVE---VCGGEIRVN--GREigaygLRELRRQFSMIPQDPVLFD 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 97 TrNVYDNVAFSLRAAgkskadiAERVPEILALVGLQDK---------------GTAYpaqlSGGQKQRVGIARAIANHPE 161
Cdd:PTZ00243 1398 G-TVRQNVDPFLEAS-------SAEVWAALELVGLRERvasesegidsrvlegGSNY----SVGQRQLMCMARALLKKGS 1465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513067 162 -VLLCDEPTS----ALDLETSASILALLKSinvrlgITIVLISHEMSVIKSiCQRMAVMTGGNIVEEG 224
Cdd:PTZ00243 1466 gFILMDEATAnidpALDRQIQATVMSAFSA------YTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMG 1526
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-173 |
5.37e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 28 TIQQGEVFGIVGTSGAGKSTLLRTINLLQRPTEGRVFLG---DTLISNASGRELrqhrqrigmiFQHFnlmhtRNVYDNv 104
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEpswDEVLKRFRGTEL----------QNYF-----KKLYNG- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 105 afSLRAAGK-------------------SKAD---IAERVPEILALVGLQDKGTAypaQLSGGQKQRVGIARAIANHPEV 162
Cdd:PRK13409 159 --EIKVVHKpqyvdlipkvfkgkvrellKKVDergKLDEVVERLGLENILDRDIS---ELSGGELQRVAIAAALLRDADF 233
|
170
....*....|.
gi 504513067 163 LLCDEPTSALD 173
Cdd:PRK13409 234 YFFDEPTSYLD 244
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
34-200 |
7.92e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.16 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 34 VFGIVGTSGAGKSTLLRTINL-LQRPTEGRVFLGDTLISNAS------------GRELRQHR--------------QRIG 86
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIRYaLYGKARSRSKLRSDLINVGSeeasvelefehgGKRYRIERrqgefaefleakpsERKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 87 MIFQHFNLMHTRNVYDNVAfSLRAAGKSKADIAERVP----EILA-LVGLQDkgtayPAQLSGGQKQRVGIARAIAnhpe 161
Cdd:COG0419 105 ALKRLLGLEIYEELKERLK-ELEEALESALEELAELQklkqEILAqLSGLDP-----IETLSGGERLRLALADLLS---- 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 504513067 162 vLLCDepTSALDLETSASILALLKSINVrlgitivlISH 200
Cdd:COG0419 175 -LILD--FGSLDEERLERLLDALEELAI--------ITH 202
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-208 |
4.36e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.75 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 37 IVGTSGAGKSTLLRTINL----LQRPTEGRVFLGDTLIsnASGRELRQhrqrIGMIFQHFN--LMHTR---NVYDNVAFS 107
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYaltgELPPNSKGGAHDPKLI--REGEVRAQ----VKLAFENANgkKYTITrslAILENVIFC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 108 lraagkskadiaeRVPEILALVGLQdkgtayPAQLSGGQKQ------RVGIARAIANHPEVLLCDEPTSALDLETSASIL 181
Cdd:cd03240 101 -------------HQGESNWPLLDM------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESL 161
|
170 180
....*....|....*....|....*...
gi 504513067 182 A-LLKSINVRLGITIVLISHEMSVIKSI 208
Cdd:cd03240 162 AeIIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
108-206 |
1.55e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 108 LRAAGKSKADIAERV-----------PEI------LALVGLQDKGTAYP-AQLSGGQKQRVGIARAIAN---HPEVLLCD 166
Cdd:PRK00635 758 VRYKGKNIADILEMTayeaekffldePSIhekihaLCSLGLDYLPLGRPlSSLSGGEIQRLKLAYELLApskKPTLYVLD 837
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 504513067 167 EPTSALDLETSASILALLKSInVRLGITIVLISHEMSVIK 206
Cdd:PRK00635 838 EPTTGLHTHDIKALIYVLQSL-THQGHTVVIIEHNMHVVK 876
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
112-207 |
6.24e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513067 112 GKSKADI-------A----ERVPEIL-ALVGLQDKGTAY-----PA-QLSGGQKQRVGIARAIA---NHPEVLLCDEPTS 170
Cdd:COG0178 779 GKNIADVldmtveeAleffENIPKIArKLQTLQDVGLGYiklgqPAtTLSGGEAQRVKLASELSkrsTGKTLYILDEPTT 858
|
90 100 110
....*....|....*....|....*....|....*....
gi 504513067 171 ALDLEtsaSILALLKSIN--VRLGITIVLISHEMSVIKS 207
Cdd:COG0178 859 GLHFH---DIRKLLEVLHrlVDKGNTVVVIEHNLDVIKT 894
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
221-260 |
2.73e-03 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 35.84 E-value: 2.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 504513067 221 VEEGEVFTIFSAPQHAYTKQLVSHTTPVELPDRFKKNNKG 260
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPG 40
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
141-200 |
5.39e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 36.95 E-value: 5.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513067 141 QLSGGQKQRVGIARAIANH---PEVLLC-DEPTSALDLETSASILALLKSINVRLGITIVlISH 200
Cdd:cd03227 77 QLSGGEKELSALALILALAslkPRPLYIlDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITH 139
|
|
| |
