|
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: 683.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQF 240
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 241 IQSTLHLDIPDDYQARLKSTATADSVPMLRMEFTGHSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGTQ 320
Cdd:PRK11153 241 IQSTLHLDLPEDYLARLQAEPTTGSGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGDP 320
|
330 340
....*....|....*....|...
gi 1447223793 321 EDTQAAIAWLQEHHVKVEVLGYV 343
Cdd:PRK11153 321 GDIQAAIAYLQEHGVKVEVLGYV 343
|
|
| 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: 641.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:TIGR02314 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQF 240
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 241 IQSTLHLDIPDDYQARLKSTATADSVPMLRMEFTGHSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGTQ 320
Cdd:TIGR02314 241 IRSTLHLSIPEDYQERLQATPFADSVPMVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMHGTQ 320
|
330 340
....*....|....*....|...
gi 1447223793 321 EDTQAAIAWLQEHHVKVEVLGYV 343
Cdd:TIGR02314 321 QDTQAAIAYLQEHNVKVEVLGYV 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: 604.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQF 240
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 241 IQSTLHLDIPDDYQARLKSTATADSVpmLRMEFTGHSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGTQ 320
Cdd:COG1135 241 LPTVLNDELPEELLARLREAAGGGRL--VRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDD 318
|
330 340
....*....|....*....|.
gi 1447223793 321 EDTQAAIAWLQEHHVKVEVLG 341
Cdd:COG1135 319 AAIDAALAYLREQGVVVEVLG 339
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-233 |
1.59e-160 |
|
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: 448.18 E-value: 1.59e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPK 233
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-222 |
4.49e-103 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 301.96 E-value: 4.49e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQ-IGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:COG1136 84 RRRhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGQLIEQ 222
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-242 |
6.85e-102 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 299.60 E-value: 6.85e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFqqGNRsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTAlSEKELTRA 80
Cdd:COG1126 1 MIEIENLHKSF--GDL--EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVAL-PLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQ 239
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234
|
...
gi 1447223793 240 FIQ 242
Cdd:COG1126 235 FLS 237
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-241 |
1.29e-96 |
|
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: 286.11 E-value: 1.29e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFqqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:COG1127 5 MIEVRNLTKSF--GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPL-ELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKtPLAQQ 239
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDD-PWVRQ 239
|
..
gi 1447223793 240 FI 241
Cdd:COG1127 240 FL 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-248 |
2.26e-96 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 294.89 E-value: 2.26e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQ-GNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTR 79
Cdd:COG1123 260 LLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 80 ARRQIGMIFQH----FNllASRTVFGNVALPLEL-DNTPQAEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIAR 153
Cdd:COG1123 340 LRRRVQMVFQDpyssLN--PRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLPPDLaDRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPK 233
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
250
....*....|....*
gi 1447223793 234 TPLAQQFIQSTLHLD 248
Cdd:COG1123 498 HPYTRALLAAVPSLD 512
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-219 |
2.04e-95 |
|
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: 282.46 E-value: 2.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRAR 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 R-QIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:cd03255 81 RrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGQL 219
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-221 |
9.36e-94 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 278.09 E-value: 9.36e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNrsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:COG2884 1 MIRFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG2884 78 RRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIE 221
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-240 |
6.97e-89 |
|
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: 266.29 E-value: 6.97e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRAR 81
Cdd:cd03261 1 IELRGLTKSF--GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPL-ELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKtPLAQQF 240
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD-PLVRQF 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-248 |
1.88e-88 |
|
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: 265.90 E-value: 1.88e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtra 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQH----FNllASRTVFGNVALPLELDNTPqaEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIARAL 155
Cdd:COG1124 78 RRRVQMVFQDpyasLH--PRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPSFlDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTP 235
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
250
....*....|...
gi 1447223793 236 LAQQFIQSTLHLD 248
Cdd:COG1124 234 YTRELLAASLAFE 246
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-220 |
3.14e-85 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 257.68 E-value: 3.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRsiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:COG3638 2 MLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPLeLDNT----------PQAEiKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVA 150
Cdd:COG3638 79 RRRIGMIFQQFNLVPRLSVLTNVLAGR-LGRTstwrsllglfPPED-RERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLI 220
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-235 |
1.54e-82 |
|
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: 253.05 E-value: 1.54e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLERP--TEGSVQVDGQELTALSEKEL 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 78 TRAR-RQIGMIFQhfNLLAS----RTVFGNVALPLEL-DNTPQAEIKRRVTELLDLVGLGDKH---DSYPANLSGGQKQR 148
Cdd:COG0444 81 RKIRgREIQMIFQ--DPMTSlnpvMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPErrlDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEV 228
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*..
gi 1447223793 229 FSHPKTP 235
Cdd:COG0444 239 FENPRHP 245
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-234 |
2.58e-82 |
|
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: 249.56 E-value: 2.58e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNrsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTalsEKELTRAR 81
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQH-FNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG1122 75 RKVGLVFQNpDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKT 234
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-222 |
3.32e-81 |
|
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: 246.65 E-value: 3.32e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQH----FNllASRTVFGNVALPLEL--DNTPQAEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIAR 153
Cdd:cd03257 81 RKEIQMVFQDpmssLN--PRMTIGEQIAEPLRIhgKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQ 222
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-202 |
2.20e-79 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 243.07 E-value: 2.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGqeltalseKELTRA 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG--------KPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMD 202
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVD 200
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-219 |
2.30e-79 |
|
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: 241.28 E-value: 2.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqGNRsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTAlSEKELTRAR 81
Cdd:cd03262 1 IEIKNLHKSF--GDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVAL-PLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-241 |
2.62e-78 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 243.47 E-value: 2.62e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQqgnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEkeltrA 80
Cdd:COG3842 5 ALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-----E 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG3842 76 KRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQF 240
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADF 235
|
.
gi 1447223793 241 I 241
Cdd:COG3842 236 I 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-228 |
1.48e-76 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 234.96 E-value: 1.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqgnRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTalseKELTRAR 81
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEV 228
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-242 |
5.57e-76 |
|
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: 234.85 E-value: 5.57e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVF-----------QQGNRSIQ---------ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGS 61
Cdd:cd03294 1 IKIKGLYKIFgknpqkafkllAKGKSKEEilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 62 VQVDGQELTALSEKELTRARRQ-IGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPAN 140
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKkISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLI 220
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
250 260
....*....|....*....|..
gi 1447223793 221 EQDTVSEVFSHPKTPLAQQFIQ 242
Cdd:cd03294 241 QVGTPEEILTNPANDYVREFFR 262
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-220 |
8.53e-76 |
|
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: 233.23 E-value: 8.53e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNrsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRAR 81
Cdd:cd03256 1 IEVENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLeLDNTP---------QAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIA 152
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVLSGR-LGRRStwrslfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLI 220
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-218 |
1.15e-75 |
|
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: 230.54 E-value: 1.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQgnrsIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALsEKELTRAR 81
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLeldntpqaeikrrvtelldlvglgdkhdsypanlSGGQKQRVAIARALASNPKV 161
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQ 218
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-241 |
6.38e-75 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 234.66 E-value: 6.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqGNRsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQEL-TALSEKEltra 80
Cdd:COG1118 3 IEVRNISKRF--GSF--TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 rRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG1118 75 -RRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 161 VLLCDEATSALDpATTRSILE-LLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQ 239
Cdd:COG1118 154 VLLLDEPFGALD-AKVRKELRrWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVAR 232
|
..
gi 1447223793 240 FI 241
Cdd:COG1118 233 FL 234
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-231 |
1.09e-74 |
|
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: 230.65 E-value: 1.09e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNrsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNV---------ALPLELDNTPQAEiKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAI 151
Cdd:TIGR02315 78 RRRIGMIFQHYNLIERLTVLENVlhgrlgykpTWRSLLGRFSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSH 231
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-218 |
1.11e-74 |
|
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: 229.28 E-value: 1.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 3 KLSNITkvFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraRR 82
Cdd:cd03225 1 ELKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL---RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 83 QIGMIFQHFNL-LASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03225 76 KVGLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQ 218
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-225 |
1.35e-74 |
|
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: 229.28 E-value: 1.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTalsekeltRAR 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT--------GPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISN--GQLIEQDTV 225
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVEV 218
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-235 |
1.94e-74 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 232.70 E-value: 1.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 10 VFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRARRQIGMIFQ 89
Cdd:COG4608 23 LFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 90 hfNLLAS----RTVFGNVALPLELDN-TPQAEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIARALASNPKVLL 163
Cdd:COG4608 103 --DPYASlnprMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPEHaDRYPHEFSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447223793 164 CDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTP 235
Cdd:COG4608 181 CDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHP 252
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-251 |
4.41e-74 |
|
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: 230.03 E-value: 4.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNR-SIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQhF--NLLASRTVFGNVAL-PLELdNTPQAEIKRRVTELLDLVGLGDK-HDSYPANLSGGQKQRVAIARALA 156
Cdd:TIGR04521 81 RKKVGLVFQ-FpeHQLFEETVYKDIAFgPKNL-GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKtpl 236
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD--- 235
|
250
....*....|....*
gi 1447223793 237 aqqFIQStLHLDIPD 251
Cdd:TIGR04521 236 ---ELEK-IGLDVPE 246
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-242 |
9.35e-74 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 233.07 E-value: 9.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFqqGNRSIQAL----------------------NNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPT 58
Cdd:COG4175 3 KIEVRNLYKIF--GKRPERALklldqgkskdeilektgqtvgvNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 59 EGSVQVDGQELTALSEKELTRARRQ-IGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSY 137
Cdd:COG4175 81 AGEVLIDGEDITKLSKKELRELRRKkMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 138 PANLSGGQKQRVAIARALASNPKVLLCDEATSALDPattrsiL-------ELLkDINRRLGLTILLITHEMDVVKRICDC 210
Cdd:COG4175 161 PDELSGGMQQRVGLARALATDPDILLMDEAFSALDP------LirremqdELL-ELQAKLKKTIVFITHDLDEALRLGDR 233
|
250 260 270
....*....|....*....|....*....|..
gi 1447223793 211 VAVISNGQLIEQDTVSEVFSHPKTPLAQQFIQ 242
Cdd:COG4175 234 IAIMKDGRIVQIGTPEEILTNPANDYVADFVE 265
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-227 |
2.10e-73 |
|
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: 226.93 E-value: 2.10e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQ-IGMIFQHFNLLASRTVFGNVALPLELDNTPQAEikRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:COG4181 88 RARhVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSE 227
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-222 |
5.16e-73 |
|
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: 225.09 E-value: 5.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqgnRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEkeltrAR 81
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP-----ER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQlIEQ 222
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGR-IVQ 211
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-246 |
2.73e-72 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 224.68 E-value: 2.73e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFqqGnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQE----------LT 70
Cdd:COG4598 8 ALEVRDLHKSF--G--DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEirlkpdrdgeLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 71 ALSEKELTRARRQIGMIFQHFNLLASRTVFGNVAL-PLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRV 149
Cdd:COG4598 84 PADRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVF 229
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVF 242
|
250
....*....|....*..
gi 1447223793 230 SHPKTPLAQQFIQSTLH 246
Cdd:COG4598 243 GNPKSERLRQFLSSSLK 259
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-272 |
1.68e-71 |
|
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: 230.95 E-value: 1.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPT---EGSVQVDGQELTALSEKEL 77
Cdd:COG1123 4 LLEVRDLSVRYPGGDV--PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 78 traRRQIGMIFQHF-NLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:COG1123 82 ---GRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPktpl 236
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP---- 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 1447223793 237 aqQFIQSTLHLDIPddyqARLKSTATADSVPMLRME 272
Cdd:COG1123 235 --QALAAVPRLGAA----RGRAAPAAAAAEPLLEVR 264
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-243 |
5.03e-71 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 221.02 E-value: 5.03e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNRsiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraR 81
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKH--DSYPANLSGGQKQRVAIARALASNP 159
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQ 239
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAE 234
|
....
gi 1447223793 240 FIQS 243
Cdd:cd03295 235 FVGA 238
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-254 |
1.29e-70 |
|
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: 220.76 E-value: 1.29e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNRsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGqeLTALSEKELTRAR 81
Cdd:TIGR04520 1 IEVENVSFSYPESEK--PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQH-FNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:TIGR04520 77 KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMD-VVKriCDCVAVISNGQLIEQDTVSEVFSHpktplaQQ 239
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEeAVL--ADRVIVMNKGKIVAEGTPREIFSQ------VE 228
|
250
....*....|....*
gi 1447223793 240 FIQStLHLDIPDDYQ 254
Cdd:TIGR04520 229 LLKE-IGLDVPFITE 242
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-233 |
1.76e-69 |
|
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: 217.60 E-value: 1.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFqqGnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltRA 80
Cdd:COG0411 4 LLEVRGLTKRF--G--GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR--IA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPLE----------LDNTPQ-----AEIKRRVTELLDLVGLGDKHDSYPANLSGGQ 145
Cdd:COG0411 78 RLGIARTFQNPRLFPELTVLENVLVAAHarlgrgllaaLLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTV 225
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
....*...
gi 1447223793 226 SEVFSHPK 233
Cdd:COG0411 238 AEVRADPR 245
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-219 |
7.38e-69 |
|
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: 214.58 E-value: 7.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGnrsIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRAR 81
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-241 |
6.28e-67 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 214.17 E-value: 6.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQqgnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltra 80
Cdd:COG3839 3 SLELENVSKSYG----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 rRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG3839 75 -RNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 161 VLLCDEATSALDP---ATTRSileLLKDINRRLGLTILLITHE----MdvvkRICDCVAVISNGQLIEQDTVSEVFSHPK 233
Cdd:COG3839 154 VFLLDEPLSNLDAklrVEMRA---EIKRLHRRLGTTTIYVTHDqveaM----TLADRIAVMNDGRIQQVGTPEELYDRPA 226
|
....*...
gi 1447223793 234 TPLAQQFI 241
Cdd:COG3839 227 NLFVAGFI 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-233 |
6.42e-67 |
|
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: 210.37 E-value: 6.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqgnRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltRAR 81
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE--IAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTP----------QAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAI 151
Cdd:cd03219 75 LGIGRTFQIPRLFPELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSH 231
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNN 233
|
..
gi 1447223793 232 PK 233
Cdd:cd03219 234 PR 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-228 |
1.94e-66 |
|
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: 208.96 E-value: 1.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqgnRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLE-----RPTEGSVQVDGQELTALSEKE 76
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 77 LTRaRRQIGMIFQHFNLLASrTVFGNVALPLEL-DNTPQAEIKRRVTELLDLVGLGD--KHDSYPANLSGGQKQRVAIAR 153
Cdd:cd03260 77 LEL-RRRVGMVFQKPNPFPG-SIYDNVAYGLRLhGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447223793 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEV 228
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-241 |
1.03e-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: 207.09 E-value: 1.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGnrsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEkeltrAR 81
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP-----HK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03300 72 RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQFI 241
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-241 |
1.72e-65 |
|
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: 206.81 E-value: 1.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQgnrsIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltrar 81
Cdd:cd03296 3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLEL----DNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALAS 157
Cdd:cd03296 74 RNVGFVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 158 NPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLA 237
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFV 233
|
....
gi 1447223793 238 QQFI 241
Cdd:cd03296 234 YSFL 237
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-248 |
7.15e-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: 213.78 E-value: 7.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 10 VFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLerPTEGSVQVDGQELTALSEKELTRARRQIGMIF 88
Cdd:COG4172 291 LFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALlRLI--PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 89 QH-FNLLASR-TVFGNVALPLELDNTPQ--AEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIARALASNPKVLL 163
Cdd:COG4172 369 QDpFGSLSPRmTVGQIIAEGLRVHGPGLsaAERRARVAEALEEVGLDPAArHRYPHEFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 164 CDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQFIQS 243
Cdd:COG4172 449 LDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAA 528
|
....*
gi 1447223793 244 TLHLD 248
Cdd:COG4172 529 APLLE 533
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-228 |
4.64e-64 |
|
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: 203.17 E-value: 4.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQqgnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTalseKELTRA 80
Cdd:COG4555 1 MIEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR----KEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEV 228
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-250 |
4.84e-63 |
|
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: 209.16 E-value: 4.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 11 FQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKS-TLIRCVNLLERP---TEGSVQVDGQELTALSEKELTRAR-RQIG 85
Cdd:COG4172 16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERELRRIRgNRIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 86 MIFQ---------HfnllasrTVFGNVALPLEL-DNTPQAEIKRRVTELLDLVGLGDKH---DSYPANLSGGQKQRVAIA 152
Cdd:COG4172 96 MIFQepmtslnplH-------TIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHP 232
Cdd:COG4172 169 MALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAP 248
|
250
....*....|....*...
gi 1447223793 233 KTPLAQQFIQSTLHLDIP 250
Cdd:COG4172 249 QHPYTRKLLAAEPRGDPR 266
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-242 |
3.00e-62 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 198.39 E-value: 3.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQgnrsIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTrA 80
Cdd:PRK09493 1 MIEFKNVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL-I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVAL-PLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQ 239
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
...
gi 1447223793 240 FIQ 242
Cdd:PRK09493 235 FLQ 237
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-241 |
1.82e-61 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 196.13 E-value: 1.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITkvFQQGNRSIQAlnnvSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEkeltrA 80
Cdd:COG3840 1 MLRLDDLT--YRYGDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-----A 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG3840 70 ERPVSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQF 240
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
|
.
gi 1447223793 241 I 241
Cdd:COG3840 230 L 230
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-241 |
2.69e-61 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 196.41 E-value: 2.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLL--ERP---TEGSVQVDGQELTAlSEKELTRARRQIGMIFQHFNL 93
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDIYD-PDVDVVELRRRVGMVFQKPNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 94 LASrTVFGNVALPLEL-DNTPQAEIKRRVTELLDLVGL----GDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEAT 168
Cdd:COG1117 104 FPK-SIYDNVAYGLRLhGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 169 SALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQFI 241
Cdd:COG1117 183 SALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-245 |
1.92e-60 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 194.20 E-value: 1.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQqGNrsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTA---LS-EKE 76
Cdd:PRK11264 3 AIEVKNLVKKFH-GQ---TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarsLSqQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 77 LTRA-RRQIGMIFQHFNLLASRTVFGNVAL-PLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARA 154
Cdd:PRK11264 79 LIRQlRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 155 LASNPKVLLCDEATSALDP-------ATTRSILEllkdiNRRlglTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSE 227
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPelvgevlNTIRQLAQ-----EKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
250
....*....|....*...
gi 1447223793 228 VFSHPKTPLAQQFIQSTL 245
Cdd:PRK11264 231 LFADPQQPRTRQFLEKFL 248
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-235 |
3.24e-60 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 193.31 E-value: 3.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQqgnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQEL---TALSEKELT 78
Cdd:COG4161 3 IQLKNINCFYG----SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 RARRQIGMIFQHFNLLASRTVFGN-VALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALAS 157
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 158 NPKVLLCDEATSALDPATTRSILELLKDINrRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTvSEVFSHPKTP 235
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTE 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
2.31e-59 |
|
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: 191.41 E-value: 2.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITkvFQQGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtra 80
Cdd:COG1120 1 MLEAENLS--VGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVAL---P-LELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:COG1120 74 ARRIAYVPQEPPAPFGLTVRELVALgryPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFS 230
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-219 |
1.42e-58 |
|
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: 186.83 E-value: 1.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGnrsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTalseKELTRAR 81
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFgnvalpleldntpqaeikrrvtELLDLvglgdkhdsypanlSGGQKQRVAIARALASNPKV 161
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVR----------------------ENLKL--------------SGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-245 |
2.92e-57 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 186.33 E-value: 2.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQE----------LTALSEKELTRARRQIGMIF 88
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqLKVADKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 89 QHFNLLASRTVFGNV-ALPLELDNTPQAEIKRRVTELLDLVGLGDK-HDSYPANLSGGQKQRVAIARALASNPKVLLCDE 166
Cdd:PRK10619 99 QHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 167 ATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQFIQSTL 245
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLKGSL 256
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-268 |
3.28e-57 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 186.76 E-value: 3.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITkvFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELtalSEKELTRAR 81
Cdd:PRK13635 6 IRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL---SEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQH-FNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK13635 81 RQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSEVFSHpktplAQQF 240
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS-----GHML 234
|
250 260
....*....|....*....|....*...
gi 1447223793 241 IQstLHLDIPddYQARLKSTATADSVPM 268
Cdd:PRK13635 235 QE--IGLDVP--FSVKLKELLKRNGILL 258
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-232 |
7.41e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 184.91 E-value: 7.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITkvFQQGNRsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGqeltalseKELTRA 80
Cdd:COG1121 6 AIELENLT--VSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG--------KPPRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASR--TVFGNVAL----PLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARA 154
Cdd:COG1121 74 RRRIGYVPQRAEVDWDFpiTVRDVVLMgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVIsNGQLIEQDTVSEVFSHP 232
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPE 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-227 |
9.44e-57 |
|
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: 183.73 E-value: 9.44e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQgnrsIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTalseKELTRAR 81
Cdd:cd03265 1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03265 73 RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSE 227
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-219 |
1.52e-56 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 183.15 E-value: 1.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNrsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK10908 78 RRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINrRLGLTILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-245 |
1.85e-56 |
|
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: 187.23 E-value: 1.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 23 NVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTAlSEKELTRA--RRQIGMIFQHFNLLASRTVF 100
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD-SARGIFLPphRRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 101 GNvalpLE--LDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:COG4148 96 GN----LLygRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 179 ILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPK-TPLAQQFIQSTL 245
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDlLPLAGGEEAGSV 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-246 |
5.40e-56 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 182.52 E-value: 5.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQqgnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQEL---TALSEKELT 78
Cdd:PRK11124 3 IQLNGINCFYG----AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 RARRQIGMIFQHFNLLASRTVFGN-VALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALAS 157
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 158 NPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEvFSHPKTPla 237
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTE-- 234
|
....*....
gi 1447223793 238 qQFIQSTLH 246
Cdd:PRK11124 235 -AFKNYLSH 242
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-222 |
7.03e-56 |
|
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: 181.30 E-value: 7.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqGNRSiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltrar 81
Cdd:cd03301 1 VELENVTKRF--GNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQlIEQ 222
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ-IQQ 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-248 |
3.74e-55 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 183.75 E-value: 3.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqGNRsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltrar 81
Cdd:PRK10851 3 IEIANIKKSF--GRT--QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLEL----DNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALAS 157
Cdd:PRK10851 74 RKVGFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 158 NPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQlIEQ-DTVSEVFSHPKTPL 236
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGN-IEQaGTPDQVWREPATRF 232
|
250
....*....|..
gi 1447223793 237 AQQFIQSTLHLD 248
Cdd:PRK10851 233 VLEFMGEVNRLQ 244
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-250 |
1.34e-54 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 179.80 E-value: 1.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITkvFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELtalSEKELTRA 80
Cdd:PRK13632 7 MIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQH-FNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK13632 82 RKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMD-VVKriCDCVAVISNGQLIEQDTVSEVFSHpktplaQ 238
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDeAIL--ADKVIVFSEGKLIAQGKPKEILNN------K 233
|
250
....*....|..
gi 1447223793 239 QFIQStLHLDIP 250
Cdd:PRK13632 234 EILEK-AKIDSP 244
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-228 |
3.04e-54 |
|
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: 188.89 E-value: 3.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITkvFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraR 81
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---R 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLaSRTVFGNVALpleldNTPQAEIKRrVTELLDLVGLGDKHDSYP-----------ANLSGGQKQRVA 150
Cdd:COG2274 549 RQIGVVLQDVFLF-SGTIRENITL-----GDPDATDEE-IIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVkRICDCVAVISNGQLIEQDTVSEV 228
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEEL 696
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
14-260 |
3.63e-54 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 180.55 E-value: 3.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 14 GNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRARRQIGMIFQhfNL 93
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQ--NP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 94 LAS----RTVFGNVALPLELdNT--PQAEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIARALASNPKVLLCDE 166
Cdd:PRK11308 102 YGSlnprKKVGQILEEPLLI-NTslSAAERREKALAMMAKVGLRPEHyDRYPHMFSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 167 ATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQFIQSTLH 246
Cdd:PRK11308 181 PVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSATPR 260
|
250
....*....|....
gi 1447223793 247 LDiPDDYQARLKST 260
Cdd:PRK11308 261 LN-PDDRRERIKLT 273
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-228 |
3.19e-53 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 182.53 E-value: 3.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFqqgnRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltrA 80
Cdd:COG1129 4 LLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD---A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQ-IGMIFQHFNLLASRTVFGNVALPLELDNTP---QAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:COG1129 77 QAAgIAIIHQELNLVPNLSVAENIFLGREPRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447223793 157 SNPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEV 228
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-219 |
6.68e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.46 E-value: 6.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITkvFQQGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSekeLTRAR 81
Cdd:COG4619 1 LELEGLS--FRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASrTVFGNVALPLELDNTPQAEikRRVTELLDLVGLGDKHDSYPA-NLSGGQKQRVAIARALASNPK 160
Cdd:COG4619 74 RQVAYVPQEPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-202 |
1.25e-52 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 174.28 E-value: 1.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSekeltrA 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG------A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRqiGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG4525 77 DR--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMD 202
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVE 196
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
11-259 |
1.99e-52 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 176.05 E-value: 1.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 11 FQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRARRQIGMIFQh 90
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQ- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 91 fNLLAS---RTVFGNV-ALPLEL--DNTPQAEIKRRVTELLDLVGL-GDKHDSYPANLSGGQKQRVAIARALASNPKVLL 163
Cdd:PRK15079 106 -DPLASlnpRMTIGEIiAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 164 CDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQFIQS 243
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSA 264
|
250
....*....|....*.
gi 1447223793 244 tlhLDIPDDYQARLKS 259
Cdd:PRK15079 265 ---VPIPDPDLERNKT 277
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-233 |
2.13e-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: 2.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKeltraRRQIGMIFQHFNLLASRTVF 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 101 GNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSIL 180
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 181 ELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPK 233
Cdd:cd03299 170 EELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-169 |
3.88e-52 |
|
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: 169.37 E-value: 3.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraRRQIGMIFQHFNLLASRTVF 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL---RKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 101 GNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHD----SYPANLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-268 |
5.05e-52 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 173.38 E-value: 5.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQgNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTalsEKELTRA 80
Cdd:PRK13650 4 IIEVKNLTFKYKE-DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQH-FNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK13650 80 RHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKrICDCVAVISNGQLIEQDTVSEVFSHpktplAQQ 239
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSR-----GND 233
|
250 260
....*....|....*....|....*....
gi 1447223793 240 FIQstLHLDIPddYQARLKSTATADSVPM 268
Cdd:PRK13650 234 LLQ--LGLDIP--FTTSLVQSLRQNGYDL 258
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-220 |
7.16e-52 |
|
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: 170.79 E-value: 7.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 3 KLSNITkvFQQGNRsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGqeltalseKELTRARR 82
Cdd:cd03235 1 EVEDLT--VSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG--------KPLEKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 83 QIGMIFQHFNLLASR--TVFGNVALPL----ELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:cd03235 69 RIGYVPQRRSIDRDFpiSVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVIsNGQLI 220
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-218 |
8.93e-52 |
|
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: 169.10 E-value: 8.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITkvFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLER---PTEGSVQVDGQELTALSEKELt 78
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLL---KLLLRlydPTSGEILIDGVDLRDLDLESL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 raRRQIGMIFQHFNLLaSRTVFGNValpleldntpqaeikrrvtelldlvglgdkhdsypanLSGGQKQRVAIARALASN 158
Cdd:cd03228 75 --RKNIAYVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRD 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 159 PKVLLCDEATSALDPATTRSILELLKdiNRRLGLTILLITHEMDVVKRiCDCVAVISNGQ 218
Cdd:cd03228 115 PPILILDEATSALDPETEALILEALR--ALAKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-227 |
9.51e-52 |
|
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: 170.76 E-value: 9.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTalseKELTRAR 81
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDInrRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSE 227
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-229 |
2.80e-51 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 171.77 E-value: 2.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNR-SIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKeLTRA 80
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNL-LASRTVFGNVAL-PLELdNTPQAEIKRRVTELLDLVGLG--DKHDSYPANLSGGQKQRVAIARALA 156
Cdd:PRK13637 82 RKKVGLVFQYPEYqLFEETIEKDIAFgPINL-GLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVF 229
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-239 |
4.67e-51 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 170.64 E-value: 4.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRARRQIGMIFQH----FNll 94
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDsisaVN-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 95 ASRTVFGNVALPLE-LDNTPQAEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
Cdd:PRK10419 104 PRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 173 PATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEV--FSHPKTPLAQQ 239
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKltFSSPAGRVLQN 252
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-243 |
6.74e-51 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 170.02 E-value: 6.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQ-----QGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKe 76
Cdd:COG4167 5 LEVRNLSKTFKyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 77 lTRARRqIGMIFQHFNL-LASRTVFGNV-ALPLELdNT--PQAEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAI 151
Cdd:COG4167 84 -YRCKH-IRMIFQDPNTsLNPRLNIGQIlEEPLRL-NTdlTAEEREERIFATLRLVGLLPEHaNFYPHMLSSGQKQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSH 231
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240
|
250
....*....|..
gi 1447223793 232 PKTPLAQQFIQS 243
Cdd:COG4167 241 PQHEVTKRLIES 252
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-218 |
6.85e-51 |
|
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: 166.27 E-value: 6.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 3 KLSNITKVFQQGnrsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraRR 82
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL---RR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 83 QIGMIFQhfnllasrtvfgnvalpleldntpqaeikrrvtelldlvglgdkhdsypanLSGGQKQRVAIARALASNPKVL 162
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 163 LCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQ 218
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-234 |
1.29e-50 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 169.49 E-value: 1.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTaLSEKELTRARRQIGMIFQHF-NLLASR 97
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVRKTVGIVFQNPdDQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 98 TVFGNVAL-PLELdNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATT 176
Cdd:PRK13639 95 TVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 177 RSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKT 234
Cdd:PRK13639 174 SQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-241 |
1.66e-50 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 172.44 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQqgnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKeltraR 81
Cdd:PRK09452 15 VELRGISKSFD----GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-----N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:PRK09452 86 RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 162 LLCDEATSALDpATTRSILEL-LKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQlIEQD-TVSEVFSHPKTPLAQQ 239
Cdd:PRK09452 166 LLLDESLSALD-YKLRKQMQNeLKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR-IEQDgTPREIYEEPKNLFVAR 243
|
..
gi 1447223793 240 FI 241
Cdd:PRK09452 244 FI 245
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-243 |
1.02e-49 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 170.40 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQqgnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTalsekELTRA 80
Cdd:PRK11607 19 LLEIRNLTKSFD----GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK11607 90 QRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 161 VLLCDEATSALDPA-TTRSILELLkDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQ 239
Cdd:PRK11607 170 LLLLDEPMGALDKKlRDRMQLEVV-DILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAE 248
|
....
gi 1447223793 240 FIQS 243
Cdd:PRK11607 249 FIGS 252
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-224 |
2.64e-49 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 173.43 E-value: 2.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKSTLircVNLLER---PTEGSVQVDGQELTALSEKELtraRRQIGMIFQHFNLLa 95
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTL---VNLLLRfydPTSGRILIDGVDIRDLTLESL---RRQIGVVPQDTFLF- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 96 SRTVFGNVALPLEldNTPQAEIKR--RVTELLDLV-GLGDKHDSY----PANLSGGQKQRVAIARALASNPKVLLCDEAT 168
Cdd:COG1132 427 SGTIRENIRYGRP--DATDEEVEEaaKAAQAHEFIeALPDGYDTVvgerGVNLSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 169 SALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDT 224
Cdd:COG1132 505 SALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-223 |
3.95e-49 |
|
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: 164.01 E-value: 3.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 23 NVSLHVPaGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEK-ELTRARRQIGMIFQHFNLLASRTVFG 101
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 102 NVALPLELDNtpQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE 181
Cdd:cd03297 95 NLAFGLKRKR--NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1447223793 182 LLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQD 223
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-222 |
7.85e-49 |
|
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: 161.83 E-value: 7.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 3 KLSNITkvFQQGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraRR 82
Cdd:cd03214 1 EVENLS--VGYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---AR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 83 QIGMIfqhfnllasrtvfgnvalpleldntPQAeikrrvtelLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVL 162
Cdd:cd03214 74 KIAYV-------------------------PQA---------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 163 LCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQ 222
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-207 |
9.15e-49 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 163.45 E-value: 9.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 R-RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK11629 85 RnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRI 207
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM 212
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-220 |
1.06e-48 |
|
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: 161.06 E-value: 1.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqgnRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltrAR 81
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD---AR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQ-IGMIFQhfnllasrtvfgnvalpleldntpqaeikrrvtelldlvglgdkhdsypanLSGGQKQRVAIARALASNPK 160
Cdd:cd03216 74 RAgIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQLI 220
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-228 |
1.89e-48 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 164.51 E-value: 1.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFqqGNRsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTAlsekeltRA 80
Cdd:COG4152 1 MLELKGLTKRF--GDK--TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-------ED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIG-----------MifqhfnllasrTVfGNVALPL-ELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQR 148
Cdd:COG4152 70 RRRIGylpeerglypkM-----------KV-GEQLVYLaRLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEV 228
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-228 |
2.84e-48 |
|
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: 161.83 E-value: 2.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 18 IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltRARRQIGMIFQHFNLLASR 97
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE--RARAGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 98 TVFGNVALPLELDntPQAEIKRRVTELLDLV-GLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATT 176
Cdd:cd03224 91 TVEENLLLGAYAR--RRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1447223793 177 RSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEV 228
Cdd:cd03224 169 EEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-234 |
4.47e-48 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 165.28 E-value: 4.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 4 LSNITKVFqqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltrarRQ 83
Cdd:PRK11432 9 LKNITKRF--GSNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-----RD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 84 IGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLL 163
Cdd:PRK11432 80 ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447223793 164 CDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKT 234
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-228 |
9.53e-48 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 167.90 E-value: 9.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFqqGnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltrA 80
Cdd:COG3845 5 ALELRGITKRF--G--GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQ-IGMIFQHFNLLASRTVFGNVAL---PLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:COG3845 78 IALgIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447223793 157 SNPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEV 228
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-232 |
6.38e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 160.57 E-value: 6.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTA-LSEKELTRARRQIGMIFQhF--NLLAS 96
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgKKNKKLKPLRKKVGIVFQ-FpeHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 97 RTVFGNVAL-PLELdNTPQAEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPA 174
Cdd:PRK13634 101 ETVEKDICFgPMNF-GVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 175 TTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHP 232
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
19-231 |
6.97e-47 |
|
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: 166.86 E-value: 6.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraRRQIGMIFQHFNLLASrT 98
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---RRQIAWVPQNPYLFAG-T 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 99 VFGNVALpleldNTPQAEiKRRVTELLDLVGLGDKHDSYP-----------ANLSGGQKQRVAIARALASNPKVLLCDEA 167
Cdd:COG4988 427 IRENLRL-----GRPDAS-DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEP 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 168 TSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSEVFSH 231
Cdd:COG4988 501 TAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-246 |
7.40e-47 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 159.31 E-value: 7.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 17 SIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLL-----ERPTEGSVQVDGQELTALSEKELtraRRQIGMIFQHF 91
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEL---RRRVQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 92 NLLASRTVFGNVALPLELDN--TPQAEIKRRVTELLDLVGL----GDKHDSYPANLSGGQKQRVAIARALASNPKVLLCD 165
Cdd:PRK14247 92 NPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 166 EATSALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQFIQSTL 245
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYVTGRL 249
|
.
gi 1447223793 246 H 246
Cdd:PRK14247 250 Y 250
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-252 |
7.87e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 159.87 E-value: 7.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQ--ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGqeLTALSEKELT 78
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 RARRQIGMIFQH-FNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALAS 157
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 158 NPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSEVFSHPK---- 233
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEmmkk 240
|
250 260
....*....|....*....|....*..
gi 1447223793 234 --------TPLAQQFIQSTlhLDIPDD 252
Cdd:PRK13633 241 igldvpqvTELAYELKKEG--VDIPSD 265
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-267 |
1.20e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 159.58 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERP---TEGSVQVDGQELTalsEKELTRARRQIGMIFQH-FNLLA 95
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLT---AKTVWDIREKVGIVFQNpDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 96 SRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 176 TRSILELLKDINRRLGLTILLITHEMDVVKrICDCVAVISNGQLIEQDTVSEVFshPKTPLAQQfiqstLHLDIPDDYQA 255
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIF--SKVEMLKE-----IGLDIPFVYKL 250
|
250
....*....|..
gi 1447223793 256 RLKSTATADSVP 267
Cdd:PRK13640 251 KNKLKEKGISVP 262
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-222 |
2.00e-46 |
|
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: 156.58 E-value: 2.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqgnRSIQALNNVSLHVPAGqIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKeltrAR 81
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDI--NRrlglTILLITHEMDVVKRICDCVAVISNGQLIEQ 222
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELgeDR----IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-264 |
3.34e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 158.40 E-value: 3.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGN-RSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALS-EKELTR 79
Cdd:PRK13646 3 IRFDNVSYTYQKGTpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 80 ARRQIGMIFQH-----FNLLASRTV-FG--NVALPLEldntpqaEIKRRVTELLDLVGLG-DKHDSYPANLSGGQKQRVA 150
Cdd:PRK13646 83 VRKRIGMVFQFpesqlFEDTVEREIiFGpkNFKMNLD-------EVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFS 230
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
250 260 270
....*....|....*....|....*....|....*...
gi 1447223793 231 HpKTPLAQQFIQ----STLHLDIPDDYQARLKSTATAD 264
Cdd:PRK13646 236 D-KKKLADWHIGlpeiVQLQYDFEQKYQTKLKDIALTE 272
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-218 |
2.06e-45 |
|
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: 154.51 E-value: 2.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVF---QQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQE----LTALS 73
Cdd:COG4778 4 LLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 74 EKELTRARRQ-IGMIFQHFNLL---ASRTVfgnVALPLELDNTPQAEIKRRVTELLDLVGLGDK-HDSYPANLSGGQKQR 148
Cdd:COG4778 84 PREILALRRRtIGYVSQFLRVIprvSALDV---VAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQ 218
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-256 |
2.33e-45 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 159.43 E-value: 2.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRARRQ-IGMIFQHFNLLASRT 98
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 99 VFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 179 ILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQFIQStlhLDIPDDYQAR 256
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG---VDISQVFSAK 277
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-245 |
5.17e-45 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 154.61 E-value: 5.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLL-----ERPTEGSVQVDGQELTAlSEKELTRARRQIGMIFQHFNL 93
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYS-PDVDPIEVRREVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 94 LASRTVFGNVALPLELDN--TPQAEIKRRVTELLDLVGL----GDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEA 167
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 168 TSALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQFIQSTL 245
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGAL 252
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-222 |
5.75e-45 |
|
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: 152.76 E-value: 5.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGnrsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEkeltrAR 81
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-----AL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPqaeiKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03268 72 RRIGALIEAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQ 222
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-219 |
1.19e-44 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 153.68 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 4 LSNITKVFqqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGsvqvdgqELTALSeKELTRARRQ 83
Cdd:PRK11247 15 LNAVSKRY--GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-------ELLAGT-APLAEARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 84 IGMIFQHFNLLASRTVFGNVALPLELDNTPQAEikrrvtELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLL 163
Cdd:PRK11247 83 TRLMFQDARLLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 164 CDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-227 |
1.79e-44 |
|
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: 152.69 E-value: 1.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 18 IQALNNVSLHVPAGQIYGVIGASGAGKSTlirCVNLLER---PTEGSVQVDGQELTALSEKELtraRRQIGMIFQHFNLL 94
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERfydPTSGEILLDGVDIRDLNLRWL---RSQIGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 95 AsRTVFGNVALplELDNTPQAEIKR--RVTELLDLV-GLGDKHDS----YPANLSGGQKQRVAIARALASNPKVLLCDEA 167
Cdd:cd03249 90 D-GTIAENIRY--GKPDATDEEVEEaaKKANIHDFImSLPDGYDTlvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 168 TSALDPATTRSILELLKdiNRRLGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSE 227
Cdd:cd03249 167 TSALDAESEKLVQEALD--RAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-220 |
9.65e-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: 149.83 E-value: 9.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTalseKELTRA 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQLI 220
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-230 |
1.47e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 151.54 E-value: 1.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTaLSEKELTRARRQIGMIFQH-FNLLASR 97
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKLRESVGMVFQDpDNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 98 TVFGNVAL-PLELdNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATT 176
Cdd:PRK13636 99 SVYQDVSFgAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 177 RSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFS 230
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-222 |
2.10e-43 |
|
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: 148.80 E-value: 2.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 25 SLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEkeltrARRQIGMIFQHFNLLASRTVFGNVA 104
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP-----ADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 105 LPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLK 184
Cdd:cd03298 93 LGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1447223793 185 DINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQ 222
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-227 |
2.86e-43 |
|
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: 156.85 E-value: 2.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITkvFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLircVNLLER---PTEGSVQVDGQELTALSEKELt 78
Cdd:COG4987 334 LELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTL---LALLLRfldPQSGSITLGGVDLRDLDEDDL- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 raRRQIGMIFQHFNLLASrTVFGNVALPLeldntPQAEiKRRVTELLDLVGLGDKHDSYP-----------ANLSGGQKQ 147
Cdd:COG4987 408 --RRRIAVVPQRPHLFDT-TLRENLRLAR-----PDAT-DEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSE 227
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEE 555
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
4.18e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 149.90 E-value: 4.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITkvFQ-QGNRSIqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtr 79
Cdd:PRK13648 7 IIVFKNVS--FQyQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 80 aRRQIGMIFQH-FNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASN 158
Cdd:PRK13648 82 -RKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 159 PKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSEVFSH 231
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-220 |
1.03e-42 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 156.42 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQ-IGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK10535 84 RREhFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRiCDCVAVISNGQLI 220
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-233 |
1.16e-42 |
|
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: 147.82 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 18 IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltRARRQIGMIFQHFNLLASR 97
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHR--IARLGIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 98 TVFGNVALPLELdNTPQAEIKRRVTELLDL--VgLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
Cdd:COG0410 94 TVEENLLLGAYA-RRDRAEVRADLERVYELfpR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 176 TRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPK 233
Cdd:COG0410 172 VEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-241 |
1.55e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 148.27 E-value: 1.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQEL---TALSEKELTRARRQIGMIFQHFNLLASR 97
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 98 TVFGNVALPLELDNTPQA-EIKRRVTELLDLVGLG----DKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 173 PATTRSILELLKDINRRlgLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQFI 241
Cdd:PRK14246 186 IVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-250 |
1.72e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 148.41 E-value: 1.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 17 SIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraRRQIGMIFQHFN-LLA 95
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV---RKFVGLVFQNPDdQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 96 SRTVFGNVAL-PLELdNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPA 174
Cdd:PRK13652 93 SPTVEQDIAFgPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 175 TTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKtplaqqfIQSTLHLDIP 250
Cdd:PRK13652 172 GVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD-------LLARVHLDLP 240
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-245 |
1.80e-42 |
|
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: 150.65 E-value: 1.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 24 VSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEK-ELTRARRQIGMIFQHFNLLASRTVFGN 102
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 103 VALPLELDNTPQAEIK-RRVTELLdlvGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE 181
Cdd:TIGR02142 96 LRYGMKRARPSERRISfERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 182 LLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQFIQSTL 245
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGSL 236
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-248 |
4.75e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 147.58 E-value: 4.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNR-SIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSE-KELTR 79
Cdd:PRK13649 3 INLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 80 ARRQIGMIFQhF--NLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDK-HDSYPANLSGGQKQRVAIARALA 156
Cdd:PRK13649 83 IRKKVGLVFQ-FpeSQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 157 SNPKVLLCDEATSALDPATTRSILELLKDINrRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSH----- 231
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDvdfle 240
|
250 260
....*....|....*....|....
gi 1447223793 232 ------PK-TPLAQQFIQSTLHLD 248
Cdd:PRK13649 241 ekqlgvPKiTKFAQRLADRGISFS 264
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
11-257 |
4.90e-42 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 147.22 E-value: 4.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 11 FQQGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRARRQIGMIFQH 90
Cdd:PRK11831 15 FTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 91 FNLLASRTVFGNVALPL-ELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:PRK11831 93 GALFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 170 ALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKtPLAQQFIQSTLHLDI 249
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD-PRVRQFLDGIADGPV 251
|
250
....*....|...
gi 1447223793 250 P-----DDYQARL 257
Cdd:PRK11831 252 PfrypaGDYHADL 264
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-217 |
5.09e-42 |
|
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: 146.07 E-value: 5.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtrarrqigMIFQHFNLLASRTVF 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 101 GNVALPLE--LDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:TIGR01184 73 ENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1447223793 179 ILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNG 217
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-270 |
7.42e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 146.80 E-value: 7.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNRsiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraR 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQH-FNLLASRTVFGNVAL-PLELDNTPqAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK13647 79 SKVGLVFQDpDDQVFSSTVWDDVAFgPVNMGLDK-DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQ---------LIEQDTVSEvfS 230
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRvlaegdkslLTDEDIVEQ--A 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1447223793 231 HPKTPLAQQfiqstLHLDIPDDYQARLKSTaTADSVPMLR 270
Cdd:PRK13647 235 GLRLPLVAQ-----IFEDLPELGQSKLPLT-VKEAVQIIR 268
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-241 |
1.35e-41 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 153.09 E-value: 1.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 10 VFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRARRQIGMIFQ 89
Cdd:PRK10261 329 LLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 90 --HFNLLASRTVFGNVALPLELDNTPQAE-IKRRVTELLDLVGLGDKHD-SYPANLSGGQKQRVAIARALASNPKVLLCD 165
Cdd:PRK10261 409 dpYASLDPRQTVGDSIMEPLRVHGLLPGKaAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 166 EATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQFI 241
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-222 |
2.86e-41 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 143.77 E-value: 2.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 R-RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGQLIEQ 222
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-222 |
3.97e-41 |
|
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: 142.80 E-value: 3.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqgnRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALsekeltrAR 81
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA-------AR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03269 70 NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQ 222
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-220 |
1.16e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 144.46 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNRS-IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQ---VDGQELTALSEKE- 76
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTeLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 77 --------LTRA---------RRQIGMIFQ--HFNLLASRT----VFGNVALpleldNTPQAEIKRRVTELLDLVGLGDK 133
Cdd:PRK13651 83 vleklviqKTRFkkikkikeiRRRVGVVFQfaEYQLFEQTIekdiIFGPVSM-----GVSKEEAKKRAAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 134 H-DSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVA 212
Cdd:PRK13651 158 YlQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTI 236
|
....*...
gi 1447223793 213 VISNGQLI 220
Cdd:PRK13651 237 FFKDGKII 244
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
2.83e-40 |
|
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: 140.69 E-value: 2.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFqqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEkeltRA 80
Cdd:COG4133 2 MLEAENLSCRR--GERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE----DY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEikRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDiNRRLGLTILLITHE 200
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-233 |
2.95e-40 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 141.71 E-value: 2.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFqqGNRsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltRA 80
Cdd:COG1137 3 TLEAENLVKSY--GKR--TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHK--RA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHfnllAS--R--TVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:COG1137 77 RLGIGYLPQE----ASifRklTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTIlLIT-HEmdvVK---RICDCVAVISNGQLIEQDTVSEVFSHP 232
Cdd:COG1137 153 TNPKFILLDEPFAGVDPIAVADIQKIIRHLKER-GIGV-LITdHN---VRetlGICDRAYIISEGKVLAEGTPEEILNNP 227
|
.
gi 1447223793 233 K 233
Cdd:COG1137 228 L 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-230 |
6.44e-40 |
|
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: 147.26 E-value: 6.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRS-IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQV----DGQELTALSEK 75
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 76 ELTRARRQIGMIFQHFNLLASRTVFGNV--ALPLELdntPQAEIKRRVTELLDLVGLGDKH-----DSYPANLSGGQKQR 148
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLteAIGLEL---PDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEV 228
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
..
gi 1447223793 229 FS 230
Cdd:TIGR03269 516 VE 517
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-220 |
9.77e-40 |
|
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: 139.31 E-value: 9.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 13 QGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELtalSEKELtraRRQIGMIFQHFN 92
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKER---RKSIGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 93 llasRTVFGN-VALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSAL 171
Cdd:cd03226 82 ----YQLFTDsVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1447223793 172 DPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLI 220
Cdd:cd03226 158 DYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-244 |
1.15e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 142.30 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVF-QQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVD----GQELTALSE- 74
Cdd:PRK13631 21 ILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 75 --------KELTRARRQIGMIFQ--HFNLLASrTV-----FGNVALpleldNTPQAEIKRRVTELLDLVGLGDKH-DSYP 138
Cdd:PRK13631 101 tnpyskkiKNFKELRRRVSMVFQfpEYQLFKD-TIekdimFGPVAL-----GVKKSEAKKLAKFYLNKMGLDDSYlERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 139 ANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDiNRRLGLTILLITHEMDVVKRICDCVAVISNGQ 218
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
250 260
....*....|....*....|....*.
gi 1447223793 219 LIEQDTVSEVFSHpktplaQQFIQST 244
Cdd:PRK13631 254 ILKTGTPYEIFTD------QHIINST 273
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-201 |
1.78e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 140.22 E-value: 1.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRS-IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltR 79
Cdd:COG1101 1 MLELKNLSKTFNPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 80 ARRqIGMIFQhfNLLA----SRTVFGNVALPLE----------LDNTPQAEIKRRVtELLDLvGLGDKHDSYPANLSGGQ 145
Cdd:COG1101 79 AKY-IGRVFQ--DPMMgtapSMTIEENLALAYRrgkrrglrrgLTKKRRELFRELL-ATLGL-GLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEM 201
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-243 |
1.83e-39 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 142.67 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGnrsIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltra 80
Cdd:PRK11650 3 GLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 rRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK11650 76 -RDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 161 VLLCDEATSALDpATTRSILEL-LKDINRRLGLTILLITHE----MDVVKRIcdcvaVISNGQLIEQ-DTVSEVFSHPKT 234
Cdd:PRK11650 155 VFLFDEPLSNLD-AKLRVQMRLeIQRLHRRLKTTSLYVTHDqveaMTLADRV-----VVMNGGVAEQiGTPVEVYEKPAS 228
|
....*....
gi 1447223793 235 PLAQQFIQS 243
Cdd:PRK11650 229 TFVASFIGS 237
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-227 |
2.58e-39 |
|
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: 138.90 E-value: 2.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNrsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRcvnLLER---PTEGSVQVDGQELTALSEKELt 78
Cdd:cd03253 1 IEFENVTFAYDPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILR---LLFRfydVSSGSILIDGQDIREVTLDSL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 raRRQIGMIFQH---FNllasRTVFGNVALPlELDNTPQAEIK-RRVTELLDLV-GLGDKHDSYPAN----LSGGQKQRV 149
Cdd:cd03253 74 --RRAIGVVPQDtvlFN----DTIGYNIRYG-RPDATDEEVIEaAKAAQIHDKImRFPDGYDTIVGErglkLSGGEKQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSE 227
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-230 |
3.68e-39 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 139.14 E-value: 3.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITkvFQQGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRcvnLLE---RPTEGSVQVDGQELTALSEKEL 77
Cdd:PRK13548 2 MLEARNLS--VRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLR---ALSgelSPDSGEVRLNGRPLADWSPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 78 TRARrqiGMIFQHFNLLASRTVFGNVAL---PLELDNTPQAEIKRRVTELLDLVGLGDKhdSYPAnLSGGQKQRVAIARA 154
Cdd:PRK13548 75 ARRR---AVLPQHSSLSFPFTVEEVVAMgraPHGLSRAEDDALVAAALAQVDLAHLAGR--DYPQ-LSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 155 LA------SNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEV 228
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEV 228
|
..
gi 1447223793 229 FS 230
Cdd:PRK13548 229 LT 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-233 |
7.47e-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: 137.67 E-value: 7.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqGNRsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltRAR 81
Cdd:cd03218 1 LRAENLSKRY--GKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK--RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03218 75 LGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPK 233
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-233 |
1.62e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 138.42 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNR-SIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTA-LSEKELTR 79
Cdd:PRK13641 3 IKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 80 ARRQIGMIFQhF--NLLASRTVFGNVAL-PLELDNTPQaEIKRRVTELLDLVGLGDK-HDSYPANLSGGQKQRVAIARAL 155
Cdd:PRK13641 83 LRKKVSLVFQ-FpeAQLFENTVLKDVEFgPKNFGFSED-EAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 156 ASNPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPK 233
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-230 |
2.09e-38 |
|
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: 136.85 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 11 FQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELtALSEKELTRarRQIGMIFQH 90
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL-ALADPAWLR--RQVGVVLQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 91 fNLLASRTVFGNVALpleldnTPQAEIKRRVTELLDLVGLGDKHDSYP-----------ANLSGGQKQRVAIARALASNP 159
Cdd:cd03252 85 -NVLFNRSIRDNIAL------ADPGMSMERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSEVFS 230
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-253 |
2.18e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 137.92 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 18 IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTAlseKELTRARRQIGMIFQH-FNLLAS 96
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWNLRRKIGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 97 RTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATT 176
Cdd:PRK13642 97 ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 177 RSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSEVFSHPK--------TPLAQQFIQS--TLH 246
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEdmveigldVPFSSNLMKDlrKNG 255
|
....*..
gi 1447223793 247 LDIPDDY 253
Cdd:PRK13642 256 FDLPEKY 262
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-230 |
2.59e-38 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 137.17 E-value: 2.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITkvFQQGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:COG4559 1 MLEAENLS--VRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RrqiGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGD-KHDSYPAnLSGGQKQRVAIARALA--- 156
Cdd:COG4559 77 R---AVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHlAGRSYQT-LSGGEQQRVQLARVLAqlw 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 157 ----SNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFS 230
Cdd:COG4559 153 epvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLT 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-227 |
3.86e-38 |
|
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: 135.82 E-value: 3.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITkvFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLircVNLLER---PTEGSVQVDGQELTALSEKELt 78
Cdd:cd03251 1 VEFKNVT--FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTL---VNLIPRfydVDSGRILIDGHDVRDYTLASL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 raRRQIGMIFQHfNLLASRTVFGNVALPLEldNTPQAEIKR--RVTELLDLV-GLGDKHDSY----PANLSGGQKQRVAI 151
Cdd:cd03251 75 --RRQIGLVSQD-VFLFNDTVAENIAYGRP--GATREEVEEaaRAANAHEFImELPEGYDTVigerGVKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 152 ARALASNPKVLLCDEATSALDPATTR----SILELLKdiNRrlglTILLITHEMDVVKRIcDCVAVISNGQLIEQDTVSE 227
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERlvqaALERLMK--NR----TTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEE 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-272 |
5.17e-38 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 142.15 E-value: 5.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKS-TLIRCVNLLERP----TEGSVQVDGQELTALSEK 75
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 76 ELTRAR-RQIGMIFQH--FNLLASRTVFGNVALPLELDNTPQAEIKR-RVTELLDLVGL---GDKHDSYPANLSGGQKQR 148
Cdd:PRK15134 85 TLRGVRgNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARgEILNCLDRVGIrqaAKRLTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEV 228
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1447223793 229 FSHPKTPLAQQFIQSTlhldiPDDYQARLkstaTADSVPMLRME 272
Cdd:PRK15134 245 FSAPTHPYTQKLLNSE-----PSGDPVPL----PEPASPLLDVE 279
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-219 |
5.97e-38 |
|
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: 133.50 E-value: 5.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraR 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLAsrtvfGNVAlplelDNTpqaeikrrvtelldlvglgdkhdsypanLSGGQKQRVAIARALASNPKV 161
Cdd:cd03246 76 DHVGYLPQDDELFS-----GSIA-----ENI----------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRiCDCVAVISNGQL 219
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-219 |
6.35e-38 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 135.09 E-value: 6.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQgnrsiQALNnVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEkeltrA 80
Cdd:PRK10771 1 MLKLTDITWLYHH-----LPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP-----S 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK10771 70 RRPVSMLFQENNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:PRK10771 150 ILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-241 |
6.38e-38 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 136.07 E-value: 6.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLER--PT---EGSVQVDGQELTAlSEKELTRARRQIGMIFQHFNLL 94
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 95 aSRTVFGNVA-------LPLELDNTPQAEIKRRVteLLDLVGlgDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEA 167
Cdd:PRK14243 104 -PKSIYDNIAygaringYKGDMDELVERSLRQAA--LWDEVK--DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 168 TSALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDCVAVIS---------NGQLIEQDTVSEVFSHPKTPLAQ 238
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQQQATR 256
|
...
gi 1447223793 239 QFI 241
Cdd:PRK14243 257 DYV 259
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-202 |
7.59e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 134.53 E-value: 7.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITkVFQQGNRSIQALNnvsLHVPAGQIYGVIGASGAGKSTLIRCVN-LLERP--TEGSVQVDGQELTALSEkel 77
Cdd:COG4136 1 MLSLENLT-ITLGGRPLLAPLS---LTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLTALPA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 78 trARRQIGMIFQ------HFNllasrtVFGNV--ALPlelDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRV 149
Cdd:COG4136 74 --EQRRIGILFQddllfpHLS------VGENLafALP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMD 202
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-223 |
1.32e-37 |
|
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: 134.38 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQ-----------------QGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQV 64
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligslkslfkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 65 DGQeltaLSEKELTRARRQIGMIF-QHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSG 143
Cdd:cd03267 81 AGL----VPWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQD 223
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
6-270 |
1.83e-37 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 136.57 E-value: 1.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 6 NITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRC-VNLLE---RPTEGSVQVDGQELTALSEKELTR-A 80
Cdd:COG4170 8 NLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAiCGITKdnwHVTADRFRWNGIDLLKLSPRERRKiI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFN--LLASRTVFGNValpleLDNTPQAEI-----------KRRVTELLDLVGLGDKHD---SYPANLSGG 144
Cdd:COG4170 88 GREIAMIFQEPSscLDPSAKIGDQL-----IEAIPSWTFkgkwwqrfkwrKKRAIELLHRVGIKDHKDimnSYPHELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDT 224
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGP 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1447223793 225 VSEVFSHPKTPLAQQFIQSTLHLDIPDDYQARLksTATADSVPMLR 270
Cdd:COG4170 243 TEQILKSPHHPYTKALLRSMPDFRQPLPHKSRL--NTLPGSIPPLQ 286
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-241 |
2.45e-37 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 134.52 E-value: 2.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLL-----ERPTEGSVQVDGQELTAlSEKELTRARRQIGMIFQHFNL 93
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYS-PRTDTVDLRKEIGMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 94 LASrTVFGNVALPLELDNTPQAEIKRRVTELlDLVG------LGDK-HDSyPANLSGGQKQRVAIARALASNPKVLLCDE 166
Cdd:PRK14239 98 FPM-SIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGasiwdeVKDRlHDS-ALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447223793 167 ATSALDPATTRSILELLkdINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQFI 241
Cdd:PRK14239 175 PTSALDPISAGKIEETL--LGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYI 247
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-245 |
2.56e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 134.78 E-value: 2.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITkvFQQGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERpTEGSVQVDGQ-ELTALSEKE---- 76
Cdd:PRK14258 8 IKVNNLS--FYYDTQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRvEFFNQNIYErrvn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 77 LTRARRQIGMIFQHFNLLaSRTVFGNVAL---------PLELDNTPQAEIKrrVTELLDLVglgdKHDSYPA--NLSGGQ 145
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLF-PMSVYDNVAYgvkivgwrpKLEIDDIVESALK--DADLWDEI----KHKIHKSalDLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISN-----GQLI 220
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLV 235
|
250 260
....*....|....*....|....*
gi 1447223793 221 EQDTVSEVFSHPKTPLAQQFIQSTL 245
Cdd:PRK14258 236 EFGLTKKIFNSPHDSRTREYVLSRL 260
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-227 |
2.76e-37 |
|
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: 141.63 E-value: 2.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITkvFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALsekELTRAR 81
Cdd:TIGR03797 452 IEVDRVT--FRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL---DVQAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLaSRTVFGNVA--LPLELDntpqaeikrRVTELLDLVGLGDKHDSYP-----------ANLSGGQKQR 148
Cdd:TIGR03797 527 RQLGVVLQNGRLM-SGSIFENIAggAPLTLD---------EAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQR 596
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKdinrRLGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSE 227
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNRTQAIVSESLE----RLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-234 |
3.45e-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: 3.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVF-----QQG------------NRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQ 63
Cdd:COG4586 1 IIEVENLSKTYrvyekEPGlkgalkglfrreYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 64 VDG----QEltalsEKELtraRRQIGMIFQH-------------FNLLAsrtvfgnvalplELDNTPQAEIKRRVTELLD 126
Cdd:COG4586 81 VLGyvpfKR-----RKEF---ARRIGVVFGQrsqlwwdlpaidsFRLLK------------AIYRIPDAEYKKRLDELVE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 127 LVGLGDKHDSyPA-NLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVK 205
Cdd:COG4586 141 LLDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIE 219
|
250 260 270
....*....|....*....|....*....|..
gi 1447223793 206 RICDCVAVISNGQLIEQDTVSEV---FSHPKT 234
Cdd:COG4586 220 ALCDRVIVIDHGRIIYDGSLEELkerFGPYKT 251
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-224 |
3.45e-37 |
|
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: 140.73 E-value: 3.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 13 QGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRcvnLLER---PTEGSVQVDGQELTALSEKELtraRRQIGMIFQ 89
Cdd:COG5265 368 DPERPI--LKGVSFEVPAGKTVAIVGPSGAGKSTLAR---LLFRfydVTSGRILIDGQDIRDVTQASL---RAAIGIVPQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 90 H---FNllasRTVFGNVALPlELDNTpQAEIKR--RVTELLDLV-GLGDKHDSYPA----NLSGGQKQRVAIARALASNP 159
Cdd:COG5265 440 DtvlFN----DTIAYNIAYG-RPDAS-EEEVEAaaRAAQIHDFIeSLPDGYDTRVGerglKLSGGEKQRVAIARTLLKNP 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDT 224
Cdd:COG5265 514 PILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGT 575
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-202 |
3.86e-37 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 134.06 E-value: 3.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSekeltrARRqiGMIFQHFNLLASRTV 99
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG------AER--GVVFQNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 100 FGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSI 179
Cdd:PRK11248 88 QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180
....*....|....*....|...
gi 1447223793 180 LELLKDINRRLGLTILLITHEMD 202
Cdd:PRK11248 168 QTLLLKLWQETGKQVLLITHDIE 190
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-258 |
1.60e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 133.21 E-value: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNR-SIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEK--ELT 78
Cdd:PRK13645 7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 RARRQIGMIFQ--HFNLLaSRTVFGNVAL-PLELDNTPQaEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIARA 154
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLF-QETIEKDIAFgPVNLGENKQ-EAYKKVPELLKLVQLPEDYvKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHpkt 234
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN--- 241
|
250 260
....*....|....*....|....
gi 1447223793 235 plaqQFIQSTLHLDIPDDYQARLK 258
Cdd:PRK13645 242 ----QELLTKIEIDPPKLYQLMYK 261
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-248 |
1.78e-36 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 134.08 E-value: 1.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKS-TLIRCVNLLERP--TEGSVQVDGQELTALSEKELTRAR-RQIGMIFQHfnlla 95
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKELNKLRaEQISMIFQD----- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 96 srtvfgnvalPLELDNtPQAEIKRRVTELLDLVGLGDKHDS----------------------YPANLSGGQKQRVAIAR 153
Cdd:PRK09473 106 ----------PMTSLN-PYMRVGEQLMEVLMLHKGMSKAEAfeesvrmldavkmpearkrmkmYPHEFSGGMRQRVMIAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPK 233
Cdd:PRK09473 175 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
|
250
....*....|....*
gi 1447223793 234 TPLAQQFIQSTLHLD 248
Cdd:PRK09473 255 HPYSIGLLNAVPRLD 269
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-228 |
2.42e-36 |
|
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: 131.11 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltRARRQIG------MIFQHFn 92
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE--RARAGIAyvpqgrEIFPRL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 93 llasrTVFGNvaLPLELDNTPQAEiKRRVTELLDLvglgdkhdsYPA----------NLSGGQKQRVAIARALASNPKVL 162
Cdd:TIGR03410 91 -----TVEEN--LLTGLAALPRRS-RKIPDEIYEL---------FPVlkemlgrrggDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 163 LCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEV 228
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-242 |
2.43e-36 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 137.53 E-value: 2.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKST----LIRCVNllerpTEGSVQVDGQELTALSEKELTRARRQIGMIFQHFN-- 92
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 93 LLASRTVFGNVALPLELdNTPQ---AEIKRRVTELLDLVGLG-DKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEAT 168
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRV-HQPTlsaAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 169 SALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQFIQ 242
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-231 |
6.24e-36 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 130.20 E-value: 6.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGN------------------RSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSV 62
Cdd:COG1134 4 MIEVENVSKSYRLYHepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 63 QVDGqELTALSEkeltrarrqIGMIFqHFNLlasrTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHD----SYp 138
Cdd:COG1134 84 EVNG-RVSALLE---------LGAGF-HPEL----TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDqpvkTY- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 139 anlSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQ 218
Cdd:COG1134 148 ---SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
250
....*....|...
gi 1447223793 219 LIEQDTVSEVFSH 231
Cdd:COG1134 224 LVMDGDPEEVIAA 236
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-219 |
7.80e-36 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 130.90 E-value: 7.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGnrsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLL---ERPTEGSVQVDGQELTALSE--K 75
Cdd:PRK09984 4 IIRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlaR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 76 ELTRARRQIGMIFQHFNLLASRTVFGNVALPlELDNTP---------QAEIKRRVTELLDLVGLGDKHDSYPANLSGGQK 146
Cdd:PRK09984 80 DIRKSRANTGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-231 |
1.03e-35 |
|
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: 136.38 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITkvFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLircVNLLER---PTEGSVQVDGQELTALSEKELt 78
Cdd:TIGR02203 331 VEFRNVT--FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTL---VNLIPRfyePDSGQILLDGHDLADYTLASL- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 raRRQIGMIFQHFNLLaSRTVFGNVALPlELDNTPQAEIKR--RVTELLDLV-----GLGDKHDSYPANLSGGQKQRVAI 151
Cdd:TIGR02203 405 --RRQVALVSQDVVLF-NDTIANNIAYG-RTEQADRAEIERalAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAI 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSEVFSH 231
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLAR 557
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
11-243 |
1.26e-35 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 131.79 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 11 FQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKS-TLIRCVNLLERP---TEGSVQVDGQELTALSEKEltraRRQI-- 84
Cdd:PRK11022 13 FGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKE----RRNLvg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 85 ---GMIFQH--FNLLASRTVFGNVALPLEL-DNTPQAEIKRRVTELLDLVGLGD---KHDSYPANLSGGQKQRVAIARAL 155
Cdd:PRK11022 89 aevAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTP 235
Cdd:PRK11022 169 ACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHP 248
|
....*...
gi 1447223793 236 LAQQFIQS 243
Cdd:PRK11022 249 YTQALLRA 256
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
2.38e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 129.72 E-value: 2.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNrsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEkeLTRA 80
Cdd:PRK13644 1 MIRLENVSYSYPDGT---PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNL-LASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK13644 76 RKLVGIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVkRICDCVAVISNGQLIEQDTVSEVFSHP 232
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-229 |
3.14e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 129.85 E-value: 3.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNR-SIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALS-EKELT 78
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 RARRQIGMIFQH-FNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIARALA 156
Cdd:PRK13643 81 PVRKKVGVVFQFpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVF 229
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-229 |
5.47e-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: 127.34 E-value: 5.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 15 NRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLER---PTEGSVQVDGQELTALSEKELtraRRQIGMIFQHf 91
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLI---NLLMRfydPQKGQILIDGIDIRDISRKSL---RSMIGVVLQD- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 92 NLLASRTVFGNVALPlelDNTPQAEikrRVTELLDLVGLGDKHDSYP-----------ANLSGGQKQRVAIARALASNPK 160
Cdd:cd03254 86 TFLFSGTIMENIRLG---RPNATDE---EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 161 VLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSEVF 229
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-214 |
1.51e-34 |
|
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: 132.41 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraRRQIGMIFQHFNLLASrTV 99
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---RDQIAWVPQHPFLFAG-TI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 100 FGNVALPlELDNTPqAEIKR--RVTELLDLV-----GLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
Cdd:TIGR02857 413 AENIRLA-RPDASD-AEIREalERAGLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1447223793 173 PATTRSILELLKDINRrlGLTILLITHEmDVVKRICDCVAVI 214
Cdd:TIGR02857 491 AETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-232 |
2.87e-34 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 126.26 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtrARRQIGMIFQHFNLLASRTV 99
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI--ARMGVVRTFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 100 FGN--VALPLELD--------NTP-----QAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLC 164
Cdd:PRK11300 98 IENllVAQHQQLKtglfsgllKTPafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 165 DEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHP 232
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-232 |
6.25e-34 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 127.68 E-value: 6.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLsNITKvfQQGNRSIQalnnVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKE-LTR 79
Cdd:PRK11144 1 MLEL-NFKQ--QLGDLCLT----VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIcLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 80 ARRQIGMIFQHFNLLASRTVFGNvaLPLELDNTPQAEIKRrVTELLdlvGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK11144 74 EKRRIGYVFQDARLFPHYKVRGN--LRYGMAKSMVAQFDK-IVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAP 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHP 232
Cdd:PRK11144 148 ELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-224 |
7.58e-34 |
|
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: 124.14 E-value: 7.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraRRQIGMIFQHfNLLASRTV 99
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL---RSRISIIPQD-PVLFSGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 100 FGNVAlPL------ELDNT-PQAEIKRRVTELLDlvGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
Cdd:cd03244 95 RSNLD-PFgeysdeELWQAlERVGLKEFVESLPG--GLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1447223793 173 PATTRSILELLKdiNRRLGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDT 224
Cdd:cd03244 172 PETDALIQKTIR--EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-247 |
1.41e-33 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 124.43 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 23 NVSLHVPAGQIYGVIGASGAGKStlIRCVNLLE------RPTEGSVQVDGQELTALSEKEltrarRQIGMIFQH----FN 92
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVAPCALRG-----RKIATIMQNprsaFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 93 LLasRTVFGNVALPLELDNTPQAEikRRVTELLDLVGLGDKH---DSYPANLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:PRK10418 94 PL--HTMHTHARETCLALGKPADD--ATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 170 ALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQFIQSTLHL 247
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAHLAL 247
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-228 |
2.67e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 123.65 E-value: 2.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFqqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtrA 80
Cdd:COG4604 1 MIEIKNVSKRY--GGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREL--A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRqIGMIFQHfNLLASR-TV-----FG-------NvalpleldntPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQ 147
Cdd:COG4604 75 KR-LAILRQE-NHINSRlTVrelvaFGrfpyskgR----------LTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSE 227
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEE 222
|
.
gi 1447223793 228 V 228
Cdd:COG4604 223 I 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-231 |
3.00e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 124.92 E-value: 3.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEkeltRARRQIGMIFQHFNLLASRTVF 100
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR----HARQRVGVVPQFDNLDPDFTVR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 101 GNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSIL 180
Cdd:PRK13537 99 ENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMW 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1447223793 181 ELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSH 231
Cdd:PRK13537 179 ERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-227 |
6.71e-33 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 121.74 E-value: 6.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqGNRSiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTalsEKELtrar 81
Cdd:TIGR03740 1 LETKNLSKRF--GKQT--AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT---RKDL---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKrrvtELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:TIGR03740 70 HKIGSLIESPPLYENLTARENLKVHTTLLGLPDSRID----EVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSE 227
Cdd:TIGR03740 146 LILDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-200 |
1.47e-32 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 124.37 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqGNRSIQalNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTalsekELTRAR 81
Cdd:PRK11000 4 VTLRNVTKAY--GDVVIS--KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-----DVPPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:PRK11000 75 RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHE 200
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-219 |
1.83e-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: 119.46 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSekelTRARRQIGMIF-----QHFNLL 94
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRS----PRDAIRAGIAYvpedrKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 95 ASRTVFGNVALPLELdntpqaeikrrvtelldlvglgdkhdsypanlSGGQKQRVAIARALASNPKVLLCDEATSALDPA 174
Cdd:cd03215 91 LDLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1447223793 175 TTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:cd03215 139 AKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-229 |
2.25e-32 |
|
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: 126.46 E-value: 2.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQqgnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLE--RPTEGSV----------------- 62
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 63 ------QVDGQELTA-------LSEKELTRARRQIGMIFQH-FNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLV 128
Cdd:TIGR03269 77 kvgepcPVCGGTLEPeevdfwnLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 129 GLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRIC 208
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|....
gi 1447223793 209 DCVAVISNGQLIEQ---DTVSEVF 229
Cdd:TIGR03269 237 DKAIWLENGEIKEEgtpDEVVAVF 260
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-251 |
7.96e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 120.59 E-value: 7.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEG-----SVQVDGQELtaLSEKELTRARRQIGMIFQHFNLLA 95
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 96 sRTVFGNVALPLELDN-TPQAEIKRRVTELLDLVGL----GDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSA 170
Cdd:PRK14271 115 -MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 171 LDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTPLAQQFIqSTLHLDIP 250
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV-AGLSGDVK 270
|
.
gi 1447223793 251 D 251
Cdd:PRK14271 271 D 271
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-220 |
2.78e-31 |
|
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: 117.31 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITkvFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraR 81
Cdd:cd03245 3 IEFRNVS--FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASrTVFGNVAL--PLELDntpqaeikRRVTELLDLVGLGDKHDSYP-----------ANLSGGQKQR 148
Cdd:cd03245 78 RNIGYVPQDVTLFYG-TLRDNITLgaPLADD--------ERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447223793 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKrICDCVAVISNGQLI 220
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-220 |
2.94e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 120.32 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKeltrAR 81
Cdd:PRK13536 42 IDLAGVSKSY--GDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL----AR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLI 220
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-199 |
5.85e-31 |
|
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: 117.49 E-value: 5.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITkvFQQGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEG-SVQVDGQELTALSEKELtr 79
Cdd:COG1119 3 LLELRNVT--VRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWEL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 80 aRRQIGMI--FQHFNLLASRTV--------FGNVALPLELDntpqAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRV 149
Cdd:COG1119 77 -RKRIGLVspALQLRFPRDETVldvvlsgfFDSIGLYREPT----DEQRERARELLELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1447223793 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITH 199
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-243 |
7.34e-31 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 117.58 E-value: 7.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGN-----RSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEK 75
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 76 elTRARRqIGMIFQH-FNLLASRTVFGNVA-LPLELDNTPQAEIK-RRVTELLDLVGLGDKHDSY-PANLSGGQKQRVAI 151
Cdd:PRK15112 84 --YRSQR-IRMIFQDpSTSLNPRQRISQILdFPLRLNTDLEPEQReKQIIETLRQVGLLPDHASYyPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSH 231
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
250
....*....|..
gi 1447223793 232 PKTPLAQQFIQS 243
Cdd:PRK15112 241 PLHELTKRLIAG 252
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-256 |
1.20e-30 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 121.17 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 4 LSNITKVFQqgnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRArrQ 83
Cdd:PRK11288 7 FDGIGKTFP----GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAA--G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 84 IGMIFQHFNLLASRTVFGNV---ALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 161 VLLCDEATSALdpaTTRSIlELLKDINRRL---GLTILLITHEMDVVKRICDCVAVISNGQLIEQ-DTVSEVfSHpktpl 236
Cdd:PRK11288 161 VIAFDEPTSSL---SAREI-EQLFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQV-DR----- 230
|
250 260
....*....|....*....|..
gi 1447223793 237 aQQFIQSTLHLDIPD--DYQAR 256
Cdd:PRK11288 231 -DQLVQAMVGREIGDiyGYRPR 251
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-228 |
1.23e-30 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 121.43 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQqgnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKelTRA 80
Cdd:PRK09700 5 YISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK--LAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNV---ALPLE----LDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIAR 153
Cdd:PRK09700 79 QLGIGIIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 154 ALASNPKVLLCDEATSALdpatTRSILELLKDINRRL---GLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEV 228
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSL----TNKEVDYLFLIMNQLrkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-271 |
1.44e-30 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 121.89 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKS-TLIRCVNLLERpTEGSVQVDGQ----------EL 69
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMllrrrsrqviEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 70 TALSEKELTRAR-RQIGMIFQH--FNLLASRTVFGNVALPLEL-DNTPQAEIKRRVTELLDLVGLGDKH---DSYPANLS 142
Cdd:PRK10261 91 SEQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQ 222
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 223 DTVSEVFSHPKTPLAQQFIQST-----------------LHLDIPDDYQARLKSTATADSVPMLRM 271
Cdd:PRK10261 251 GSVEQIFHAPQHPYTRALLAAVpqlgamkgldyprrfplISLEHPAKQEPPIEQDTVVDGEPILQV 316
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-220 |
1.65e-30 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 120.80 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 6 NITKVFQqgnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLeRPT---EGSVQVDGQELTALSEKELTRArr 82
Cdd:PRK13549 10 NITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNIRDTERA-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 83 QIGMIFQHFNLLASRTVFGNVALPLELdnTPQ-----AEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALAS 157
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEI--TPGgimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 158 NPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLI 220
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-232 |
1.90e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 121.75 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 17 SIQALNNVSLHVPAGQIYGVIGASGAGKSTlirCVNLLER---PTEGSVQVDGQELTALSEKELtraRRQIGMIFQHfNL 93
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNlyqPTGGQVLLDGVPLVQYDHHYL---HRQVALVGQE-PV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 94 LASRTVFGNVALPLelDNTPQAEIKRRVTELLDLVGLGDKHDSYPAN-------LSGGQKQRVAIARALASNPKVLLCDE 166
Cdd:TIGR00958 566 LFSGSVRENIAYGL--TDTPDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 167 ATSALDPATTRsileLLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSEVFSHP 232
Cdd:TIGR00958 644 ATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-227 |
2.12e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 121.22 E-value: 2.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 11 FQQGNRSiQALNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLER---PTEGSVQVDGQELTALSEKELtraRRQIGMI 87
Cdd:PRK13657 342 FSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLI---NLLQRvfdPQSGRILIDGTDIRTVTRASL---RRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 88 FQHFNLLAsRTVFGNVALPLElDNTPqAEIKR--RVTELLDLVGlgDKHDSYPAN-------LSGGQKQRVAIARALASN 158
Cdd:PRK13657 415 FQDAGLFN-RSIEDNIRVGRP-DATD-EEMRAaaERAQAHDFIE--RKPDGYDTVvgergrqLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 159 PKVLLCDEATSALDPATTRSILELLKDInrRLGLTILLITHEMDVVkRICDCVAVISNGQLIEQDTVSE 227
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTV-RNADRILVFDNGRVVESGSFDE 555
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-220 |
5.38e-30 |
|
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: 113.03 E-value: 5.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVN--LLERPTEGSVQVDGQELtalsekELTRARRQIGMIFQHFNLLASRT 98
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL------DKRSFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 99 VFGNVALpleldntpQAEIKrrvtelldlvglgdkhdsypaNLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:cd03213 99 VRETLMF--------AAKLR---------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1447223793 179 ILELLKDInRRLGLTILLITHE-MDVVKRICDCVAVISNGQLI 220
Cdd:cd03213 150 VMSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-251 |
6.49e-30 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 116.44 E-value: 6.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCV------NLleRPTEGSVQVDGQELTALSE 74
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdNW--RVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 75 KELTR-ARRQIGMIFQHFN--LLASRTVFGNValpleLDNTPQAEIK-----------RRVTELLDLVGLGDKHD---SY 137
Cdd:PRK15093 81 RERRKlVGHNVSMIFQEPQscLDPSERVGRQL-----MQNIPGWTYKgrwwqrfgwrkRRAIELLHRVGIKDHKDamrSF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 138 PANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNG 217
Cdd:PRK15093 156 PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCG 235
|
250 260 270
....*....|....*....|....*....|....
gi 1447223793 218 QLIEQDTVSEVFSHPKTPLAQQFIQStlhldIPD 251
Cdd:PRK15093 236 QTVETAPSKELVTTPHHPYTQALIRA-----IPD 264
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-219 |
7.40e-30 |
|
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: 113.72 E-value: 7.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITkvFQQGNRS-IQALNNVSLHVPAGQIYGVIGASGAGKSTlirCVNLLER---PTEGSVQVDGQELTALSEKEL 77
Cdd:cd03248 12 VKFQNVT--FAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENfyqPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 78 traRRQIGMIFQHfNLLASRTVFGNVALPL---ELDNTPQAEIKRRVTELLDLVGLGDKHDS--YPANLSGGQKQRVAIA 152
Cdd:cd03248 87 ---HSKVSLVGQE-PVLFARSLQDNIAYGLqscSFECVKEAAQKAHAHSFISELASGYDTEVgeKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447223793 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRiCDCVAVISNGQL 219
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-221 |
7.78e-30 |
|
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: 113.78 E-value: 7.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVF------------------QQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQ 63
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 64 VDGQ-----ELTALSEKELTrARRqigmifqhfnllasrtvfgNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYP 138
Cdd:cd03220 81 VRGRvssllGLGGGFNPELT-GRE-------------------NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 139 ANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQ 218
Cdd:cd03220 141 KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
...
gi 1447223793 219 LIE 221
Cdd:cd03220 220 IRF 222
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-246 |
1.52e-29 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 118.97 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITkvFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLircVNLLER---PTEGSVQVDGQELtalSEKELT 78
Cdd:PRK11176 342 IEFRNVT--FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTI---ANLLTRfydIDEGEILLDGHDL---RDYTLA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 RARRQIGMIFQHFNLLaSRTVFGNVALPLElDNTPQAEIKR--RVTELLDLV-----GLGDKHDSYPANLSGGQKQRVAI 151
Cdd:PRK11176 414 SLRNQVALVSQNVHLF-NDTIANNIAYART-EQYSREQIEEaaRMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAI 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRrlglTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSEVf 229
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALDELqkNR----TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAEL- 565
|
250
....*....|....*..
gi 1447223793 230 shpktpLAQQFIQSTLH 246
Cdd:PRK11176 566 ------LAQNGVYAQLH 576
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-230 |
1.75e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.57 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFqqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRa 80
Cdd:PRK11231 2 TLRTENLTVGY--GTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 rrQIGMIFQHFNLLASRTVFGNVAL---P-LELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:PRK11231 77 --RLALLPQHHLTPEGITVRELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFS 230
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-230 |
4.45e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 112.29 E-value: 4.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 6 NITKVFQqGNRSIQalnNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKEltRARRQIG 85
Cdd:PRK10895 8 NLAKAYK-GRRVVE---DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 86 MIFQHFNLLASRTVFGNVALPLEL-DNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLC 164
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 165 DEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFS 230
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-230 |
6.81e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 112.41 E-value: 6.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTaLSEKELTRARRQIGMIFQHfnllASRT 98
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQVATVFQD----PEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 99 VF-----GNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDP 173
Cdd:PRK13638 90 IFytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1447223793 174 ATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFS 230
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-220 |
1.11e-28 |
|
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: 115.69 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQqgnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIR--CVNLLERPTEGSVQVDGQELTALSEKELT 78
Cdd:TIGR02633 1 LLEMKGIVKTFG----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKilSGVYPHGTWDGEIYWSGSPLKASNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 RArrQIGMIFQHFNLLASRTVFGNVALPLEL----DNTPQAEIKRRVTELLDLVGLGDKHDSYP-ANLSGGQKQRVAIAR 153
Cdd:TIGR02633 77 RA--GIVIIHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447223793 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLI 220
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-211 |
1.15e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 110.57 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 11 FQQGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKeltRARRQIGMIFQH 90
Cdd:PRK10247 15 YLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---IYRQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 91 FNLLASrTVFGNVALPLELDNtpQAEIKRRVTELLDLVGLGDKHDSYPAN-LSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:PRK10247 90 PTLFGD-TVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1447223793 170 ALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCV 211
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-222 |
1.48e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 116.08 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITkvFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLER---PTEGSVQVDGQELTALSEKELt 78
Cdd:PRK11160 339 LTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL---QLLTRawdPQQGEILLNGQPIADYSEAAL- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 raRRQIGMIFQHFNLLaSRTVFGNVALPLeldntPQAeIKRRVTELLDLVGLGDKHDSYPA----------NLSGGQKQR 148
Cdd:PRK11160 413 --RQAISVVSQRVHLF-SATLRDNLLLAA-----PNA-SDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITH------EMDvvkRICdcvaVISNGQLIEQ 222
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHrltgleQFD---RIC----VMDNGQIIEQ 554
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
6-199 |
2.34e-28 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 109.67 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 6 NITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLERP--TEGSVQVDGQELtalsEKELTRARr 82
Cdd:cd03234 8 DVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNGQPR----KPDQFQKC- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 83 qIGMIFQHFNLLASRTVFGNV--ALPLELDN-TPQAEIKRRV-TELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASN 158
Cdd:cd03234 83 -VAYVRQDDILLPGLTVRETLtyTAILRLPRkSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1447223793 159 PKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITH 199
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIH 201
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-231 |
2.77e-28 |
|
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: 115.23 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRC-VNLLeRPTEGSVQVDGQELTALSEKELtra 80
Cdd:COG4618 331 LSVENLTVVPPGSKRPI--LRGVSFSLEPGEVLGVIGPSGSGKSTLARLlVGVW-PPTAGSVRLDGADLSQWDREEL--- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASrTVFGNVALPLELDntPQAeikrrVTELLDLVGLgdkHD---SYP-----------ANLSGGQK 146
Cdd:COG4618 405 GRHIGYLPQDVELFDG-TIAENIARFGDAD--PEK-----VVAAAKLAGV---HEmilRLPdgydtrigeggARLSGGQR 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVkRICDCVAVISNGQLIEQDTVS 226
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLL-AAVDKLLVLRDGRVQAFGPRD 551
|
....*
gi 1447223793 227 EVFSH 231
Cdd:COG4618 552 EVLAR 556
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-228 |
6.87e-28 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 109.49 E-value: 6.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRarrQIGMIFQHFNLLASRTVF 100
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR---KVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 101 GNVALplelDNTP--------QAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
Cdd:PRK10575 104 ELVAI----GRYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 173 PATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEV 228
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-227 |
1.28e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 113.40 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLE--RPTEGSVQVDGQELTALsekELTRARRQIGMIFQHFNLLAS 96
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLL---NALLgfLPYQGSLKINGIELREL---DPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 97 rTVFGNVALpleldNTPQAEiKRRVTELLDLVGLGDKHDSYP-----------ANLSGGQKQRVAIARALASNPKVLLCD 165
Cdd:PRK11174 438 -TLRDNVLL-----GNPDAS-DEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447223793 166 EATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSE 227
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAE 569
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-219 |
3.23e-27 |
|
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: 112.80 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 4 LSNITKVFQQGNRSiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELtalsEKELTRARRQ 83
Cdd:TIGR01257 931 VKNLVKIFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 84 IGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLL 163
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 164 CDEATSALDPATTRSILELLkdINRRLGLTILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-199 |
5.17e-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: 111.30 E-value: 5.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraRRQIGMIFQHFNLLASrTV 99
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---RRRVSVCAQDAHLFDT-TV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 100 FGNVALPLElDNTPQAeikrrVTELLDLVGLGDKHDSYP-----------ANLSGGQKQRVAIARALASNPKVLLCDEAT 168
Cdd:TIGR02868 426 RENLRLARP-DATDEE-----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|.
gi 1447223793 169 SALDPATTRSILELLKDINRrlGLTILLITH 199
Cdd:TIGR02868 500 EHLDAETADELLEDLLAALS--GRTVVLITH 528
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-245 |
1.61e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 105.78 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 6 NITKVFqqGNRsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQ-----ELTALSEKELTR- 79
Cdd:PRK11701 11 GLTKLY--GPR--KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 80 ARRQIGMIFQHF--NLLASRTVFGNVALPL-ELDNTPQAEIKRRVTELLDLVGLG-DKHDSYPANLSGGQKQRVAIARAL 155
Cdd:PRK11701 87 LRTEWGFVHQHPrdGLRMQVSAGGNIGERLmAVGARHYGDIRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQIARNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKTP 235
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHP 246
|
250
....*....|
gi 1447223793 236 LAQQFIQSTL 245
Cdd:PRK11701 247 YTQLLVSSVL 256
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-224 |
2.04e-26 |
|
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: 104.03 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQEltaLSEKELTRARRQIGMIFQHFNLLaSRT 98
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGID---ISTIPLEDLRSSLTIIPQDPTLF-SGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 99 VFGNVALPLELDNtpqaeikRRVTELLDLVGLGDkhdsypaNLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT--- 175
Cdd:cd03369 98 IRSNLDPFDEYSD-------EEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATdal 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1447223793 176 -TRSILELLKDInrrlglTILLITHEMDVVKRiCDCVAVISNGQLIEQDT 224
Cdd:cd03369 164 iQKTIREEFTNS------TILTIAHRLRTIID-YDKILVMDAGEVKEYDH 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-220 |
5.54e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.23 E-value: 5.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 4 LSNITKVFqqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQEltalsekeltrarrQ 83
Cdd:COG0488 1 LENLSKSF--GGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL--------------R 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 84 IGMIFQHFNLLASRTVFGNV--------ALPLELD------NTPQAEIKR--RVTELLD--------------LVGLG-- 131
Cdd:COG0488 63 IGYLPQEPPLDDDLTVLDTVldgdaelrALEAELEeleaklAEPDEDLERlaELQEEFEalggweaearaeeiLSGLGfp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 132 -DKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDpATTRSILE-LLKDINRrlglTILLITHE---MD-VVK 205
Cdd:COG0488 143 eEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-LESIEWLEeFLKNYPG----TVLVVSHDryfLDrVAT 217
|
250
....*....|....*
gi 1447223793 206 RICDcvavISNGQLI 220
Cdd:COG0488 218 RILE----LDRGKLT 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-222 |
7.17e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 101.62 E-value: 7.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITkvFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRcvnLLER---PTEGSVQVDGQELTALsEKELt 78
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQ---LLTGdlkPQQGEITLDGVPVSDL-EKAL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 raRRQIGMIFQHFNLLAsrtvfgnvalpleldntpqaeikrrvTELLDLVGlgdkhdsypANLSGGQKQRVAIARALASN 158
Cdd:cd03247 74 --SSLISVLNQRPYLFD--------------------------TTLRNNLG---------RRFSGGERQRLALARILLQD 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 159 PKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRIcDCVAVISNGQLIEQ 222
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-217 |
1.74e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 105.69 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFqqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTra 80
Cdd:PRK09536 3 MIDVSDLSVEF--GDTTV--LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 rRQIGMIFQH----FNLLASRTVfgnvalplELDNTPQ-------AEIKRR-VTELLDLVGLGDKHDSYPANLSGGQKQR 148
Cdd:PRK09536 77 -RRVASVPQDtslsFEFDVRQVV--------EMGRTPHrsrfdtwTETDRAaVERAMERTGVAQFADRPVTSLSGGERQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447223793 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLkdinRRL---GLTILLITHEMDVVKRICDCVAVISNG 217
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELV----RRLvddGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-220 |
8.32e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.72 E-value: 8.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 14 GNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSekelTRARRQIGMIF----- 88
Cdd:COG3845 267 DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS----PRERRRLGVAYipedr 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 89 QHFNLLASRTVFGNVALpLELDNTP--------QAEIKRRVTELLDlvglgdKHD------SYPA-NLSGGQKQRVAIAR 153
Cdd:COG3845 343 LGRGLVPDMSVAENLIL-GRYRRPPfsrggfldRKAIRAFAEELIE------EFDvrtpgpDTPArSLSGGNQQKVILAR 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447223793 154 ALASNPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQLI 220
Cdd:COG3845 416 ELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-224 |
1.20e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 99.95 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQgnrsIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTra 80
Cdd:PRK11614 5 MLSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNLLASRTVFGNVAL-PLELDNTPQAEIKRRVTELLDLvgLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEENLAMgGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447223793 160 KVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDT 224
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-230 |
3.28e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 99.68 E-value: 3.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 23 NVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRarrQIGMIFQHFNLLASRTVFGN 102
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR---RIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 103 VA---LPLE-LDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:PRK10253 102 VArgrYPHQpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1447223793 179 ILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFS 230
Cdd:PRK10253 182 LLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-205 |
4.28e-24 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 98.11 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCV--NLLERPTEGSVQVDGQELTalsekeltrarrqigmifqhfnllasrt 98
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFG---------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 99 vfGNVALpleLDNTPQAEIKRRVTELLDLVGLGDKHdSY---PANLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
Cdd:COG2401 98 --REASL---IDAIGRKGDFKDAVELLNAVGLSDAV-LWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190
....*....|....*....|....*....|
gi 1447223793 176 TRSILELLKDINRRLGLTILLITHEMDVVK 205
Cdd:COG2401 172 AKRVARNLQKLARRAGITLVVATHHYDVID 201
|
|
| NIL |
smart00930 |
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ... |
267-340 |
5.88e-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: 5.88e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 267 PMLRMEFTGHSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGTQEDTQAAIAWLQEHHVKVEVL 340
Cdd:smart00930 3 RLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGDEEDIEAALAYLREQGVEVEVL 76
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-221 |
5.93e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.45 E-value: 5.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFqqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVdGQELtalsekeltra 80
Cdd:COG0488 315 VLELEGLSKSY--GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 rrQIGMIFQHFNLL-ASRTVFGNVAlpleldntpQAEIKRRVTELLDLVGL----GDKHDSYPANLSGGQKQRVAIARAL 155
Cdd:COG0488 379 --KIGYFDQHQEELdPDKTVLDELR---------DGAPGGTEQEVRGYLGRflfsGDDAFKPVGVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 156 ASNPKVLLCDEATSALDPATTRSILELLKDINrrlGlTILLITHEMDVVKRICDCVAVISNGQLIE 221
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-227 |
6.00e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 102.00 E-value: 6.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQqgnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:PRK10762 4 LLQLKGIDKAFP----GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 rrQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLD--LVGLGDKHDSYP--ANLSGGQKQRVAIARALA 156
Cdd:PRK10762 80 --GIGIIHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADklLARLNLRFSSDKlvGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447223793 157 SNPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSE 227
Cdd:PRK10762 158 FESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVAD 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-209 |
7.45e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 102.51 E-value: 7.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVN-LLErPTEGSVQVDGQELTAlseKELtRARRQIGMIFQHFNLLASRT 98
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTgLLP-ASEGEAWLFGQPVDA---GDI-ATRRRVGYMSQAFSLYGELT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 99 VFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180 190
....*....|....*....|....*....|.
gi 1447223793 179 ILELLKDINRRLGLTILLITHEMDVVKRiCD 209
Cdd:NF033858 436 FWRLLIELSREDGVTIFISTHFMNEAER-CD 465
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-227 |
1.27e-23 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 101.34 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 4 LSNITKVFQqgnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRArrQ 83
Cdd:PRK10982 1 MSNISKSFP----GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALEN--G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 84 IGMIFQHFNLLASRTVFGNVAL---PLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK10982 75 ISMVHQELNLVLQRSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 161 VLLCDEATSALdpaTTRSILELLKDIN--RRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSE 227
Cdd:PRK10982 155 IVIMDEPTSSL---TEKEVNHLFTIIRklKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAG 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-224 |
1.53e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 101.74 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraRRQIGMIFQHfNLLASRTV 99
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL---RQFINYLPQE-PYIFSGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 100 FGNVALPLElDNTPQAEIKR--RVTELLDLV-----GLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
Cdd:TIGR01193 565 LENLLLGAK-ENVSQDEIWAacEIAEIKDDIenmplGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1447223793 173 PATTRSILELLKDINRRlglTILLITHEMDVVKRIcDCVAVISNGQLIEQDT 224
Cdd:TIGR01193 644 TITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGS 691
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-199 |
3.34e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.27 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQV-DGQELTALSEkeltRARRQIGmifqhfNLlasRTV 99
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPQ----RPYLPLG------TL---REA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 100 fgnVALPLELDNTPQAEIKrrvtELLDLVGLG------DKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDP 173
Cdd:COG4178 446 ---LLYPATAEAFSDAELR----EALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180
....*....|....*....|....*.
gi 1447223793 174 ATTRSILELLKDinRRLGLTILLITH 199
Cdd:COG4178 519 ENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-224 |
4.73e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 99.79 E-value: 4.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNRsiqALNNVSLHVPAGQIYGVIGASGAGKSTLircVNLLE---RPTEGSVQVDGQELTALSEKELt 78
Cdd:PRK10790 341 IDIDNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTL---ASLLMgyyPLTEGEIRLDGRPLSSLSHSVL- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 raRRQIGMIFQHFNLLASrTVFGNVALPLELDntpqaeiKRRVTELLDLVGLGDKHDSYPA-----------NLSGGQKQ 147
Cdd:PRK10790 414 --RQGVAMVQQDPVVLAD-TFLANVTLGRDIS-------EEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447223793 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRiCDCVAVISNGQLIEQDT 224
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGT 557
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-227 |
9.72e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 9.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA--------RRQIGmifqhf 91
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAgiayvpedRKGEG------ 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 92 nLLASRTVFGNVALPLeLDNT------PQAEIKRRVTELLDLVGLGDKHDSYPA-NLSGGQKQRVAIARALASNPKVLLC 164
Cdd:COG1129 341 -LVLDLSIRENITLAS-LDRLsrggllDRRRERALAEEYIKRLRIKTPSPEQPVgNLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 165 DEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQL---IEQDTVSE 227
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIvgeLDREEATE 483
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-218 |
1.07e-22 |
|
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: 94.07 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVnLLE-RPTEGSVQVDGQelTALSEkeltrarrQIGMIFqhfnllaSRT 98
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGElEKLSGSVSVPGS--IAYVS--------QEPWIQ-------NGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 99 VFGNVALPLELDntpqaeiKRRVTELLDLVGLGDKHDSYPA-----------NLSGGQKQRVAIARALASNPKVLLCDEA 167
Cdd:cd03250 82 IRENILFGKPFD-------EERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 168 TSALDPATTRSILE--LLKDInrRLGLTILLITHEMDVVKRiCDCVAVISNGQ 218
Cdd:cd03250 155 LSAVDAHVGRHIFEncILGLL--LNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-230 |
4.32e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 93.37 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLerPTEGSVQVDGQELTALSEKELTRARrqiGMIFQHFNLLASRTV 99
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILLNGRPLSDWSAAELARHR---AYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 100 FGNVALPLElDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARAL-----ASNP--KVLLCDEATSALD 172
Cdd:COG4138 87 FQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 173 PATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFS 230
Cdd:COG4138 166 VAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-227 |
1.02e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 95.63 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 6 NITKVFQqgnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLE--RPT---EGSVQVDGQELT--ALSEKElt 78
Cdd:NF040905 6 GITKTFP----GVKALDDVNLSVREGEIHALCGENGAGKSTLM---KVLSgvYPHgsyEGEILFDGEVCRfkDIRDSE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 raRRQIGMIFQHFNLLASRTVFGNVALPLEldntpQA--------EIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVA 150
Cdd:NF040905 77 --ALGIVIIHQELALIPYLSIAENIFLGNE-----RAkrgvidwnETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQLIE-----QDTV 225
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIEtldcrADEV 228
|
..
gi 1447223793 226 SE 227
Cdd:NF040905 229 TE 230
|
|
| NIL |
pfam09383 |
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ... |
267-339 |
2.05e-21 |
|
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: 86.35 E-value: 2.05e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 267 PMLRMEFTGHSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGTQEDTQAAIAWLQEHHVKVEV 339
Cdd:pfam09383 1 RLVRLTFPGESADEPVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELPGDPEQIEAALAYLREQGVEVEV 73
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-200 |
1.63e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.42 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLERPTEGSVQVDGQEL---TALSEKELtraRRQIGMIFQHFNLLASR 97
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGSGSVLlngMPIDAKEM---RAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 98 TVFGNVALPLEL---DNTPQAEIKRRVTELLDLVGLGDKHDS------YPANLSGGQKQRVAIARALASNPKVLLCDEAT 168
Cdd:TIGR00955 115 TVREHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190
....*....|....*....|....*....|..
gi 1447223793 169 SALDPATTRSILELLKDINRRlGLTILLITHE 200
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQ 225
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-221 |
2.12e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 87.58 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCV--NLLERPTEGSVQVDGQELTALSEKEltRARRQIGMIFQHfnllasrt 98
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE--RARLGIFLAFQY-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 99 vfgnvalPLELDNTpqaeikrRVTELLDLVGLGdkhdsypanLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:cd03217 86 -------PPEIPGV-------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1447223793 179 ILELLKDInRRLGLTILLITHEMDVVKRI-CDCVAVISNGQLIE 221
Cdd:cd03217 143 VAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-218 |
2.29e-20 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 85.96 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDgqeltalsekeltrar 81
Cdd:cd03221 1 IELENLSKTY--GGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 rqigmifqhfnllaSRTVFGnvalpleldntpqaeikrrvtelldlvglgdkhdsYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03221 61 --------------STVKIG-----------------------------------YFEQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDINRrlglTILLITHEMDVVKRICDCVAVISNGQ 218
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-214 |
3.33e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.79 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNrsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRAR 81
Cdd:PRK15056 7 IVVNDVTVTWRNGH---TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:PRK15056 84 PQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 162 LLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVI 214
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-240 |
4.26e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 88.07 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 24 VSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLerPTEGSVQVDGQELTALSEKELTRARrqiGMIFQHFNLLASRTVFGN 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMaGLL--PGSGSIQFAGQPLEAWSAAELARHR---AYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 103 VALPLElDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARAL-----ASNP--KVLLCDEATSALDPAT 175
Cdd:PRK03695 90 LTLHQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447223793 176 TRSILELLKDINrRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPKtpLAQQF 240
Cdd:PRK03695 169 QAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN--LAQVF 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-217 |
6.12e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.50 E-value: 6.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQqgnrSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEkelTRA 80
Cdd:PRK15439 11 LLCARSISKQYS----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP---AKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 rRQIG--MIFQHFNLLASRTVFGNVALPLeldnTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASN 158
Cdd:PRK15439 84 -HQLGiyLVPQEPLLFPNLSVKENILFGL----PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 159 PKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNG 217
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-199 |
2.52e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 14 GNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQEltalseKELTRARRQIGMIfQHFNL 93
Cdd:PRK13539 13 GGRVL--FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD------IDDPDVAEACHYL-GHRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 94 L-ASRTVFGNVALPLELDNTPQAEIkrrvTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
Cdd:PRK13539 84 MkPALTVAENLEFWAAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....*....
gi 1447223793 173 PATTRSILELlkdINRRL--GLTILLITH 199
Cdd:PRK13539 160 AAAVALFAEL---IRAHLaqGGIVIAATH 185
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-200 |
1.33e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 82.69 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELtalsEKELTRARRQIGMIFQHFNLLASRTVF 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 101 GNVALPLELDNTPQAeikrrVTELLDLVGLGDKHDsYPAN-LSGGQKQRVAIARALASNPKVLLCDEATSALDpatTRSI 179
Cdd:PRK13540 93 ENCLYDIHFSPGAVG-----ITELCRLFSLEHLID-YPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELSL 163
|
170 180
....*....|....*....|...
gi 1447223793 180 LELLKDI--NRRLGLTILLITHE 200
Cdd:PRK13540 164 LTIITKIqeHRAKGGAVLLTSHQ 186
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-204 |
2.80e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.85 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFqqGNRsiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQeltalsekeltra 80
Cdd:PRK09544 4 LVSLENVSVSF--GQR--RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 rRQIGMIFQHFNLLASrtvfgnvaLPLELD-------NTPQAEIkrrvTELLDLVGLGDKHDSYPANLSGGQKQRVAIAR 153
Cdd:PRK09544 67 -LRIGYVPQKLYLDTT--------LPLTVNrflrlrpGTKKEDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLAR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1447223793 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVV 204
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-231 |
7.82e-18 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 84.17 E-value: 7.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNRSIQ----------------ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVD 65
Cdd:PRK13545 5 VKFEHVTKKYKMYNKPFDklkdlffrskdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 66 GQ-ELTALSEkeltrarrqigmifqhfNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGG 144
Cdd:PRK13545 85 GSaALIAISS-----------------GLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDT 224
Cdd:PRK13545 148 MKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGD 226
|
....*..
gi 1447223793 225 VSEVFSH 231
Cdd:PRK13545 227 IKEVVDH 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-219 |
1.83e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.18 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 23 NVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSekelTRARRQIGMIF-----QHFNLLASR 97
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS----TAQRLARGLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 98 TVFGNVA------LPLELDNTPQAEIKRRVTELLdlvGLGDKHDSYPA-NLSGGQKQRVAIARALASNPKVLLCDEATSA 170
Cdd:PRK15439 357 PLAWNVCalthnrRGFWIKPARENAVLERYRRAL---NIKFNHAEQAArTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1447223793 171 LDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-199 |
3.66e-17 |
|
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: 78.55 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEkELTRARRQIGmifqHFNLLASR-T 98
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLG----HLPGLKPElS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 99 VFGNVALPLELDNTPQaeikRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQ----RTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|.
gi 1447223793 179 ILELLKDINRRLGLtILLITH 199
Cdd:TIGR01189 166 LAGLLRAHLARGGI-VLLTTH 185
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-232 |
4.44e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 82.07 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLERP---TEGSVQVDGQELTALsekELTRARRQIGMIFQHfNLLAS 96
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLL---SLIQRHfdvSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQT-PFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 97 RTVFGNVAL--PleldNTPQAEIKRrVTELL----DLVGLGDKHDSYPAN----LSGGQKQRVAIARALASNPKVLLCDE 166
Cdd:PRK10789 403 DTVANNIALgrP----DATQQEIEH-VARLAsvhdDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 167 ATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSEVFSHP 232
Cdd:PRK10789 478 ALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-232 |
5.37e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 82.38 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 3 KLSNITKV------FQQGNRS-IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQEltALSEK 75
Cdd:PTZ00265 376 KLKDIKKIqfknvrFHYDTRKdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 76 ELTRARRQIGMIFQHfNLLASRTVFGNVALPL--------------ELDNTPQAEIKRRV-------------------T 122
Cdd:PTZ00265 454 NLKWWRSKIGVVSQD-PLLFSNSIKNNIKYSLyslkdlealsnyynEDGNDSQENKNKRNscrakcagdlndmsnttdsN 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 123 ELL------------------------DLV-GLGDKHD----SYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDp 173
Cdd:PTZ00265 533 ELIemrknyqtikdsevvdvskkvlihDFVsALPDKYEtlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD- 611
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 174 atTRSILELLKDINRRLG----LTIlLITHEMDVVkRICDCVAVISNGQLIEQDTVSEVFSHP 232
Cdd:PTZ00265 612 --NKSEYLVQKTINNLKGnenrITI-IIAHRLSTI-RYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
60-216 |
2.95e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.07 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 60 GSVQVDGQELTALSEKELtrarRQIGMIFQHFNLLASRTVFGNVALPLEldNTPQAEIKR-----RVTELLDlvGLGDKH 134
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDL----RNLFSIVSQEPMLFNMSIYENIKFGKE--DATREDVKRackfaAIDEFIE--SLPNKY 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 135 DS----YPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDC 210
Cdd:PTZ00265 1349 DTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDK 1427
|
....*.
gi 1447223793 211 VAVISN 216
Cdd:PTZ00265 1428 IVVFNN 1433
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-244 |
3.75e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 79.63 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSekeLTRARRQIGMIFQHfNLLASRTVF 100
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRRVLSIIPQS-PVLFSGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 101 GNVALPLELDNTPQAEIKRRvTELLDLV-----GLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
Cdd:PLN03232 1328 FNIDPFSEHNDADLWEALER-AHIKDVIdrnpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 176 TRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSEVFSHPKTPLAqQFIQST 244
Cdd:PLN03232 1407 DSLIQRTIREEFK--SCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFF-RMVHST 1471
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-199 |
5.58e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 75.22 E-value: 5.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELtALSEKELTRARRQIGmifqHFNLLASR-TV 99
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLG----HAPGIKTTlSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 100 FGNVALPLELDNTPQAEikrrvtELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSI 179
Cdd:cd03231 91 LENLRFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|
gi 1447223793 180 LELLKDINRRLGLtILLITH 199
Cdd:cd03231 165 AEAMAGHCARGGM-VVLTTH 183
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-241 |
5.89e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.01 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTalSEKELTRARRQIGMIFQHF--NLLAS 96
Cdd:NF033858 15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAVCPRIAYMPQGLgkNLYPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 97 RTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSyPA-NLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
Cdd:NF033858 93 LSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADR-PAgKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 176 TRSILELLKDI-NRRLGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSEVFSHPKTP-LAQQFI 241
Cdd:NF033858 172 RRQFWELIDRIrAERPGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTGADtLEAAFI 238
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
20-222 |
6.70e-16 |
|
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: 78.46 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraRRQIGMIFQHFNLlasrtv 99
Cdd:TIGR01194 357 ALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDY---RDLFSAIFADFHL------ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 100 FGNVALPLELD--NTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTR 177
Cdd:TIGR01194 428 FDDLIGPDEGEhaSLDNAQQYLQRLEIADKVKIEDGGFSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFKR 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1447223793 178 SIL-ELLKDINRRlGLTILLITHEmDVVKRICDCVAVISNGQLIEQ 222
Cdd:TIGR01194 508 FFYeELLPDLKRQ-GKTIIIISHD-DQYFELADQIIKLAAGCIVKD 551
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-227 |
7.93e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.29 E-value: 7.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 10 VFQQGN---RSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKE--------LT 78
Cdd:PRK09700 265 VFEVRNvtsRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkkgmayIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 RARRQIGMiFQHF----NLLASRTVF-----GNVALPLELDNTPQAEIKRrvtELLDLvglgdKHDSYPAN---LSGGQK 146
Cdd:PRK09700 345 ESRRDNGF-FPNFsiaqNMAISRSLKdggykGAMGLFHEVDEQRTAENQR---ELLAL-----KCHSVNQNiteLSGGNQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIE----Q 222
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQiltnR 494
|
....*
gi 1447223793 223 DTVSE 227
Cdd:PRK09700 495 DDMSE 499
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-252 |
1.49e-15 |
|
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: 78.13 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQqgNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQE-LTALSEkeltr 79
Cdd:TIGR01257 1937 ILRLNELTKVYS--GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISD----- 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 80 ARRQIGMIFQHF---NLLASRTvfgNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:TIGR01257 2010 VHQNMGYCPQFDaidDLLTGRE---HLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVsevfSHPKTPL 236
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI----QHLKSKF 2161
|
250
....*....|....*.
gi 1447223793 237 AQQFIqSTLHLDIPDD 252
Cdd:TIGR01257 2162 GDGYI-VTMKIKSPKD 2176
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-199 |
1.76e-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: 72.96 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQEltalsekeltrarrqiGMIFqhfnlLASRTVF 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----------------DLLF-----LPQRPYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 101 GNVALpleldntpqaeikrRvtELLdlvglgdkhdSYP--ANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:cd03223 76 PLGTL--------------R--EQL----------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180
....*....|....*....|.
gi 1447223793 179 ILELLKDinrrLGLTILLITH 199
Cdd:cd03223 130 LYQLLKE----LGITVISVGH 146
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-242 |
2.74e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.09 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVnLLERPT--EGSVQVDGqeltalsekelTRAR-RQIGMIFqhfnllaSR 97
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAM-LGELPPrsDASVVIRG-----------TVAYvPQVSWIF-------NA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 98 TVFGNVALPLELDnTPQAEIKRRVTEL---LDLVGLGDKHD--SYPANLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
Cdd:PLN03130 694 TVRDNILFGSPFD-PERYERAIDVTALqhdLDLLPGGDLTEigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447223793 173 PATTRSILEllKDINRRL-GLTILLITHEMDVVKRIcDCVAVISNGQLIEQDTVSEVFSHpkTPLAQQFIQ 242
Cdd:PLN03130 773 AHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN--GPLFQKLME 838
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-220 |
3.50e-15 |
|
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: 73.07 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPT---EGSVQVDGQEltalSEKELT 78
Cdd:cd03233 4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP----YKEFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 RARRQIGMIFQHFNLLASRTVFgnvalpleldntpqaeikrrvtELLDLVgLGDKHDSYPANLSGGQKQRVAIARALASN 158
Cdd:cd03233 80 KYPGEIIYVSEEDVHFPTLTVR----------------------ETLDFA-LRCKGNEFVRGISGGERKRVSIAEALVSR 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447223793 159 PKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHE-----MDVVKRICdcvaVISNGQLI 220
Cdd:cd03233 137 ASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQasdeiYDLFDKVL----VLYEGRQI 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-184 |
1.13e-14 |
|
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: 75.33 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 4 LSNITKVFQQGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRC-VNLLErpTEGSVQVDGQELTALSekeLTRARR 82
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSAlLRLLS--TEGEIQIDGVSWNSVT---LQTWRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 83 QIGMIFQHFNLLaSRTVFGNvalpleLDNTPQ---AEIKRRVTElldlVGLGDKHDSYPANL-----------SGGQKQR 148
Cdd:TIGR01271 1293 AFGVIPQKVFIF-SGTFRKN------LDPYEQwsdEEIWKVAEE----VGLKSVIEQFPDKLdfvlvdggyvlSNGHKQL 1361
|
170 180 190
....*....|....*....|....*....|....*.
gi 1447223793 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLK 184
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLK 1397
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-219 |
1.41e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.56 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 24 VSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA--------RRQIGMIFQH----- 90
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgimlcpedRKAEGIIPVHsvadn 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 91 FNLLASR--TVFGNValpleLDNTPQAEIKRRVTELLDLVGLGDKHDSypANLSGGQKQRVAIARALASNPKVLLCDEAT 168
Cdd:PRK11288 352 INISARRhhLRAGCL-----INNRWEAENADRFIRSLNIKTPSREQLI--MNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1447223793 169 SALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-219 |
2.66e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.04 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRcvnllerptegsvqvdgqelTALSEKELTRAR----RQIGMIFQHFNLLAS 96
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQ--------------------SLLSQFEISEGRvwaeRSIAYVPQQAWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 97 rTVFGNValpLELDNTPQAEIKR--RVTEL-LDLVGLGDKHDS----YPANLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:PTZ00243 736 -TVRGNI---LFFDEEDAARLADavRVSQLeADLAQLGGGLETeigeKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1447223793 170 ALDPATTRSILELLKdINRRLGLTILLITHEMDVVKRiCDCVAVISNGQL 219
Cdd:PTZ00243 812 ALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRV 859
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-252 |
2.73e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.78 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 16 RSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIR------CVNLLER--PTEGSVQVDGQELTALSEKELTRARRQIGMi 87
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKalagdlTGGGAPRgaRVTGDVTLNGEPLAAIDAPRLARLRAVLPQ- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 88 fqhfnllASRTVFGNVALPL-ELDNTPQA-----------EIKRRVTELLDLVGLgDKHDSypANLSGGQKQRVAIARAL 155
Cdd:PRK13547 91 -------AAQPAFAFSAREIvLLGRYPHArragalthrdgEIAWQALALAGATAL-VGRDV--TTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 156 A---------SNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVS 226
Cdd:PRK13547 161 AqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250 260
....*....|....*....|....*.
gi 1447223793 227 EVFShpKTPLAQQFIQSTLHLDIPDD 252
Cdd:PRK13547 241 DVLT--PAHIARCYGFAVRLVDAGDG 264
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-232 |
2.81e-14 |
|
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: 74.21 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRARRQIGMIFQH-FNLLASRTV 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKaLNEKYYQQV 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 100 FGNVALPLELDNTPQAeikrrvtellDLVGLGDKHdsypANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSI 179
Cdd:TIGR00957 734 LEACALLPDLEILPSG----------DRTEIGEKG----VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 180 LE-------LLKDINRrlgltiLLITHEMDVVKRIcDCVAVISNGQlieqdtVSEVFSHP 232
Cdd:TIGR00957 800 FEhvigpegVLKNKTR------ILVTHGISYLPQV-DVIIVMSGGK------ISEMGSYQ 846
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-230 |
3.55e-14 |
|
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: 73.83 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraRRQIGMIFQHFNLLASrtvf 100
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL---RFKITIIPQDPVLFSG---- 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 101 gnvALPLELDNTPQAEiKRRVTELLDLVGLGDKHDSYPA-----------NLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:TIGR00957 1375 ---SLRMNLDPFSQYS-DEEVWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447223793 170 ALDPATTRSILELLKdiNRRLGLTILLITHEMDVVKRICDcVAVISNGQLIEQDTVSEVFS 230
Cdd:TIGR00957 1451 AVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTR-VIVLDKGEVAEFGAPSNLLQ 1508
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-219 |
7.97e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.96 E-value: 7.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLERpTEGSVQVDGQELTALSEKE--------LTRARRQIGMIF--- 88
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPR-TSGYVTLDGHEVVTRSPQDglangivyISEDRKRDGLVLgms 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 89 --QHFNLLASRTvFGNVALPLELDNTPQAeikrrVTELLDLVGLGD-KHDSYPANLSGGQKQRVAIARALASNPKVLLCD 165
Cdd:PRK10762 347 vkENMSLTALRY-FSRAGGSLKHADEQQA-----VSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 166 EATSALDPATTRSILELlkdINR--RLGLTILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQL---INQfkAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
17-226 |
8.64e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.06 E-value: 8.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 17 SIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCvnLLERP----TEGSVQVDGQELTALSEKEltRARRQIGMIFQH-- 90
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKV--IAGHPaykiLEGDILFKGESILDLEPEE--RAHLGIFLAFQYpi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 91 ---------FNLLA--SRTVFGNvaLPlELDNTPQAEIkrrVTELLDLVGLGDKHDSYPAN--LSGGQKQRVAIARALAS 157
Cdd:CHL00131 95 eipgvsnadFLRLAynSKRKFQG--LP-ELDPLEFLEI---INEKLKLVGMDPSFLSRNVNegFSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447223793 158 NPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHE---MDVVKRicDCVAVISNGQLIEQDTVS 226
Cdd:CHL00131 169 DSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYqrlLDYIKP--DYVHVMQNGKIIKTGDAE 237
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-201 |
1.03e-13 |
|
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: 69.28 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 18 IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQ-ELTALSEKELTRARRQIGMIFQHFNLLAS 96
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnESEPSFEATRSRNRYSVAYAAQKPWLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 97 rTVFGNVALpleldNTP-QAEIKRRVTEL------LDLVGLGDKHD--SYPANLSGGQKQRVAIARALASNPKVLLCDEA 167
Cdd:cd03290 94 -TVEENITF-----GSPfNKQRYKAVTDAcslqpdIDLLPFGDQTEigERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 1447223793 168 TSALDPATT-----RSILELLKDINRrlglTILLITHEM 201
Cdd:cd03290 168 FSALDIHLSdhlmqEGILKFLQDDKR----TLVLVTHKL 202
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-269 |
1.04e-13 |
|
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: 70.27 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFQQGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTL----IRCVNllerpTEGSVQVDGQELTALSekeL 77
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVP---L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 78 TRARRQIGMIFQHFNLLASrtvfgnvalPLELDNTPQAEIK-RRVTELLDLVGLGDKHDSYPAN-----------LSGGQ 145
Cdd:cd03289 73 QKWRKAFGVIPQKVFIFSG---------TFRKNLDPYGKWSdEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKdiNRRLGLTILLITHEMDVVKRiCDCVAVISNGQLIEQDTV 225
Cdd:cd03289 144 KQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSI 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1447223793 226 SEVFShpKTPLAQQFIQSTLHLDIpddYQARLKSTATADSVPML 269
Cdd:cd03289 221 QKLLN--EKSHFKQAISPSDRLKL---FPRRNSSKSKRKPRPQI 259
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
15-231 |
2.48e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 69.07 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 15 NRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGqeltalsekeltrarrQIGMIFQHFNLL 94
Cdd:PRK13546 34 NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 95 ASRTVFGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPA 174
Cdd:PRK13546 98 GQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1447223793 175 TTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSH 231
Cdd:PRK13546 178 FAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-219 |
2.57e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.73 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 6 NITkVFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLERPTEGSVQVDGQELTALSEKELTRA---- 80
Cdd:PRK13549 264 NLT-AWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPQQAIAQgiam 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 ----RRQIG----MIFQHFNLLASRTVFGNVAL---PLELDnTPQAEIKR-RV-TELLDLVglgdkhdsyPANLSGGQKQ 147
Cdd:PRK13549 343 vpedRKRDGivpvMGVGKNITLAALDRFTGGSRiddAAELK-TILESIQRlKVkTASPELA---------IARLSGGNQQ 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447223793 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:PRK13549 413 KAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-200 |
2.70e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.73 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 4 LSNITKVFQqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGsvqvdgqeltalsekeltRARRQ 83
Cdd:TIGR03719 7 MNRVSKVVP-PKKEI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG------------------EARPQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 84 ----IGMIFQHFNLLASRTVFGNVALPL--------ELD------NTPQAEIK---RRVTELLDLVGLGDKH-------- 134
Cdd:TIGR03719 66 pgikVGYLPQEPQLDPTKTVRENVEEGVaeikdaldRFNeisakyAEPDADFDklaAEQAELQEIIDAADAWdldsqlei 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447223793 135 ----------DSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDpATTRSILE-LLKDINrrlGlTILLITHE 200
Cdd:TIGR03719 146 amdalrcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD-AESVAWLErHLQEYP---G-TVVAVTHD 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-208 |
2.93e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.35 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDgqELTALSEKELTRAr 81
Cdd:TIGR03719 323 IEAENLTKAF--GDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETVKLAYVDQSRD- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 rqigmifqhfNLLASRTVFGNVALPLELDNTPQAEIKRRVtelldLVGL----GDKHDSYPANLSGGQKQRVAIARALAS 157
Cdd:TIGR03719 396 ----------ALDPNKTVWEEISGGLDIIKLGKREIPSRA-----YVGRfnfkGSDQQKKVGQLSGGERNRVHLAKTLKS 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1447223793 158 NPKVLLCDEATSALDPATTRSILELLKDinrrLGLTILLITHEMDVVKRIC 208
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVETLRALEEALLN----FAGCAVVISHDRWFLDRIA 507
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-219 |
3.82e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.85 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 15 NRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLERPTEGSVQVDGQELTALSEKELTRA--------RRQIG 85
Cdd:TIGR02633 270 NPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQAIRAgiamvpedRKRHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 86 MIFQ-------HFNLLASRTVFGNVALPLELDNTpQAEIKRrvtelldlVGLGDKHDSYP-ANLSGGQKQRVAIARALAS 157
Cdd:TIGR02633 350 IVPIlgvgkniTLSVLKSFCFKMRIDAAAELQII-GSAIQR--------LKVKTASPFLPiGRLSGGNQQKAVLAKMLLT 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447223793 158 NPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:TIGR02633 421 NPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-200 |
4.89e-13 |
|
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: 66.88 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCvnLLERPT----EGSVQVDGQELTalseKELtraRRQIGMIFQHFNLL 94
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDV--LAGRKTagviTGEILINGRPLD----KNF---QRSTGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 95 ASRTVfgnvalpleldntpqaeikrRVTELldlvglgdkhdsYPANLSG---GQKQRVAIARALASNPKVLLCDEATSAL 171
Cdd:cd03232 92 PNLTV--------------------REALR------------FSALLRGlsvEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
170 180
....*....|....*....|....*....
gi 1447223793 172 DPATTRSILELLKDINRRlGLTILLITHE 200
Cdd:cd03232 140 DSQAAYNIVRFLKKLADS-GQAILCTIHQ 167
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-200 |
1.26e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.98 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCvnLLERPTEGSVQvDGQELTALSEKELTRARRqIGMIFQHFNLLASRT 98
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNV--LAERVTTGVIT-GGDRLVNGRPLDSSFQRS-IGYVQQQDLHLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 99 V-----F-GNVALPLELdntPQAEIKRRVTELLDLVGLGDKHDSYPA----NLSGGQKQRVAIARALASNPKVLL-CDEA 167
Cdd:TIGR00956 853 VreslrFsAYLRQPKSV---SKSEKMEYVEEVIKLLEMESYADAVVGvpgeGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190
....*....|....*....|....*....|....*.
gi 1447223793 168 TSALDPATTRSILELLkdinRRL---GLTILLITHE 200
Cdd:TIGR00956 930 TSGLDSQTAWSICKLM----RKLadhGQAILCTIHQ 961
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-264 |
1.32e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.85 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVnLLERPTEGSVQVDGQELTALSEkeltrarrQIGMIFqhfnllaSRTVF 100
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAM-LGELSHAETSSVVIRGSVAYVP--------QVSWIF-------NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 101 GNVALPLELDNTpqaeikrRVTELLDLVGLGDKHDSYPA-----------NLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:PLN03232 697 ENILFGSDFESE-------RYWRAIDVTALQHDLDLLPGrdlteigergvNISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 170 ALDPATTRSILE-LLKDINRrlGLTILLITHEMDVVKRIcDCVAVISNGQLIEQDTVSEVFShpKTPLAQQFIQ------ 242
Cdd:PLN03232 770 ALDAHVAHQVFDsCMKDELK--GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSK--SGSLFKKLMEnagkmd 844
|
250 260
....*....|....*....|..
gi 1447223793 243 STLHLDIPDDYQARLKSTATAD 264
Cdd:PLN03232 845 ATQEVNTNDENILKLGPTVTID 866
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-199 |
2.22e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.21 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 23 NVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEkELTRARRQIGmifqHFNLLASR-TVFG 101
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLG----HQPGIKTElTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 102 NVALPLELDNTPQAEikrRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE 181
Cdd:PRK13538 94 NLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEA 170
|
170
....*....|....*...
gi 1447223793 182 LLKDINRRLGLTIlLITH 199
Cdd:PRK13538 171 LLAQHAEQGGMVI-LTTH 187
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-221 |
3.23e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.30 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITkvFQQGNRSIqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTAlseKELTRAR 81
Cdd:PRK10522 323 LELRNVT--FAYQDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA---EQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 RQIGMIFQHFNLlasrtvFGNValpleLDNTPQAEIKRRVTELLDLVGLGDK---HDSYPAN--LSGGQKQRVAIARALA 156
Cdd:PRK10522 397 KLFSAVFTDFHL------FDQL-----LGPEGKPANPALVEKWLERLKMAHKlelEDGRISNlkLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHE---MDVVKRICDcvavISNGQLIE 221
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDdhyFIHADRLLE----MRNGQLSE 529
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-221 |
7.02e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 66.73 E-value: 7.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraRRQIGMIFQHfNLLASRTVF 100
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL---RRQFSMIPQD-PVLFDGTVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 101 GNVALPLEldnTPQAEikrrVTELLDLVGLGDKHDSYP-----------ANLSGGQKQRVAIARA-LASNPKVLLCDEAT 168
Cdd:PTZ00243 1402 QNVDPFLE---ASSAE----VWAALELVGLRERVASESegidsrvleggSNYSVGQRQLMCMARAlLKKGSGFILMDEAT 1474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 169 SALDPATTRSILELLkdINRRLGLTILLITHEMDVVKRiCDCVAVISNGQLIE 221
Cdd:PTZ00243 1475 ANIDPALDRQIQATV--MSAFSAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAE 1524
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-244 |
8.23e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 8.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSekeLTRARRQIGMIFQHfNLLASRTVF 100
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKVLGIIPQA-PVLFSGTVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 101 GNVALPLELDNTPQAEIKRRvTELLDLV-----GLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
Cdd:PLN03130 1331 FNLDPFNEHNDADLWESLER-AHLKDVIrrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 176 ----TRSILELLKdinrrlGLTILLITHEMDVVkrI-CDCVAVISNGQLIEQDTVSEVFSHPKTPLAqQFIQST 244
Cdd:PLN03130 1410 daliQKTIREEFK------SCTMLIIAHRLNTI--IdCDRILVLDAGRVVEFDTPENLLSNEGSAFS-KMVQST 1474
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
21-237 |
1.64e-11 |
|
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: 63.77 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTL----IRCVNLLErpteGSVQVDGQELTALSEKELtraRRQIGMIFQHFNLLAs 96
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHTL---RSRLSIILQDPILFS- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 97 rtvfGNVALPLELDNTPQAEikrRVTELLDLVGLGDKHDSYPA-----------NLSGGQKQRVAIARALASNPKVLLCD 165
Cdd:cd03288 109 ----GSIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGgldavvteggeNFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 166 EATSALDPAtTRSILE--LLKDINRRlglTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSEVFSHPKTPLA 237
Cdd:cd03288 182 EATASIDMA-TENILQkvVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-181 |
2.14e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 2 IKLSNITKVFqqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVdGQelTAlsekeltrar 81
Cdd:PRK11819 325 IEAENLSKSF--GDRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE--TV---------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 82 rQIGMIFQ-HFNLLASRTVFGNVALPLELDNTPQAEIKRRV---------TELLDLVGlgdkhdsypaNLSGGQKQRVAI 151
Cdd:PRK11819 388 -KLAYVDQsRDALDPNKTVWEEISGGLDIIKVGNREIPSRAyvgrfnfkgGDQQKKVG----------VLSGGERNRLHL 456
|
170 180 190
....*....|....*....|....*....|
gi 1447223793 152 ARALASNPKVLLCDEATSALDPATTRSiLE 181
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLDVETLRA-LE 485
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-218 |
2.86e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.52 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 3 KLSNITKVFQQgnRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVnllerptEGSVQVDGQELTALSE--KELTRA 80
Cdd:PLN03211 70 KISDETRQIQE--RTI--LNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQGNNFTGTILANnrKPTKQI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQH---FNLLASRTVFGNVALpLELDNTPQAEIKRRVTE-LLDLVGLGDKHDSYPAN-----LSGGQKQRVAI 151
Cdd:PLN03211 139 LKRTGFVTQDdilYPHLTVRETLVFCSL-LRLPKSLTKQEKILVAEsVISELGLTKCENTIIGNsfirgISGGERKRVSI 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447223793 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHE-MDVVKRICDCVAVISNGQ 218
Cdd:PLN03211 218 AHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-256 |
3.85e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 25 SLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELtraRRQIGMIFQHFN---LLASRTVFG 101
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQL---QKLVSDEWQRNNtdmLSPGEDDTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 102 NVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYpanLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE 181
Cdd:PRK10938 100 RTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 182 LLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHpktPLAQQFIQST----LHLDIPDDYQAR 256
Cdd:PRK10938 177 LLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ---ALVAQLAHSEqlegVQLPEPDEPSAR 251
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-209 |
1.76e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNllerpteGSVQVDGQELTAlsEKELTRARRQigmifQHFNLLASRTVF 100
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDDGRIIY--EQDLIVARLQ-----QDPPRNVEGTVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 101 GNVALPLEldntPQAE-IKR---------------------RVTELLD--------------LVGLGDKHDSYPANLSGG 144
Cdd:PRK11147 85 DFVAEGIE----EQAEyLKRyhdishlvetdpseknlnelaKLQEQLDhhnlwqlenrinevLAQLGLDPDAALSSLSGG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINrrlGlTILLITHEMDVVK----RICD 209
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ---G-SIIFISHDRSFIRnmatRIVD 225
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-206 |
3.04e-10 |
|
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: 58.49 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRcvnllerptegsvQVDGQELTALSEKELTRARRQ-IGMIFQHFNLLAsrt 98
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------------EGLYASGKARLISFLPKFSRNkLIFIDQLQFLID--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 99 vfgnvalpleldntpqaeikrrvtelldlVGLGDKHDSYPAN-LSGGQKQRVAIARALASNPK--VLLCDEATSALDPAT 175
Cdd:cd03238 74 -----------------------------VGLGYLTLGQKLStLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190
....*....|....*....|....*....|.
gi 1447223793 176 TRSILELLKDInRRLGLTILLITHEMDVVKR 206
Cdd:cd03238 125 INQLLEVIKGL-IDLGNTVILIEHNLDVLSS 154
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-214 |
3.26e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.69 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 22 NNVSLH---VPA-GQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVD-----------GQEL----TALSEKELTRARR 82
Cdd:cd03236 13 NSFKLHrlpVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPpdwdeildefrGSELqnyfTKLLEGDVKVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 83 QigmifQHFNLLaSRTVFGNVALPLEldNTPQAEIKRRVTELLDLVGLGDKHDSypaNLSGGQKQRVAIARALASNPKVL 162
Cdd:cd03236 93 P-----QYVDLI-PKAVKGKVGELLK--KKDERGKLDELVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 163 LCDEATSALDP----ATTRSILELLKDINrrlglTILLITHEMDVVKRICDCVAVI 214
Cdd:cd03236 162 FFDEPSSYLDIkqrlNAARLIRELAEDDN-----YVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-219 |
3.64e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQgnrSIQalnNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKE---- 76
Cdd:PRK10982 250 ILEVRNLTSLRQP---SIR---DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainh 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 77 ----LTRARRQIGmIFQH----FNLLAS--RTVFGNVALpleLDNTpqaEIKRRVTELLDLVGLGD-KHDSYPANLSGGQ 145
Cdd:PRK10982 324 gfalVTEERRSTG-IYAYldigFNSLISniRNYKNKVGL---LDNS---RMKSDTQWVIDSMRVKTpGHRTQIGSLSGGN 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:PRK10982 397 QQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-206 |
5.27e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.38 E-value: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 31 GQIYGVIGASGAGKSTLIRCV-NLLERPTEGSVQVDGQELTalsekeltrarrqigmifqhfnllasrtvfgnvalplel 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDIL--------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 110 dntpqaeikrrvtELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILEL-----LK 184
Cdd:smart00382 43 -------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLL 109
|
170 180
....*....|....*....|..
gi 1447223793 185 DINRRLGLTILLITHEMDVVKR 206
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGP 131
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-199 |
5.46e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSnitKVFQqGNRSIqaLNNVSLH-VPAGQIyGVIGASGAGKSTLIRCVNLLERPTEGsvqvdgqeltalsekeltR 79
Cdd:PRK11819 9 MNRVS---KVVP-PKKQI--LKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKEFEG------------------E 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 80 ARRQ----IGMIFQHFNLLASRTVFGNV--------ALPLELD------NTPQAE----IKR--RVTELLDLVGLGD--- 132
Cdd:PRK11819 64 ARPApgikVGYLPQEPQLDPEKTVRENVeegvaevkAALDRFNeiyaayAEPDADfdalAAEqgELQEIIDAADAWDlds 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 133 ------------KHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDpATTRSILE-LLKDINrrlGlTILLITH 199
Cdd:PRK11819 144 qleiamdalrcpPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD-AESVAWLEqFLHDYP---G-TVVAVTH 218
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
114-228 |
7.09e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 114 QAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLT 193
Cdd:NF000106 118 RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GAT 196
|
90 100 110
....*....|....*....|....*....|....*
gi 1447223793 194 ILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEV 228
Cdd:NF000106 197 VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-219 |
1.09e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFqqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLErPTEGSVQVD-GQELTALsekelt 78
Cdd:PRK15064 1 MLSTANITMQF--GAKPL--FENISVKFGGGNRYGLIGANGCGKSTFMKILgGDLE-PSAGNVSLDpNERLGKL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 rarRQIGMIFQHFNLLasRTVF-GNV-------------ALP--LELDNTPQAEIK------------RRVTELLDLVGL 130
Cdd:PRK15064 70 ---RQDQFAFEEFTVL--DTVImGHTelwevkqerdriyALPemSEEDGMKVADLEvkfaemdgytaeARAGELLLGVGI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 131 G-DKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRrlglTILLITHEMDVVKRICD 209
Cdd:PRK15064 145 PeEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNS----TMIIISHDRHFLNSVCT 220
|
250
....*....|
gi 1447223793 210 CVAVISNGQL 219
Cdd:PRK15064 221 HMADLDYGEL 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
16-172 |
2.35e-09 |
|
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: 57.03 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 16 RSIQALNNVSLHVPAG-----QIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDG-------QELTALSE---KELTRA 80
Cdd:cd03237 5 TMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvsykpQYIKADYEgtvRDLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGMIFQHFNllasrtvfGNVALPLELDNTpqaeIKRRVTElldlvglgdkhdsypanLSGGQKQRVAIARALASNPK 160
Cdd:cd03237 85 ITKDFYTHPYFK--------TEIAKPLQIEQI----LDREVPE-----------------LSGGELQRVAIAACLSKDAD 135
|
170
....*....|..
gi 1447223793 161 VLLCDEATSALD 172
Cdd:cd03237 136 IYLLDEPSAYLD 147
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
21-199 |
2.78e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIY-----GVIGASGAGKSTLIRCVNLLERPTEGSVQVD------GQELTALSEKELTRARRQIGMIFq 89
Cdd:PRK13409 350 LGDFSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykPQYIKPDYDGTVEDLLRSITDDL- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 90 hfnllASRTVFGNVALPLELDntpqaeikrrvtELLDlvglgdkhdSYPANLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:PRK13409 429 -----GSSYYKSEIIKPLQLE------------RLLD---------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
170 180 190
....*....|....*....|....*....|....*...
gi 1447223793 170 ALDP----ATTRSIlellkdinRRL----GLTILLITH 199
Cdd:PRK13409 483 HLDVeqrlAVAKAI--------RRIaeerEATALVVDH 512
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-173 |
3.78e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.01 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 27 HVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGqeltalseKELTRARRQIGMIF-QHF-NLLASRTVFGNVA 104
Cdd:PRK13543 33 HVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG--------KTATRGDRSRFMAYlGHLpGLKADLSTLENLH 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447223793 105 LpleLDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDP 173
Cdd:PRK13543 105 F---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-233 |
4.05e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 31 GQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVD-----------GQEL----TALSEKELtRARRQIGMIFQhfnllA 95
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEpswdevlkrfrGTELqnyfKKLYNGEI-KVVHKPQYVDL-----I 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 96 SRTVFGNVAlplE-LDNTPQAEIKRRVTELLDLVGLGDKHDSypaNLSGGQKQRVAIARALASNPKVLLCDEATSALDP- 173
Cdd:PRK13409 173 PKVFKGKVR---ElLKKVDERGKLDEVVERLGLENILDRDIS---ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIr 246
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 174 ---ATTRSILELLKDInrrlglTILLITHEMDVVKRICDCVaVISNGqlieQDTVSEVFSHPK 233
Cdd:PRK13409 247 qrlNVARLIRELAEGK------YVLVVEHDLAVLDYLADNV-HIAYG----EPGAYGVVSKPK 298
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
21-172 |
5.34e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.49 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIY-----GVIGASGAGKSTLIRCVNLLERPTEGSVQVD------GQELTALSEkeltrarrqigmifq 89
Cdd:COG1245 351 YGGFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykPQYISPDYD--------------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 90 hfnllasrtvfGNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:COG1245 416 -----------GTVEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
...
gi 1447223793 170 ALD 172
Cdd:COG1245 485 HLD 487
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-214 |
6.16e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.10 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 25 SLHVP-AGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVD-----------GQEL----TALSEKELTRARR--QIGM 86
Cdd:COG1245 92 GLPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEpswdevlkrfrGTELqdyfKKLANGEIKVAHKpqYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 87 IFQHFNllasrtvfGNV-ALpleLDNTPQAEIKRRVTELLDLVGLGDKHDSypaNLSGGQKQRVAIARALASNPKVLLCD 165
Cdd:COG1245 172 IPKVFK--------GTVrEL---LEKVDERGKLDELAEKLGLENILDRDIS---ELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1447223793 166 EATSALDP----ATTRSILELLKDinrrlGLTILLITHEMDVVKRICDCVAVI 214
Cdd:COG1245 238 EPSSYLDIyqrlNVARLIRELAEE-----GKYVLVVEHDLAILDYLADYVHIL 285
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-199 |
1.69e-08 |
|
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: 55.91 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITKVFQQGNRSIQALNnvsLHVPAGQIYGVIGASGAGKSTLIRCVNLLeRPTEGSVqvdgqeltalsekeLTRA 80
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLS---FEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGR--------------LTKP 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRqiGMIFqhfnLLASRTVFGNVAL------PLELDntpqaEIKRR------VTELLDLVGLGD---KHDSYPA------ 139
Cdd:TIGR00954 513 AK--GKLF----YVPQRPYMTLGTLrdqiiyPDSSE-----DMKRRglsdkdLEQILDNVQLTHileREGGWSAvqdwmd 581
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 140 NLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLkdinRRLGLTILLITH 199
Cdd:TIGR00954 582 VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-218 |
1.94e-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: 53.77 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 36 VIGASGAGKSTLIRCVNLL---ERPTEGSVQVDGQELTALSEKeltraRRQIGMIFQHFN---LLASRT--VFGNVALpl 107
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKLIREGEV-----RAQVKLAFENANgkkYTITRSlaILENVIF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 108 eldnTPQAEIKrrvTELLDLVGlgdkhdsypaNLSGGQKQ------RVAIARALASNPKVLLCDEATSALDPATTR-SIL 180
Cdd:cd03240 100 ----CHQGESN---WPLLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLA 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1447223793 181 ELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGQ 218
Cdd:cd03240 163 EIIEERKSQKNFQLIVITHDEELVDAADHIYRVEKDGR 200
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
21-205 |
2.27e-08 |
|
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: 53.80 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLI----------RCVN-----------LLERPtegsvQVDgqELTALS-----E 74
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVEslsayarqflgQMDKP-----DVD--SIEGLSpaiaiD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 75 KELTR--ARRQIGMIFQHFNLLasRTVFGNVAlpleldntpqaeIKRRVTELLDlVGLGDKHDSYPAN-LSGGQKQRVAI 151
Cdd:cd03270 84 QKTTSrnPRSTVGTVTEIYDYL--RLLFARVG------------IRERLGFLVD-VGLGYLTLSRSAPtLSGGEAQRIRL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447223793 152 ARALASNPKVLL--CDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVK 205
Cdd:cd03270 149 ATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIR 203
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-295 |
5.11e-08 |
|
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: 54.53 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQeltalsekeltrarrqIGMIFQhFNLLASRTVF 100
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR----------------ISFSPQ-TSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 101 GNVALPLELDNTPQAEIKRRVTELLDLVGLGDKhDSYP-----ANLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
Cdd:TIGR01271 505 DNIIFGLSYDEYRYTSVIKACQLEEDIALFPEK-DKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 176 TRSILE--LLKDINRRlglTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSEVfsHPKTPlaqQFIQSTLHLDIPDDY 253
Cdd:TIGR01271 584 EKEIFEscLCKLMSNK---TRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL--QAKRP---DFSSLLLGLEAFDNF 654
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1447223793 254 QARLKSTatadsvpmlrmeftghsvdapLLSETARRFNVNNN 295
Cdd:TIGR01271 655 SAERRNS---------------------ILTETLRRVSIDGD 675
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
21-209 |
1.07e-07 |
|
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: 52.23 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLI------RCVNLLERPTEGSVQVDGQE-------LTALSEKELTRARR----- 82
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLHLKKEQPGNHDRIEglehidkVIVIDQSPIGRTPRsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 83 ------QIGMIF------QHFN--LLASRTVFGNVALPLEL---------DNTPQaeIKRRVTELLDlVGLGDKHDSYPA 139
Cdd:cd03271 91 ytgvfdEIRELFcevckgKRYNreTLEVRYKGKSIADVLDMtveealeffENIPK--IARKLQTLCD-VGLGYIKLGQPA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447223793 140 -NLSGGQKQRVAIARALA--SNPKVL-LCDEATSALDPATTRSILELLkdinRRL---GLTILLITHEMDVVKrICD 209
Cdd:cd03271 168 tTLSGGEAQRIKLAKELSkrSTGKTLyILDEPTTGLHFHDVKKLLEVL----QRLvdkGNTVVVIEHNLDVIK-CAD 239
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-281 |
1.19e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDG--------QELTALSEKELT------RARRQIGM 86
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPALEyvidgdREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 87 IFQHFNLL----ASRTVFGnvalplELDNTPQAEIKRRVTELLDLVGLGDKHDSYP-ANLSGGQKQRVAIARALASNPKV 161
Cdd:PRK10636 97 QLHDANERndghAIATIHG------KLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 162 LLCDEATSALDpatTRSILELLKDINRRLGlTILLITHEMDVVKRICDCVAVISNGQLIEQDTVSEVFSHPK-TPLAQQF 240
Cdd:PRK10636 171 LLLDEPTNHLD---LDAVIWLEKWLKSYQG-TLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRaTRLAQQQ 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 241 I------QSTLHLdipDDYQARLKSTAT----ADS-VPML-RMEFTGHS-VDAP 281
Cdd:PRK10636 247 AmyesqqERVAHL---QSYIDRFRAKATkakqAQSrIKMLeRMELIAPAhVDNP 297
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-221 |
1.36e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.72 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNItKVFQQGNRSIQALNnvsLHVPAGQIYGVIGASGAGKSTLIRCVNLLE--RPTEGSVQVDGQELTALSEKElt 78
Cdd:PRK09580 1 MLSIKDL-HVSVEDKAILRGLN---LEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 79 RARRQIGMIFQ----------HFNLLASRTVFGNVALPLELDNTPQAEIKRRVTELLDLvglgdkhdsyPANL------- 141
Cdd:PRK09580 75 RAGEGIFMAFQypveipgvsnQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKM----------PEDLltrsvnv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 142 --SGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE---LLKDINRrlglTILLITHEMDVVKRI-CDCVAVIS 215
Cdd:PRK09580 145 gfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADgvnSLRDGKR----SFIIVTHYQRILDYIkPDYVHVLY 220
|
....*.
gi 1447223793 216 NGQLIE 221
Cdd:PRK09580 221 QGRIVK 226
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
116-250 |
3.18e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.94 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 116 EIKRRVTELLDlVGLGDKHDSYPAN-LSGGQKQRVAIARALASN-PKVL-LCDEATSALDPATTRSILELLKDInRRLGL 192
Cdd:TIGR00630 464 EIRERLGFLID-VGLDYLSLSRAAGtLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRL-RDLGN 541
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 193 TILLITHEMDVVkRICDCV------AVISNGQLIEQDTVSEVFSHPKTpLAQQFIQSTLHLDIP 250
Cdd:TIGR00630 542 TLIVVEHDEDTI-RAADYVidigpgAGEHGGEVVASGTPEEILANPDS-LTGQYLSGRKKIEVP 603
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-228 |
4.92e-07 |
|
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: 50.63 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQeltalsekeltrarrqIGMIFQhFNLLASRTVF 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR----------------ISFSSQ-FSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 101 GNVALPLELDNTPQAEIKRRVTELLDLVGLGDKHDSYPA----NLSGGQKQRVAIARALASNPKVLLCDEATSALDPATT 176
Cdd:cd03291 116 ENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 177 RSILE--LLKDINRRlglTILLITHEMDVVKRiCDCVAVISNGQLIEQDTVSEV 228
Cdd:cd03291 196 KEIFEscVCKLMANK---TRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSEL 245
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-196 |
6.80e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 16 RSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNL----LERPTEGSVQVDGqeltaLSEKELTRARRQ----IGMI 87
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDG-----ITPEEIKKHYRGdvvyNAET 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 88 FQHFNLLasrTVFGNVALPLELdNTPQAEIK--------RRVTEL-LDLVGLGDKHDSYPAN-----LSGGQKQRVAIAR 153
Cdd:TIGR00956 147 DVHFPHL---TVGETLDFAARC-KTPQNRPDgvsreeyaKHIADVyMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAE 222
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1447223793 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILL 196
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLV 265
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-205 |
1.52e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 1 MIKLSNITkvFQQGNRSIQALNNVSLhvPAGQIYgVIGASGAGKSTLIRCVNLLERPTEGSVQVDGQELTALSEKELTRA 80
Cdd:PRK13541 1 MLSLHQLQ--FNIEQKNLFDLSITFL--PSAITY-IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 81 RRQIGmifqhfnLLASRTVFGNVALPLELDN---TPQAEIKR-RVTELLDlvglgdkhdSYPANLSGGQKQRVAIARALA 156
Cdd:PRK13541 76 GHNLG-------LKLEMTVFENLKFWSEIYNsaeTLYAAIHYfKLHDLLD---------EKCYSLSSGMQKIVAIARLIA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1447223793 157 SNPKVLLCDEATSALDpATTRSILELLKDINRRLGLTILLITHEMDVVK 205
Cdd:PRK13541 140 CQSDLWLLDEVETNLS-KENRDLLNNLIVMKANSGGIVLLSSHLESSIK 187
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
110-205 |
4.79e-06 |
|
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: 48.47 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 110 DNTPQaeIKRRVTELLDlVGLGDKHDSYPA-NLSGGQKQRVAIARAL---ASNPKVLLCDEATSALDPATTRSILELLKD 185
Cdd:TIGR00630 801 EAVPS--ISRKLQTLCD-VGLGYIRLGQPAtTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQR 877
|
90 100
....*....|....*....|
gi 1447223793 186 InRRLGLTILLITHEMDVVK 205
Cdd:TIGR00630 878 L-VDKGNTVVVIEHNLDVIK 896
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-220 |
1.01e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 10 VFQQGNRSIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCV--NLLERPTEGSVQVDGQELTALSEKE--------LTR 79
Cdd:NF040905 265 VYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDGKEVDVSTVSDaidaglayVTE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 80 ARRQIGMIfqhfnllasrtvfgnvalpleLDNTpqaeIKRRVTelldLVGLG--------DKHDSYPA------------ 139
Cdd:NF040905 345 DRKGYGLN---------------------LIDD----IKRNIT----LANLGkvsrrgviDENEEIKVaeeyrkkmnikt 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 140 --------NLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELlkdINR--RLGLTILLITHEMDVVKRICD 209
Cdd:NF040905 396 psvfqkvgNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTI---INElaAEGKGVIVISSELPELLGMCD 472
|
250
....*....|.
gi 1447223793 210 CVAVISNGQLI 220
Cdd:NF040905 473 RIYVMNEGRIT 483
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
116-205 |
1.66e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.56 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 116 EIKRRVTELLDlVGLGdkhdsY-----PAN-LSGGQKQRVAIARALA--SNPKVL-LCDEATSALDPATTRSILELLkdi 186
Cdd:COG0178 802 KIARKLQTLQD-VGLG-----YiklgqPATtLSGGEAQRVKLASELSkrSTGKTLyILDEPTTGLHFHDIRKLLEVL--- 872
|
90 100
....*....|....*....|..
gi 1447223793 187 nRRL---GLTILLITHEMDVVK 205
Cdd:COG0178 873 -HRLvdkGNTVVVIEHNLDVIK 893
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-172 |
1.88e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLE---RPTEGSV-----QVDGQELTAL-----SEKELTRARRQIGMI 87
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAidgIPKNCQIlhveqEVVGDDTTALqcvlnTDIERTQLLEEEAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 88 FQHFNLLASRTVFGNVALP----LELDNTPQ--AEIKRRVtELLD-----------LVGLG---DKHDSYPANLSGGQKQ 147
Cdd:PLN03073 273 VAQQRELEFETETGKGKGAnkdgVDKDAVSQrlEEIYKRL-ELIDaytaearaasiLAGLSftpEMQVKATKTFSGGWRM 351
|
170 180
....*....|....*....|....*
gi 1447223793 148 RVAIARALASNPKVLLCDEATSALD 172
Cdd:PLN03073 352 RIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
117-262 |
2.77e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 117 IKRRVTELLDLvGLGD-KHDSYPANLSGGQKQRVAIARALASNPK--VLLCDEATSALDPATTRSILELLKDInRRLGLT 193
Cdd:PRK00635 453 LKSRLSILIDL-GLPYlTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKL-RDQGNT 530
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447223793 194 ILLITHEMDVVK---RICDC--VAVISNGQLIEQDTVSEvFSHPKTPLAQQFIQSTLHLDIPddyQARLKSTAT 262
Cdd:PRK00635 531 VLLVEHDEQMISladRIIDIgpGAGIFGGEVLFNGSPRE-FLAKSDSLTAKYLRQELTIPIP---EKRTNSLGT 600
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-218 |
2.87e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 10 VFQQGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVnllerpTEGSVQVDGQELTAL-----SEKELTRARRQI 84
Cdd:PRK10938 267 VVSYNDRPI--LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI------TGDHPQGYSNDLTLFgrrrgSGETIWDIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 85 GMIFQ--HFNLLASRTVFgNVALPLELDNTP--QAEIKRR---VTELLDLVGLGDKHDSYP-ANLSGGQKQRVAIARALA 156
Cdd:PRK10938 339 GYVSSslHLDYRVSTSVR-NVILSGFFDSIGiyQAVSDRQqklAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALV 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447223793 157 SNPKVLLCDEATSALDPattrsilellkdINRRLgltillithemdvVKRICDcvAVISNGQ 218
Cdd:PRK10938 418 KHPTLLILDEPLQGLDP------------LNRQL-------------VRRFVD--VLISEGE 452
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-172 |
3.13e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 4 LSNITKVFqqGNRSIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRC-VNLLErPTEGSVQVD--------GQELTALSE 74
Cdd:PRK15064 322 VENLTKGF--DNGPL--FKNLNLLLEAGERLAIIGENGVGKTTLLRTlVGELE-PDSGTVKWSenanigyyAQDHAYDFE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 75 KELT-----RARRQIGMIFQHFNLLASRTVFGnvalpleldntpQAEIKRRVTelldlvglgdkhdsypaNLSGGQKQRV 149
Cdd:PRK15064 397 NDLTlfdwmSQWRQEGDDEQAVRGTLGRLLFS------------QDDIKKSVK-----------------VLSGGEKGRM 447
|
170 180
....*....|....*....|...
gi 1447223793 150 AIARALASNPKVLLCDEATSALD 172
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
117-205 |
9.47e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.29 E-value: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 117 IKRRVTELLDlVGLGdkhdsY-----PAN-LSGGQKQRVAIARALA--SNPKVL-LCDEATSALDPATTRSILELLKdin 187
Cdd:PRK00349 807 IARKLQTLVD-VGLG-----YiklgqPATtLSGGEAQRVKLAKELSkrSTGKTLyILDEPTTGLHFEDIRKLLEVLH--- 877
|
90 100
....*....|....*....|.
gi 1447223793 188 rRL---GLTILLITHEMDVVK 205
Cdd:PRK00349 878 -RLvdkGNTVVVIEHNLDVIK 897
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
17-247 |
1.86e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 17 SIQALNNVSLHVPAGQIYGVIGASGAGKSTLIR-----CV-NLLERPTEGSVQVDGQELTAL----------SEK----- 75
Cdd:PRK00635 607 TKHNLKDLTISLPLGRLTVVTGVSGSGKSSLINdtlvpAVeEFIEQGFCSNLSIQWGAISRLvhitrdlpgrSQRsiplt 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 76 -------------ELTRARRQiGMIFQHFNL------------LASRTVFGN---VALPLELDNTPQAEI------KRRV 121
Cdd:PRK00635 687 yikafddlrelfaEQPRSKRL-GLTKSHFSFntplgacaecqgLGSITTTDNrtsIPCPSCLGKRFLPQVlevrykGKNI 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 122 TELLD----------------------LVGLGDKHdsYP-----ANLSGGQKQRVAIARALAS---NPKVLLCDEATSAL 171
Cdd:PRK00635 766 ADILEmtayeaekffldepsihekihaLCSLGLDY--LPlgrplSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGL 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 172 DPATTRSILELLKDINRrLGLTILLITHEMDVVKrICDCVAVIS------NGQLIEQDTVSEVFsHPKTPLA---QQFIQ 242
Cdd:PRK00635 844 HTHDIKALIYVLQSLTH-QGHTVVIIEHNMHVVK-VADYVLELGpeggnlGGYLLASCSPEELI-HLHTPTAkalRPYLS 920
|
....*
gi 1447223793 243 STLHL 247
Cdd:PRK00635 921 SPQEL 925
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
36-219 |
2.13e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 36 VIGASGAGKSTLIRCVNLLERPTEGSV--------------QVDGQELTalSEKELTRARRQIGMIFQHFNL-LASRTVF 100
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDLS--SNPLLYMMRCFPGVPEQKLRAhLGSFGVT 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 101 GNVAL-PLeldntpqaeikrrvtelldlvglgdkhdsypANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSI 179
Cdd:PLN03073 618 GNLALqPM-------------------------------YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL 666
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1447223793 180 LEllkdinrrlGLT-----ILLITHEMDVVKRICDCVAVISNGQL 219
Cdd:PLN03073 667 IQ---------GLVlfqggVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
140-233 |
3.89e-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: 40.63 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 140 NLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNgql 219
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG--- 147
|
90
....*....|....
gi 1447223793 220 ieQDTVSEVFSHPK 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 |
4.18e-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: 38.76 E-value: 4.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 139 ANLSGGQKQR---VAIARALAS----------NPKVLLCDEATSALDPATTRSILELLKD 185
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
141-229 |
8.77e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.37 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILL-ITHEMDVVKRICDCVAVISNGQL 219
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMsLLQPAPETFDLFDDIILLSEGQI 416
|
90
....*....|...
gi 1447223793 220 IEQ---DTVSEVF 229
Cdd:PLN03140 417 VYQgprDHILEFF 429
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
141-206 |
1.39e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.88 E-value: 1.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 141 LSGGQKQRVAIARALAS---NPKVLLC-DEATSALDPATTRSILELLKDiNRRLGLTILLITHEMDVVKR 206
Cdd:cd03227 78 LSGGEKELSALALILALaslKPRPLYIlDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLPELAEL 146
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
33-199 |
2.09e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.84 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 33 IYGVIGASGAGKSTLIRCVNL-LERPTEGSVQVDGQELTALSEK---ELT--------RARRQIGMIFQHFNLLAS---- 96
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIRYaLYGKARSRSKLRSDLINVGSEEasvELEfehggkryRIERRQGEFAEFLEAKPSerke 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447223793 97 --RTVFG--------------NVALPLELDNTPQAEIKRRVTeLLDLVGLGDkhdsyPANLSGGQKQRVAIARALAsnpk 160
Cdd:COG0419 105 alKRLLGleiyeelkerlkelEEALESALEELAELQKLKQEI-LAQLSGLDP-----IETLSGGERLRLALADLLS---- 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1447223793 161 vLLCDeaTSALDPATTRSILELLKDINrrlgltilLITH 199
Cdd:COG0419 175 -LILD--FGSLDEERLERLLDALEELA--------IITH 202
|
|
| |
