|
Name |
Accession |
Description |
Interval |
E-value |
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-343 |
0e+00 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 673.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEF 240
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 241 IKSTLHLDIPEDYLQKLQSEFAPDLSPLLKLEFTGKSVDAPLISMAVRRFNIDISILSSQMDYAGGVKFGVMLAELDGES 320
Cdd:PRK11153 241 IQSTLHLDLPEDYLARLQAEPTTGSGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGDP 320
|
330 340
....*....|....*....|...
gi 502950432 321 DSINATIAFLEDHHVKVEVLGYV 343
Cdd:PRK11153 321 GDIQAAIAYLQEHGVKVEVLGYV 343
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-341 |
0e+00 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 595.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEF 240
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 241 IKSTLHLDIPEDYLQKLQSEFAPDlsPLLKLEFTGKSVDAPLISMAVRRFNIDISILSSQMDYAGGVKFGVMLAELDGES 320
Cdd:COG1135 241 LPTVLNDELPEELLARLREAAGGG--RLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDD 318
|
330 340
....*....|....*....|.
gi 502950432 321 DSINATIAFLEDHHVKVEVLG 341
Cdd:COG1135 319 AAIDAALAYLREQGVVVEVLG 339
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
1-343 |
0e+00 |
|
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: 588.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:TIGR02314 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEF 240
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 241 IKSTLHLDIPEDYLQKLQSEFAPDLSPLLKLEFTGKSVDAPLISMAVRRFNIDISILSSQMDYAGGVKFGVMLAELDGES 320
Cdd:TIGR02314 241 IRSTLHLSIPEDYQERLQATPFADSVPMVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMHGTQ 320
|
330 340
....*....|....*....|...
gi 502950432 321 DSINATIAFLEDHHVKVEVLGYV 343
Cdd:TIGR02314 321 QDTQAAIAYLQEHNVKVEVLGYV 343
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-233 |
3.40e-156 |
|
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: 437.01 E-value: 3.40e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPK 233
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-222 |
1.03e-100 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 296.18 E-value: 1.03e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQ-IGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSP 159
Cdd:COG1136 84 RRRhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502950432 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDQVAVISGGQLIEQ 222
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-242 |
3.29e-100 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 295.36 E-value: 3.29e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFqqGTRsiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTsLSERELTRA 80
Cdd:COG1126 1 MIEIENLHKSF--GDL--EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVAL-PLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSP 159
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 160 KVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQE 239
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234
|
...
gi 502950432 240 FIK 242
Cdd:COG1126 235 FLS 237
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-221 |
8.70e-95 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 280.79 E-value: 8.70e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTrsiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:COG2884 1 MIRFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:COG2884 78 RRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIE 221
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-248 |
1.91e-93 |
|
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: 287.57 E-value: 1.91e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQ-GTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTR 79
Cdd:COG1123 260 LLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 80 ARRQIGMIFQH-FNLLSSR-TVFGNVALPLELNNT-PKAEIKTRVNELLELVSLADKH-DAYPANLSGGQKQRVAIARAL 155
Cdd:COG1123 340 LRRRVQMVFQDpYSSLNPRmTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLaDRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 156 ANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTP 235
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
250
....*....|...
gi 502950432 236 VAQEFIKSTLHLD 248
Cdd:COG1123 500 YTRALLAAVPSLD 512
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-241 |
6.98e-93 |
|
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: 276.86 E-value: 6.98e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFqqGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:COG1127 5 MIEVRNLTKSF--GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVALPL-ELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSP 159
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKtPVAQE 239
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDD-PWVRQ 239
|
..
gi 502950432 240 FI 241
Cdd:COG1127 240 FL 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-219 |
3.07e-92 |
|
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: 274.37 E-value: 3.07e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRAR 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 R-QIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:cd03255 81 RrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDQVAVISGGQL 219
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-220 |
5.31e-84 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 254.21 E-value: 5.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRsikALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:COG3638 2 MLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVALPLeLNNTP---------KAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAI 151
Cdd:COG3638 79 RRRIGMIFQQFNLVPRLSVLTNVLAGR-LGRTStwrsllglfPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 152 ARALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLI 220
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-248 |
1.93e-81 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 247.79 E-value: 1.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTslsERELTRA 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT---RRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFnlLSS----RTVFGNVALPLELNNTPkaEIKTRVNELLELVSLADKH-DAYPANLSGGQKQRVAIARAL 155
Cdd:COG1124 78 RRRVQMVFQDP--YASlhprHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPSFlDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 156 ANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTP 235
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
250
....*....|...
gi 502950432 236 VAQEFIKSTLHLD 248
Cdd:COG1124 234 YTRELLAASLAFE 246
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-232 |
2.66e-81 |
|
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: 247.03 E-value: 2.66e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFqqGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRAR 81
Cdd:cd03261 1 IELRGLTKSF--GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVALPL-ELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHP 232
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-222 |
4.55e-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: 243.57 E-value: 4.55e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQhfNLLSS----RTVFGNVALPLELN--NTPKAEIKTRVNELLELVSLADKH-DAYPANLSGGQKQRVAIAR 153
Cdd:cd03257 81 RKEIQMVFQ--DPMSSlnprMTIGEQIAEPLRIHgkLSKKEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 154 ALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQ 222
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-265 |
6.24e-80 |
|
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: 246.50 E-value: 6.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCV-NMLERP--TSGQVLVNGQDLTSLSEREL 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 78 TRAR-RQIGMIFQhfNLLSS----RTVFGNVALPLELNN-TPKAEIKTRVNELLELVSLADKH---DAYPANLSGGQKQR 148
Cdd:COG0444 81 RKIRgREIQMIFQ--DPMTSlnpvMTVGDQIAEPLRIHGgLSKAEARERAIELLERVGLPDPErrlDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 149 VAIARALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEI 228
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 502950432 229 FSHPKTPVAQEFIKSTLHLDIPEDYLQKLQSEfAPDL 265
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDPDGRRLIPIPGE-PPSL 274
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-241 |
1.08e-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: 244.62 E-value: 1.08e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTrsikALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEreltrA 80
Cdd:COG3842 5 ALELENVSKRYGDVT----ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-----E 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:COG3842 76 KRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTP-VAqE 239
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRfVA-D 234
|
..
gi 502950432 240 FI 241
Cdd:COG3842 235 FI 236
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-234 |
4.56e-78 |
|
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: 238.39 E-value: 4.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTrsiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraR 81
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQH-FNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:COG1122 75 RKVGLVFQNpDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKT 234
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-219 |
7.60e-78 |
|
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: 237.43 E-value: 7.60e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFqqGTRsiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSlSERELTRAR 81
Cdd:cd03262 1 IEIKNLHKSF--GDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVAL-PLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-217 |
1.20e-77 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 238.45 E-value: 1.20e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGqdltslseRELTRA 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG--------KPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMD--VvkRICDQVAVISGG 217
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeaV--FLADRVVVLSAR 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-223 |
7.41e-76 |
|
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: 232.41 E-value: 7.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFqqgtRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEReltraR 81
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKV 161
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502950432 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQD 223
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-235 |
3.15e-75 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 234.63 E-value: 3.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 10 IFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRARRQIGMIFQ 89
Cdd:COG4608 23 LFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 90 H-FNLLSSR-TVFGNVALPLELNN-TPKAEIKTRVNELLELVSLADKH-DAYPANLSGGQKQRVAIARALANSPKVLLCD 165
Cdd:COG4608 103 DpYASLNPRmTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPEHaDRYPHEFSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 166 EATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTP 235
Cdd:COG4608 183 EPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHP 252
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-228 |
4.28e-75 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 231.11 E-value: 4.28e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFqqgtRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTslseRELTRAR 81
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKV 161
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEI 228
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-241 |
1.92e-74 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 233.50 E-value: 1.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFqqgtRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDL-TSLSEREltra 80
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 rRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:COG1118 75 -RRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 161 VLLCDEATSALDpATTRSILE-LLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQE 239
Cdd:COG1118 154 VLLLDEPFGALD-AKVRKELRrWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVAR 232
|
..
gi 502950432 240 FI 241
Cdd:COG1118 233 FL 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-220 |
2.14e-74 |
|
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: 229.76 E-value: 2.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTrsiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRAR 81
Cdd:cd03256 1 IEVENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNV---------ALPLELNNTPKAEIKtRVNELLELVSLADKHDAYPANLSGGQKQRVAIA 152
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVlsgrlgrrsTWRSLFGLFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 153 RALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLI 220
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-216 |
1.67e-73 |
|
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: 226.58 E-value: 1.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQdltslserELTRAR 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE--------PVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKV 161
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502950432 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISG 216
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-218 |
4.30e-73 |
|
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: 225.04 E-value: 4.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 11 FQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQH 90
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL---RRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 91 FNL-LSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATS 169
Cdd:cd03225 84 PDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502950432 170 ALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQ 218
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
8-242 |
6.09e-73 |
|
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: 226.76 E-value: 6.09e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 8 NKIFQQgTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRARRQ-IGM 86
Cdd:cd03294 28 EEILKK-TGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKkISM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 87 IFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDE 166
Cdd:cd03294 107 VFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502950432 167 ATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFIK 242
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFR 262
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-231 |
1.34e-71 |
|
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: 222.56 E-value: 1.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTrsiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNV---------ALPLELNNTPKAEiKTRVNELLELVSLADKHDAYPANLSGGQKQRVAI 151
Cdd:TIGR02315 78 RRRIGMIFQHYNLIERLTVLENVlhgrlgykpTWRSLLGRFSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 152 ARALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSH 231
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-221 |
1.54e-71 |
|
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: 221.92 E-value: 1.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQ-IGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEikTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSP 159
Cdd:COG4181 88 RARhVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502950432 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDQVAVISGGQLIE 221
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-242 |
2.09e-71 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 226.91 E-value: 2.09e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRARRQ-IGMIFQHFNLLSSRT 98
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELRELRRKkMSMVFQHFALLPHRT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 99 VFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPattrs 178
Cdd:COG4175 122 VLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDP----- 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502950432 179 iL-------ELLkDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFIK 242
Cdd:COG4175 197 -LirremqdELL-ELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVE 265
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-258 |
8.97e-71 |
|
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: 221.56 E-value: 8.97e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTR-SIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQhF--NLLSSRTVFGNVAL-PLELNnTPKAEIKTRVNELLELVSLADK-HDAYPANLSGGQKQRVAIARALA 156
Cdd:TIGR04521 81 RKKVGLVFQ-FpeHQLFEETVYKDIAFgPKNLG-LSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 157 NSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPktpv 236
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV---- 234
|
250 260
....*....|....*....|....
gi 502950432 237 aqEFIKStLHLDIPE--DYLQKLQ 258
Cdd:TIGR04521 235 --DELEK-IGLDVPEitELARKLK 255
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-219 |
1.11e-70 |
|
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: 219.20 E-value: 1.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTrsiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRAR 81
Cdd:cd03292 1 IEFINVTKTYPNGT---AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKV 161
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-218 |
1.30e-70 |
|
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: 217.83 E-value: 1.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQgtrsIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLsERELTRAR 81
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVALPLelnntpkaeiktrvnellelvsladkhdaypanlSGGQKQRVAIARALANSPKV 161
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQ 218
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-246 |
4.78e-70 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 219.29 E-value: 4.78e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFqqGtrSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQ----------DLT 70
Cdd:COG4598 8 ALEVRDLHKSF--G--DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpdrdgELV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 71 SLSERELTRARRQIGMIFQHFNLLSSRTVFGNVAL-PLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRV 149
Cdd:COG4598 84 PADRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 150 AIARALANSPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIF 229
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVF 242
|
250
....*....|....*..
gi 502950432 230 SHPKTPVAQEFIKSTLH 246
Cdd:COG4598 243 GNPKSERLRQFLSSSLK 259
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-243 |
1.48e-69 |
|
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: 217.17 E-value: 1.48e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTrsiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraR 81
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKH--DAYPANLSGGQKQRVAIARALANSP 159
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQE 239
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAE 234
|
....
gi 502950432 240 FIKS 243
Cdd:cd03295 235 FVGA 238
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-233 |
3.16e-68 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 222.09 E-value: 3.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 11 FQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPT---SGQVLVNGQDLTSLSERELtraRRQIGMI 87
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR---GRRIGMV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 88 FQHF-NLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDE 166
Cdd:COG1123 89 FQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 167 ATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPK 233
Cdd:COG1123 169 PTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
18-233 |
6.81e-67 |
|
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: 211.05 E-value: 6.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 18 IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltRARRQIGMIFQHFNLLSSR 97
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR--IARLGIARTFQNPRLFPEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 98 TVFGNVALPLE----------LNNTPK-----AEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVL 162
Cdd:COG0411 95 TVLENVLVAAHarlgrgllaaLLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502950432 163 LCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPK 233
Cdd:COG0411 175 LLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-228 |
9.63e-67 |
|
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: 209.73 E-value: 9.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFqqgtRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNML-----ERPTSGQVLVNGQDLTSLSERE 76
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 77 LTRaRRQIGMIFQHFNLLSSrTVFGNVALPLELNNT-PKAEIKTRVNELLELVSLAD--KHDAYPANLSGGQKQRVAIAR 153
Cdd:cd03260 77 LEL-RRRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502950432 154 ALANSPKVLLCDEATSALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEI 228
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-248 |
1.85e-65 |
|
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: 215.32 E-value: 1.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 10 IFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLErPTSGQVLVNGQDLTSLSERELTRARRQIGMIFQ 89
Cdd:COG4172 291 LFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 90 H-FNLLSSR-TVFGNVALPLELNNTP--KAEIKTRVNELLELVSL-ADKHDAYPANLSGGQKQRVAIARALANSPKVLLC 164
Cdd:COG4172 370 DpFGSLSPRmTVGQIIAEGLRVHGPGlsAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 165 DEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFIKST 244
Cdd:COG4172 450 DEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAA 529
|
....
gi 502950432 245 LHLD 248
Cdd:COG4172 530 PLLE 533
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-241 |
4.57e-65 |
|
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: 205.55 E-value: 4.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTrsikALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEreltrAR 81
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP-----HK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKV 161
Cdd:cd03300 72 RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFI 241
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-241 |
4.82e-65 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 209.16 E-value: 4.82e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQqgtrSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltra 80
Cdd:COG3839 3 SLELENVSKSYG----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 rRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:COG3839 75 -RNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 161 VLLCDEATSALDP---ATTRSileLLKDINRRLGLTILLITHE----MdvvkRICDQVAVISGGQLIEQDIVSEIFSHPK 233
Cdd:COG3839 154 VFLLDEPLSNLDAklrVEMRA---EIKRLHRRLGTTTIYVTHDqveaM----TLADRIAVMNDGRIQQVGTPEELYDRPA 226
|
....*....
gi 502950432 234 TP-VAQeFI 241
Cdd:COG3839 227 NLfVAG-FI 234
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-261 |
2.34e-64 |
|
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: 204.97 E-value: 2.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTRsiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDltSLSERELTRAR 81
Cdd:TIGR04520 1 IEVENVSFSYPESEK--PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQH-FNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:TIGR04520 77 KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMD-VVKriCDQVAVISGGQLIEQDIVSEIFSHpktpvaQE 239
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEeAVL--ADRVIVMNKGKIVAEGTPREIFSQ------VE 228
|
250 260
....*....|....*....|..
gi 502950432 240 FIKStLHLDIPedYLQKLQSEF 261
Cdd:TIGR04520 229 LLKE-IGLDVP--FITELAKAL 247
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-233 |
1.32e-63 |
|
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: 201.90 E-value: 1.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 18 IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltRARRQIGMIFQHFNLLSSR 97
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE--IARLGIGRTFQIPRLFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 98 TVFGNVALPLELNNTP----------KAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEA 167
Cdd:cd03219 91 TVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502950432 168 TSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPK 233
Cdd:cd03219 171 AAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-241 |
3.02e-63 |
|
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: 201.03 E-value: 3.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQgtrsIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltrar 81
Cdd:cd03296 3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVALPLEL----NNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALAN 157
Cdd:cd03296 74 RNVGFVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 158 SPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVA 237
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFV 233
|
....
gi 502950432 238 QEFI 241
Cdd:cd03296 234 YSFL 237
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-241 |
6.18e-63 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 200.65 E-value: 6.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVN-MLER-P---TSGQVLVNGQDLTSlSERELTRARRQIGMIFQHFNL 93
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrMNDLiPgarVEGEILLDGEDIYD-PDVDVVELRRRVGMVFQKPNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 94 LSSrTVFGNVALPLELN-NTPKAEIKTRVNELLELVSL----ADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEAT 168
Cdd:COG1117 104 FPK-SIYDNVAYGLRLHgIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502950432 169 SALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFI 241
Cdd:COG1117 183 SALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-242 |
1.08e-62 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 199.55 E-value: 1.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTrsikALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLT--SLSERELt 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQ----VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 79 raRRQIGMIFQHFNLLSSRTVFGNVAL-PLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALAN 157
Cdd:PRK09493 76 --RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 158 SPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVA 237
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRL 232
|
....*
gi 502950432 238 QEFIK 242
Cdd:PRK09493 233 QEFLQ 237
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-242 |
3.87e-61 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 195.36 E-value: 3.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINkiFQQGTRSIKAlsdiDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEreltrA 80
Cdd:COG3840 1 MLRLDDLT--YRYGDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-----A 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:COG3840 70 ERPVSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEF 240
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
|
..
gi 502950432 241 IK 242
Cdd:COG3840 230 LG 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-272 |
8.11e-61 |
|
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: 203.38 E-value: 8.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 11 FQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKS-TLIRCVNMLERP---TSGQVLVNGQDLTSLSERELTRAR-RQIG 85
Cdd:COG4172 16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERELRRIRgNRIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 86 MIFQ---------HfnllssrTVFGNVALPLEL-NNTPKAEIKTRVNELLELVSLADKH---DAYPANLSGGQKQRVAIA 152
Cdd:COG4172 96 MIFQepmtslnplH-------TIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 153 RALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHP 232
Cdd:COG4172 169 MALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAP 248
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 502950432 233 KTPVAQEFIKSTLHLDIPedylqklqsEFAPDLSPLLKLE 272
Cdd:COG4172 249 QHPYTRKLLAAEPRGDPR---------PVPPDAPPLLEAR 279
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-242 |
8.88e-61 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 194.85 E-value: 8.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQqgtrSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDL---TSLSERELT 78
Cdd:COG4161 3 IQLKNINCFYG----SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 79 RARRQIGMIFQHFNLLSSRTVFGN-VALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALAN 157
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 158 SPKVLLCDEATSALDPATTRSILELLKDINrRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDiVSEIFSHPKTPVA 237
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQPQTEAF 236
|
....*
gi 502950432 238 QEFIK 242
Cdd:COG4161 237 AHYLS 241
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-228 |
5.27e-59 |
|
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: 190.07 E-value: 5.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQqgtrSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTslseRELTRA 80
Cdd:COG4555 1 MIEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR----KEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEI 228
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-245 |
1.93e-58 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 189.19 E-value: 1.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTrsikALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNgqDLT-----SLSER 75
Cdd:PRK11264 3 AIEVKNLVKKFHGQT----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DITidtarSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 76 E-LTRA-RRQIGMIFQHFNLLSSRTVFGNVAL-PLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIA 152
Cdd:PRK11264 77 KgLIRQlRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 153 RALANSPKVLLCDEATSALDP-------ATTRSILEllkdiNRRlglTILLITHEMDVVKRICDQVAVISGGQLIEQDIV 225
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPelvgevlNTIRQLAQ-----EKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
|
250 260
....*....|....*....|
gi 502950432 226 SEIFSHPKTPVAQEFIKSTL 245
Cdd:PRK11264 229 KALFADPQQPRTRQFLEKFL 248
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-219 |
1.78e-57 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 185.85 E-value: 1.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTrsiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:PRK10908 78 RRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDINrRLGLTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
2.39e-57 |
|
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: 186.40 E-value: 2.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINkiFQQGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtra 80
Cdd:COG1120 1 MLEAENLS--VGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVAL---P-LELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALA 156
Cdd:COG1120 74 ARRIAYVPQEPPAPFGLTVRELVALgryPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502950432 157 NSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFS 230
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-235 |
9.16e-57 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 184.45 E-value: 9.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQqgtrSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQ--DLTS-LSERELT 78
Cdd:PRK11124 3 IQLNGINCFYG----AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKtPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 79 RARRQIGMIFQHFNLLSSRTVFGN-VALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALAN 157
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 158 SPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEiFSHPKTP 235
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTE 234
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-222 |
6.90e-55 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 178.60 E-value: 6.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQqgtrSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltrar 81
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKV 161
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502950432 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQlIEQ 222
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ-IQQ 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-228 |
9.26e-55 |
|
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: 178.72 E-value: 9.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTslseRELTRARRQIGMIFQHFNLLSSRTV 99
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRRRIGIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSI 179
Cdd:cd03265 91 WENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502950432 180 LELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEI 228
Cdd:cd03265 171 WEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-219 |
2.03e-54 |
|
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: 176.05 E-value: 2.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTrsikALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTslseRELTRAR 81
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFgnvalplelnntpkaeiktrvnELLELvsladkhdaypanlSGGQKQRVAIARALANSPKV 161
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVR----------------------ENLKL--------------SGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-248 |
4.29e-54 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 181.05 E-value: 4.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQgtrsIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltrar 81
Cdd:PRK10851 3 IEIANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVALPLEL---NNTP-KAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALAN 157
Cdd:PRK10851 74 RKVGFVFQHYALFRHMTVFDNIAFGLTVlprRERPnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 158 SPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQlIEQ-DIVSEIFSHPKTPV 236
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGN-IEQaGTPDQVWREPATRF 232
|
250
....*....|..
gi 502950432 237 AQEFIKSTLHLD 248
Cdd:PRK10851 233 VLEFMGEVNRLQ 244
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
14-267 |
8.00e-54 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 179.39 E-value: 8.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 14 GTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRARRQIGMIFQH-FN 92
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 93 LLSSRTVFGNV-ALPLELN-NTPKAEIKTRVNELLELVSLADKH-DAYPANLSGGQKQRVAIARALANSPKVLLCDEATS 169
Cdd:PRK11308 104 SLNPRKKVGQIlEEPLLINtSLSAAERREKALAMMAKVGLRPEHyDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 170 ALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFIKSTLHLDi 249
Cdd:PRK11308 184 ALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSATPRLN- 262
|
250 260
....*....|....*....|
gi 502950432 250 PEDYLQ--KLQSEFAPDLSP 267
Cdd:PRK11308 263 PDDRREriKLTGELPSPLNP 282
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-232 |
3.10e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 175.28 E-value: 3.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTslsereltRARRQIGMIFQHFNLLSSR-- 97
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR--------RARRRIGYVPQRAEVDWDFpi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 98 TVFGNVAL----PLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDP 173
Cdd:COG1121 93 TVRDVVLMgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 174 ATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQL--------IEQDIVSEIFSHP 232
Cdd:COG1121 173 ATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVahgppeevLTPENLSRAYGGP 238
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-232 |
5.75e-53 |
|
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: 178.37 E-value: 5.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 23 DIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSlSERELTRA--RRQIGMIFQHFNLLSSRTVF 100
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD-SARGIFLPphRRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 GNvalpLE--LNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRS 178
Cdd:COG4148 96 GN----LLygRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502950432 179 ILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHP 232
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-245 |
8.65e-53 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 174.77 E-value: 8.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQD----------LTSLSERELTRARRQIGMIF 88
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqLKVADKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 89 QHFNLLSSRTVFGNV-ALPLELNNTPKAEIKTRVNELLELVSLADK-HDAYPANLSGGQKQRVAIARALANSPKVLLCDE 166
Cdd:PRK10619 99 QHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 167 ATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFIKSTL 245
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLKGSL 256
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-259 |
1.39e-52 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 174.82 E-value: 1.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQdltSLSERELTRARRQIGMIFQH-FNLLSSRT 98
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVRRQVGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 99 VFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRS 178
Cdd:PRK13635 99 VQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRRE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 179 ILELLKDINRRLGLTILLITHEMDVVKRiCDQVAVISGGQLIEQDIVSEIFSHpktpvAQEFIKstLHLDIPedYLQKLQ 258
Cdd:PRK13635 179 VLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS-----GHMLQE--IGLDVP--FSVKLK 248
|
.
gi 502950432 259 S 259
Cdd:PRK13635 249 E 249
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-219 |
1.48e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 172.31 E-value: 1.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINkiFQQGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraR 81
Cdd:COG4619 1 LELEGLS--FRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSrTVFGNVALPLELNNtpKAEIKTRVNELLELVSLAD---KHDAypANLSGGQKQRVAIARALANS 158
Cdd:COG4619 74 RQVAYVPQEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPPdilDKPV--ERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502950432 159 PKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-241 |
2.11e-52 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 177.06 E-value: 2.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTrsikALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEReltraR 81
Cdd:PRK09452 15 VELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-----N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKV 161
Cdd:PRK09452 86 RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 162 LLCDEATSALDpATTRSILEL-LKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQlIEQD-IVSEIFSHPKTPVAQE 239
Cdd:PRK09452 166 LLLDESLSALD-YKLRKQMQNeLKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR-IEQDgTPREIYEEPKNLFVAR 243
|
..
gi 502950432 240 FI 241
Cdd:PRK09452 244 FI 245
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-241 |
2.32e-52 |
|
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: 172.91 E-value: 2.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEReltraRRQIGMIFQHFNLLSSRTVF 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 GNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSIL 180
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502950432 181 ELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFI 241
Cdd:cd03299 170 EELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-239 |
4.63e-52 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 173.33 E-value: 4.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRARRQIGMIFQH----FNllSS 96
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDsisaVN--PR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 97 RTVFGNVALPLE-LNNTPKAEIKTRVNELLELVSLADKH-DAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPA 174
Cdd:PRK10419 106 KTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 175 TTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEI--FSHPKTPVAQE 239
Cdd:PRK10419 186 LQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKltFSSPAGRVLQN 252
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
20-288 |
5.79e-51 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 173.48 E-value: 5.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEReltraRRQIGMIFQHFNLLSSRTV 99
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY-----QRPINMMFQSYALFPHMTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPA-TTRS 178
Cdd:PRK11607 109 EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlRDRM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 179 ILELLkDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFIKStlhLDIPEDYLQKLQ 258
Cdd:PRK11607 189 QLEVV-DILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS---VNVFEGVLKERQ 264
|
250 260 270
....*....|....*....|....*....|....
gi 502950432 259 SEF----APDLSPLLKLEFTGKSVDAPLISMAVR 288
Cdd:PRK11607 265 EDGlvidSPGLVHPLKVDADASVVDNVPVHVALR 298
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-234 |
6.05e-51 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 172.98 E-value: 6.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 4 LTQINKIFQQGTrsikALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltrarRQ 83
Cdd:PRK11432 9 LKNITKRFGSNT----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-----RD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 84 IGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLL 163
Cdd:PRK11432 80 ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502950432 164 CDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKT 234
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-216 |
7.95e-51 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 168.84 E-value: 7.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 R-RQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSP 159
Cdd:PRK11629 85 RnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISG 216
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-222 |
1.10e-50 |
|
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: 179.26 E-value: 1.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINkiFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraR 81
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---R 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHfNLLSSRTVFGNVALplelnNTPKAEIKtRVNELLELVSLADKHDAYP-----------ANLSGGQKQRVA 150
Cdd:COG2274 549 RQIGVVLQD-VFLFSGTIRENITL-----GDPDATDE-EIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502950432 151 IARALANSPKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVkRICDQVAVISGGQLIEQ 222
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIVED 690
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
11-235 |
2.37e-50 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 170.66 E-value: 2.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 11 FQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRARRQIGMIFQH 90
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 91 -FNLLSSRTVFGNV-ALPLEL--NNTPKAEIKTRVNELLELVSL-ADKHDAYPANLSGGQKQRVAIARALANSPKVLLCD 165
Cdd:PRK15079 107 pLASLNPRMTIGEIiAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 166 EATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTP 235
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHP 256
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-202 |
4.80e-50 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 167.73 E-value: 4.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSereltrA 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG------A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRqiGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:COG4525 77 DR--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMD 202
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVE 196
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-220 |
4.83e-50 |
|
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: 166.53 E-value: 4.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFqqGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSlserELTRAR 81
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKV 161
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 162 LLCDEATSALDPATTRSILELLKDInrRLGLTILLITHEMDVVKRICDQVAVISGGQLI 220
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-246 |
2.05e-49 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 165.86 E-value: 2.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 8 NKIFQQGTR----SIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNML-----ERPTSGQVLVNGQDLTSLSERELt 78
Cdd:PRK14247 2 NKIEIRDLKvsfgQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 79 raRRQIGMIFQHFNLLSSRTVFGNVALPLELNN--TPKAEIKTRVNELLELVSL----ADKHDAYPANLSGGQKQRVAIA 152
Cdd:PRK14247 81 --RRRVQMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 153 RALANSPKVLLCDEATSALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHP 232
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
250
....*....|....
gi 502950432 233 KTPVAQEFIKSTLH 246
Cdd:PRK14247 237 RHELTEKYVTGRLY 250
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-243 |
5.88e-49 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 165.01 E-value: 5.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGT-----RSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERe 76
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 77 lTRARRqIGMIFQHFNL-LSSRTVFGNV-ALPLELN-NTPKAEIKTRVNELLELVSLADKH-DAYPANLSGGQKQRVAIA 152
Cdd:COG4167 84 -YRCKH-IRMIFQDPNTsLNPRLNIGQIlEEPLRLNtDLTAEEREERIFATLRLVGLLPEHaNFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 153 RALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHP 232
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
250
....*....|.
gi 502950432 233 KTPVAQEFIKS 243
Cdd:COG4167 242 QHEVTKRLIES 252
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-169 |
5.92e-49 |
|
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: 161.28 E-value: 5.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLLSSRTVF 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL---RKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502950432 101 GNVALPLELNNTPKAEIKTRVNELLELVSLADKHD----AYPANLSGGQKQRVAIARALANSPKVLLCDEATS 169
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-217 |
1.13e-48 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 162.70 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTslsereltRARRQIGMIFQHFNLLSSR-- 97
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE--------KERKRIGYVPQRRSIDRDFpi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 98 TVFGNVALPL----ELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDP 173
Cdd:cd03235 86 SVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502950432 174 ATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGG 217
Cdd:cd03235 166 KTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-254 |
1.13e-48 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 164.90 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTslsERELTRARRQIGMIFQH-FNLLSSRTV 99
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWDIRHKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSI 179
Cdd:PRK13650 100 EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 180 LELLKDINRRLGLTILLITHEMDVVKrICDQVAVISGGQLIEQDIVSEIFSHPK--------TPVAQEFIKSTLH--LDI 249
Cdd:PRK13650 180 IKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNdllqlgldIPFTTSLVQSLRQngYDL 258
|
....*
gi 502950432 250 PEDYL 254
Cdd:PRK13650 259 PEGYL 263
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-218 |
6.14e-48 |
|
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: 159.09 E-value: 6.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 11 FQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQH 90
Cdd:cd03228 8 FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---RKNIAYVPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 91 FNLLSsRTVFGNValplelnntpkaeiktrvnellelvsladkhdaypanLSGGQKQRVAIARALANSPKVLLCDEATSA 170
Cdd:cd03228 85 PFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502950432 171 LDPATTRSILELLKdiNRRLGLTILLITHEMDVVKRiCDQVAVISGGQ 218
Cdd:cd03228 127 LDPETEALILEALR--ALAKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-228 |
1.57e-47 |
|
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: 159.91 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 18 IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltRARRQIGMIFQHFNLLSSR 97
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE--RARAGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 98 TVFGNVALPLELNntPKAEIKTRVNELLELVS-LADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATT 176
Cdd:cd03224 91 TVEENLLLGAYAR--RRAKRKARLERVYELFPrLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502950432 177 RSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEI 228
Cdd:cd03224 169 EEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-218 |
3.27e-47 |
|
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: 157.02 E-value: 3.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 3 RLTQINKIFQQGTrsikALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRR 82
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL---RR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 83 QIGMIFQhfnllssrtvfgnvalplelnntpkaeiktrvnellelvsladkhdaypanLSGGQKQRVAIARALANSPKVL 162
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502950432 163 LCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQ 218
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-229 |
4.12e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 160.98 E-value: 4.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTR-SIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSlSERELTRA 80
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNL-LSSRTVFGNVAL-PLELNNTpKAEIKTRVNELLELVSLA--DKHDAYPANLSGGQKQRVAIARALA 156
Cdd:PRK13637 82 RKKVGLVFQYPEYqLFEETIEKDIAFgPINLGLS-EEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502950432 157 NSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIF 229
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-222 |
6.60e-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: 6.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQhfnllssrtvf 100
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---ARKIAYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 gnvalplelnntpkaeiktrvneLLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSIL 180
Cdd:cd03214 81 -----------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502950432 181 ELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQ 222
Cdd:cd03214 138 ELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-234 |
2.12e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 158.70 E-value: 2.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLtSLSERELTRARRQIGMIFQHF-NLLSSRT 98
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKTVGIVFQNPdDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 99 VFGNVAL-PLELNnTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTR 177
Cdd:PRK13639 96 VEEDVAFgPLNLG-LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 178 SILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKT 234
Cdd:PRK13639 175 QIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-223 |
2.29e-46 |
|
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: 156.69 E-value: 2.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 23 DIDLHVPqGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSER-ELTRARRQIGMIFQHFNLLSSRTVFG 101
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 102 NVALPLELNNtpKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILE 181
Cdd:cd03297 95 NLAFGLKRKR--NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502950432 182 LLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQD 223
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-228 |
3.07e-46 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 163.65 E-value: 3.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFqqgtRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltrA 80
Cdd:COG1129 4 LLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD---A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQ-IGMIFQHFNLLSSRTVFGNVALPLELNNTP---KAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALA 156
Cdd:COG1129 77 QAAgIAIIHQELNLVPNLSVAENIFLGREPRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502950432 157 NSPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEI 228
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-218 |
3.93e-46 |
|
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: 156.44 E-value: 3.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIF---QQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQ----DLTSLS 73
Cdd:COG4778 4 LLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 74 ERELTRARRQ-IGMIFQHFNLL---SSRTVfgnVALPLELNNTPKAEIKTRVNELLELVSLADK-HDAYPANLSGGQKQR 148
Cdd:COG4778 84 PREILALRRRtIGYVSQFLRVIprvSALDV---VAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 149 VAIARALANSPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQ 218
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-245 |
4.09e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 157.31 E-value: 4.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNML-----ERPTSGQVLVNGQDLTSlSERELTRARRQIGMIFQHFNLLS 95
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYS-PDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 96 SRTVFGNVALPLELNN--TPKAEIKTRVNELLELVSL----ADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATS 169
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502950432 170 ALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFIKSTL 245
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGAL 252
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-222 |
5.73e-46 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 164.57 E-value: 5.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIYGVIGSSGAGKSTLircVNMLER---PTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLLS 95
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTL---VNLLLRfydPTSGRILIDGVDIRDLTLESL---RRQIGVVPQDTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 96 sRTVFGNVALPLElnNTPKAEIKtrvnELLELVSLADKHDAYP-----------ANLSGGQKQRVAIARALANSPKVLLC 164
Cdd:COG1132 428 -GTIRENIRYGRP--DATDEEVE----EAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 165 DEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDQVAVISGGQLIEQ 222
Cdd:COG1132 501 DEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-222 |
5.85e-46 |
|
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: 155.73 E-value: 5.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 23 DIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEreltrARRQIGMIFQHFNLLSSRTVFGN 102
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP-----ADRPVSMLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 103 VALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILEL 182
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502950432 183 LKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQ 222
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-272 |
1.14e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 157.10 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTR-SIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTS-LSERELTR 79
Cdd:PRK13634 3 ITFQKVEHRYQYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 80 ARRQIGMIFQhF--NLLSSRTVFGNVAL-PLELNnTPKAEIKTRVNELLELVSL-ADKHDAYPANLSGGQKQRVAIARAL 155
Cdd:PRK13634 83 LRKKVGIVFQ-FpeHQLFEETVEKDICFgPMNFG-VSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 156 ANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTP 235
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 502950432 236 VAqefikstLHLDIPE--DYLQKLQSEFAPDL-SPLLKLE 272
Cdd:PRK13634 241 EA-------IGLDLPEtvKFKRALEEKFGISFpKPCLTLE 273
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-220 |
2.52e-45 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 161.35 E-value: 2.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFqqGtrSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltrA 80
Cdd:COG3845 5 ALELRGITKRF--G--GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQ-IGMIFQHFNLLSSRTVFGNVAL---PLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALA 156
Cdd:COG3845 78 IALgIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502950432 157 NSPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLI 220
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-250 |
3.81e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 155.15 E-value: 3.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTqiNKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSereLTRA 80
Cdd:PRK13632 7 MIKVE--NVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN---LKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQH-FNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSP 159
Cdd:PRK13632 82 RKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMD-VVKriCDQVAVISGGQLIEQDIVSEIFSHpktpvaQ 238
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDeAIL--ADKVIVFSEGKLIAQGKPKEILNN------K 233
|
250
....*....|..
gi 502950432 239 EFIKStLHLDIP 250
Cdd:PRK13632 234 EILEK-AKIDSP 244
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-219 |
5.17e-45 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 154.45 E-value: 5.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 3 RLTQ-----INKIFQQ-GTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGqdlTSLSEre 76
Cdd:PRK11247 6 RLNQgtpllLNAVSKRyGERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT---APLAE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 77 ltrARRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEiktrvnELLELVSLADKHDAYPANLSGGQKQRVAIARALA 156
Cdd:PRK11247 79 ---AREDTRLMFQDARLLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502950432 157 NSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
1.21e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 154.24 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTrsiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLtSLSERELTRA 80
Cdd:PRK13636 5 ILKVEELNYNYSDGT---HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQH-FNLLSSRTVFGNVAL-PLELNnTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANS 158
Cdd:PRK13636 81 RESVGMVFQDpDNQLFSASVYQDVSFgAVNLK-LPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502950432 159 PKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFS 230
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-254 |
1.25e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 154.09 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 15 TRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDltSLSERELTRARRQIGMIFQH-FNL 93
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD--TSDEENLWDIRNKAGMVFQNpDNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 94 LSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDP 173
Cdd:PRK13633 98 IVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 174 ATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDQVAVISGGQLIEQDIVSEIFSHPK------------TPVAQEFI 241
Cdd:PRK13633 178 SGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEmmkkigldvpqvTELAYELK 256
|
250
....*....|...
gi 502950432 242 KSTlhLDIPEDYL 254
Cdd:PRK13633 257 KEG--VDIPSDIL 267
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-220 |
3.88e-44 |
|
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: 149.12 E-value: 3.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFqqgtRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltrAR 81
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD---AR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQ-IGMIFQhfnllssrtvfgnvalplelnntpkaeiktrvnellelvsladkhdaypanLSGGQKQRVAIARALANSPK 160
Cdd:cd03216 74 RAgIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLI 220
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-228 |
5.80e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 152.96 E-value: 5.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFqqGTRsiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSlsereltRA 80
Cdd:COG4152 1 MLELKGLTKRF--GDK--TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-------ED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIG-----------MifqhfnllssrTVfGNVALPL-ELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQR 148
Cdd:COG4152 70 RRRIGylpeerglypkM-----------KV-GEQLVYLaRLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 149 VAIARALANSPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEI 228
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-220 |
6.37e-44 |
|
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: 150.60 E-value: 6.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDlTSLSEREltrA 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD-VVKEPAE---A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLI 220
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-242 |
7.30e-44 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 155.58 E-value: 7.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRARRQ-IGMIFQHFNLLSSRT 98
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 99 VFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRS 178
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502950432 179 ILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFIK 242
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-222 |
1.39e-43 |
|
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: 149.27 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFqqgtRSIKALSDIDLHVPQGqIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTslseRELTRAR 81
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKV 161
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502950432 162 LLCDEATSALDPATTRSILELLKDI--NRrlglTILLITHEMDVVKRICDQVAVISGGQLIEQ 222
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELgeDR----IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-261 |
1.66e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 151.47 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGT-RSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLS-ERELTR 79
Cdd:PRK13646 3 IRFDNVSYTYQKGTpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 80 ARRQIGMIFQH-----FNLLSSRTV-FG--NVALPLElnntpkaEIKTRVNELL-ELVSLADKHDAYPANLSGGQKQRVA 150
Cdd:PRK13646 83 VRKRIGMVFQFpesqlFEDTVEREIiFGpkNFKMNLD-------EVKNYAHRLLmDLGFSRDVMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 151 IARALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFS 230
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
250 260 270
....*....|....*....|....*....|.
gi 502950432 231 HpKTPVAQefikstLHLDIPEdyLQKLQSEF 261
Cdd:PRK13646 236 D-KKKLAD------WHIGLPE--IVQLQYDF 257
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-260 |
2.70e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 150.72 E-value: 2.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRARRQIGMIFQH-FNLLSSRT 98
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKVGIVFQNpDNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 99 VFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRS 178
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 179 ILELLKDINRRLGLTILLITHEMDVVKrICDQVAVISGGQLIEQDIVSEIFSHPktpvaqEFIKStLHLDIPedYLQKLQ 258
Cdd:PRK13640 182 ILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKV------EMLKE-IGLDIP--FVYKLK 251
|
..
gi 502950432 259 SE 260
Cdd:PRK13640 252 NK 253
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
20-222 |
4.13e-43 |
|
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: 156.46 E-value: 4.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLLSSrTV 99
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---RRQIAWVPQNPYLFAG-TI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVALplelnNTPKAEiKTRVNELLELVSLADKHDAYP-----------ANLSGGQKQRVAIARALANSPKVLLCDEAT 168
Cdd:COG4988 428 RENLRL-----GRPDAS-DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPT 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502950432 169 SALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDQVAVISGGQLIEQ 222
Cdd:COG4988 502 AHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQ 552
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
11-231 |
3.14e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 147.59 E-value: 3.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 11 FQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQH 90
Cdd:PRK13648 15 FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL---RKHIGIVFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 91 -FNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATS 169
Cdd:PRK13648 92 pDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502950432 170 ALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDQVAVISGGQLIEQDIVSEIFSH 231
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
11-238 |
3.92e-42 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 147.60 E-value: 3.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 11 FQQGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRARRQIGMIFQH 90
Cdd:PRK11831 15 FTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 91 FNLLSSRTVFGNVALPL-ELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATS 169
Cdd:PRK11831 93 GALFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 170 ALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQ 238
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQ 241
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-222 |
5.14e-42 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 145.05 E-value: 5.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTrsikALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEreltrAR 81
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-----AL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAeiktRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKV 161
Cdd:cd03268 72 RRIGALIEAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502950432 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQ 222
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-220 |
5.15e-42 |
|
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: 145.09 E-value: 5.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 6 QINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLtSLSEReltraRRQIG 85
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-KAKER-----RKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 86 MIFQHFNllssRTVFGN-VALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLC 164
Cdd:cd03226 75 YVMQDVD----YQLFTDsVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502950432 165 DEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLI 220
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-238 |
9.63e-42 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 153.73 E-value: 9.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQ-IGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSP 159
Cdd:PRK10535 84 RREhFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 160 KVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRiCDQVAVISGGQlieqdIVSEIFSHPKTPVAQ 238
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGE-----IVRNPPAQEKVNVAG 235
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
15-250 |
1.04e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 146.49 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 15 TRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFN-L 93
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV---RKFVGLVFQNPDdQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 94 LSSRTVFGNVAL-PLELNnTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALD 172
Cdd:PRK13652 91 IFSPTVEQDIAFgPINLG-LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 173 PATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKtpvaqefIKSTLHLDIP 250
Cdd:PRK13652 170 PQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD-------LLARVHLDLP 240
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-222 |
6.63e-41 |
|
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: 143.40 E-value: 6.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 11 FQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQH 90
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL---RRQVGVVLQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 91 fNLLSSRTVFGNVALplelnntpkAEIKTRVNELLELVSLADKHD-------AYP-------ANLSGGQKQRVAIARALA 156
Cdd:cd03252 85 -NVLFNRSIRDNIAL---------ADPGMSMERVIEAAKLAGAHDfiselpeGYDtivgeqgAGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502950432 157 NSPKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDQVAVISGGQLIEQ 222
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQ 217
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-217 |
9.96e-41 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 142.60 E-value: 9.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtrarrqigMIFQHFNLLSSRTVF 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 GNVALPLE--LNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRS 178
Cdd:TIGR01184 73 ENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 502950432 179 ILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGG 217
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-248 |
1.43e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 143.73 E-value: 1.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTR-SIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSE-RELTR 79
Cdd:PRK13649 3 INLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 80 ARRQIGMIFQhF--NLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADK-HDAYPANLSGGQKQRVAIARALA 156
Cdd:PRK13649 83 IRKKVGLVFQ-FpeSQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 157 NSPKVLLCDEATSALDPATTRSILELLKDINrRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSH----- 231
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDvdfle 240
|
250 260
....*....|....*....|....
gi 502950432 232 ------PK-TPVAQEFIKSTLHLD 248
Cdd:PRK13649 241 ekqlgvPKiTKFAQRLADRGISFS 264
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-201 |
1.60e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 142.92 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRS-IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltR 79
Cdd:COG1101 1 MLELKNLSKTFNPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 80 ARRqIGMIFQhfNLL----SSRTVFGNVALPLE----------LNNTPKAEIKTRVnELLELvSLADKHDAYPANLSGGQ 145
Cdd:COG1101 79 AKY-IGRVFQ--DPMmgtaPSMTIEENLALAYRrgkrrglrrgLTKKRRELFRELL-ATLGL-GLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502950432 146 KQRVAIARALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEM 201
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
6-222 |
3.15e-40 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 141.07 E-value: 3.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 6 QINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRAR-RQI 84
Cdd:PRK10584 11 HLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 85 GMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLC 164
Cdd:PRK10584 91 GFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 165 DEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDQVAVISGGQLIEQ 222
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-219 |
6.29e-40 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 140.49 E-value: 6.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIkalsdiDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEreltrA 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRF------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP-----S 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:PRK10771 70 RRPVSMLFQENNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:PRK10771 150 ILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-222 |
9.52e-40 |
|
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: 140.37 E-value: 9.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 18 IKALSDIDLHVPQGQIYGVIGSSGAGKSTlirCVNMLER---PTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLL 94
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERfydPTSGEILLDGVDIRDLNLRWL---RSQIGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 95 SsRTVFGNVALplELNNTPKAEIK--TRVNELLELV-SLADKHD----AYPANLSGGQKQRVAIARALANSPKVLLCDEA 167
Cdd:cd03249 90 D-GTIAENIRY--GKPDATDEEVEeaAKKANIHDFImSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502950432 168 TSALDPATTRSILELLKdiNRRLGLTILLITHEMDVVKRiCDQVAVISGGQLIEQ 222
Cdd:cd03249 167 TSALDAESEKLVQEALD--RAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQ 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-233 |
1.06e-39 |
|
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: 139.99 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFqqGTRsiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltRAR 81
Cdd:cd03218 1 LRAENLSKRY--GKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK--RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKV 161
Cdd:cd03218 75 LGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502950432 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPK 233
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-241 |
1.06e-39 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 140.68 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNML-----ERPTSGQVLVNGQDLTSlSERELTRARRQIGMIFQHFNL 93
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYS-PRTDTVDLRKEIGMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 94 LSSrTVFGNVALPLELNNTP-KAEIKTRVNELLELVSLADK-----HDAyPANLSGGQKQRVAIARALANSPKVLLCDEA 167
Cdd:PRK14239 98 FPM-SIYENVVYGLRLKGIKdKQVLDEAVEKSLKGASIWDEvkdrlHDS-ALGLSGGQQQRVCIARVLATSPKIILLDEP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502950432 168 TSALDPATTRSILELLkdINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFI 241
Cdd:PRK14239 176 TSALDPISAGKIEETL--LGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYI 247
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-233 |
1.24e-39 |
|
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: 139.73 E-value: 1.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 18 IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltRARRQIGMIFQHFNLLSSR 97
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHR--IARLGIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 98 TVFGNVALPLELNNtPKAEIKTRVNELLELV-SLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATT 176
Cdd:COG0410 94 TVEENLLLGAYARR-DRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 177 RSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPK 233
Cdd:COG0410 173 EEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-245 |
1.51e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 140.56 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNML-----ERPTSGQVLVNGQdltSLSERE--LTRARRQIGMIFQHF 91
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQ---NIYERRvnLNRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 92 NLLSsRTVFGNVALPLELNN-TPKAEIKTRVNELLELVSLAD--KHDAYPA--NLSGGQKQRVAIARALANSPKVLLCDE 166
Cdd:PRK14258 98 NLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDeiKHKIHKSalDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 167 ATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISG-----GQLIEQDIVSEIFSHPKTPVAQEFI 241
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTREYV 256
|
....
gi 502950432 242 KSTL 245
Cdd:PRK14258 257 LSRL 260
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-202 |
1.85e-39 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 138.38 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVN-MLERP--TSGQVLVNGQDLTSLSEReltraRRQIGMIFQ------HF 91
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLTALPAE-----QRRIGILFQddllfpHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 92 NllssrtVFGNV--ALPlelNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATS 169
Cdd:COG4136 92 S------VGENLafALP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190
....*....|....*....|....*....|...
gi 502950432 170 ALDPATTRSILELLKDINRRLGLTILLITHEMD 202
Cdd:COG4136 163 KLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-235 |
4.24e-39 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 146.15 E-value: 4.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 10 IFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRARRQIGMIFQ 89
Cdd:PRK10261 329 LLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 90 --HFNLLSSRTVFGNVALPLELNNTPKAE-IKTRVNELLELVSLADKHD-AYPANLSGGQKQRVAIARALANSPKVLLCD 165
Cdd:PRK10261 409 dpYASLDPRQTVGDSIMEPLRVHGLLPGKaAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 166 EATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTP 235
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHP 558
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-235 |
8.08e-39 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 141.02 E-value: 8.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 23 DIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSER-ELTRARRQIGMIFQHFNLLSSRTVFG 101
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 102 NvaLPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILE 181
Cdd:TIGR02142 95 N--LRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502950432 182 LLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTP 235
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLP 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-243 |
1.36e-38 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 140.36 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIKalsDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltra 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIK---GIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 rRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNE---LLELVSLADKHdayPANLSGGQKQRVAIARALAN 157
Cdd:PRK11650 76 -RDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEaarILELEPLLDRK---PRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 158 SPKVLLCDEATSALDpATTRSILEL-LKDINRRLGLTILLITHemDVVK--RICDQVAVISGGQlIEQdIVS--EIFSHP 232
Cdd:PRK11650 152 EPAVFLFDEPLSNLD-AKLRVQMRLeIQRLHRRLKTTSLYVTH--DQVEamTLADRVVVMNGGV-AEQ-IGTpvEVYEKP 226
|
250
....*....|.
gi 502950432 233 KTPVAQEFIKS 243
Cdd:PRK11650 227 ASTFVASFIGS 237
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-223 |
2.12e-38 |
|
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: 136.69 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 10 IFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGqdLTSLSEREltRARRQIGMIF- 88
Cdd:cd03267 26 LFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRK--KFLRRIGVVFg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 89 QHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEAT 168
Cdd:cd03267 102 QKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502950432 169 SALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQD 223
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-222 |
3.36e-38 |
|
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: 142.98 E-value: 3.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLircVNMLER---PTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLLSS 96
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTL---LALLLRfldPQSGSITLGGVDLRDLDEDDL---RRRIAVVPQRPHLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 97 rTVFGN--VALPlelnNTPKAEIKtrvnELLELVSLADKHDAYP-----------ANLSGGQKQRVAIARALANSPKVLL 163
Cdd:COG4987 424 -TLRENlrLARP----DATDEELW----AALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 164 CDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDQVAVISGGQLIEQ 222
Cdd:COG4987 495 LDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQ 550
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-241 |
3.84e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 136.72 E-value: 3.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNML------ERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLL 94
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKL---RKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 95 SSRTVFGNVALPLELNNTP-KAEIKTRVNELLELVSL----ADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATS 169
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502950432 170 ALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFI 241
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-257 |
3.96e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 137.17 E-value: 3.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 11 FQQGTRSIKALSdidLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQH 90
Cdd:PRK13647 14 YKDGTKALKGLS---LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---RSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 91 -FNLLSSRTVFGNVAL-PLELNNTPKaEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEAT 168
Cdd:PRK13647 88 pDDQVFSSTVWDDVAFgPVNMGLDKD-EVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 169 SALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQ---------LIEQDIVSEifSHPKTPVAqe 239
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRvlaegdkslLTDEDIVEQ--AGLRLPLV-- 241
|
250
....*....|....*...
gi 502950432 240 fikSTLHLDIPEDYLQKL 257
Cdd:PRK13647 242 ---AQIFEDLPELGQSKL 256
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-228 |
4.48e-38 |
|
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: 142.25 E-value: 4.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRS-IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVN-GQ---DLTSLSER 75
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDewvDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 76 ELTRARRQIGMIFQHFNLLSSRTVFGNV--ALPLELnntPKAEIKTRVNELLELVSLADKH-----DAYPANLSGGQKQR 148
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLteAIGLEL---PDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 149 VAIARALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIE----QDI 224
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKigdpEEI 515
|
....
gi 502950432 225 VSEI 228
Cdd:TIGR03269 516 VEEL 519
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-230 |
6.99e-38 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 136.05 E-value: 6.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINkiFQQGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:PRK13548 2 MLEARNLS--VRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RrqiGMIFQHFNLLSSRTVFGNVAL---PLELNNTPKAEIKTRVNELLELVSLADKHdaYPAnLSGGQKQRVAIARALA- 156
Cdd:PRK13548 78 R---AVLPQHSSLSFPFTVEEVVAMgraPHGLSRAEDDALVAAALAQVDLAHLAGRD--YPQ-LSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 157 -----NSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFS 230
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-220 |
1.56e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 136.37 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTRS-IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQV---LVNGQDLTSLSERE- 76
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTeLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 77 --------LTRA---------RRQIGMIFQ--HFNLLSSRT----VFGNVALplelnNTPKAEIKTRVNELLELVSLADK 133
Cdd:PRK13651 83 vleklviqKTRFkkikkikeiRRRVGVVFQfaEYQLFEQTIekdiIFGPVSM-----GVSKEEAKKRAAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 134 H-DAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVA 212
Cdd:PRK13651 158 YlQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTI 236
|
....*...
gi 502950432 213 VISGGQLI 220
Cdd:PRK13651 237 FFKDGKII 244
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-231 |
3.99e-37 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 133.98 E-value: 3.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGtrsiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNML---ERPTSGQVLVNGQDLTSLSE--R 75
Cdd:PRK09984 4 IIRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlaR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 76 ELTRARRQIGMIFQHFNLLSSRTVFGNVaLPLELNNTP---------KAEIKTRVNELLELVSLAdkHDAYP--ANLSGG 144
Cdd:PRK09984 80 DIRKSRANTGYIFQQFNLVNRLSVLENV-LIGALGSTPfwrtcfswfTREQKQRALQALTRVGMV--HFAHQrvSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 145 QKQRVAIARALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLI---- 220
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFydgs 236
|
250
....*....|.
gi 502950432 221 EQDIVSEIFSH 231
Cdd:PRK09984 237 SQQFDNERFDH 247
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-296 |
4.12e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 135.60 E-value: 4.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 11 FQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRcvnMLE---RPTSGQVLVNGQDLTslseRELTRARRQIGMi 87
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIK---MLTgilVPTSGEVRVLGYVPF----KRRKEFARRIGV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 88 fqhfnllssrtVFGNVA-----LP----LELN----NTPKAEIKTRVNELLELVSLADKHDAyPA-NLSGGQKQRVAIAR 153
Cdd:COG4586 100 -----------VFGQRSqlwwdLPaidsFRLLkaiyRIPDAEYKKRLDELVELLDLGELLDT-PVrQLSLGQRMRCELAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 154 ALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEI---FS 230
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELkerFG 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 231 HPKTpVAQEFIKSTLHLDIPEdYLQKLQSEfapdlSPLLKLEFTGKSVDAPLISMAVRRFNI-DISI 296
Cdd:COG4586 248 PYKT-IVLELAEPVPPLELPR-GGEVIERE-----GNRVRLEVDPRESLAEVLARLLARYPVrDLTI 307
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-254 |
6.98e-37 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 135.24 E-value: 6.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKS-TLIRCVNMLERP--TSGQVLVNGQDLTSLSERELTRAR-RQIGMIFQHfnlls 95
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKELNKLRaEQISMIFQD----- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 96 srtvfgnvalPL-ELNntPKAEIKTRVNELLELVSLADKHDA----------------------YPANLSGGQKQRVAIA 152
Cdd:PRK09473 106 ----------PMtSLN--PYMRVGEQLMEVLMLHKGMSKAEAfeesvrmldavkmpearkrmkmYPHEFSGGMRQRVMIA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 153 RALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHP 232
Cdd:PRK09473 174 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
250 260
....*....|....*....|..
gi 502950432 233 KTPVAQEFIKSTLHLDIPEDYL 254
Cdd:PRK09473 254 SHPYSIGLLNAVPRLDAEGESL 275
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-233 |
9.60e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 132.46 E-value: 9.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFqqGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltRA 80
Cdd:COG1137 3 TLEAENLVKSY--GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHK--RA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGM------IFQhfNLlssrTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARA 154
Cdd:COG1137 77 RLGIGYlpqeasIFR--KL----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 155 LANSPKVLLCDEATSALDPATTRSILELLKDINRRlGLTIlLIT-HEmdvVK---RICDQVAVISGGQLIEQDIVSEIFS 230
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADIQKIIRHLKER-GIGV-LITdHN---VRetlGICDRAYIISEGKVLAEGTPEEILN 225
|
...
gi 502950432 231 HPK 233
Cdd:COG1137 226 NPL 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-241 |
9.64e-37 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 132.98 E-value: 9.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLER--PT---SGQVLVNGQDLTSlSERELTRARRQIGMIFQHFNLL 94
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 95 SsRTVFGNVALPLELNNtpkaeIKTRVNELLELV--------SLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDE 166
Cdd:PRK14243 104 P-KSIYDNIAYGARING-----YKGDMDELVERSlrqaalwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 167 ATSALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDQVAVISG---------GQLIEQDIVSEIFSHPKTPVA 237
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNVeltegggryGYLVEFDRTEKIFNSPQQQAT 255
|
....
gi 502950432 238 QEFI 241
Cdd:PRK14243 256 RDYV 259
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-222 |
9.76e-37 |
|
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: 131.63 E-value: 9.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 7 INKIFqqgtRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTslserelTRARRQIGM 86
Cdd:cd03269 6 VTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-------IAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 87 IFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDE 166
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502950432 167 ATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQ 222
Cdd:cd03269 155 PFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-270 |
1.30e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 133.59 E-value: 1.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSER--ELTRARRQIGMIFQ--HFNLL 94
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVKRLRKEIGLVFQfpEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 95 SSrTVFGNVAL-PLELNNTpKAEIKTRVNELLELVSLADKH-DAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALD 172
Cdd:PRK13645 105 QE-TIEKDIAFgPVNLGEN-KQEAYKKVPELLKLVQLPEDYvKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 173 PATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHpktpvaQEFIkSTLHLDIPED 252
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN------QELL-TKIEIDPPKL 255
|
250 260 270
....*....|....*....|....*....|....
gi 502950432 253 Y--LQKLQS--------------EFAPDLSPLLK 270
Cdd:PRK13645 256 YqlMYKLKNkgidllnknirtieEFAKELAKVLK 289
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
23-243 |
1.90e-36 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 135.16 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 23 DIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTslserELTRARRQIGMIFQHFNLLSSRTVFGN 102
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-----DVPPAERGVGMVFQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 103 VALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILEL 182
Cdd:PRK11000 96 MSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502950432 183 LKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFIKS 243
Cdd:PRK11000 176 ISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGS 236
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-243 |
3.12e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 133.33 E-value: 3.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIYGVIGSSGAGKS----TLIRCVNMLERPTSGQVLVNGQDLTSLSEREltraRRQI-----GMIFQ 89
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKE----RRNLvgaevAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 90 H--FNLLSSRTVFGNVALPLELNNT-PKAEIKTRVNELLELVSLAD---KHDAYPANLSGGQKQRVAIARALANSPKVLL 163
Cdd:PRK11022 97 DpmTSLNPCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 164 CDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFIKS 243
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRA 256
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
8-256 |
3.56e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 132.14 E-value: 3.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 8 NKIFQQGTRS-IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGM 86
Cdd:PRK13642 9 NLVFKYEKESdVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL---RRKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 87 IFQH-FNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCD 165
Cdd:PRK13642 86 VFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 166 EATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDQVAVISGGQLIEQDIVSEIFSHPK--------TPVA 237
Cdd:PRK13642 166 ESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEdmveigldVPFS 244
|
250 260
....*....|....*....|.
gi 502950432 238 QEFIKS--TLHLDIPEDYLQK 256
Cdd:PRK13642 245 SNLMKDlrKNGFDLPEKYLSE 265
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
4.00e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 131.65 E-value: 4.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTrsiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEreLTRA 80
Cdd:PRK13644 1 MIRLENVSYSYPDGT---PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNL-LSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSP 159
Cdd:PRK13644 76 RKLVGIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502950432 160 KVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVkRICDQVAVISGGQLIEQDIVSEIFSHP 232
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
11-231 |
4.74e-36 |
|
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: 137.16 E-value: 4.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 11 FQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLircVNMLER---PTSGQVLVNGQDLTSLSERELtraRRQIGMI 87
Cdd:TIGR02203 338 FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTL---VNLIPRfyePDSGQILLDGHDLADYTLASL---RRQVALV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 88 FQHFNLLSSrTVFGNVALPlELNNTPKAEIKtrvnELLELVSLADKHDAYP-----------ANLSGGQKQRVAIARALA 156
Cdd:TIGR02203 412 SQDVVLFND-TIANNIAYG-RTEQADRAEIE----RALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502950432 157 NSPKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDQVAVISGGQLIEQDIVSEIFSH 231
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLAR 557
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-259 |
6.59e-36 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 132.72 E-value: 6.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 12 QQGTrsIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRC-VNMLE---RPTSGQVLVNGQDLTSLSERELTR-ARRQIGM 86
Cdd:COG4170 16 PQGR--VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAiCGITKdnwHVTADRFRWNGIDLLKLSPRERRKiIGREIAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 87 IFQHFN--LLSSRTVFGNV--ALPlelNNTPKAEI-------KTRVNELLELVSLADKHD---AYPANLSGGQKQRVAIA 152
Cdd:COG4170 94 IFQEPSscLDPSAKIGDQLieAIP---SWTFKGKWwqrfkwrKKRAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 153 RALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHP 232
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
250 260
....*....|....*....|....*..
gi 502950432 233 KTPVAQEFIKSTLHLDIPEDYLQKLQS 259
Cdd:COG4170 251 HHPYTKALLRSMPDFRQPLPHKSRLNT 277
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
8.16e-36 |
|
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: 128.75 E-value: 8.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFqqGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEReltrA 80
Cdd:COG4133 2 MLEAENLSCRR--GERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED----Y 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIktRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDiNRRLGLTILLITHE 200
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-238 |
1.20e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 129.85 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINkiFQQGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:COG4559 1 MLEAENLS--VRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RrqiGMIFQHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLAD-KHDAYPAnLSGGQKQRVAIARALA--- 156
Cdd:COG4559 77 R---AVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHlAGRSYQT-LSGGEQQRVQLARVLAqlw 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 157 ----NSPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQ---------D 223
Cdd:COG4559 153 epvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQgtpeevltdE 231
|
250 260
....*....|....*....|..
gi 502950432 224 IVSEIFS-------HPKTPVAQ 238
Cdd:COG4559 232 LLERVYGadlrvlaHPEGGCPQ 253
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-244 |
1.29e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 131.51 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 18 IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQV----LVNGQDLTSLSE---------RELTRARRQI 84
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELitnpyskkiKNFKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 85 GMIFQ--HFNLLSSrTV-----FGNVALplelnNTPKAEIKTRVNELLELVSLADKH-DAYPANLSGGQKQRVAIARALA 156
Cdd:PRK13631 119 SMVFQfpEYQLFKD-TIekdimFGPVAL-----GVKKSEAKKLAKFYLNKMGLDDSYlERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 157 NSPKVLLCDEATSALDPATTRSILELLKDiNRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHpktpv 236
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTD----- 266
|
....*...
gi 502950432 237 aQEFIKST 244
Cdd:PRK13631 267 -QHIINST 273
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-256 |
1.51e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 130.62 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTR-SIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLS-ERELT 78
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 79 RARRQIGMIFQH-FNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKH-DAYPANLSGGQKQRVAIARALA 156
Cdd:PRK13643 81 PVRKKVGVVFQFpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 157 NSPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPV 236
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLK 239
|
250 260
....*....|....*....|.
gi 502950432 237 AQEF-IKSTLHLdipEDYLQK 256
Cdd:PRK13643 240 AHELgVPKATHF---ADQLQK 257
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-233 |
1.96e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 130.33 E-value: 1.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQQGTR-SIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTS-LSERELTR 79
Cdd:PRK13641 3 IKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 80 ARRQIGMIFQhF--NLLSSRTVFGNVAL-PLELNNTPKaEIKTRVNELLELVSLADK-HDAYPANLSGGQKQRVAIARAL 155
Cdd:PRK13641 83 LRKKVSLVFQ-FpeAQLFENTVLKDVEFgPKNFGFSED-EAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 156 ANSPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPK 233
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-263 |
2.46e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 130.70 E-value: 2.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 23 DIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEReltrARRQIGMIFQHFNLLSSRTVFGN 102
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH----ARQRVGVVPQFDNLDPDFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 103 VALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILEL 182
Cdd:PRK13537 101 LLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWER 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 183 LKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDivseifshpktpVAQEFIKSTLHLDIPEDY---LQKLQS 259
Cdd:PRK13537 181 LRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG------------APHALIESEIGCDVIEIYgpdPVALRD 247
|
....
gi 502950432 260 EFAP 263
Cdd:PRK13537 248 ELAP 251
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-202 |
4.76e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 128.28 E-value: 4.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSereltrARRqiGMIFQHFNLLSSRTV 99
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG------AER--GVVFQNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSI 179
Cdd:PRK11248 88 QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180
....*....|....*....|...
gi 502950432 180 LELLKDINRRLGLTILLITHEMD 202
Cdd:PRK11248 168 QTLLLKLWQETGKQVLLITHDIE 190
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-222 |
6.53e-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: 127.35 E-value: 6.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSereLTRARRQIGMIFQH---FNlls 95
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRRAIGVVPQDtvlFN--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 96 sRTVFGNVALPlELNNTP----KAEIKTRVNEllELVSLADKHDAYPAN----LSGGQKQRVAIARALANSPKVLLCDEA 167
Cdd:cd03253 89 -DTIGYNIRYG-RPDATDeeviEAAKAAQIHD--KIMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502950432 168 TSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDQVAVISGGQLIEQ 222
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVER 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-272 |
6.87e-35 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 133.29 E-value: 6.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 11 FQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKS-TLIRCVNMLERP----TSGQVLVNGQDLTSLSERELTRAR-RQI 84
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRgNKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 85 GMIFQH--FNLLSSRTVFGNVALPLELNNTPKAE-IKTRVNELLELVSL---ADKHDAYPANLSGGQKQRVAIARALANS 158
Cdd:PRK15134 95 AMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREaARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 159 PKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQ 238
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ 254
|
250 260 270
....*....|....*....|....*....|....
gi 502950432 239 EFIKSTlhldiPEDYLQKLQSefapDLSPLLKLE 272
Cdd:PRK15134 255 KLLNSE-----PSGDPVPLPE----PASPLLDVE 279
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-228 |
7.59e-35 |
|
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: 127.26 E-value: 7.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltRARRQIG------MIFQHFnl 93
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE--RARAGIAyvpqgrEIFPRL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 94 lssrTVFGNVALPLELNNTPKAEIKTRVNELLELvsLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDP 173
Cdd:TIGR03410 91 ----TVEENLLTGLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502950432 174 ATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEI 228
Cdd:TIGR03410 165 SIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-219 |
7.73e-35 |
|
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: 125.41 E-value: 7.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLLSSrTVF 100
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---GDHVGYLPQDDELFSG-SIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 GNValplelnntpkaeiktrvnellelvsladkhdaypanLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSIL 180
Cdd:cd03246 94 ENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 502950432 181 ELLKDINRRlGLTILLITHEMDVVKRiCDQVAVISGGQL 219
Cdd:cd03246 137 QAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-222 |
7.91e-35 |
|
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: 126.96 E-value: 7.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 18 IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHfNLLSSR 97
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---RSMIGVVLQD-TFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 98 TVFGNVALPlelNNTPKAEiktRVNELLELV-------SLADKHDAYP----ANLSGGQKQRVAIARALANSPKVLLCDE 166
Cdd:cd03254 92 TIMENIRLG---RPNATDE---EVIEAAKEAgahdfimKLPNGYDTVLgengGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502950432 167 ATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDQVAVISGGQLIEQ 222
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEE 218
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
20-222 |
9.28e-35 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 134.31 E-value: 9.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLLSSrTV 99
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAV---RRQLGVVLQNGRLMSG-SI 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVA----LPLElnntpkaeiktRVNELLELVSLADKHDAYP-----------ANLSGGQKQRVAIARALANSPKVLLC 164
Cdd:TIGR03797 544 FENIAggapLTLD-----------EAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRILLF 612
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 165 DEATSALDPATTRSILELLKdinrRLGLTILLITHEMDVVKRiCDQVAVISGGQLIEQ 222
Cdd:TIGR03797 613 DEATSALDNRTQAIVSESLE----RLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQ 665
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-222 |
1.53e-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: 126.58 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 11 FQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLircVNMLER---PTSGQVLVNGQDLTSLSERELtraRRQIGMI 87
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTL---VNLIPRfydVDSGRILIDGHDVRDYTLASL---RRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 88 FQHFNLLSSrTVFGNVALPLElnNTPKAEIK--TRVNELLELV-SLADKHDAY----PANLSGGQKQRVAIARALANSPK 160
Cdd:cd03251 82 SQDVFLFND-TVAENIAYGRP--GATREEVEeaARAANAHEFImELPEGYDTVigerGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502950432 161 VLLCDEATSALDPATTRSILELLkdinRRL--GLTILLITHEMDVVKRIcDQVAVISGGQLIEQ 222
Cdd:cd03251 159 ILILDEATSALDTESERLVQAAL----ERLmkNRTTFVIAHRLSTIENA-DRIVVLEDGKIVER 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-241 |
2.41e-34 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 132.14 E-value: 2.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKST----LIRCVNmlerpTSGQVLVNGQDLTSLSERELTRARRQIGMIFQHFN-LL 94
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNsSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 95 SSR-TVFGNVALPLELNNTP--KAEIKTRVNELLELVSL-ADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSA 170
Cdd:PRK15134 376 NPRlNVLQIIEEGLRVHQPTlsAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502950432 171 LDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFI 241
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-222 |
8.50e-33 |
|
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: 128.40 E-value: 8.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRcvnMLER---PTSGQVLVNGQDLTSLSERELtraRRQIGMIFQH---FNll 94
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLAR---LLFRfydVTSGRILIDGQDIRDVTQASL---RAAIGIVPQDtvlFN-- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 95 ssRTVFGNVAL--PlelnNTPKAEIKT--RVNELLELV-SLADKHDAYPA----NLSGGQKQRVAIARALANSPKVLLCD 165
Cdd:COG5265 446 --DTIAYNIAYgrP----DASEEEVEAaaRAAQIHDFIeSLPDGYDTRVGerglKLSGGEKQRVAIARTLLKNPPILIFD 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 166 EATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDQVAVISGGQLIEQ 222
Cdd:COG5265 520 EATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVER 573
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-247 |
4.04e-32 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 120.57 E-value: 4.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 22 SDIDLHVPQGQIYGVIGSSGAGKStlIRCVNMLE------RPTSGQVLVNGQDLTSLSEREltrarRQIGMIFQH----F 91
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVAPCALRG-----RKIATIMQNprsaF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 92 NLLssRTVFGNVAlplelnNTPKAEIKTRVN----ELLELVSLADKH---DAYPANLSGGQKQRVAIARALANSPKVLLC 164
Cdd:PRK10418 93 NPL--HTMHTHAR------ETCLALGKPADDatltAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 165 DEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFIKST 244
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAH 244
|
...
gi 502950432 245 LHL 247
Cdd:PRK10418 245 LAL 247
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-219 |
9.42e-32 |
|
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: 117.53 E-value: 9.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA--------RRQIGmifqh 90
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedRKREG----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 91 fnLLSSRTVFGNVALPLELnntpkaeiktrvnellelvsladkhdaypanlSGGQKQRVAIARALANSPKVLLCDEATSA 170
Cdd:cd03215 89 --LVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502950432 171 LDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:cd03215 135 VDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-232 |
1.20e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 119.32 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtrARRQIGMIFQHFNLLSSRTV 99
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI--ARMGVVRTFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGN--VALPLELN--------NTP-----KAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLC 164
Cdd:PRK11300 98 IENllVAQHQQLKtglfsgllKTPafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 165 DEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHP 232
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-233 |
2.74e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 119.05 E-value: 2.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSG-----QVLVNGQDLtsLSERELTRARRQIGMIFQHFNLLS 95
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 96 sRTVFGNVALPLELNN-TPKAEIK----TRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSA 170
Cdd:PRK14271 115 -MSIMDNVLAGVRAHKlVPRKEFRgvaqARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502950432 171 LDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPK 233
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-232 |
2.97e-31 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 120.75 E-value: 2.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 23 DIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERE-LTRARRQIGMIFQHFNLLSSRTVFG 101
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIcLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 102 NvalpleLNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILE 181
Cdd:PRK11144 96 N------LRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502950432 182 LLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHP 232
Cdd:PRK11144 170 YLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-220 |
3.88e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 119.94 E-value: 3.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSlserELTRARRQIGMIFQHFNLLSSRTVF 100
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA----RARLARARIGVVPQFDNLDLEFTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 GNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSIL 180
Cdd:PRK13536 133 ENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIW 212
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502950432 181 ELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLI 220
Cdd:PRK13536 213 ERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
19-214 |
6.76e-31 |
|
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: 122.40 E-value: 6.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLLSSrT 98
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---RDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 99 VFGNVAlpLELNNTPKAEIKtrvnELLELVSLADKHDAYP-----------ANLSGGQKQRVAIARALANSPKVLLCDEA 167
Cdd:TIGR02857 412 IAENIR--LARPDASDAEIR----EALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502950432 168 TSALDPATTRSILELLKDINRrlGLTILLITHEmDVVKRICDQVAVI 214
Cdd:TIGR02857 486 TAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-220 |
1.26e-30 |
|
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: 115.76 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 18 IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLLSSr 97
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---RRNIGYVPQDVTLFYG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 98 TVFGNVALPLELNNTpkAEIkTRVNELLELVSLADKH-DAYP-------ANLSGGQKQRVAIARALANSPKVLLCDEATS 169
Cdd:cd03245 93 TLRDNITLGAPLADD--ERI-LRAAELAGVTDFVNKHpNGLDlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502950432 170 ALDPATTRSILELLKDINRrlGLTILLITHEMDVVKrICDQVAVISGGQLI 220
Cdd:cd03245 170 AMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-227 |
2.27e-30 |
|
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: 115.19 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 6 QINKIFQQGTrsikALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTslsERELtrarRQIG 85
Cdd:TIGR03740 5 NLSKRFGKQT----AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT---RKDL----HKIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 86 MIFQHFNLLSSRTVFGNVALPLELNNTPKAEIktrvNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCD 165
Cdd:TIGR03740 74 SLIESPPLYENLTARENLKVHTTLLGLPDSRI----DEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502950432 166 EATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSE 227
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-222 |
2.89e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 121.37 E-value: 2.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTlirCVNMLER---PTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHfNLLSSR 97
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNlyqPTGGQVLLDGVPLVQYDHHYL---HRQVALVGQE-PVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 98 TVFGNVALPLelNNTPKAEIktrvnelLELVSLADKHD-------AYPAN-------LSGGQKQRVAIARALANSPKVLL 163
Cdd:TIGR00958 570 SVRENIAYGL--TDTPDEEI-------MAAAKAANAHDfimefpnGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLI 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 164 CDEATSALDPATTRsileLLKDINRRLGLTILLITHEMDVVKRiCDQVAVISGGQLIEQ 222
Cdd:TIGR00958 641 LDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEM 694
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-243 |
3.07e-30 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 116.04 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 18 IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERelTRARRqIGMIFQH-FNLLSS 96
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS--YRSQR-IRMIFQDpSTSLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 97 RTVFGNVA-LPLELNNTPKAEIK-TRVNELLELVSLADKHDAY-PANLSGGQKQRVAIARALANSPKVLLCDEATSALDP 173
Cdd:PRK15112 103 RQRISQILdFPLRLNTDLEPEQReKQIIETLRQVGLLPDHASYyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 174 ATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFIKS 243
Cdd:PRK15112 183 SMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAG 252
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-223 |
3.77e-30 |
|
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: 114.51 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCV-NMLErPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLLSSrT 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALfRLVE-LSSGSILIDGVDISKIGLHDL---RSRISIIPQDPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 99 VFGNVAlPLelNNTPKAEIktrvNELLELVSLADKHDAYP-----------ANLSGGQKQRVAIARALANSPKVLLCDEA 167
Cdd:cd03244 94 IRSNLD-PF--GEYSDEEL----WQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502950432 168 TSALDPATTRSILELLKdiNRRLGLTILLITHEMDVVKRiCDQVAVISGGQLIEQD 223
Cdd:cd03244 167 TASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
14-230 |
7.47e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 114.73 E-value: 7.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 14 GTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTrarRQIGMIFQHFNL 93
Cdd:PRK11231 13 GTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA---RRLALLPQHHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 94 LSSRTVFGNVA------LPL--ELNNTPKAEIkTRVNELLELVSLADKHdayPANLSGGQKQRVAIARALANSPKVLLCD 165
Cdd:PRK11231 88 PEGITVRELVAygrspwLSLwgRLSAEDNARV-NQAMEQTRINHLADRR---LTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502950432 166 EATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFS 230
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-231 |
1.45e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 113.64 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQ---QGTRSIK---------------ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQV 62
Cdd:COG1134 4 MIEVENVSKSYRlyhEPSRSLKelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 63 LVNGQdLTSLSEreltrarrqIGMIFQhfnllSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAyPA-NL 141
Cdd:COG1134 84 EVNGR-VSALLE---------LGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQ-PVkTY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 142 SGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLIE 221
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
250
....*....|
gi 502950432 222 QDIVSEIFSH 231
Cdd:COG1134 227 DGDPEEVIAA 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-220 |
2.12e-29 |
|
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: 111.49 E-value: 2.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERP--TSGQVLVNGQDltslseRELTRARRQIGMIFQHFNLLSSRT 98
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRP------LDKRSFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 99 VFGNVALplelnntpKAEIKtrvnellelvsladkhdaypaNLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRS 178
Cdd:cd03213 99 VRETLMF--------AAKLR---------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502950432 179 ILELLKDInRRLGLTILLITHE-MDVVKRICDQVAVISGGQLI 220
Cdd:cd03213 150 VMSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-228 |
2.80e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 112.87 E-value: 2.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTrsikALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtrA 80
Cdd:COG4604 1 MIEIKNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREL--A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRqIGMIFQHfNLLSSR-TV-----FG-------NvalplelnntPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQ 147
Cdd:COG4604 75 KR-LAILRQE-NHINSRlTVrelvaFGrfpyskgR----------LTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 148 RVAIARALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSE 227
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEE 222
|
.
gi 502950432 228 I 228
Cdd:COG4604 223 I 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-219 |
3.31e-29 |
|
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: 112.18 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTlirCVNMLER---PTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHfNLLSSR 97
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKST---VVALLENfyqPQGGQVLLDGKPISQYEHKYL---HSKVSLVGQE-PVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 98 TVFGNVALPLElnNTPKAEIKtrvnellELVSLADKHDAYP--------------ANLSGGQKQRVAIARALANSPKVLL 163
Cdd:cd03248 103 SLQDNIAYGLQ--SCSFECVK-------EAAQKAHAHSFISelasgydtevgekgSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502950432 164 CDEATSALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRiCDQVAVISGGQL 219
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-232 |
3.76e-29 |
|
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: 112.49 E-value: 3.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINkiFQQGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVL-VNGQDLTSLSERELtr 79
Cdd:COG1119 3 LLELRNVT--VRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERRGGEDVWEL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 80 aRRQIGMI--FQHFNLLSSRTVFgNVALP-----LELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIA 152
Cdd:COG1119 77 -RKRIGLVspALQLRFPRDETVL-DVVLSgffdsIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 153 RALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEM-DVVKRIcDQVAVISGGQLIEQ--------- 222
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVeEIPPGI-THVLLLKDGRVVAAgpkeevlts 233
|
250
....*....|
gi 502950432 223 DIVSEIFSHP 232
Cdd:COG1119 234 ENLSEAFGLP 243
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-217 |
4.30e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 115.71 E-value: 4.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 17 SIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTrarRQIGMIFQHFNL--- 93
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS---RRVASVPQDTSLsfe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 94 LSSRTVfgnvalpLELNNTPK-------AEIKTR-VNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCD 165
Cdd:PRK09536 92 FDVRQV-------VEMGRTPHrsrfdtwTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502950432 166 EATSALDPATTRSILELLkdinRRL---GLTILLITHEMDVVKRICDQVAVISGG 217
Cdd:PRK09536 165 EPTASLDINHQVRTLELV----RRLvddGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-220 |
4.73e-29 |
|
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: 111.59 E-value: 4.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCV-NMLERP--TSGQVLVNGQDLtslsERELTRARrqIGMIFQHFNLLS 95
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNGQPR----KPDQFQKC--VAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 96 SRTVFGNV--ALPLELNNTPKAEIKTRVNELLELVSLADKH--DAYPANLSGGQKQRVAIARALANSPKVLLCDEATSAL 171
Cdd:cd03234 95 GLTVRETLtyTAILRLPRKSSDAIRKKRVEDVLLRDLALTRigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502950432 172 DPATTRSILELLKDINRRlGLTILLITHE--MDVVkRICDQVAVISGGQLI 220
Cdd:cd03234 175 DSFTALNLVSTLSQLARR-NRIVILTIHQprSDLF-RLFDRILLLSSGEIV 223
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-243 |
5.12e-29 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 114.13 E-value: 5.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 18 IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLE----RPTSGQVLVNGQDLTSLSERELTR-ARRQIGMIFQH-F 91
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRERRKlVGHNVSMIFQEpQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 92 NLLSSRTVFGNVALPLELNNTPKAEIKTRVN-------ELLELVSLADKHDA---YPANLSGGQKQRVAIARALANSPKV 161
Cdd:PRK15093 100 SCLDPSERVGRQLMQNIPGWTYKGRWWQRFGwrkrraiELLHRVGIKDHKDAmrsFPYELTEGECQKVMIAIALANQPRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFI 241
Cdd:PRK15093 180 LIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQALI 259
|
..
gi 502950432 242 KS 243
Cdd:PRK15093 260 RA 261
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-238 |
9.09e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 116.88 E-value: 9.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKST--------------LIRCVNMLERPTSGQVLvng 66
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrlleqaggLVQCDKMLLRRRSRQVI--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 67 qDLTSLSERELTRAR-RQIGMIFQH--FNLLSSRTVFGNVALPLELN-NTPKAEIKTRVNELLELVSLADKHDA---YPA 139
Cdd:PRK10261 89 -ELSEQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHqGASREEAMVEAKRMLDQVRIPEAQTIlsrYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 140 NLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
250
....*....|....*....
gi 502950432 220 IEQDIVSEIFSHPKTPVAQ 238
Cdd:PRK10261 248 VETGSVEQIFHAPQHPYTR 266
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-229 |
1.40e-28 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 115.67 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFQqgtrSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLE--RPTSGQVLVN-------------- 65
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 66 --GQ--------------DLTSLSERELTRARRQIGMIFQH-FNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELV 128
Cdd:TIGR03269 77 kvGEpcpvcggtlepeevDFWNLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 129 SLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRIC 208
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|....
gi 502950432 209 DQVAVISGGQLIEQ---DIVSEIF 229
Cdd:TIGR03269 237 DKAIWLENGEIKEEgtpDEVVAVF 260
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-211 |
3.60e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.42 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 4 LTQINKI-FQQGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEReltRARR 82
Cdd:PRK10247 7 LLQLQNVgYLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---IYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 83 QIGMIFQHFNLLSSrTVFGNVALPLELNNtpKAEIKTRVNELLELVSLADKHDAYPAN-LSGGQKQRVAIARALANSPKV 161
Cdd:PRK10247 82 QVSYCAQTPTLFGD-TVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502950432 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDQV 211
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-219 |
3.91e-28 |
|
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: 115.50 E-value: 3.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 9 KIFQQGTRSikALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLtslsERELTRARRQIGMIF 88
Cdd:TIGR01257 936 KIFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 89 QHFNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEAT 168
Cdd:TIGR01257 1010 QHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502950432 169 SALDPATTRSILELLkdINRRLGLTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-230 |
1.04e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 108.44 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSEREltRARRQIGMIFQHFNLLSSRT 98
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 99 VFGNVALPLELNNTPKAEI-KTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTR 177
Cdd:PRK10895 95 VYDNLMAVLQIRDDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502950432 178 SILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFS 230
Cdd:PRK10895 175 DIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-230 |
1.18e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 109.33 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 13 QGTRSIKALS-DIDLHVpqgqIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLtSLSERELTRARRQIGMIFQHf 91
Cdd:PRK13638 12 QDEPVLKGLNlDFSLSP----VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVATVFQD- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 92 nllSSRTVF-----GNVALPLELNNTPKAEIKTRVNELLELVSlADKHDAYPAN-LSGGQKQRVAIARALANSPKVLLCD 165
Cdd:PRK13638 86 ---PEQQIFytdidSDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502950432 166 EATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFS 230
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-228 |
4.74e-27 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 107.18 E-value: 4.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRarrQIGMIFQHFNLLSSRTVF 100
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR---KVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 GNVALplelNNTP--------KAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALD 172
Cdd:PRK10575 104 ELVAI----GRYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502950432 173 PATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEI 228
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-199 |
8.13e-27 |
|
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: 110.53 E-value: 8.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLLSSrTV 99
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---RRRVSVCAQDAHLFDT-TV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVALPLElnNTPKAEIKtrvnELLELVSLADKHDAYP-----------ANLSGGQKQRVAIARALANSPKVLLCDEAT 168
Cdd:TIGR02868 426 RENLRLARP--DATDEELW----AALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|.
gi 502950432 169 SALDPATTRSILELLKDINRrlGLTILLITH 199
Cdd:TIGR02868 500 EHLDAETADELLEDLLAALS--GRTVVLITH 528
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
19-245 |
9.17e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 106.16 E-value: 9.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQ-----DLTSLSERELTR-ARRQIGMIFQHF- 91
Cdd:PRK11701 20 KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRlLRTEWGFVHQHPr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 92 -NLLSSRTVFGNVALPL-ELNNTPKAEIKTRVNELLELVSL-ADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEAT 168
Cdd:PRK11701 100 dGLRMQVSAGGNIGERLmAVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPT 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 169 SALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSHPKTPVAQEFIKSTL 245
Cdd:PRK11701 180 GGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLLVSSVL 256
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-222 |
9.42e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 110.82 E-value: 9.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIrcvNMLER---PTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHfNLLSS 96
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLI---NLLQRvfdPQSGRILIDGTDIRTVTRASL---RRNIAVVFQD-AGLFN 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 97 RTVFGNVALPLElNNTPKaeiktrvnELLELVSLADKHD-------AYPAN-------LSGGQKQRVAIARALANSPKVL 162
Cdd:PRK13657 423 RSIEDNIRVGRP-DATDE--------EMRAAAERAQAHDfierkpdGYDTVvgergrqLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 163 LCDEATSALDPATTRSILELLKDInrRLGLTILLITHEMDVVkRICDQVAVISGGQLIEQ 222
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTV-RNADRILVFDNGRVVES 550
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-219 |
2.31e-26 |
|
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: 109.45 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRC-VNMLeRPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLLSSrTV 99
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLlVGVW-PPTAGSVRLDGADLSQWDREEL---GRHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVALpleLNNTPKAEI-----KTRVNELLelVSLADKHD----AYPANLSGGQKQRVAIARALANSPKVLLCDEATSA 170
Cdd:COG4618 423 AENIAR---FGDADPEKVvaaakLAGVHEMI--LRLPDGYDtrigEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502950432 171 LDPATTRSILELLKDINRRlGLTILLITHEMDVVkRICDQVAVISGGQL 219
Cdd:COG4618 498 LDDEGEAALAAAIRALKAR-GATVVVITHRPSLL-AAVDKLLVLRDGRV 544
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-220 |
3.04e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 108.86 E-value: 3.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 18 IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLeRPT---SGQVLVNGQDLTSLSERELTRArrQIGMIFQHFNLL 94
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNIRDTERA--GIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 95 SSRTVFGNVALPLELnnTPK-----AEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATS 169
Cdd:PRK13549 95 KELSVLENIFLGNEI--TPGgimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502950432 170 ALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLI 220
Cdd:PRK13549 173 SLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-228 |
3.69e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 108.72 E-value: 3.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQqgtrSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERelTRA 80
Cdd:PRK09700 5 YISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK--LAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLLSSRTVFGNV---ALPLE----LNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIAR 153
Cdd:PRK09700 79 QLGIGIIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 154 ALANSPKVLLCDEATSALdpatTRSILELLKDINRRL---GLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEI 228
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSL----TNKEVDYLFLIMNQLrkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-220 |
4.43e-26 |
|
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: 108.37 E-value: 4.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 17 SIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIR--CVNMLERPTSGQVLVNGQDLTSLSERELTRArrQIGMIFQHFNLL 94
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKilSGVYPHGTWDGEIYWSGSPLKASNIRDTERA--GIVIIHQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 95 SSRTVFGNVALPLELNN----TPKAEIKTRVNELLELVSLADKHDAYP-ANLSGGQKQRVAIARALANSPKVLLCDEATS 169
Cdd:TIGR02633 91 PELSVAENIFLGNEITLpggrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502950432 170 ALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLI 220
Cdd:TIGR02633 171 SLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
8-231 |
4.97e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 108.57 E-value: 4.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 8 NKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLircVNMLER---PTSGQVLVNGQDLtslSERELTRARRQI 84
Cdd:PRK11176 346 NVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTI---ANLLTRfydIDEGEILLDGHDL---RDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 85 GMIFQHFNLLSSrTVFGNVALPLElNNTPKAEIKT--RVNELLELVS-LADKHDAY----PANLSGGQKQRVAIARA-LA 156
Cdd:PRK11176 420 ALVSQNVHLFND-TIANNIAYART-EQYSREQIEEaaRMAYAMDFINkMDNGLDTVigenGVLLSGGQRQRIAIARAlLR 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 157 NSPkVLLCDEATSALDPATTRSILELLKDI--NRrlglTILLITHEMDVVKRiCDQVAVISGGQLIEQDIVSEIFSH 231
Cdd:PRK11176 498 DSP-ILILDEATSALDTESERAIQAALDELqkNR----TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQ 568
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3-221 |
7.53e-26 |
|
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: 103.00 E-value: 7.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 3 RLTQINKIFQQGTRSIK-ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQdLTSLSEreltrar 81
Cdd:cd03220 19 SLKKLGILGRKGEVGEFwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSLLG------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 rqIGMIFQhfnllSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKV 161
Cdd:cd03220 91 --LGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIE 221
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-221 |
1.54e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 106.92 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 18 IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRArrQIGMIFQHFNLLSSR 97
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAA--GVAIIYQELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 98 TVFGNV---ALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALdpa 174
Cdd:PRK11288 95 TVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL--- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502950432 175 TTRSIlELLKDINRRL---GLTILLITHEMDVVKRICDQVAVISGGQLIE 221
Cdd:PRK11288 172 SAREI-EQLFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-222 |
1.87e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 106.85 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 24 IDLHVPQGQIYGVIGSSGAGKSTLIrcvNMLE--RPTSGQVLVNGQDLTSLserELTRARRQIGMIFQHFNLLSSrTVFG 101
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLL---NALLgfLPYQGSLKINGIELREL---DPESWRKHLSWVGQNPQLPHG-TLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 102 NVALplelnNTPKAEiKTRVNELLELVSLADKHDAYP-----------ANLSGGQKQRVAIARALANSPKVLLCDEATSA 170
Cdd:PRK11174 442 NVLL-----GNPDAS-DEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502950432 171 LDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDQVAVISGGQLIEQ 222
Cdd:PRK11174 516 LDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQ 564
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-222 |
2.29e-25 |
|
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: 107.13 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 6 QINKI-FQQGTRSiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQI 84
Cdd:TIGR01193 475 VINDVsYSYGYGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL---RQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 85 GMIFQHFNLLSsrtvfGNVALPLELNNTPKAEIKtRVNELLELVSLADKHDAYP-----------ANLSGGQKQRVAIAR 153
Cdd:TIGR01193 551 NYLPQEPYIFS-----GSILENLLLGAKENVSQD-EIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALAR 624
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 154 ALANSPKVLLCDEATSALDPATTRSILELLKDINRRlglTILLITHEMDVVKRIcDQVAVISGGQLIEQ 222
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQ 689
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-222 |
3.04e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 106.45 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINkiFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIrcvNMLER---PTSGQVLVNGQDLTSLSERELt 78
Cdd:PRK11160 339 LTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL---QLLTRawdPQQGEILLNGQPIADYSEAAL- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 79 raRRQIGMIFQHFNLLSSrTVFGNVALPLELNNTPK-AEIKTRVnELLELVSLADKHDAYPAN----LSGGQKQRVAIAR 153
Cdd:PRK11160 413 --RQAISVVSQRVHLFSA-TLRDNLLLAAPNASDEAlIEVLQQV-GLEKLLEDDKGLNAWLGEggrqLSGGEQRRLGIAR 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 154 ALANSPKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRIcDQVAVISGGQLIEQ 222
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQ 554
|
|
| NIL |
smart00930 |
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ... |
267-340 |
5.64e-24 |
|
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: 93.34 E-value: 5.64e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502950432 267 PLLKLEFTGKSVDAPLISMAVRRFNIDISILSSQMDYAGGVKFGVMLAELDGESDSINATIAFLEDHHVKVEVL 340
Cdd:smart00930 3 RLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGDEEDIEAALAYLREQGVEVEVL 76
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-222 |
8.24e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 102.10 E-value: 8.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLLSSrTVF 100
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---RQGVAMVQQDPVVLAD-TFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 GNVALPLELNntpkaeiKTRVNELLELVSLADKHDAYPA-----------NLSGGQKQRVAIARALANSPKVLLCDEATS 169
Cdd:PRK10790 433 ANVTLGRDIS-------EEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATA 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502950432 170 ALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRiCDQVAVISGGQLIEQ 222
Cdd:PRK10790 506 NIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-212 |
1.91e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 101.35 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSlseRELtRARRQIGMIFQHFNLLSSRTV 99
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA---GDI-ATRRRVGYMSQAFSLYGELTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSI 179
Cdd:NF033858 357 RQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMF 436
|
170 180 190
....*....|....*....|....*....|...
gi 502950432 180 LELLKDINRRLGLTILLITHEMDVVKRiCDQVA 212
Cdd:NF033858 437 WRLLIELSREDGVTIFISTHFMNEAER-CDRIS 468
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-218 |
2.74e-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: 95.61 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCV--NMleRPTSGQVLVNGQD-LTSlsereltrarrQIGMIFqhfnllsS 96
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgEL--EKLSGSVSVPGSIaYVS-----------QEPWIQ-------N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 97 RTVFGNVALPLELNntpkaeiKTRVNELLELVSLADKHDAYPA-----------NLSGGQKQRVAIARALANSPKVLLCD 165
Cdd:cd03250 80 GTIRENILFGKPFD-------EERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502950432 166 EATSALDPATTRSILE--LLKDInrRLGLTILLITHEMDVVKRiCDQVAVISGGQ 218
Cdd:cd03250 153 DPLSAVDAHVGRHIFEncILGLL--LNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-220 |
3.34e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.10 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 16 RSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSerelTRARRQIGMIF-----QH 90
Cdd:COG3845 269 RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS----PRERRRLGVAYipedrLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 91 FNLLSSRTVFGNVALpLELNNTP--------KAEIKTRVNELLEL--VSLADkHDAYPANLSGGQKQRVAIARALANSPK 160
Cdd:COG3845 345 RGLVPDMSVAENLIL-GRYRRPPfsrggfldRKAIRAFAEELIEEfdVRTPG-PDTPARSLSGGNQQKVILARELSRDPK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 161 VLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLI 220
Cdd:COG3845 423 LLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-230 |
4.34e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 96.59 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 23 DIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRarrQIGMIFQHFNLLSSRTVFGN 102
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR---RIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 103 VA---LPLE-LNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRS 178
Cdd:PRK10253 102 VArgrYPHQpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502950432 179 ILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFS 230
Cdd:PRK10253 182 LLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-223 |
9.30e-23 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 94.02 E-value: 9.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLserELTRARRQIGMIFQHFNLLSsrt 98
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLRSSLTIIPQDPTLFS--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 99 vfGNVALPLELNNTPKAEiktrvnELLELVSLADKHDaypaNLSGGQKQRVAIARALANSPKVLLCDEATSALDPAT--- 175
Cdd:cd03369 96 --GTIRSNLDPFDEYSDE------EIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATdal 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502950432 176 -TRSILELLKDInrrlglTILLITHEMDVVKRiCDQVAVISGGQLIEQD 223
Cdd:cd03369 164 iQKTIREEFTNS------TILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-222 |
9.77e-23 |
|
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: 93.15 E-value: 9.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINkiFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLsERELtraR 81
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKAL---S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 RQIGMIFQHFNLLSSrTVFGNVALPLelnntpkaeiktrvnellelvsladkhdaypanlSGGQKQRVAIARALANSPKV 161
Cdd:cd03247 75 SLISVLNQRPYLFDT-TLRNNLGRRF----------------------------------SGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502950432 162 LLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRIcDQVAVISGGQLIEQ 222
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| NIL |
pfam09383 |
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ... |
267-339 |
5.59e-22 |
|
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: 87.89 E-value: 5.59e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502950432 267 PLLKLEFTGKSVDAPLISMAVRRFNIDISILSSQMDYAGGVKFGVMLAELDGESDSINATIAFLEDHHVKVEV 339
Cdd:pfam09383 1 RLVRLTFPGESADEPVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELPGDPEQIEAALAYLREQGVEVEV 73
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-220 |
8.79e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.86 E-value: 8.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA--------RRQIGmifqh 90
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAgiayvpedRKGEG----- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 91 fnLLSSRTVFGNVALPLeLNNT------PKAEIKTRVNELLELVSL-ADKHDAYPANLSGGQKQRVAIARALANSPKVLL 163
Cdd:COG1129 341 --LVLDLSIRENITLAS-LDRLsrggllDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 164 CDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLI 220
Cdd:COG1129 418 LDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-230 |
2.42e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 91.44 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLErPTSGQVLVNGQDLTSLSERELTRARrqiGMIFQHFNLLSSRTVF 100
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHR---AYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 GNVALPLElNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARAL------AN-SPKVLLCDEATSALDP 173
Cdd:COG4138 88 QYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 174 ATTRSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFS 230
Cdd:COG4138 167 AQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-205 |
2.44e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 90.79 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCV--NMLERPTSGQVLVngQDLTSLSERELtrarrqigmifqhfnllssrt 98
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDV--PDNQFGREASL--------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 99 vfgnvalpleLNNTPKAEIKTRVNELLELVSLADkhdAY-----PANLSGGQKQRVAIARALANSPKVLLCDEATSALDP 173
Cdd:COG2401 103 ----------IDAIGRKGDFKDAVELLNAVGLSD---AVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190
....*....|....*....|....*....|..
gi 502950432 174 ATTRSILELLKDINRRLGLTILLITHEMDVVK 205
Cdd:COG2401 170 QTAKRVARNLQKLARRAGITLVVATHHYDVID 201
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-223 |
3.11e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.71 E-value: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 18 IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTraRRQIGMIFQHFNLLSSR 97
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM--REAVAIVPEGRRVFSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 98 TVFGNVALPLELNNtpKAEIKTRVNELLELV-SLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATT 176
Cdd:PRK11614 96 TVEENLAMGGFFAE--RDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502950432 177 RSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQD 223
Cdd:PRK11614 174 QQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLED 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-199 |
7.50e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.33 E-value: 7.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLV-NGQDLTSLSEREltrarrqigmifqHFNLLSSRTV 99
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPQRP-------------YLPLGTLREA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 fgnVALPLELNNTPKAEIKtrvnELLELVSLA------DKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDP 173
Cdd:COG4178 446 ---LLYPATAEAFSDAELR----EALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180
....*....|....*....|....*.
gi 502950432 174 ATTRSILELLKDinRRLGLTILLITH 199
Cdd:COG4178 519 ENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-216 |
3.07e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.79 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRARRQIGMIFQHFNLLSSRTV 99
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSI 179
Cdd:PRK15056 102 MMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 502950432 180 LELLKDInRRLGLTILLITHEMDVVKRICDQVAVISG 216
Cdd:PRK15056 182 ISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-220 |
3.96e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 3.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 4 LTQINKIFqqGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGqDLTslsereltrarrq 83
Cdd:COG0488 1 LENLSKSF--GGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 84 IGMIFQHFNLLSSRTVFGNValplELNNTPKAEIKTRVNELLELVSLADK--------------HDAYPA---------- 139
Cdd:COG0488 63 IGYLPQEPPLDDDLTVLDTV----LDGDAELRALEAELEELEAKLAEPDEdlerlaelqeefeaLGGWEAearaeeilsg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 140 -------------NLSGGQKQRVAIARALANSPKVLLCDEATSALDpATTRSILE-LLKDINRrlglTILLITHEMDVVK 205
Cdd:COG0488 139 lgfpeedldrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-LESIEWLEeFLKNYPG----TVLVVSHDRYFLD 213
|
250
....*....|....*
gi 502950432 206 RICDQVAVISGGQLI 220
Cdd:COG0488 214 RVATRILELDRGKLT 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-228 |
4.52e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.83 E-value: 4.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQqgtrSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA 80
Cdd:PRK10762 4 LLQLKGIDKAFP----GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 rrQIGMIFQHFNLLSSRTVFGNVALPLELNNTPKA----EIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALA 156
Cdd:PRK10762 80 --GIGIIHQELNLIPQLTIAENIFLGREFVNRFGRidwkKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502950432 157 NSPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEI 228
Cdd:PRK10762 158 FESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-220 |
1.13e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.11 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 31 GQIYGVIGSSGAGKSTLI-----RCVNMLERptSGQVLVNGQDLTSLSERELTRARRQIGMIFQHFNLLSSRTVFGNVAL 105
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMnalafRSPKGVKG--SGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRM 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 106 PlelNNTPKAEIKTRVNELLELVSLADKHD------AYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSI 179
Cdd:TIGR00955 129 P---RRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502950432 180 LELLKDINRRlGLTILLITHEMDV-VKRICDQVAVISGGQLI 220
Cdd:TIGR00955 206 VQVLKGLAQK-GKTIICTIHQPSSeLFELFDKIILMAEGRVA 246
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-211 |
2.83e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.55 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFqqGTRsiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVlvngqdltslsEREltrA 80
Cdd:PRK09544 4 LVSLENVSVSF--GQR--RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRN---G 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQIGMIFQHFNLlssrtvfgNVALPLELN-------NTPKAEIKTrvneLLELVSLADKHDAYPANLSGGQKQRVAIAR 153
Cdd:PRK09544 66 KLRIGYVPQKLYL--------DTTLPLTVNrflrlrpGTKKEDILP----ALKRVQAGHLIDAPMQKLSGGETQRVLLAR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 154 ALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQV 211
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-220 |
3.52e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 88.25 E-value: 3.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 4 LTQINKIFQqgtrSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRArrQ 83
Cdd:PRK10982 1 MSNISKSFP----GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALEN--G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 84 IGMIFQHFNLLSSRTVFGNvalpLELNNTPKA-----------EIKTRVNELLELVSLADKhdayPANLSGGQKQRVAIA 152
Cdd:PRK10982 75 ISMVHQELNLVLQRSVMDN----MWLGRYPTKgmfvdqdkmyrDTKAIFDELDIDIDPRAK----VATLSVSQMQMIEIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 153 RALANSPKVLLCDEATSALdpaTTRSILELLKDIN--RRLGLTILLITHEMDVVKRICDQVAVISGGQLI 220
Cdd:PRK10982 147 KAFSYNAKIVIMDEPTSSL---TEKEVNHLFTIIRklKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-239 |
4.60e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.80 E-value: 4.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQqGTRSIKAlsdIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSErelTRA 80
Cdd:PRK15439 11 LLCARSISKQYS-GVEVLKG---IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP---AKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 rRQIG--MIFQHFNLLSSRTVFGNVALPLelnntPK-AEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALAN 157
Cdd:PRK15439 84 -HQLGiyLVPQEPLLFPNLSVKENILFGL-----PKrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 158 SPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGG---------QLIEQDIVSEI 228
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGtialsgktaDLSTDDIIQAI 236
|
250
....*....|.
gi 502950432 229 fshpkTPVAQE 239
Cdd:PRK15439 237 -----TPAARE 242
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
59-215 |
1.06e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 87.39 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 59 SGQVLVNGQDLTSLSERELtrarRQIGMIFQHFNLLSSRTVFGNVALPLE---LNNTPKAEIKTRVNELLElvSLADKHD 135
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDL----RNLFSIVSQEPMLFNMSIYENIKFGKEdatREDVKRACKFAAIDEFIE--SLPNKYD 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 136 A----YPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDQV 211
Cdd:PTZ00265 1350 TnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKI 1428
|
....
gi 502950432 212 AVIS 215
Cdd:PTZ00265 1429 VVFN 1432
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-221 |
1.15e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFqqGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVnGQDLtslsereltra 80
Cdd:COG0488 315 VLELEGLSKSY--GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 rrQIGMIFQHFNLL-SSRTVFGNVAlplelnNTPKAEIKTRVNELLE--LVSlADKHDAYPANLSGGQKQRVAIARALAN 157
Cdd:COG0488 379 --KIGYFDQHQEELdPDKTVLDELR------DGAPGGTEQEVRGYLGrfLFS-GDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502950432 158 SPKVLLCDEATSALDPATTRSILELLKDINrrlGlTILLITHEMDVVKRICDQVAVISGGQLIE 221
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-224 |
2.54e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 81.80 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCV--NMLERPTSGQVLVNGQDLTSLSEREltRARRQIGMIFQHfnllssrt 98
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE--RARLGIFLAFQY-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 99 vfgnvalPLELNNtpkaeikTRVNELLELVSladkhdaypANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRS 178
Cdd:cd03217 86 -------PPEIPG-------VKNADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502950432 179 ILELLKDInRRLGLTILLITH--------EMDVVKRICDQVAVISGGQLIEQDI 224
Cdd:cd03217 143 VAEVINKL-REEGKSVLIITHyqrlldyiKPDRVHVLYDGRIVKSGDKELALEI 195
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-215 |
2.95e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 86.24 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 3 RLTQINKI------FQQGTRS-IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNgqDLTSLSER 75
Cdd:PTZ00265 376 KLKDIKKIqfknvrFHYDTRKdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 76 ELTRARRQIGMIFQHfNLLSSRTVFGNV-----------ALPLELN-------------NTPKAEIK---------TRVN 122
Cdd:PTZ00265 454 NLKWWRSKIGVVSQD-PLLFSNSIKNNIkyslyslkdleALSNYYNedgndsqenknkrNSCRAKCAgdlndmsntTDSN 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 123 ELLEL-------------------------VSLADKHD----AYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDp 173
Cdd:PTZ00265 533 ELIEMrknyqtikdsevvdvskkvlihdfvSALPDKYEtlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD- 611
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 502950432 174 atTRSILELLKDINRRLG----LTIlLITHEMDVVkRICDQVAVIS 215
Cdd:PTZ00265 612 --NKSEYLVQKTINNLKGnenrITI-IIAHRLSTI-RYANTIFVLS 653
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-222 |
3.68e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 82.67 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 28 VPQGQIYGVIGSSGAGKSTLIRCVNMLeRPTSGQVLVNGQDLTSLSERELTRARrqiGMIFQHFNLLSSRTVFGNVALPL 107
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR---AYLSQQQTPPFAMPVFQYLTLHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 108 ElNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARAL-----ANSP--KVLLCDEATSALDPATTRSIL 180
Cdd:PRK03695 95 P-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDVAQQAALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502950432 181 ELLKDINrRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQ 222
Cdd:PRK03695 174 RLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLAS 214
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
20-222 |
4.62e-18 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 85.01 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLlssrtv 99
Cdd:TIGR01194 357 ALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDY---RDLFSAIFADFHL------ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVALPLELN--NTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTR 177
Cdd:TIGR01194 428 FDDLIGPDEGEhaSLDNAQQYLQRLEIADKVKIEDGGFSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFKR 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502950432 178 SIL-ELLKDINRRlGLTILLITHEmDVVKRICDQVAVISGGQLIEQ 222
Cdd:TIGR01194 508 FFYeELLPDLKRQ-GKTIIIISHD-DQYFELADQIIKLAAGCIVKD 551
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-221 |
7.32e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.07 E-value: 7.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 18 IKALSDIDLHVPQGQIYGVIGSSGAGKSTLIrcvNMLE--RPT---SGQVLVNGQDLT--SLSEREltraRRQIGMIFQH 90
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLM---KVLSgvYPHgsyEGEILFDGEVCRfkDIRDSE----ALGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 91 FNLLSSRTVFGNVALPLE-----LNNTPKAEIKTRvnELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCD 165
Cdd:NF040905 87 LALIPYLSIAENIFLGNErakrgVIDWNETNRRAR--ELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502950432 166 EATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLIE 221
Cdd:NF040905 165 EPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-268 |
3.11e-17 |
|
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: 83.14 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTQINKIFQqGTRSiKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQD-LTSLSEreltr 79
Cdd:TIGR01257 1937 ILRLNELTKVYS-GTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISD----- 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 80 ARRQIGMIFQHF---NLLSSRTvfgNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALA 156
Cdd:TIGR01257 2010 VHQNMGYCPQFDaidDLLTGRE---HLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 157 NSPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVseifSHPKTPV 236
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI----QHLKSKF 2161
|
250 260 270
....*....|....*....|....*....|..
gi 502950432 237 AQEFIkSTLHLDIPEDylqklqsEFAPDLSPL 268
Cdd:TIGR01257 2162 GDGYI-VTMKIKSPKD-------DLLPDLNPV 2185
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
6-201 |
4.60e-17 |
|
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: 78.91 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 6 QINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLS-ERELTRARRQI 84
Cdd:cd03290 2 QVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSfEATRSRNRYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 85 GMIFQHFNLLSSrTVFGNVALPLELNntpkaeiKTRVNELLELVSLADKHDAYP-----------ANLSGGQKQRVAIAR 153
Cdd:cd03290 82 AYAAQKPWLLNA-TVEENITFGSPFN-------KQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502950432 154 ALANSPKVLLCDEATSALDPATT-----RSILELLKDINRrlglTILLITHEM 201
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIHLSdhlmqEGILKFLQDDKR----TLVLVTHKL 202
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-218 |
4.69e-17 |
|
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: 76.72 E-value: 4.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 2 IRLTQINKIFqqGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNgqdltslsereltrar 81
Cdd:cd03221 1 IELENLSKTY--GGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 82 rqigmifqhfnllssrtvfgnvalplelnntPKAEIktrvnellelvsladkhdAYPANLSGGQKQRVAIARALANSPKV 161
Cdd:cd03221 61 -------------------------------STVKI------------------GYFEQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 162 LLCDEATSALDPATTRSILELLKDINRrlglTILLITHEMDVVKRICDQVAVISGGQ 218
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-199 |
2.00e-16 |
|
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: 76.63 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSErELTRARRQIGmifqHFNLLSSR-T 98
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLG----HLPGLKPElS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 99 VFGNVALPLELNNTPKAEIktrvNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRS 178
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|.
gi 502950432 179 ILELLKDINRRLGLtILLITH 199
Cdd:TIGR01189 166 LAGLLRAHLARGGI-VLLTTH 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-219 |
2.03e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 22 SDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSerelTRARRQIGMIFqhfnLLSSRTVFG 101
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS----TAQRLARGLVY----LPEDRQSSG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 102 -NVALPLELN------NTPKAEIKT-RVNELLELV--SLADK--HDAYPA-NLSGGQKQRVAIARALANSPKVLLCDEAT 168
Cdd:PRK15439 352 lYLDAPLAWNvcalthNRRGFWIKPaRENAVLERYrrALNIKfnHAEQAArTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502950432 169 SALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-199 |
2.06e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.84 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRarrQIGmifqHFNLL-SSRTV 99
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH---YLG----HRNAMkPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVALPLELNNTPKaeikTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARAL-ANSPkVLLCDEATSALDPATTRS 178
Cdd:PRK13539 91 AENLEFWAAFLGGEE----LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLvSNRP-IWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|...
gi 502950432 179 ILELlkdINRRL--GLTILLITH 199
Cdd:PRK13539 166 FAEL---IRAHLaqGGIVIAATH 185
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-199 |
2.36e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 76.38 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSErELTRARRQIGmifqHFNLLSSR-TV 99
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLG----HAPGIKTTlSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVALPLELNNTPKAEiktrvnELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSI 179
Cdd:cd03231 91 LENLRFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|
gi 502950432 180 LELLKDINRRLGLtILLITH 199
Cdd:cd03231 165 AEAMAGHCARGGM-VVLTTH 183
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-230 |
3.55e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.02 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 35 GVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSereLTRARRQIGMIFQHfNLLSSRTVFGNVALPLELNNTPk 114
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRRVLSIIPQS-PVLFSGTVRFNIDPFSEHNDAD- 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 115 aeiktrVNELLELVSLADKHDAYP-----------ANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILELL 183
Cdd:PLN03232 1341 ------LWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTI 1414
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502950432 184 KDINRrlGLTILLITHEMDVVKRiCDQVAVISGGQLIEQDIVSEIFS 230
Cdd:PLN03232 1415 REEFK--SCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-222 |
4.93e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 78.99 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLserELTRARRQIGMIFQHfNLLSSRTV 99
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQT-PFLFSDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVAL--PlelnNTPKAEIKtrvnellELVSLADKHD-------AYPAN-------LSGGQKQRVAIARALANSPKVLL 163
Cdd:PRK10789 406 ANNIALgrP----DATQQEIE-------HVARLASVHDdilrlpqGYDTEvgergvmLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 164 CDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDQVAVISGGQLIEQ 222
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQR 530
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
16-245 |
1.07e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 16 RSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERE--------LTRARRQIGMi 87
Cdd:PRK09700 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkkgmayITESRRDNGF- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 88 FQHFNLLSsrtvfgNVALPLELNN----------TPKAEIKTRVNElLELVSLadKHDAYPAN---LSGGQKQRVAIARA 154
Cdd:PRK09700 353 FPNFSIAQ------NMAISRSLKDggykgamglfHEVDEQRTAENQ-RELLAL--KCHSVNQNiteLSGGNQQKVLISKW 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 155 LANSPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLieqdivSEIFSHPKT 234
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL------TQILTNRDD 496
|
250
....*....|.
gi 502950432 235 PVAQEFIKSTL 245
Cdd:PRK09700 497 MSEEEIMAWAL 507
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-220 |
2.81e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.09 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRARrqIGMIFQHF--NLLSSR 97
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPR--IAYMPQGLgkNLYPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 98 TVFGNVALPLELNNTPKAEIKTRVNELLE---LVSLADKhdayPA-NLSGGQKQRVAIARALANSPKVLLCDEATSALDP 173
Cdd:NF033858 94 SVFENLDFFGRLFGQDAAERRRRIDELLRatgLAPFADR----PAgKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502950432 174 ATTRSILELLKDI-NRRLGLTILLITHEMDVVKRiCDQVAVISGGQLI 220
Cdd:NF033858 170 LSRRQFWELIDRIrAERPGMSVLVATAYMEEAER-FDWLVAMDAGRVL 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-199 |
3.02e-15 |
|
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: 72.57 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVlvngqdltSLSEREltrarrqiGMIFqhfnlLSSRTVF 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGE--------DLLF-----LPQRPYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 GNVALplelnntpkaeiktrvNELLelvsladkhdAYP--ANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRS 178
Cdd:cd03223 76 PLGTL----------------REQL----------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180
....*....|....*....|.
gi 502950432 179 ILELLKDinrrLGLTILLITH 199
Cdd:cd03223 130 LYQLLKE----LGITVISVGH 146
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-200 |
5.92e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 72.68 E-value: 5.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLtslsERELTRARRQIGMIFQHFNLLSSRTVF 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 GNVALPLELNNTpkaeiKTRVNELLELVSLADKHDaYPAN-LSGGQKQRVAIARALANSPKVLLCDEATSALDpatTRSI 179
Cdd:PRK13540 93 ENCLYDIHFSPG-----AVGITELCRLFSLEHLID-YPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELSL 163
|
170 180
....*....|....*....|...
gi 502950432 180 LELLKDI--NRRLGLTILLITHE 200
Cdd:PRK13540 164 LTIITKIqeHRAKGGAVLLTSHQ 186
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-230 |
6.80e-15 |
|
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: 76.14 E-value: 6.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLLSSRtvf 100
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL---RFKITIIPQDPVLFSGS--- 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 gnvalpLELNNTPKAEIKTR-VNELLELVSLADKHDAYPA-----------NLSGGQKQRVAIARALANSPKVLLCDEAT 168
Cdd:TIGR00957 1376 ------LRMNLDPFSQYSDEeVWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502950432 169 SALDPATTRSILELLKdiNRRLGLTILLITHEMDVvkrICD--QVAVISGGQLIEQDIVSEIFS 230
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNT---IMDytRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-222 |
5.18e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.01 E-value: 5.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 16 RSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIR------CVNMLER--PTSGQVLVNGQDLTSLSERELTRARRQIGMI 87
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKalagdlTGGGAPRgaRVTGDVTLNGEPLAAIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 88 FQHFNLLSSRTVfgnvalpLELNNTPKA-----------EIKTRVNELLELVSLaDKHDAypANLSGGQKQRVAIARALA 156
Cdd:PRK13547 92 AQPAFAFSAREI-------VLLGRYPHArragalthrdgEIAWQALALAGATAL-VGRDV--TTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502950432 157 N---------SPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGGQLIEQ 222
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-219 |
6.58e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.25 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 22 SDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRA--------RRQIGMIFQHF-- 91
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgimlcpedRKAEGIIPVHSva 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 92 -NL-LSSRTVFgnVALPLELNNTPKAE----------IKTRVNELLELvsladkhdaypaNLSGGQKQRVAIARALANSP 159
Cdd:PRK11288 350 dNInISARRHH--LRAGCLINNRWEAEnadrfirslnIKTPSREQLIM------------NLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 160 KVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-230 |
1.28e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.08 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 35 GVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLLSsrtvfGNVALPLE-LNNTP 113
Cdd:PLN03130 1269 GIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL---RKVLGIIPQAPVLFS-----GTVRFNLDpFNEHN 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 114 KAEIKtrvnELLELVSLAD-------KHDAYPA----NLSGGQKQRVAIARALANSPKVLLCDEATSALDPAT----TRS 178
Cdd:PLN03130 1341 DADLW----ESLERAHLKDvirrnslGLDAEVSeageNFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTdaliQKT 1416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502950432 179 ILELLKdinrrlGLTILLITHEMDVVkrI-CDQVAVISGGQLIEQDIVSEIFS 230
Cdd:PLN03130 1417 IREEFK------SCTMLIIAHRLNTI--IdCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
18-228 |
1.90e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 70.53 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 18 IKALSDIDLHVPQGQIYGVIGSSGAGKSTlircvnmlerpTSGQVLVNGQDLTSLSERELT-----RA-RRQIG----MI 87
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**R-----------GALPAHV*GPDAGRRPWRF*TwcanrRAlRRTIG*hrpVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 88 FQHFNLLSSRTVFGNVALPLELNntpKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEA 167
Cdd:NF000106 95 *GRRESFSGRENLYMIGR*LDLS---RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502950432 168 TSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEI 228
Cdd:NF000106 172 TTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-220 |
2.16e-13 |
|
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: 68.06 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 6 QINKIFQQGTRSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPT---SGQVLVNGQDltslSERELTRARR 82
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP----YKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 83 QIGMIFQHFNLLSSRTVFgnvalplelnntpkaeiktrvnELLELvSLADKHDAYPANLSGGQKQRVAIARALANSPKVL 162
Cdd:cd03233 84 EIIYVSEEDVHFPTLTVR----------------------ETLDF-ALRCKGNEFVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 163 LCDEATSALDPATTRSILELLKDINRRLGLTILLITHEM-DVVKRICDQVAVISGGQLI 220
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQAsDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-221 |
7.04e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.23 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLlssrtv 99
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY---RKLFSAVFTDFHL------ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNValpleLNNTPKAEIKTRVNELLELVSLADK-----HDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPA 174
Cdd:PRK10522 409 FDQL-----LGPEGKPANPALVEKWLERLKMAHKleledGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502950432 175 TTRSILELLKDINRRLGLTILLITHEmDVVKRICDQVAVISGGQLIE 221
Cdd:PRK10522 484 FRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSE 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-219 |
1.49e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERE--------LTRARRQ----IGMIF 88
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDRKRdglvLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 89 QHFNLLSSRTVFGNVALPLElnntpKAEIKTRVNELLELVSL-ADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEA 167
Cdd:PRK10762 348 KENMSLTALRYFSRAGGSLK-----HADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502950432 168 TSALDPATTRSILELlkdINR--RLGLTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:PRK10762 423 TRGVDVGAKKEIYQL---INQfkAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-199 |
1.74e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.60 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 22 SDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSErELTRARRQIGmifqHFNLLSSR-TVF 100
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLG----HQPGIKTElTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 GNVALPLELNNTPKAEiktRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSIL 180
Cdd:PRK13538 93 ENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLE 169
|
170
....*....|....*....
gi 502950432 181 ELLKDINRRLGLTIlLITH 199
Cdd:PRK13538 170 ALLAQHAEQGGMVI-LTTH 187
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-200 |
1.95e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 68.04 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTqinKIFQqGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQvlvngqdltslsereltrA 80
Cdd:TIGR03719 7 MNRVS---KVVP-PKKEI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE------------------A 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQ----IGMIFQHFNLLSSRTVFGNVALPL--------ELN------NTPKAEIK---TRVNELLELVSLADKH----- 134
Cdd:TIGR03719 63 RPQpgikVGYLPQEPQLDPTKTVRENVEEGVaeikdaldRFNeisakyAEPDADFDklaAEQAELQEIIDAADAWdldsq 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 135 -------------DAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDpATTRSILE-LLKDINrrlGlTILLITHE 200
Cdd:TIGR03719 143 leiamdalrcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD-AESVAWLErHLQEYP---G-TVVAVTHD 217
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-231 |
2.23e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 67.61 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQ-DLTSLSEreltrarrqigmifqhfNLLSSRT 98
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaALIAISS-----------------GLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 99 VFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRS 178
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502950432 179 ILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFSH 231
Cdd:PRK13545 182 CLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-232 |
3.06e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 67.66 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRARRQIGMIFQH-FNLLSSRTV 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKaLNEKYYQQV 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVALPLELNNTPKAEiKTRVNEllelvsladkhdaYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSI 179
Cdd:TIGR00957 734 LEACALLPDLEILPSGD-RTEIGE-------------KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 180 LE-------LLKDINRrlgltiLLITHEMDVVKRIcDQVAVISGGQlieqdiVSEIFSHP 232
Cdd:TIGR00957 800 FEhvigpegVLKNKTR------ILVTHGISYLPQV-DVIIVMSGGK------ISEMGSYQ 846
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
21-237 |
3.78e-12 |
|
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: 65.32 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTL----IRCVNMLErptsGQVLVNGQDLTSLSERELtraRRQIGMIFQHFNLLSS 96
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHTL---RSRLSIILQDPILFSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 97 RtvfgnvalpLELNNTPKAE-IKTRVNELLELVSLADKHDAYPA-----------NLSGGQKQRVAIARALANSPKVLLC 164
Cdd:cd03288 110 S---------IRFNLDPECKcTDDRLWEALEIAQLKNMVKSLPGgldavvteggeNFSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502950432 165 DEATSALDPAtTRSILE--LLKDINRRlglTILLITHEMDVVKRiCDQVAVISGGQLIEQDIVSEIFSHPKTPVA 237
Cdd:cd03288 181 DEATASIDMA-TENILQkvVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-219 |
6.99e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.11 E-value: 6.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 16 RSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCV-NMLERPTSGQVLVNGQDLTSLSERELTRA--------RRQIG- 85
Cdd:PRK13549 273 PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPQQAIAQgiamvpedRKRDGi 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 86 ---MIFQHFNLLSSRTVFGNVALpleLNNTpkAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVL 162
Cdd:PRK13549 353 vpvMGVGKNITLAALDRFTGGSR---IDDA--AELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 163 LCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-222 |
7.39e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 7.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCvnML-ERPT--SGQVLVNGqdltslserelTRAR-RQIGMIFqhfnllsS 96
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISA--MLgELPPrsDASVVIRG-----------TVAYvPQVSWIF-------N 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 97 RTVFGNVALPLELNnTPKAEIKTRVNELLELVSLADKHDAYP-----ANLSGGQKQRVAIARALANSPKVLLCDEATSAL 171
Cdd:PLN03130 693 ATVRDNILFGSPFD-PERYERAIDVTALQHDLDLLPGGDLTEigergVNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502950432 172 DPATTRSILEllKDINRRL-GLTILLITHEMDVVKRIcDQVAVISGGQLIEQ 222
Cdd:PLN03130 772 DAHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEE 820
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-208 |
1.34e-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: 65.34 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNgqDLTSLSERELTRArrqigmifqhfNLLSSRTVF 100
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETVKLAYVDQSRD-----------ALDPNKTVW 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 GNVALPLELNNTPKAEIKTRvnellelvsladkhdAYPA--------------NLSGGQKQRVAIARALANSPKVLLCDE 166
Cdd:TIGR03719 405 EEISGGLDIIKLGKREIPSR---------------AYVGrfnfkgsdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502950432 167 ATSALDPATTRSILELLKDinrrLGLTILLITHEMDVVKRIC 208
Cdd:TIGR03719 470 PTNDLDVETLRALEEALLN----FAGCAVVISHDRWFLDRIA 507
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-200 |
1.43e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.90 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCvnMLERP-----TSGQVLVNGQDLTSlserelTRARRqIGMIFQHFNLLS 95
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNV--LAERVttgviTGGDRLVNGRPLDS------SFQRS-IGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 96 SRTV-----F-GNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPA-NLSGGQKQRVAIARALANSPKVLL-CDEA 167
Cdd:TIGR00956 850 TSTVreslrFsAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGeGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190
....*....|....*....|....*....|....*.
gi 502950432 168 TSALDPATTRSILELLkdinRRL---GLTILLITHE 200
Cdd:TIGR00956 930 TSGLDSQTAWSICKLM----RKLadhGQAILCTIHQ 961
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-230 |
2.25e-11 |
|
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: 65.32 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 11 FQQGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERpTSGQVLVNGQDLTSLSereLTRARRQIGMIFQH 90
Cdd:TIGR01271 1227 YTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVT---LQTWRKAFGVIPQK 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 91 FNLLSsrtvfGNVALPLELNNTPKAEIKTRVNELLELVSL----ADKHDAYPAN----LSGGQKQRVAIARALANSPKVL 162
Cdd:TIGR01271 1301 VFIFS-----GTFRKNLDPYEQWSDEEIWKVAEEVGLKSVieqfPDKLDFVLVDggyvLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 163 LCDEATSALDPATTRSILELLKdiNRRLGLTILLITHEMDVVKRiCDQVAVISGGQLIEQDIVSEIFS 230
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLK--QSFSNCTVILSEHRVEALLE-CQQFLVIEGSSVKQYDSIQKLLN 1440
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-219 |
3.12e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.08 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 16 RSIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCV-NMLERPTSGQVLVNGQDLTSLSERELTRARrqIGMI---FQHF 91
Cdd:TIGR02633 271 PHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQAIRAG--IAMVpedRKRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 92 NLLSSRTVFGNVALPLeLNNTPKaeiKTRVNELLEL---------VSLADKHDAYP-ANLSGGQKQRVAIARALANSPKV 161
Cdd:TIGR02633 349 GIVPILGVGKNITLSV-LKSFCF---KMRIDAAAELqiigsaiqrLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-199 |
3.45e-11 |
|
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: 64.05 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 24 IDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTslsERELTRARRQIGMIFQHFNLLSsrtvfgnv 103
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAYRQLFSAVFSDFHLFD-------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 104 alplELNNTPKAEIKTRVNELLELVSLADK----HDAY-PANLSGGQKQRVAIARALA-NSPkVLLCDEATSALDPaTTR 177
Cdd:COG4615 420 ----RLLGLDGEADPARARELLERLELDHKvsveDGRFsTTDLSQGQRKRLALLVALLeDRP-ILVFDEWAADQDP-EFR 493
|
170 180
....*....|....*....|....
gi 502950432 178 SI--LELLKDInRRLGLTILLITH 199
Cdd:COG4615 494 RVfyTELLPEL-KARGKTVIAISH 516
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-219 |
4.07e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.41 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRcvnmlerptsgqvlvngqdlTSLSERELTRAR----RQIGMIFQHFNLLSS 96
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQ--------------------SLLSQFEISEGRvwaeRSIAYVPQQAWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 97 rTVFGNVaLPLELNNTPKAEIKTRVNEL-LELVSLADKHDA----YPANLSGGQKQRVAIARALANSPKVLLCDEATSAL 171
Cdd:PTZ00243 736 -TVRGNI-LFFDEEDAARLADAVRVSQLeADLAQLGGGLETeigeKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502950432 172 DPATTRSILELLKdINRRLGLTILLITHEMDVVKRiCDQVAVISGGQL 219
Cdd:PTZ00243 814 DAHVGERVVEECF-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRV 859
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
35-221 |
6.20e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 35 GVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMIFQHfNLLSSRTVFGNVALPLELNNtpk 114
Cdd:PTZ00243 1340 GIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL---RRQFSMIPQD-PVLFDGTVRQNVDPFLEASS--- 1412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 115 AEiktrVNELLELVSLADKHDAYP-----------ANLSGGQKQRVAIARAL-ANSPKVLLCDEATSALDPATTRSILEL 182
Cdd:PTZ00243 1413 AE----VWAALELVGLRERVASESegidsrvleggSNYSVGQRQLMCMARALlKKGSGFILMDEATANIDPALDRQIQAT 1488
|
170 180 190
....*....|....*....|....*....|....*....
gi 502950432 183 LkdINRRLGLTILLITHEMDVVKRiCDQVAVISGGQLIE 221
Cdd:PTZ00243 1489 V--MSAFSAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAE 1524
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-221 |
7.90e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 61.76 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGqdltslsereltrarrQIGMIFQHFNLLSSRTV 99
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSI 179
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502950432 180 LELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQLIE 221
Cdd:PRK13546 183 LDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
17-221 |
1.95e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.43 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 17 SIKALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVnmLERP----TSGQVLVNGQDLTSLSEREltRARRQIGMIFQH-- 90
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHPaykiLEGDILFKGESILDLEPEE--RAHLGIFLAFQYpi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 91 -----FNLLSSRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYPAN--LSGGQKQRVAIARALANSPKVLL 163
Cdd:CHL00131 95 eipgvSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNegFSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 164 CDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRIC-DQVAVISGGQLIE 221
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIK 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-229 |
2.17e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCvnMLerptsGQVlvNGQDLTSLSERELTRARRQIGMIFQhfNLLSSRTVF 100
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISA--ML-----GEL--SHAETSSVVIRGSVAYVPQVSWIFN--ATVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 GNvalPLELNNTPKAEIKTRVNELLELVSLADKHD--AYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRS 178
Cdd:PLN03232 702 GS---DFESERYWRAIDVTALQHDLDLLPGRDLTEigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502950432 179 ILE-LLKDINRrlGLTILLITHEMDVVKRIcDQVAVISGGQLIEQDIVSEIF 229
Cdd:PLN03232 779 VFDsCMKDELK--GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-200 |
8.56e-10 |
|
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: 57.64 E-value: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNmlERPTS----GQVLVNGQDLTSlsereltRARRQIGMIFQHFNLLSS 96
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAgvitGEILINGRPLDK-------NFQRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 97 RTvfgnvalplelnntpkaeiktrVNELLELvsladkhDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATT 176
Cdd:cd03232 94 LT----------------------VREALRF-------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180
....*....|....*....|....
gi 502950432 177 RSILELLKDINRRlGLTILLITHE 200
Cdd:cd03232 145 YNIVRFLKKLADS-GQAILCTIHQ 167
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-181 |
1.02e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 23 DIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVnGQDLtslsereltrarrQIGMIFQ-HFNLLSSRTVFG 101
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-------------KLAYVDQsRDALDPNKTVWE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 102 NVALPLELNNTPKAEIKTRvnellelvsladkhdAYPA--------------NLSGGQKQRVAIARALANSPKVLLCDEA 167
Cdd:PRK11819 408 EISGGLDIIKVGNREIPSR---------------AYVGrfnfkggdqqkkvgVLSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
170
....*....|....
gi 502950432 168 TSALDPATTRSiLE 181
Cdd:PRK11819 473 TNDLDVETLRA-LE 485
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-230 |
1.66e-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: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTL----IRCVNmlerpTSGQVLVNGQDLTSLSereLTRARRQIGMIFQHFNLLSs 96
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVP---LQKWRKAFGVIPQKVFIFS- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 97 rtvfGNVALPLELNNTPKAEIKTRVNELLELVSLADKhdaYPANL-----------SGGQKQRVAIARALANSPKVLLCD 165
Cdd:cd03289 91 ----GTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQ---FPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502950432 166 EATSALDPATTRSILELLKdiNRRLGLTILLITHEMDVVKRiCDQVAVISGGQLIEQDIVSEIFS 230
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLN 225
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-218 |
1.93e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.74 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 31 GQIYGVIGSSGAGKSTLIRCV--NMLERPTSGQVLVNGQDLTSlsereltRARRQIGMIFQH---FNLLSSRTVFGNVAL 105
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALagRIQGNNFTGTILANNRKPTK-------QILKRTGFVTQDdilYPHLTVRETLVFCSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 106 pLELNNTPKAEIKTRVNE-LLELVSLADKHDAYPAN-----LSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSI 179
Cdd:PLN03211 167 -LRLPKSLTKQEKILVAEsVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502950432 180 LELLKDINRRlGLTILLITHE-MDVVKRICDQVAVISGGQ 218
Cdd:PLN03211 246 VLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-199 |
2.60e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 1 MIRLTqinKIFQqGTRSIkaLSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQvlvngqdltslsereltrA 80
Cdd:PRK11819 9 MNRVS---KVVP-PKKQI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE------------------A 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 81 RRQ----IGMIFQHFNLLSSRTVFGNValplELNNTPKAEIKTRVNELLELVS--------LADKH-------------- 134
Cdd:PRK11819 65 RPApgikVGYLPQEPQLDPEKTVRENV----EEGVAEVKAALDRFNEIYAAYAepdadfdaLAAEQgelqeiidaadawd 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 135 -----------------DAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDpATTRSILE-LLKDINrrlGlTILL 196
Cdd:PRK11819 141 ldsqleiamdalrcppwDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD-AESVAWLEqFLHDYP---G-TVVA 215
|
...
gi 502950432 197 ITH 199
Cdd:PRK11819 216 VTH 218
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-206 |
3.87e-09 |
|
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: 54.69 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 30 QGQIYGVIGSSGAGKSTLIRCV-NMLERPTSGQVLVNGQDLTslsereltrarrqigmifqhfnllssrtvfgnvalple 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDIL-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 109 lnntpkaeiktrvnELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILEL-----L 183
Cdd:smart00382 43 --------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlL 108
|
170 180
....*....|....*....|...
gi 502950432 184 KDINRRLGLTILLITHEMDVVKR 206
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGP 131
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-173 |
4.48e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.01 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSlSEREltrarRQIGMIFQHFNLLSSRTVF 100
Cdd:PRK13543 27 FGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR-GDRS-----RFMAYLGHLPGLKADLSTL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502950432 101 GNVALpleLNNTPKAEIKTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDP 173
Cdd:PRK13543 101 ENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
119-209 |
1.23e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 119 TRVNELLELVSLadKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILELLKDINrrlGlTILLIT 198
Cdd:PRK11147 137 NRINEVLAQLGL--DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ---G-SIIFIS 210
|
90
....*....|....*
gi 502950432 199 HEMDVVK----RICD 209
Cdd:PRK11147 211 HDRSFIRnmatRIVD 225
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-216 |
2.60e-08 |
|
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: 53.95 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 30 QGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVngqDLTSLSERELTRARRQIGMIFQhfnLLSSRTVfgnvalplel 109
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI---ELDTVSYKPQYIKADYEGTVRD---LLSSITK---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 110 NNTPKAEIKTRVNELLELVSLADKHdayPANLSGGQKQRVAIARALANSPKVLLCDEATSALDP----ATTRSIlellkd 185
Cdd:cd03237 88 DFYTHPYFKTEIAKPLQIEQILDRE---VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVI------ 158
|
170 180 190
....*....|....*....|....*....|....*
gi 502950432 186 inRRLGL----TILLITHEMDVVKRICDQVAVISG 216
Cdd:cd03237 159 --RRFAEnnekTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-230 |
2.60e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 11 FQQGTRSI---KALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELtraRRQIGMI 87
Cdd:PRK10938 6 ISQGTFRLsdtKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQL---QKLVSDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 88 FQHFN--LLS-SRTVFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDAYpanLSGGQKQRVAIARALANSPKVLLC 164
Cdd:PRK10938 83 WQRNNtdMLSpGEDDTGRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502950432 165 DEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQLIEQDIVSEIFS 230
Cdd:PRK10938 160 DEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-219 |
2.81e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERE--------LTRARRQIGmIFQH- 90
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfalVTEERRSTG-IYAYl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 91 ---FNLLSS--RTVFGNVALpleLNNTpkaEIKTRVNELLELVSL-ADKHDAYPANLSGGQKQRVAIARALANSPKVLLC 164
Cdd:PRK10982 342 digFNSLISniRNYKNKVGL---LDNS---RMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502950432 165 DEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-216 |
4.57e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.41 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 26 LHVPQ-GQIYGVIGSSGAGKSTlirCVNMLerptSGQVLVN-GQDLTSLSERELTRARRQIGMiFQHFNLLSSRTVfgNV 103
Cdd:COG1245 93 LPVPKkGKVTGILGPNGIGKST---ALKIL----SGELKPNlGDYDEEPSWDEVLKRFRGTEL-QDYFKKLANGEI--KV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 104 AL-PLELNNTPKAeIKTRVNELLE-------LVSLADKHDAYP------ANLSGGQKQRVAIARALANSPKVLLCDEATS 169
Cdd:COG1245 163 AHkPQYVDLIPKV-FKGTVRELLEkvdergkLDELAEKLGLENildrdiSELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502950432 170 ALDP----ATTRSILELLKDinrrlGLTILLITHEMDVVKRICDQVAVISG 216
Cdd:COG1245 242 YLDIyqrlNVARLIRELAEE-----GKYVLVVEHDLAILDYLADYVHILYG 287
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
7-207 |
5.37e-08 |
|
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: 52.61 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 7 INKIFQQGTRSIKALSDIDLHVPqgqIYGVIGSSGAGKSTLIRCVNML---ERPTSGQVLVNGQDLTSLSEReltraRRQ 83
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSP---LTLIVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKLIREGEV-----RAQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 84 IGMIFQHFN---LLSSRT--VFGNVALplelnnTPKAEIktrvNELLELVsladkhdayPANLSGGQKQ------RVAIA 152
Cdd:cd03240 73 VKLAFENANgkkYTITRSlaILENVIF------CHQGES----NWPLLDM---------RGRCSGGEKVlasliiRLALA 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502950432 153 RALANSPKVLLCDEATSALDPATTR-SILELLKDINRRLGLTILLITHEMDVVKRI 207
Cdd:cd03240 134 ETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-206 |
1.01e-07 |
|
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: 51.17 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 20 ALSDIDLHVPQGQIYGVIGSSGAGKSTLirCVNMLErpTSGQVLVNgqDLTSLSERELTRARRQigmifqhfnlLSSRTV 99
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY--ASGKARLI--SFLPKFSRNKLIFIDQ----------LQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 100 FGNVALPLELNntpkaeiktrvnellelvsladkhdayPANLSGGQKQRVAIARALANSPK--VLLCDEATSALDPATTR 177
Cdd:cd03238 74 VGLGYLTLGQK---------------------------LSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180
....*....|....*....|....*....
gi 502950432 178 SILELLKDInRRLGLTILLITHEMDVVKR 206
Cdd:cd03238 127 QLLEVIKGL-IDLGNTVILIEHNLDVLSS 154
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-216 |
1.16e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.98 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 26 LHVPQ-GQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNG--------------QD-LTSLSERELTRARRQigmifQ 89
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdeildefrgselQNyFTKLLEGDVKVIVKP-----Q 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 90 HFNLLSsRTVFGNVALPLElnNTPKAEIKTRVNELLELVSLADKHdayPANLSGGQKQRVAIARALANSPKVLLCDEATS 169
Cdd:cd03236 95 YVDLIP-KAVKGKVGELLK--KKDERGKLDELVDQLELRHVLDRN---IDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502950432 170 ALDP----ATTRSILELLKDINrrlglTILLITHEMDVVKRICDQVAVISG 216
Cdd:cd03236 169 YLDIkqrlNAARLIRELAEDDN-----YVLVVEHDLAVLDYLSDYIHCLYG 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-233 |
1.50e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 26 LHVPQ-GQIYGVIGSSGAGKSTlirCVNMLerptSGQVLVN-GQDLTSLSERELTRARRQIGMiFQHFNLLSSRTVfgNV 103
Cdd:PRK13409 93 LPIPKeGKVTGILGPNGIGKTT---AVKIL----SGELIPNlGDYEEEPSWDEVLKRFRGTEL-QNYFKKLYNGEI--KV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 104 AL-PLELNNTPKAeIKTRVNELLELVSLADKHDAYP-------------ANLSGGQKQRVAIARALANSPKVLLCDEATS 169
Cdd:PRK13409 163 VHkPQYVDLIPKV-FKGKVRELLKKVDERGKLDEVVerlglenildrdiSELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 170 ALDP----ATTRSILELLKDInrrlglTILLITHEMDVVKRICDQVAVISG--GqlieqdiVSEIFSHPK 233
Cdd:PRK13409 242 YLDIrqrlNVARLIRELAEGK------YVLVVEHDLAVLDYLADNVHIAYGepG-------AYGVVSKPK 298
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-216 |
3.65e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 18 IKALSDIDLHVPQGQIY-----GVIGSSGAGKSTLIRCVNMLERPTSGQVLVN------GQDLTSLSERELTRARRQIGM 86
Cdd:PRK13409 347 TKKLGDFSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykPQYIKPDYDGTVEDLLRSITD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 87 IFqhfnllSSRTVFGNVALPLELNntpkaeiktrvnELLelvsladkhDAYPANLSGGQKQRVAIARALANSPKVLLCDE 166
Cdd:PRK13409 427 DL------GSSYYKSEIIKPLQLE------------RLL---------DKNVKDLSGGELQRVAIAACLSRDADLYLLDE 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 167 ATSALDP----ATTRSIlellkdinRRL----GLTILLITHEMDVVKRICDQVAVISG 216
Cdd:PRK13409 480 PSAHLDVeqrlAVAKAI--------RRIaeerEATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-221 |
4.14e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.56 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLE--RPTSGQVLVNGQDLTSLSEREltRARRQIGMIFQHfnllssRT 98
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED--RAGEGIFMAFQY------PV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 99 VFGNVALPLELNNTPKAEIKTRVNELLELVSLADKHDA------YPANL---------SGGQKQRVAIARALANSPKVLL 163
Cdd:PRK09580 89 EIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEkiallkMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502950432 164 CDEATSALDPATTRSILE---LLKDINRrlglTILLITHEMDVVKRI-CDQVAVISGGQLIE 221
Cdd:PRK09580 169 LDESDSGLDIDALKIVADgvnSLRDGKR----SFIIVTHYQRILDYIkPDYVHVLYQGRIVK 226
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-205 |
4.78e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.48 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 38 GSSGAGKSTLIRCVNMLERPTSGQVLVNGQDLTSLSERELTRARRQIGmifqhfnLLSSRTVFGNVALPLELNNTpkaei 117
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLG-------LKLEMTVFENLKFWSEIYNS----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 118 KTRVNELLELVSLADKHDAYPANLSGGQKQRVAIARALANSPKVLLCDEATSALDpATTRSILELLKDINRRLGLTILLI 197
Cdd:PRK13541 101 AETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS-KENRDLLNNLIVMKANSGGIVLLS 179
|
....*...
gi 502950432 198 THEMDVVK 205
Cdd:PRK13541 180 SHLESSIK 187
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-172 |
1.07e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 31 GQIYGVIGSSGAGKSTLIRCVNMLE---RPTSGQVL-----VNGQDLTSL-----SERELTRARRQIGMIFQHFNLLSSR 97
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMAMHAidgIPKNCQILhveqeVVGDDTTALqcvlnTDIERTQLLEEEAQLVAQQRELEFE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 98 TVFGNVALPLElNNTPKAEIKTRVNEL---LELVsladkhDAYPA-----------------------NLSGGQKQRVAI 151
Cdd:PLN03073 283 TETGKGKGANK-DGVDKDAVSQRLEEIykrLELI------DAYTAearaasilaglsftpemqvkatkTFSGGWRMRIAL 355
|
170 180
....*....|....*....|.
gi 502950432 152 ARALANSPKVLLCDEATSALD 172
Cdd:PLN03073 356 ARALFIEPDLLLLDEPTNHLD 376
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
19-216 |
1.59e-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: 49.78 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIY-----GVIGSSGAGKSTLIRcvnML---ERPTSG------------QVLVNGQDLTSlseRELT 78
Cdd:COG1245 349 KSYGGFSLEVEGGEIRegevlGIVGPNGIGKTTFAK---ILagvLKPDEGevdedlkisykpQYISPDYDGTV---EEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 79 RArrqigmifQHFNLLSSRTVFGNVALPLELNNtpkaeiktrvneLLelvsladkhDAYPANLSGGQKQRVAIARALANS 158
Cdd:COG1245 423 RS--------ANTDDFGSSYYKTEIIKPLGLEK------------LL---------DKNVKDLSGGELQRVAIAACLSRD 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502950432 159 PKVLLCDEATSALDP----ATTRSIlellkdinRRL----GLTILLITHEMDVVKRICDQVAVISG 216
Cdd:COG1245 474 ADLYLLDEPSAHLDVeqrlAVAKAI--------RRFaenrGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
141-199 |
2.02e-06 |
|
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: 49.36 E-value: 2.02e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 502950432 141 LSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILELLkdinRRLGLTILLITH 199
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-217 |
2.66e-06 |
|
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: 49.14 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQdlTSLSEReltrarrqigmifqhFNLLSSRTVF 100
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSPQ---------------TSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 GNVALPLELNNTPKAEIkTRVNELLELVSLADKHDAYP-----ANLSGGQKQRVAIARALANSPKVLLCDEATSALDPAT 175
Cdd:TIGR01271 505 DNIIFGLSYDEYRYTSV-IKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502950432 176 TRSILE--LLKDINRRlglTILLITHEMDVVKRiCDQVAVISGG 217
Cdd:TIGR01271 584 EKEIFEscLCKLMSNK---TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
21-222 |
3.56e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.25 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLircvnmlerpTSGQVLVNGQD--LTSLSerelTRARRQIGM------------ 86
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL----------AFDTIYAEGQRryVESLS----AYARQFLGQmdkpdvdsiegl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 87 -----IFQHFNLLSSRTVFGNVAlplELNNT-----PKAEIKTRVNELLEL----VSLadkhDAYPANLSGGQKQRVAIA 152
Cdd:cd03270 77 spaiaIDQKTTSRNPRSTVGTVT---EIYDYlrllfARVGIRERLGFLVDVglgyLTL----SRSAPTLSGGEAQRIRLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 153 RAL-ANSPKVL-LCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVkRICDQV------AVISGGQLIEQ 222
Cdd:cd03270 150 TQIgSGLTGVLyVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTI-RAADHVidigpgAGVHGGEIVAQ 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
142-242 |
4.26e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 142 SGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILL-ITHEMDVVKRICDQVAVISGGQli 220
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVaIYQCSQDAYELFDKVIVLYEGY-- 288
|
90 100
....*....|....*....|..
gi 502950432 221 eqdivsEIFSHPKTPVAQEFIK 242
Cdd:TIGR00956 289 ------QIYFGPADKAKQYFEK 304
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-218 |
8.45e-06 |
|
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: 46.77 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 21 LSDIDLHVPQGQIYGVIGSSGAGKSTLIRCVNMLERPTSGQVLVNGQdlTSLSEReltrarrqigmifqhFNLLSSRTVF 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSSQ---------------FSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 GNVALPLELNNTP-KAEIKT-RVNEllELVSLADKHDAYPA----NLSGGQKQRVAIARALANSPKVLLCDEATSALDPA 174
Cdd:cd03291 116 ENIIFGVSYDEYRyKSVVKAcQLEE--DITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502950432 175 TTRSILE--LLKDINRRlglTILLITHEMDVVKRiCDQVAVISGGQ 218
Cdd:cd03291 194 TEKEIFEscVCKLMANK---TRILVTSKMEHLKK-ADKILILHEGS 235
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
36-219 |
2.24e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 36 VIGSSGAGKSTLIRCVNMLERPTSGQVL--------------VNGQDLTSlsERELTRARRQIGMIFQHFNL-LSSRTVF 100
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDLSS--NPLLYMMRCFPGVPEQKLRAhLGSFGVT 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 101 GNVALplelnntpkaeiktrvnellelvsladkHDAYpaNLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSIL 180
Cdd:PLN03073 618 GNLAL----------------------------QPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALI 667
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502950432 181 EllkdinrrlGLT-----ILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:PLN03073 668 Q---------GLVlfqggVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
31-219 |
3.02e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 31 GQIYGVIGSSGAGKSTLIRCV-NMLErPTSGQV-LVNGQDLTSLsereltrarRQIGMIFQHFNLLSsrTVF-GNV---- 103
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILgGDLE-PSAGNVsLDPNERLGKL---------RQDQFAFEEFTVLD--TVImGHTelwe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 104 ---------ALP------------LElnnTPKAEI-----KTRVNELLELVSLA-DKHDAYPANLSGGQKQRVAIARALA 156
Cdd:PRK15064 95 vkqerdriyALPemseedgmkvadLE---VKFAEMdgytaEARAGELLLGVGIPeEQHYGLMSEVAPGWKLRVLLAQALF 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502950432 157 NSPKVLLCDEATSALDPATTRSILELLKDINRrlglTILLITHEMDVVKRICDQVAVISGGQL 219
Cdd:PRK15064 172 SNPDILLLDEPTNNLDINTIRWLEDVLNERNS----TMIIISHDRHFLNSVCTHMADLDYGEL 230
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
141-222 |
4.84e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.14 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 141 LSGGQKQRVAIARAL---ANSPKVLLCDEATSALDPATTRSILELLkdinRRL---GLTILLITHEMDVVKrICDQVAVI 214
Cdd:cd03271 170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVL----QRLvdkGNTVVVIEHNLDVIK-CADWIIDL 244
|
90
....*....|....
gi 502950432 215 S------GGQLIEQ 222
Cdd:cd03271 245 GpeggdgGGQVVAS 258
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-205 |
8.14e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 8.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502950432 141 LSGGQKQRVAIARAL---ANSPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVK 205
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNLDVIK 896
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-251 |
8.62e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 139 ANLSGGQKQRVAIARALAN--SPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKrICDQV----- 211
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAelIGITYILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQMIS-LADRIidigp 552
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 502950432 212 -AVISGGQLIEQDIVSEIFSHPKTPVAQeFIKSTLHLDIPE 251
Cdd:PRK00635 553 gAGIFGGEVLFNGSPREFLAKSDSLTAK-YLRQELTIPIPE 592
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
140-233 |
1.13e-04 |
|
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: 42.17 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 140 NLSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDQVAVISGgql 219
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG--- 147
|
90
....*....|....
gi 502950432 220 ieQDIVSEIFSHPK 233
Cdd:cd03222 148 --EPGVYGIASQPK 159
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
139-185 |
1.93e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 39.91 E-value: 1.93e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 139 ANLSGGQKQR---VAIARALA----------NSPKVLLCDEATSALDPATTRSILELLKD 185
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-247 |
2.08e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 141 LSGGQKQRVAIARALANS---PKVLLCDEATSALDPATTRSILELLKDINRrLGLTILLITHEMDVVKrICDQVAVIS-- 215
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTH-QGHTVVIIEHNMHVVK-VADYVLELGpe 887
|
90 100 110
....*....|....*....|....*....|....*....
gi 502950432 216 ----GGQLIEQDIVSEIFsHPKTPVA---QEFIKSTLHL 247
Cdd:PRK00635 888 ggnlGGYLLASCSPEELI-HLHTPTAkalRPYLSSPQEL 925
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-241 |
2.30e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 19 KALSDIDLHVPQGQIYGVIGSSGAGKSTLIRCV--NMLERPTSGQVLVNGQDLTSLSERE--------LTRARRQIGMif 88
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDGKEVDVSTVSDaidaglayVTEDRKGYGL-- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 89 qhfNLLSsrTVFGNVALPlelnNTPKAEIKTRVNELLELV-------SLADKH---DAYPANLSGGQKQRVAIARALANS 158
Cdd:NF040905 352 ---NLID--DIKRNITLA----NLGKVSRRGVIDENEEIKvaeeyrkKMNIKTpsvFQKVGNLSGGNQQKVVLSKWLFTD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 159 PKVLLCDEATSALDPATTRSILELlkdINR--RLGLTILLITHEMDVVKRICDQVAVISGGQlieqdIVSEIfshPKTPV 236
Cdd:NF040905 423 PDVLILDEPTRGIDVGAKYEIYTI---INElaAEGKGVIVISSELPELLGMCDRIYVMNEGR-----ITGEL---PREEA 491
|
....*
gi 502950432 237 AQEFI 241
Cdd:NF040905 492 SQERI 496
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
141-222 |
4.56e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 141 LSGGQKQRVAIARALANSPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILL-ITHEMDVVKRICDQVAVISGGQL 219
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMsLLQPAPETFDLFDDIILLSEGQI 416
|
...
gi 502950432 220 IEQ 222
Cdd:PLN03140 417 VYQ 419
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
49-251 |
7.69e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 49 RCVNMLERPTSGQVLVNGQDLTSLSERELTRArrqigMIFqhFNLLSSRTVFGNVALPLelnntpKAEIKTRVNEL---- 124
Cdd:TIGR00630 410 SCGGTRLKPEALAVTVGGKSIADVSELSIREA-----HEF--FNQLTLTPEEKKIAEEV------LKEIRERLGFLidvg 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 125 LELVSLAdkHDAypANLSGGQKQRVAIAR----ALANSPKVLlcDEATSALDPATTRSILELLKDInRRLGLTILLITHE 200
Cdd:TIGR00630 477 LDYLSLS--RAA--GTLSGGEAQRIRLATqigsGLTGVLYVL--DEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD 549
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 201 MDVVkRICDQV------AVISGGQLIEQDIVSEIFSHPKTPVAQeFIKSTLHLDIPE 251
Cdd:TIGR00630 550 EDTI-RAADYVidigpgAGEHGGEVVASGTPEEILANPDSLTGQ-YLSGRKKIEVPA 604
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
141-206 |
1.11e-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: 39.27 E-value: 1.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502950432 141 LSGGQKQRVAIARALAN-----SPKVLLcDEATSALDPATTRSILELLKDiNRRLGLTILLITHEMDVVKR 206
Cdd:cd03227 78 LSGGEKELSALALILALaslkpRPLYIL-DEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLPELAEL 146
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
37-200 |
1.88e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.93 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 37 IGSSGAGKSTLIRCvnMLE--RPTSGQVLVNgqdlTSLsereltrarrQIGMIFQHFNLLS-SRTVFGNVAlplelnnTP 113
Cdd:PRK11147 351 IGPNGCGKTTLLKL--MLGqlQADSGRIHCG----TKL----------EVAYFDQHRAELDpEKTVMDNLA-------EG 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 114 KAEIKTRVNELLELVSLAD-----KHDAYPAN-LSGGQKQRVAIARALANSPKVLLCDEATSALDPATtrsiLELLKDIN 187
Cdd:PRK11147 408 KQEVMVNGRPRHVLGYLQDflfhpKRAMTPVKaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET----LELLEELL 483
|
170
....*....|...
gi 502950432 188 RRLGLTILLITHE 200
Cdd:PRK11147 484 DSYQGTVLLVSHD 496
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-62 |
5.17e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.72 E-value: 5.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502950432 2 IRLTQINKIFQQGTrSIKALS----------DIDLHVPQGQIYGVIGSSGAGKSTLIRC-VNMLErPTSGQV 62
Cdd:PRK15064 307 IRFEQDKKLHRNAL-EVENLTkgfdngplfkNLNLLLEAGERLAIIGENGVGKTTLLRTlVGELE-PDSGTV 376
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-205 |
7.94e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 7.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502950432 138 PAN-LSGGQKQRVAIARALA--NSPKVL-LCDEATSALDPATTRSILELLkdinRRL---GLTILLITHEMDVVK 205
Cdd:COG0178 823 PATtLSGGEAQRVKLASELSkrSTGKTLyILDEPTTGLHFHDIRKLLEVL----HRLvdkGNTVVVIEHNLDVIK 893
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
7-77 |
8.69e-03 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 37.78 E-value: 8.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502950432 7 INKIFQQGTRSIKALsdidLHVPQGQIYGVIGSSGAGKSTLIrcvNMLERPTSGQVLV------NGQDLTSLSEREL 77
Cdd:PRK07721 138 IREPMEVGVRAIDSL----LTVGKGQRVGIFAGSGVGKSTLM---GMIARNTSADLNVialigeRGREVREFIERDL 207
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
5-66 |
8.76e-03 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 37.84 E-value: 8.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502950432 5 TQINKIFQQGTRSIKALsdidLHVPQGQIYGVIGSSGAGKSTLIrcvNMLERPTSGQVLVNG 66
Cdd:PRK07960 153 TPIEHVLDTGVRAINAL----LTVGRGQRMGLFAGSGVGKSVLL---GMMARYTQADVIVVG 207
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
33-218 |
9.11e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 36.86 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 33 IYGVIGSSGAGKSTLIRCVNM--------LERPTSGQVLVN-GQDLTSLS-----ERELTRARRQIGMIFQHFnllsSRT 98
Cdd:cd03279 30 LFLICGPTGAGKSTILDAITYalygktprYGRQENLRSVFApGEDTAEVSftfqlGGKKYRVERSRGLDYDQF----TRI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502950432 99 VFgnvaLPlelnntpkaeiKTRVNELLElvsladkHDAypANLSGGQKQRVAIARALANSPKV----------LLCDEAT 168
Cdd:cd03279 106 VL----LP-----------QGEFDRFLA-------RPV--STLSGGETFLASLSLALALSEVLqnrggarleaLFIDEGF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502950432 169 SALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDQVAVISGGQ 218
Cdd:cd03279 162 GTLDPEALEAVATALELI-RTENRMVGVISHVEELKERIPQRLEVIKTPG 210
|
|
| |
