|
Name |
Accession |
Description |
Interval |
E-value |
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-350 |
1.09e-169 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 475.72 E-value: 1.09e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 14 HIKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQL 93
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 94 RQRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQQQITQE- 252
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRf 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 253 -LLNLEQLELPFSISPEVTTDTTHSIIKLRYASSVQYSPDLKVIFEQFEHPVHLYQSHIDSIQNHLVGSLIVAVADLNLD 331
Cdd:COG1135 241 lPTVLNDELPEELLARLREAAGGGRLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDDAA 320
|
330
....*....|....*....
gi 2314388301 332 TDLLQQKLKQHIAQIEAIG 350
Cdd:COG1135 321 IDAALAYLREQGVVVEVLG 339
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
15-351 |
1.47e-143 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 409.96 E-value: 1.47e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR 94
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQQQITqelL 254
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLT---R 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 255 NLEQLELPFSISPEVT-------TDTTHSIIKLRYASSVQYSPDLKVIFEQFEHPVHLYQSHIDSIQNHLVGSLIVAVAD 327
Cdd:PRK11153 239 EFIQSTLHLDLPEDYLarlqaepTTGSGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTG 318
|
330 340
....*....|....*....|....
gi 2314388301 328 LNLDTDLLQQKLKQHIAQIEAIGY 351
Cdd:PRK11153 319 DPGDIQAAIAYLQEHGVKVEVLGY 342
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
15-246 |
2.17e-137 |
|
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: 390.02 E-value: 2.17e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR 94
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
15-351 |
2.13e-104 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 310.28 E-value: 2.13e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR 94
Cdd:TIGR02314 2 IKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:TIGR02314 82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQQQ-----I 249
Cdd:TIGR02314 162 LLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPlaqkfI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 250 TQELLNLEQLELPFSISPEVTTDtTHSIIKLRYASSVQYSPDLKVIFEQFEHPVHLYQSHIDSIQNHLVGSLIVAVADLN 329
Cdd:TIGR02314 242 RSTLHLSIPEDYQERLQATPFAD-SVPMVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMHGTQ 320
|
330 340
....*....|....*....|..
gi 2314388301 330 LDTDLLQQKLKQHIAQIEAIGY 351
Cdd:TIGR02314 321 QDTQAAIAYLQEHNVKVEVLGY 342
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
15-250 |
7.95e-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: 299.99 E-value: 7.95e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLaGLTHAELIQLR 94
Cdd:COG1126 2 IEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVAL-PLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:COG1126 77 RKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEInQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQQQIT 250
Cdd:COG1126 157 VMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERT 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
15-234 |
4.17e-94 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 279.62 E-value: 4.17e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR 94
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 -QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:COG1136 85 rRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIrEICDQVVVIEKGEIVE 234
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVS 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-250 |
8.67e-93 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 286.41 E-value: 8.67e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEVQGKS-VHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELI 91
Cdd:COG1123 259 PLLEVRNLSKRYPVRGKGgVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 92 QLRQRIGMIFQH----FNlmSAKTVWENVALPLKVAN-YKKSDIDTRVNEVLQLVGLS-DKAQNYPSQLSGGQKQRVGIA 165
Cdd:COG1123 339 ELRRRVQMVFQDpyssLN--PRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 166 RALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNP 245
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
....*
gi 2314388301 246 QQQIT 250
Cdd:COG1123 497 QHPYT 501
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
13-236 |
2.90e-92 |
|
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: 275.70 E-value: 2.90e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEvqgkSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQ 92
Cdd:COG1127 4 PMIEVRNLTKSFG----DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQRIGMIFQHFNLMSAKTVWENVALPLKV-ANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHH 171
Cdd:COG1127 80 LRRRIGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 172 PEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
15-237 |
1.58e-91 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 273.08 E-value: 1.58e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR 94
Cdd:COG2884 2 IRFENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:COG2884 79 RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQkLGITIVLITHEMQVIREICDQVVVIEKGEIVESGE 237
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
15-232 |
1.38e-85 |
|
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: 257.80 E-value: 1.38e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR 94
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 -QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIrEICDQVVVIEKGEI 232
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
15-232 |
1.19e-84 |
|
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: 255.15 E-value: 1.19e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLaGLTHAELIQLR 94
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVAL-PLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEI 232
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
15-246 |
5.43e-81 |
|
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: 249.59 E-value: 5.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQ---ISEGHIHIHQQDLAGLTHAELI 91
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 92 QLR-QRIGMIFQhfNLMSA----KTVWENVALPLKVAN-YKKSDIDTRVNEVLQLVGLSDKAQ---NYPSQLSGGQKQRV 162
Cdd:COG0444 82 KIRgREIQMIFQ--DPMTSlnpvMTVGDQIAEPLRIHGgLSKAEARERAIELLERVGLPDPERrldRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 163 GIARALVHHPEILLCDEATSALDPestSV---VLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVW 239
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDV---TIqaqILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVE 236
|
....*..
gi 2314388301 240 SVFSNPQ 246
Cdd:COG0444 237 ELFENPR 243
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
15-236 |
5.82e-81 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 246.64 E-value: 5.82e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR 94
Cdd:cd03261 1 IELRGLTKSFG--GRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKV-ANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREhTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
13-233 |
1.53e-80 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 246.12 E-value: 1.53e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYevqGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQ 92
Cdd:COG3638 1 PMLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQRIGMIFQHFNLMSAKTVWENV---ALP----LKVA--NYKKSDIDtRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVG 163
Cdd:COG3638 78 LRRRIGMIFQQFNLVPRLSVLTNVlagRLGrtstWRSLlgLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 164 IARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIV 233
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
13-234 |
2.62e-77 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 238.07 E-value: 2.62e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLthaeliq 92
Cdd:COG1116 6 PALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 lRQRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHP 172
Cdd:COG1116 79 -GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 173 EILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEmqvIRE---ICDQVVVIEK--GEIVE 234
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD---VDEavfLADRVVVLSArpGRIVE 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
15-246 |
4.35e-77 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 236.46 E-value: 4.35e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLaglTHAELIQLR 94
Cdd:COG1122 1 IELENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQH-FNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:COG1122 75 RKVGLVFQNpDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
15-236 |
2.36e-76 |
|
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: 234.71 E-value: 2.36e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR 94
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQhfNLMSA----KTVWENVALPLKVA--NYKKSDIDTRVNEVLQLVGLSDK-AQNYPSQLSGGQKQRVGIARA 167
Cdd:cd03257 82 KEIQMVFQ--DPMSSlnprMTIGEQIAEPLRIHgkLSKKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2314388301 168 LVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
15-250 |
4.55e-76 |
|
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: 234.70 E-value: 4.55e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLaglTHAELIQLR 94
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV---TRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFnlMSA----KTVWENVALPLKVanYKKSDIDTRVNEVLQLVGLSDK-AQNYPSQLSGGQKQRVGIARALV 169
Cdd:COG1124 79 RRVQMVFQDP--YASlhprHTVDRILAEPLRI--HGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 170 HHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQQQI 249
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
.
gi 2314388301 250 T 250
Cdd:COG1124 235 T 235
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
13-246 |
2.07e-75 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 236.53 E-value: 2.07e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThAEliq 92
Cdd:COG3842 4 PALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP-PE--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 lrQR-IGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHH 171
Cdd:COG3842 76 --KRnVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 172 PEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQvirE---ICDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQE---EalaLADRIAVMNDGRIEQVGTPEEIYERPA 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-250 |
9.17e-75 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 231.46 E-value: 9.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYevqGKSvHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGL-EQIS----EGHIHIHQQDLAGlTH 87
Cdd:COG1117 10 PKIEVRNLNVYY---GDK-QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIPgarvEGEILLDGEDIYD-PD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 88 AELIQLRQRIGMIFQHFNLMsAKTVWENVALPLKVANYK-KSDIDTRVNEVLQLVGL----SDKAQNYPSQLSGGQKQRV 162
Cdd:COG1117 85 VDVVELRRRVGMVFQKPNPF-PKSIYDNVAYGLRLHGIKsKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 163 GIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLgiTIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVF 242
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
....*...
gi 2314388301 243 SNPQQQIT 250
Cdd:COG1117 242 TNPKDKRT 249
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
15-236 |
1.71e-74 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 229.33 E-value: 1.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAeliqlR 94
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
15-241 |
3.08e-74 |
|
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: 229.37 E-value: 3.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQI-----SEGHIHIHQQDLAGLThAE 89
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLD-VD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 90 LIQLRQRIGMIFQHFNLMSaKTVWENVALPLKVANYK-KSDIDTRVNEVLQLVGLSDKAQN--YPSQLSGGQKQRVGIAR 166
Cdd:cd03260 76 VLELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKlKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 167 ALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlgITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSV 241
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-233 |
3.98e-74 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 229.38 E-value: 3.98e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR 94
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENV---ALPLK------VANYKKSDIDtRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIA 165
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVlsgRLGRRstwrslFGLFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 166 RALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIV 233
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
15-238 |
8.65e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 228.41 E-value: 8.65e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAglthAELIQLR 94
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEV 238
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
15-233 |
4.69e-72 |
|
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: 224.10 E-value: 4.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR 94
Cdd:TIGR02315 2 LEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENV---------ALPLKVANYKKSDIDtRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIA 165
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVlhgrlgykpTWRSLLGRFSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 166 RALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIV 233
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
13-246 |
7.34e-70 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 221.53 E-value: 7.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEVQG-------KSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGL 85
Cdd:COG4608 6 PLLEVRDLKKHFPVRGglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 86 THAELIQLRQRIGMIFQhfNLMSA----KTVWENVALPLKVAN-YKKSDIDTRVNEVLQLVGLS-DKAQNYPSQLSGGQK 159
Cdd:COG4608 86 SGRELRPLRRRMQMVFQ--DPYASlnprMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRpEHADRYPHEFSGGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 160 QRVGIARALVHHPEILLCDEATSALDpesTSV---VLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALD---VSIqaqVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250
....*....|
gi 2314388301 237 EVWSVFSNPQ 246
Cdd:COG4608 241 PRDELYARPL 250
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
21-231 |
1.20e-69 |
|
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: 216.95 E-value: 1.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 21 NKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThaeLIQLRQRIGMI 100
Cdd:cd03225 4 NLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 101 FQHFNLM-SAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDE 179
Cdd:cd03225 81 FQNPDDQfFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 180 ATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGE 231
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
15-231 |
2.56e-69 |
|
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: 214.74 E-value: 2.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThAELIQLR 94
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE-DELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLkvanykksdidtrvnevlqlvglsdkaqnypsqlSGGQKQRVGIARALVHHPEI 174
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGE 231
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
13-236 |
6.35e-69 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 220.75 E-value: 6.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYY-----EV-----QGKS----------VHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISE 72
Cdd:COG4175 2 PKIEVRNLYKIFgkrpeRAlklldQGKSkdeilektgqTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 73 GHIHIHQQDLAGLTHAELIQLRQ-RIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYP 151
Cdd:COG4175 82 GEVLIDGEDITKLSKKELRELRRkKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 152 SQLSGGQKQRVGIARALVHHPEILLCDEATSALDP--------EstsvvlsLLkEINQKLGITIVLITHEMQ-VIReICD 222
Cdd:COG4175 162 DELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirremqdE-------LL-ELQAKLKKTIVFITHDLDeALR-LGD 232
|
250
....*....|....
gi 2314388301 223 QVVVIEKGEIVESG 236
Cdd:COG4175 233 RIAIMKDGRIVQIG 246
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
15-246 |
1.01e-68 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 215.65 E-value: 1.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHI--HQQDLAGLTHAELI- 91
Cdd:PRK11124 3 IQLNGINCFY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSKTPSDKAIr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 92 QLRQRIGMIFQHFNLMSAKTVWEN-VALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVH 170
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 171 HPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVwSVFSNPQ 246
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQ 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
15-238 |
2.03e-68 |
|
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: 213.87 E-value: 2.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHaeliqlr 94
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 qRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03293 74 -DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEmqvIRE---ICDQVVVIEK--GEIVESGEV 238
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD---IDEavfLADRVVVLSArpGRIVAEVEV 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
15-246 |
2.46e-68 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 214.49 E-value: 2.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHI--HQQDL-AGLTHAELI 91
Cdd:COG4161 3 IQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIagHQFDFsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 92 QLRQRIGMIFQHFNLMSAKTVWEN-VALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVH 170
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 171 HPEILLCDEATSALDPESTSVVLSLLKEInQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVwSVFSNPQ 246
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQ 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-246 |
1.56e-67 |
|
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: 213.66 E-value: 1.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 4 FGSQVAFSVPHIKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLA 83
Cdd:cd03294 10 FGKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 84 GLTHAELIQLR-QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRV 162
Cdd:cd03294 90 AMSRKELRELRrKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 163 GIARALVHHPEILLCDEATSALDP----ESTSVVLSLLKEinqkLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEV 238
Cdd:cd03294 170 GLARALAVDPDILLMDEAFSALDPlirrEMQDELLRLQAE----LQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
|
....*...
gi 2314388301 239 WSVFSNPQ 246
Cdd:cd03294 246 EEILTNPA 253
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
15-245 |
2.51e-67 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 215.71 E-value: 2.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLthaeliQLR 94
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL------PPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QR-IGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:COG3839 74 DRnIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEmQVirE---ICDQVVVIEKGEIVESGEVWSVFSNP 245
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD-QV--EamtLADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
13-234 |
4.56e-66 |
|
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: 208.44 E-value: 4.56e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQ 92
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LR-QRIGMIFQHFNLMSAKTVWENVALPLKVANYKksDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHH 171
Cdd:COG4181 87 LRaRHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 172 PEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREiCDQVVVIEKGEIVE 234
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
15-246 |
5.52e-66 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 211.93 E-value: 5.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAeliqlR 94
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPP-----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QR-IGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:COG1118 74 ERrVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-247 |
8.05e-66 |
|
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: 216.31 E-value: 8.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEvqGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQIS---EGHIHIHQQDLAGLTHAE 89
Cdd:COG1123 3 PLLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 90 LiqlRQRIGMIFQhfNLMSA---KTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIAR 166
Cdd:COG1123 81 R---GRRIGMVFQ--DPMTQlnpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 167 ALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
.
gi 2314388301 247 Q 247
Cdd:COG1123 236 A 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-250 |
3.18e-64 |
|
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: 212.62 E-value: 3.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQG-------KSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQiSEGHIHIHQQDLAGLTH 87
Cdd:COG4172 276 LEARDLKVWFPIKRglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 88 AELIQLRQRIGMIFQH-FNLMSAK-TVWENVALPLKVAN--YKKSDIDTRVNEVLQLVGLSDKAQN-YPSQLSGGQKQRV 162
Cdd:COG4172 355 RALRPLRRRMQVVFQDpFGSLSPRmTVGQIIAEGLRVHGpgLSAAERRARVAEALEEVGLDPAARHrYPHEFSGGQRQRI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 163 GIARALVHHPEILLCDEATSALDpesTSV---VLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVW 239
Cdd:COG4172 435 AIARALILEPKLLVLDEPTSALD---VSVqaqILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTE 511
|
250
....*....|.
gi 2314388301 240 SVFSNPQQQIT 250
Cdd:COG4172 512 QVFDAPQHPYT 522
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
15-250 |
4.51e-64 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 203.91 E-value: 4.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVqgksVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHI------HQQDLAG-LTH 87
Cdd:TIGR03005 1 VRFSDVTKRFGI----LTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVegeqlyHMPGRNGpLVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 88 AE---LIQLRQRIGMIFQHFNLMSAKTVWENVAL-PLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVG 163
Cdd:TIGR03005 77 ADekhLRQMRNKIGMVFQSFNLFPHKTVLDNVTEaPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 164 IARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFS 243
Cdd:TIGR03005 157 IARALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFR 236
|
....*..
gi 2314388301 244 NPQQQIT 250
Cdd:TIGR03005 237 QPKEERT 243
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
15-246 |
2.27e-63 |
|
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: 201.70 E-value: 2.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqgkSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGL-THaeliql 93
Cdd:cd03300 1 IELENVSKFYG----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLpPH------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 94 RQRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
11-246 |
2.36e-63 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 202.34 E-value: 2.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 11 SVPHIKIRNLNKYYEvqgkSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLA------G 84
Cdd:COG4598 5 APPALEVRDLHKSFG----DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 85 LTHA----ELIQLRQRIGMIFQHFNLMSAKTVWENVAL-PLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQK 159
Cdd:COG4598 81 ELVPadrrQLQRIRTRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 160 QRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVW 239
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPA 239
|
....*..
gi 2314388301 240 SVFSNPQ 246
Cdd:COG4598 240 EVFGNPK 246
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
15-248 |
3.42e-62 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 198.78 E-value: 3.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqGKSVhALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGlTHAELIQLR 94
Cdd:PRK09493 2 IEFKNVSKHF---GPTQ-VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVAL-PLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQQQ 248
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-244 |
4.68e-61 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 196.88 E-value: 4.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLagLTHAELIQLR 94
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQH-FNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:TIGR04520 77 KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREiCDQVVVIEKGEIVESGEVWSVFSN 244
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-246 |
1.04e-60 |
|
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: 196.13 E-value: 1.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevQGKS---VHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELI 91
Cdd:TIGR04521 1 IKLKNVSYIY--QPGTpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 92 QLRQRIGMIFQH-----FnlmsAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDK-AQNYPSQLSGGQKQRVGIA 165
Cdd:TIGR04521 79 DLRKKVGLVFQFpehqlF----EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 166 RALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNP 245
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
.
gi 2314388301 246 Q 246
Cdd:TIGR04521 235 D 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-232 |
1.78e-60 |
|
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: 193.39 E-value: 1.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR 94
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEI 232
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
15-250 |
2.92e-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: 2.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHI------------HQQDL 82
Cdd:PRK11264 4 IEVKNLVKKF--HGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 83 aglthaeLIQLRQRIGMIFQHFNLMSAKTVWENVAL-PLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQR 161
Cdd:PRK11264 80 -------IRQLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 162 VGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSV 241
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
....*....
gi 2314388301 242 FSNPQQQIT 250
Cdd:PRK11264 232 FADPQQPRT 240
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
15-245 |
6.58e-60 |
|
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: 192.90 E-value: 6.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLthaELIQLR 94
Cdd:cd03295 1 IEFENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ---DPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDK--AQNYPSQLSGGQKQRVGIARALVHHP 172
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 173 EILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNP 245
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-247 |
5.28e-59 |
|
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: 198.76 E-value: 5.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKS----SLLRTLNGLEQISEGHIHIHQQDLAGLTHAEL 90
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 91 IQLR-QRIGMIFQhfNLMSA----KTVWENVALPLKV-ANYKKSDIDTRVNEVLQLVGLSDKAQ---NYPSQLSGGQKQR 161
Cdd:COG4172 87 RRIRgNRIAMIFQ--EPMTSlnplHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERrldAYPHQLSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 162 VGIARALVHHPEILLCDEATSALDpesTSV---VLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEV 238
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALD---VTVqaqILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPT 241
|
....*....
gi 2314388301 239 WSVFSNPQQ 247
Cdd:COG4172 242 AELFAAPQH 250
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
15-232 |
3.97e-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: 186.06 E-value: 3.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLagltHAELIQLR 94
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENValplkvanykksdidtrvnevlqlvglsdkaqnypsQLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEI 232
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
15-236 |
4.49e-58 |
|
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: 187.08 E-value: 4.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqgkSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAEliqlr 94
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-236 |
7.42e-58 |
|
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: 199.29 E-value: 7.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEvqGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELiq 92
Cdd:COG2274 472 GDIELENVSFRYP--GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL-- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 lRQRIGMIFQHFNLMSAkTVWENVALPLKVANykksdiDTRVNEVLQLVGLSDKAQNYP-----------SQLSGGQKQR 161
Cdd:COG2274 548 -RRQIGVVLQDVFLFSG-TIRENITLGDPDAT------DEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 162 VGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIReICDQVVVIEKGEIVESG 236
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
15-246 |
9.40e-58 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 187.16 E-value: 9.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqgkSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThaelIQLR 94
Cdd:cd03296 3 IEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP----VQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QrIGMIFQHFNLMSAKTVWENVALPLKVANYK----KSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVH 170
Cdd:cd03296 75 N-VGFVFQHYALFRHMTVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 171 HPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
15-232 |
1.18e-57 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 186.18 E-value: 1.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNkyYEVQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThaeLIQLR 94
Cdd:COG4619 1 LELEGLS--FRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMsAKTVWENVALPLKVANYKKSDidTRVNEVLQLVGLSDKAQNYP-SQLSGGQKQRVGIARALVHHPE 173
Cdd:COG4619 74 RQVAYVPQEPALW-GGTVRDNLPFPFQLRERKFDR--ERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEI 232
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
15-238 |
1.30e-57 |
|
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: 186.99 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLagltHAELIQLR 94
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV----RKEPREAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:COG4555 74 RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINqKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEV 238
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSL 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
15-243 |
8.88e-57 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 185.25 E-value: 8.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELiqlR 94
Cdd:COG1120 2 LEAENLSVGY--GGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL---A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVAL---PLK--VANYKKSDIDtRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALV 169
Cdd:COG1120 75 RRIAYVPQEPPAPFGLTVRELVALgryPHLglFGRPSAEDRE-AVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 170 HHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFS 243
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-243 |
2.24e-56 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 183.75 E-value: 2.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqgkSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAglthaeliQLR 94
Cdd:COG1121 7 IELENLTVSYG----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR--------RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAK--TVWENVALPLK-----VANYKKSDIDtRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARA 167
Cdd:COG1121 75 RRIGYVPQRAEVDWDFpiTVRDVVLMGRYgrrglFRRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 168 LVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGeIVESGEVWSVFS 243
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLT 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
15-245 |
1.73e-55 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 181.11 E-value: 1.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqgksvHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAeliqlr 94
Cdd:COG3840 2 LRLDDLTYRYG------DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QR-IGMIFQHFNLMSAKTVWENVALPLKvANYKKSDID-TRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHP 172
Cdd:COG3840 70 ERpVSMLFQENNLFPHLTVAQNIGLGLR-PGLKLTAEQrAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 173 EILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNP 245
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
15-250 |
3.71e-54 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 178.88 E-value: 3.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQG-----KSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLaglTHAE 89
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL---EYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 90 LIQLRQRIGMIFQHFN--LMSAKTVWENVALPLKVA-NYKKSDIDTRVNEVLQLVGLS-DKAQNYPSQLSGGQKQRVGIA 165
Cdd:COG4167 82 YKYRCKHIRMIFQDPNtsLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLLpEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 166 RALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNP 245
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
....*
gi 2314388301 246 QQQIT 250
Cdd:COG4167 242 QHEVT 246
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
15-241 |
6.70e-54 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 181.05 E-value: 6.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqGKSvHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLtHAEliqlR 94
Cdd:PRK10851 3 IEIANIKKSF---GRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL-HAR----D 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKK----SDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVH 170
Cdd:PRK10851 74 RKVGFVFQHYALFRHMTVFDNIAFGLTVLPRRErpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 171 HPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG---EVWSV 241
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGtpdQVWRE 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
13-246 |
1.05e-53 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 177.54 E-value: 1.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYevqGkSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIq 92
Cdd:COG0411 3 PLLEVRGLTKRF---G-GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 lRQRIGMIFQHFNLMSAKTVWENVALP-------------LKVANYKKSD--IDTRVNEVLQLVGLSDKAQNYPSQLSGG 157
Cdd:COG0411 78 -RLGIARTFQNPRLFPELTVLENVLVAaharlgrgllaalLRLPRARREEreARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 158 QKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGE 237
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
....*....
gi 2314388301 238 VWSVFSNPQ 246
Cdd:COG0411 237 PAEVRADPR 245
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
34-246 |
8.82e-53 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 175.16 E-value: 8.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQD----------LAGLTHAELIQLRQRIGMIFQH 103
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqLKVADKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 104 FNLMSAKTVWENV-ALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQ-NYPSQLSGGQKQRVGIARALVHHPEILLCDEAT 181
Cdd:PRK10619 101 FNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 182 SALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQ 244
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-231 |
4.21e-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: 170.26 E-value: 4.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELiqlR 94
Cdd:cd03228 1 IEFKNVSFSYP--GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAkTVWENValplkvanykksdidtrvnevlqlvglsdkaqnypsqLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03228 76 KNIAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIReICDQVVVIEKGE 231
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
15-236 |
7.07e-52 |
|
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: 171.22 E-value: 7.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGkIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAeliqLR 94
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
15-246 |
9.43e-52 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 171.85 E-value: 9.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIqlR 94
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVAN----------YKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGI 164
Cdd:cd03219 75 LGIGRTFQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 165 ARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSN 244
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNN 233
|
..
gi 2314388301 245 PQ 246
Cdd:cd03219 234 PR 235
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
13-236 |
2.50e-51 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 174.75 E-value: 2.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEvqGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThAEliq 92
Cdd:PRK09452 13 PLVELRGISKSFD--GKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 lrQR-IGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHH 171
Cdd:PRK09452 85 --NRhVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 172 PEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
14-250 |
3.49e-51 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 173.35 E-value: 3.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 14 HIKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQL 93
Cdd:PRK15079 17 HFDIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 94 RQRIGMIFQH--FNLMSAKTVWENVALPLKV--ANYKKSDIDTRVNEVLQLVGLSDKAQN-YPSQLSGGQKQRVGIARAL 168
Cdd:PRK15079 97 RSDIQMIFQDplASLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPNLINrYPHEFSGGQCQRIGIARAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 169 VHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQQQ 248
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHP 256
|
..
gi 2314388301 249 IT 250
Cdd:PRK15079 257 YT 258
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
32-233 |
4.75e-51 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 169.67 E-value: 4.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 32 HALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLRQRIGMIFQHFNLMSAKT 111
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 112 VWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSV 191
Cdd:PRK10908 96 VYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2314388301 192 VLSLLKEINqKLGITIVLITHEMQVIREICDQVVVIEKGEIV 233
Cdd:PRK10908 176 ILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-250 |
5.71e-51 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 170.09 E-value: 5.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLnkyyEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGL-----EQISEGHIHIHQQDLAGLthaE 89
Cdd:PRK14247 4 IEIRDL----KVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKM---D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 90 LIQLRQRIGMIFQHFNLMSAKTVWENVALPLKVANYKKS--DIDTRVNEVLQLVGLSDKAQNY----PSQLSGGQKQRVG 163
Cdd:PRK14247 77 VIELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSkkELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 164 IARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLgiTIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFS 243
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
....*..
gi 2314388301 244 NPQQQIT 250
Cdd:PRK14247 235 NPRHELT 241
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-250 |
1.77e-50 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 168.87 E-value: 1.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQIS-----EGHIHIHQQDLAGlTHAE 89
Cdd:PRK14267 5 IETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYS-PDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 90 LIQLRQRIGMIFQHFNLMSAKTVWENVALPLKVANYKKS--DIDTRVNEVLQLVGLSDKAQN----YPSQLSGGQKQRVG 163
Cdd:PRK14267 80 PIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSkkELDERVEWALKKAALWDEVKDrlndYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 164 IARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLgiTIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFS 243
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
....*..
gi 2314388301 244 NPQQQIT 250
Cdd:PRK14267 238 NPEHELT 244
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
15-236 |
3.49e-50 |
|
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: 167.16 E-value: 3.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqgkSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAglthAELIQLR 94
Cdd:cd03265 1 IEVENLVKKYG----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03265 73 RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
15-236 |
5.79e-50 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 166.53 E-value: 5.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLagltHAELIQLR 94
Cdd:cd03263 1 LQIRNLTKTYK--KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEInqKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
34-182 |
5.82e-50 |
|
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: 163.97 E-value: 5.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDlagLTHAELIQLRQRIGMIFQHFNLMSAKTVW 113
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 114 ENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKA----QNYPSQLSGGQKQRVGIARALVHHPEILLCDEATS 182
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
22-236 |
2.80e-49 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 167.57 E-value: 2.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 22 KYYevqGKSVhALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAglthAELIQLRQRIGMIF 101
Cdd:TIGR01188 1 KVY---GDFK-AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV----REPRKVRRSIGIVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 102 QHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEAT 181
Cdd:TIGR01188 73 QYASVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPT 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 182 SALDPESTSVVLSLLKEINqKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:TIGR01188 153 TGLDPRTRRAIWDYIRALK-EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEG 206
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
33-236 |
7.48e-49 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 172.66 E-value: 7.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELiqlRQRIGMIFQHFNLMSAkTV 112
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL---RRQIGVVPQDTFLFSG-TI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 113 WENVAlplkvanYKKSDI-DTRVNEVLQLVGLSDKAQNYP-----------SQLSGGQKQRVGIARALVHHPEILLCDEA 180
Cdd:COG1132 431 RENIR-------YGRPDAtDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 181 TSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIREiCDQVVVIEKGEIVESG 236
Cdd:COG1132 504 TSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
16-236 |
8.13e-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: 162.22 E-value: 8.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 16 KIRNLNKYYevQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAEliqLRQ 95
Cdd:cd03214 1 EVENLSVGY--GGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE---LAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 96 RIGMIFQhfnlmsaktvwenvalplkvanykksdidtrvneVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEIL 175
Cdd:cd03214 74 KIAYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 176 LCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
17-232 |
8.84e-49 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 164.85 E-value: 8.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 17 IRNLNKYYevQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIhihqqdLAGltHAELIQLRQR 96
Cdd:PRK11247 15 LNAVSKRY--GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAG--TAPLAEARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 97 IGMIFQHFNLMSAKTVWENVALPLKvANYKksdidTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILL 176
Cdd:PRK11247 83 TRLMFQDARLLPWKKVIDNVGLGLK-GQWR-----DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 177 CDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEI 232
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
15-246 |
8.87e-49 |
|
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: 164.05 E-value: 8.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgkSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThaeliQLR 94
Cdd:cd03299 1 LKVENLSKDW-----KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP-----PEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03299 71 RDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-236 |
1.61e-48 |
|
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: 171.49 E-value: 1.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 5 GSQVAFSVPHIKIRNLNKYYEvqGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAG 84
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 85 LTHAeliQLRQRIGMIFQHFNLMSAkTVWENvalpLKVANYKKSDidTRVNEVLQLVGLSDKAQNYP-----------SQ 153
Cdd:COG4987 402 LDED---DLRRRIAVVPQRPHLFDT-TLREN----LRLARPDATD--EELWAALERVGLGDWLAALPdgldtwlgeggRR 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 154 LSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIrEICDQVVVIEKGEIV 233
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGL-ERMDRILVLEDGRIV 548
|
...
gi 2314388301 234 ESG 236
Cdd:COG4987 549 EQG 551
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
11-246 |
3.34e-48 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 165.14 E-value: 3.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 11 SVPHIKIRNLNKYYEV-QG-----KSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAG 84
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVkRGlfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 85 LTHAELIQLRQRIGMIFQ--HFNLMSAKTVWENVALPLKV-ANYKKSDIDTRVNEVLQLVGL-SDKAQNYPSQLSGGQKQ 160
Cdd:PRK11308 82 ADPEAQKLLRQKIQIVFQnpYGSLNPRKKVGQILEEPLLInTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 161 RVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWS 240
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 241
|
....*.
gi 2314388301 241 VFSNPQ 246
Cdd:PRK11308 242 IFNNPR 247
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
13-236 |
1.15e-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: 169.17 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEvQGKsvHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAeliQ 92
Cdd:COG4988 335 PSIELEDVSFSYP-GGR--PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPA---S 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQRIGMIFQHFNLMSAkTVWENVALplkvanYKKSDIDTRVNEVLQLVGLSDKAQNYP-----------SQLSGGQKQR 161
Cdd:COG4988 409 WRRQIAWVPQNPYLFAG-TIRENLRL------GRPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 162 VGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIREiCDQVVVIEKGEIVESG 236
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQG 553
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
16-231 |
1.93e-47 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 157.79 E-value: 1.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 16 KIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLaglTHAELIQLRQ 95
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI---AKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 96 RIGMIFQhfnlmsaktvwenvalplkvanykksdidtrvnevlqlvglsdkaqnypsqLSGGQKQRVGIARALVHHPEIL 175
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 176 LCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGE 231
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
13-245 |
2.18e-47 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 164.62 E-value: 2.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEVQgksvHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAglthaeLIQ 92
Cdd:PRK11607 18 PLLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS------HVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQR-IGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHH 171
Cdd:PRK11607 88 PYQRpINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 172 PEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNP 245
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
32-236 |
3.25e-47 |
|
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: 159.24 E-value: 3.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 32 HALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAglthaeliQLRQRIGMIFQHFNLMSAK- 110
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE--------KERKRIGYVPQRRSIDRDFp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 111 -TVWENVALPL-----KVANYKKSDIDtRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSAL 184
Cdd:cd03235 85 iSVRDVVLMGLyghkgLFRRLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 185 DPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKgEIVESG 236
Cdd:cd03235 164 DPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
15-236 |
1.28e-46 |
|
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: 157.98 E-value: 1.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqGKSvHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIqlR 94
Cdd:cd03224 1 LEVENLNAGY---GKS-QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENvalpLKVANY--KKSDIDTRVNEVLQLV-GLSDKAQNYPSQLSGGQKQRVGIARALVHH 171
Cdd:cd03224 75 AGIGYVPEGRRIFPELTVEEN----LLLGAYarRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 172 PEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-244 |
2.54e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 159.10 E-value: 2.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEV--QGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHaeLIQ 92
Cdd:PRK13633 5 IKCKNVSYKYESneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQRIGMIFQH-FNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHH 171
Cdd:PRK13633 83 IRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 172 PEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREiCDQVVVIEKGEIVESGEVWSVFSN 244
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
15-250 |
5.02e-46 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 157.64 E-value: 5.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqGKSVhALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQI-----SEGHIHIHQQDLAGlTHAE 89
Cdd:PRK14243 11 LRTENLNVYY---GSFL-AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYA-PDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 90 LIQLRQRIGMIFQHFNLMSaKTVWENVALPLKVANYKkSDIDTRVNEVLQLVGL----SDKAQNYPSQLSGGQKQRVGIA 165
Cdd:PRK14243 86 PVEVRRRIGMVFQKPNPFP-KSIYDNIAYGARINGYK-GDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 166 RALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLgiTIVLITHEMQVIREICD-----QVVVIEK----GEIVESG 236
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDmtaffNVELTEGggryGYLVEFD 241
|
250
....*....|....
gi 2314388301 237 EVWSVFSNPQQQIT 250
Cdd:PRK14243 242 RTEKIFNSPQQQAT 255
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
13-224 |
7.25e-46 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 156.51 E-value: 7.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQ 92
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQR-IGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHH 171
Cdd:PRK11629 84 LRNQkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 172 PEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQV 224
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-212 |
6.56e-45 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 154.63 E-value: 6.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGlTHAEliq 92
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGAD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 lrqRiGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHP 172
Cdd:COG4525 78 ---R-GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2314388301 173 EILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITH 212
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
15-236 |
6.57e-45 |
|
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: 153.29 E-value: 6.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIhqqdlAGL-THAELIQL 93
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-----DGFdVVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 94 RQRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEInQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
15-238 |
1.04e-44 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 154.46 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYE---VQGKSVH--ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAE 89
Cdd:PRK10419 4 LNVSGLSHHYAhggLSGKHQHqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 90 LIQLRQRIGMIFQhfNLMSA----KTVWENVALPLK-VANYKKSDIDTRVNEVLQLVGLSDK-AQNYPSQLSGGQKQRVG 163
Cdd:PRK10419 84 RKAFRRDIQMVFQ--DSISAvnprKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 164 IARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEV 238
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPV 236
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
36-245 |
1.44e-44 |
|
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: 156.41 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 36 NINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLagLTHAELIQL---RQRIGMIFQHFNLMSAKTV 112
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGIFLpphRRRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 113 WENVALPLKVAnyKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVV 192
Cdd:COG4148 95 RGNLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 193 LSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNP 245
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
33-246 |
1.46e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 154.47 E-value: 1.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAgLTHAELIQLRQRIGMIFQHF-NLMSAKT 111
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVRKTVGIVFQNPdDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 112 VWENVAL-PLKVAnYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTS 190
Cdd:PRK13639 96 VEEDVAFgPLNLG-LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 191 VVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:PRK13639 175 QIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-244 |
5.54e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 153.28 E-value: 5.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYeVQGKSVH--ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGlTHAELIQ 92
Cdd:PRK13637 3 IKIENLTHIY-MEGTPFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQRIGMIFQH--FNLMSaKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLS-----DKAqnyPSQLSGGQKQRVGIA 165
Cdd:PRK13637 81 IRKKVGLVFQYpeYQLFE-ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyedykDKS---PFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2314388301 166 RALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSN 244
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-230 |
1.07e-43 |
|
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: 150.66 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKY---YEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQ----DLAGLTH 87
Cdd:COG4778 5 LEVENLSKTftlHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 88 AELIQLRQR-IGMIFQHFNLM---SAKTVwenVALPLKVANYKKSDIDTRVNEVLQLVGLSDK-AQNYPSQLSGGQKQRV 162
Cdd:COG4778 85 REILALRRRtIGYVSQFLRVIprvSALDV---VAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 163 GIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKG 230
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-243 |
1.30e-43 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 152.09 E-value: 1.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 16 KIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLaglTHAELIQLRQ 95
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL---SEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 96 RIGMIFQH-FNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:PRK13635 82 QVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEmqvIREI--CDQVVVIEKGEIVESGEVWSVFS 243
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHD---LDEAaqADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
36-236 |
1.86e-43 |
|
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: 149.37 E-value: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 36 NINLDIPEGKIfGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLagLTHAELIQL---RQRIGMIFQHFNLMSAKTV 112
Cdd:cd03297 16 KIDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL--FDSRKKINLppqQRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 113 WENVALPLKVANYKKSDIdtRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVV 192
Cdd:cd03297 93 RENLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2314388301 193 LSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-238 |
4.15e-43 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 155.96 E-value: 4.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 11 SVPHIKIRNLNKYYevqGkSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIH--QQDLAGLTHA 88
Cdd:COG3845 2 MPPALELRGITKRF---G-GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkPVRIRSPRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 89 eliqLRQRIGMIFQHFNLMSAKTVWENVAL---PLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIA 165
Cdd:COG3845 78 ----IALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 166 RALVHHPEILLCDEATSALDPESTSVVLSLLKEInQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEV 238
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDT 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
32-250 |
4.18e-43 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 156.40 E-value: 4.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 32 HALKNINLDIPEGKIFGIIGKSGAGKSS----LLRTLNgleqiSEGHIHIHQQDLAGLTHAELIQLRQRIGMIFQHFN-- 105
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 106 LMSAKTVWENVALPLKV--ANYKKSDIDTRVNEVLQLVGLS-DKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATS 182
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 183 ALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQQQIT 250
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
15-236 |
6.66e-43 |
|
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: 147.75 E-value: 6.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAglthaELIQLR 94
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-----KNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDtrvnEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03268 72 RRIGALIEAPGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-238 |
7.13e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 150.64 E-value: 7.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThaeliqlR 94
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED-------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIG-----------MifqhfnlmsakTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVG 163
Cdd:COG4152 71 RRIGylpeerglypkM-----------KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 164 IARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEV 238
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSV 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
15-242 |
2.68e-42 |
|
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: 154.19 E-value: 2.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqgkSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQI--SEGHIHIH-------------- 78
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 79 ----------------QQDLAGLTHAELIQLRQRIGMIFQH-FNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLV 141
Cdd:TIGR03269 77 kvgepcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 142 GLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREIC 221
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|....
gi 2314388301 222 DQVVVIEKGEIVESG---EVWSVF 242
Cdd:TIGR03269 237 DKAIWLENGEIKEEGtpdEVVAVF 260
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
17-236 |
2.75e-42 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 150.64 E-value: 2.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 17 IRNLNKYYevqGKSVhALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLaglTHAElIQLRQr 96
Cdd:PRK11432 9 LKNITKRF---GSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRS-IQQRD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 97 IGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILL 176
Cdd:PRK11432 80 ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 177 CDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIG 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
15-233 |
4.38e-42 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 155.27 E-value: 4.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR 94
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 -QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:PRK10535 85 rEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREiCDQVVVIEKGEIV 233
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
15-236 |
1.36e-41 |
|
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: 153.96 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLthaELIQLR 94
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLI--LDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL---DVQAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAkTVWENVA----LPLKVANykksdidtrvnEVLQLVGLSDKAQNYP-----------SQLSGGQK 159
Cdd:TIGR03797 527 RQLGVVLQNGRLMSG-SIFENIAggapLTLDEAW-----------EAARMAGLAEDIRAMPmgmhtviseggGTLSGGQR 594
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 160 QRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKeinqKLGITIVLITHEMQVIREiCDQVVVIEKGEIVESG 236
Cdd:TIGR03797 595 QRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLE----RLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
33-245 |
1.70e-41 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 149.41 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR-QRIGMIFQHFNLMSAKT 111
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 112 VWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSV 191
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 192 VLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNP 245
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-243 |
3.18e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 145.76 E-value: 3.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLaGLTHAELIQLR 94
Cdd:PRK13636 6 LKVEELNYNY---SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQH--FNLMSAkTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSdKAQNYPSQ-LSGGQKQRVGIARALVHH 171
Cdd:PRK13636 82 ESVGMVFQDpdNQLFSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIE-HLKDKPTHcLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 172 PEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFS 243
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
33-246 |
6.28e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 145.16 E-value: 6.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDL-AGLTHAELIQLRQRIGMIFQhF--NLMSA 109
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLRKKVGIVFQ-FpeHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 110 KTVWENVAL-PLkvaNY--KKSDIDTRVNEVLQLVGLSDKA-QNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALD 185
Cdd:PRK13634 101 ETVEKDICFgPM---NFgvSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 186 PESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
15-246 |
7.72e-41 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 147.10 E-value: 7.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqgkSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAEliqlr 94
Cdd:PRK11000 4 VTLRNVTKAYG----DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVN---EVLQLVGLSDKAqnyPSQLSGGQKQRVGIARALVHH 171
Cdd:PRK11000 75 RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNqvaEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 172 PEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
24-246 |
8.17e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 144.51 E-value: 8.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 24 YEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQdlaGLTHAELIQLRQRIGMIFQH 103
Cdd:PRK13648 15 FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ---AITDDNFEKLRKHIGIVFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 104 -FNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATS 182
Cdd:PRK13648 92 pDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 183 ALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREiCDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
13-236 |
1.03e-40 |
|
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: 142.81 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYevqGKSvHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIq 92
Cdd:COG0410 2 PMLEVENLHAGY---GGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 lRQRIGM------IFQHFnlmsakTVWENVALPLKVANyKKSDIDTRVNEVLQL--VgLSDKAQNYPSQLSGGQKQRVGI 164
Cdd:COG0410 77 -RLGIGYvpegrrIFPSL------TVEENLLLGAYARR-DRAEVRADLERVYELfpR-LKERRRQRAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 165 ARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEG 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
15-246 |
1.70e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 143.59 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLnkYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIhqqDLAGLTHAELIQLR 94
Cdd:PRK13632 8 IKVENV--SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI---DGITISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQH-FNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:PRK13632 83 KKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEM-QVIreICDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMdEAI--LADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-250 |
1.73e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 143.26 E-value: 1.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 23 YYEVQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDL---AGLTHAELIQLRQRIGM 99
Cdd:PRK14246 17 YLYINDKAI--LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLRKEVGM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 100 IFQHFNLMSAKTVWENVALPLKVANYK-KSDIDTRVNEVLQLVGL----SDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:PRK14246 95 VFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKlgITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQQQIT 250
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-233 |
2.47e-40 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 139.49 E-value: 2.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqgkSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAEliQLR 94
Cdd:cd03216 1 LELRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--ARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQhfnlmsaktvwenvalplkvanykksdidtrvnevlqlvglsdkaqnypsqLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03216 75 AGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEInQKLGITIVLITHEMQVIREICDQVVVIEKGEIV 233
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
15-236 |
2.83e-40 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 141.19 E-value: 2.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELiqlR 94
Cdd:cd03245 3 IEFRNVSFSYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAkTVWENVALPLKVANykksdiDTRVNEVLQLVGLSDKAQNYP-----------SQLSGGQKQRVG 163
Cdd:cd03245 78 RNIGYVPQDVTLFYG-TLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 164 IARALVHHPEILLCDEATSALDPESTSVVLSLLKEInqKLGITIVLITHEMQVIrEICDQVVVIEKGEIVESG 236
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
15-235 |
2.97e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 142.95 E-value: 2.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLN-KYYEVQGKsvHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLaglTHAELIQL 93
Cdd:PRK13650 5 IEVKNLTfKYKEDQEK--YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---TEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 94 RQRIGMIFQH-FNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHP 172
Cdd:PRK13650 80 RHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 173 EILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIrEICDQVVVIEKGEiVES 235
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQ-VES 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-238 |
8.21e-40 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 146.70 E-value: 8.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 11 SVPHIKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLT--HA 88
Cdd:COG1129 1 AEPLLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 89 EliqlRQRIGMIFQHFNLMSAKTVWENVAL---PLK--VANYKKSDIDTRvnEVLQLVGLSDKAQNYPSQLSGGQKQRVG 163
Cdd:COG1129 77 Q----AAGIAIIHQELNLVPNLSVAENIFLgrePRRggLIDWRAMRRRAR--ELLARLGLDIDPDTPVGDLSVAQQQLVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 164 IARALVHHPEILLCDEATSALDPESTSVVLSLLKEInQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEV 238
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPV 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-250 |
1.15e-39 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 140.68 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYevqGKSvHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGL-----EQISEGHIHIHQQDLAGlTH 87
Cdd:PRK14239 4 PILQVSDLSVYY---NKK-KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYS-PR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 88 AELIQLRQRIGMIFQHFNLMSAkTVWENVALPLKVANYK-KSDIDTRVNEVLQLVGLSDKAQN--YPSQ--LSGGQKQRV 162
Cdd:PRK14239 79 TDTVDLRKEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKdKQVLDEAVEKSLKGASIWDEVKDrlHDSAlgLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 163 GIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLgiTIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVF 242
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
....*...
gi 2314388301 243 SNPQQQIT 250
Cdd:PRK14239 236 MNPKHKET 243
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-246 |
1.55e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 141.03 E-value: 1.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLagltHAELIQ-L 93
Cdd:PRK13647 5 IEVEDLHFRYK---DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV----NAENEKwV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 94 RQRIGMIFQH-FNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHP 172
Cdd:PRK13647 78 RSKVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 173 EILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVwSVFSNPQ 246
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDED 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
15-236 |
2.05e-39 |
|
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: 138.95 E-value: 2.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIhqqDLAGLTHAEliqlR 94
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF---DGKPLDIAA----R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03269 70 NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
27-233 |
2.10e-39 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 138.54 E-value: 2.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 27 QGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAglthaeLIQLRQRIGMIFQH--F 104
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK------AKERRKSIGYVMQDvdY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 105 NLMSaKTVWENVALPLKVAnykkSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSAL 184
Cdd:cd03226 83 QLFT-DSVREELLLGLKEL----DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2314388301 185 DPESTSVVLSLLKEInQKLGITIVLITHEMQVIREICDQVVVIEKGEIV 233
Cdd:cd03226 158 DYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-236 |
3.27e-39 |
|
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: 138.90 E-value: 3.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAeliQLR 94
Cdd:cd03254 3 IEFENVNFSYD---EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK---SLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAkTVWENVALPLKVANykksdiDTRVNEVLQLVGLSDKAQNYP-----------SQLSGGQKQRVG 163
Cdd:cd03254 77 SMIGVVLQDTFLFSG-TIMENIRLGRPNAT------DEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 164 IARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIREiCDQVVVIEKGEIVESG 236
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
13-236 |
4.26e-39 |
|
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: 138.40 E-value: 4.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEVQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLthaELIQ 92
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI---GLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQRIGMIFQHFNLMSAkTVWENVAlPLKVANykksdiDTRVNEVLQLVGLSDKAQNYP-----------SQLSGGQKQR 161
Cdd:cd03244 76 LRSRISIIPQDPVLFSG-TIRSNLD-PFGEYS------DEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 162 VGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEinQKLGITIVLITHEMQVIREiCDQVVVIEKGEIVESG 236
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
39-236 |
9.67e-39 |
|
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: 137.24 E-value: 9.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 39 LDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAEliqlrQRIGMIFQHFNLMSAKTVWENVAL 118
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-----RPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 119 PLkVANYKKSDID-TRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLK 197
Cdd:cd03298 94 GL-SPGLKLTAEDrQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 2314388301 198 EINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
32-240 |
2.08e-38 |
|
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: 140.25 E-value: 2.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 32 HALKnINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAglTHAELIQL---RQRIGMIFQHFNLMS 108
Cdd:TIGR02142 12 FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF--DSRKGIFLppeKRRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 109 AKTVWENValplkVANYKKSDIDTRV---NEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALD 185
Cdd:TIGR02142 89 HLSVRGNL-----RYGMKRARPSERRisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 186 PESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG---EVWS 240
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGpiaEVWA 221
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
15-250 |
2.12e-38 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 138.00 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQG-----KSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLaglTHAE 89
Cdd:PRK15112 5 LEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL---HFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 90 LIQLRQRIGMIFQ--HFNLMSAKTVWENVALPLKV-ANYKKSDIDTRVNEVLQLVGL-SDKAQNYPSQLSGGQKQRVGIA 165
Cdd:PRK15112 82 YSYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 166 RALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNP 245
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
....*
gi 2314388301 246 QQQIT 250
Cdd:PRK15112 242 LHELT 246
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
15-236 |
2.27e-38 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 137.84 E-value: 2.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvQGKSVHAlknINLDIPEGKIFGIIGKSGAGKSSLLRTLNGL---EQISEGHIHI--HQQDLAGLTHAE 89
Cdd:PRK09984 5 IRVEKLAKTFN-QHQALHA---VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELlgRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 90 LIQLRQRIGMIFQHFNLMSAKTVWENVAL------PL--KVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQR 161
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENVLIgalgstPFwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 162 VGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
15-232 |
2.72e-38 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 139.98 E-value: 2.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqGKsVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAEliqlr 94
Cdd:PRK11650 4 LKLQAVRKSYD--GK-TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 qR-IGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:PRK11650 76 -RdIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 174 ILLCDEATSALDPeSTSVVLSL-LKEINQKLGITIVLITHEmQVirE---ICDQVVVIEKGEI 232
Cdd:PRK11650 155 VFLFDEPLSNLDA-KLRVQMRLeIQRLHRRLKTTSLYVTHD-QV--EamtLADRVVVMNGGVA 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
33-248 |
3.36e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 137.81 E-value: 3.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThaELIQLRQRIGMIFQHFNL-MSAKT 111
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIRKLVGIVFQNPETqFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 112 VWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSV 191
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 192 VLSLLKEINQKlGITIVLITHEMQVIrEICDQVVVIEKGEIVESGEVWSVFSNPQQQ 248
Cdd:PRK13644 175 VLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-236 |
4.04e-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: 136.46 E-value: 4.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 21 NKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAgltHAELIQLRQRIGMI 100
Cdd:cd03252 5 HVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA---LADPAWLRRQVGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 101 FQHfNLMSAKTVWENVALPLKVANYKksdidtRVNEVLQLVGLSDKAQNYP-----------SQLSGGQKQRVGIARALV 169
Cdd:cd03252 82 LQE-NVLFNRSIRDNIALADPGMSME------RVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 170 HHPEILLCDEATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIREiCDQVVVIEKGEIVESG 236
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-236 |
4.50e-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: 136.21 E-value: 4.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThaeLIQLR 94
Cdd:cd03251 1 VEFKNVTFRYP--GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAkTVWENVAlplkvanYKKSDI-DTRVNEVLQLVGLSDKAQNYP-----------SQLSGGQKQRV 162
Cdd:cd03251 76 RQIGLVSQDVFLFND-TVAENIA-------YGRPGAtREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 163 GIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIREIcDQVVVIEKGEIVESG 236
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENA-DRIVVLEDGKIVERG 218
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-245 |
7.96e-38 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 136.01 E-value: 7.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNkyYEVQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR 94
Cdd:COG4559 2 LEAENLS--VRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 qriGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQ-NYPsQLSGGQKQRVGIARAL--VHH 171
Cdd:COG4559 78 ---AVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLaqLWE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2314388301 172 PE-----ILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNP 245
Cdd:COG4559 154 PVdggprWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDE 231
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
34-236 |
8.22e-38 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 135.44 E-value: 8.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThaeLIQLRQRIGMIFQH---FNlmsaK 110
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRRAIGVVPQDtvlFN----D 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 111 TVWENVALplkvANYKKSDIDtrVNEVLQLVGLSDKAQNYPSQ-----------LSGGQKQRVGIARALVHHPEILLCDE 179
Cdd:cd03253 90 TIGYNIRY----GRPDATDEE--VIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 180 ATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIREiCDQVVVIEKGEIVESG 236
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
36-249 |
1.27e-37 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 136.05 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 36 NINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLRQRIGMIFQHFNLMSAKTVWEN 115
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 116 VALPLKV-ANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLS 194
Cdd:PRK11831 105 VAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 195 LLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQQQI 249
Cdd:PRK11831 185 LISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRV 239
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
33-242 |
1.88e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 135.64 E-value: 1.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDL-AGLTHAELIQLRQRIGMIFQhF--NLMSA 109
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIRKKVGLVFQ-FpeSQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 110 KTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKA-QNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPES 188
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 189 TSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVF 242
Cdd:PRK13649 181 RKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
15-243 |
2.65e-37 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 134.51 E-value: 2.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNkyYEVQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR 94
Cdd:PRK13548 3 LEARNLS--VRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 qriGMIFQHFNLMSAKTVWENVAL---PLKVANYKKSDIdtrVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALV-- 169
Cdd:PRK13548 79 ---AVLPQHSSLSFPFTVEEVVAMgraPHGLSRAEDDAL---VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 170 ----HHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFS 243
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
34-248 |
3.28e-37 |
|
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: 133.75 E-value: 3.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLaglthaeliqlrQRIG----MIFQHFNLMSA 109
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI------------TEPGpdrmVVFQNYSLLPW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 110 KTVWENVALPLKVANY--KKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPE 187
Cdd:TIGR01184 69 LTVRENIALAVDRVLPdlSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 188 STSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSV-FSNPQQQ 248
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDR 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
34-213 |
3.41e-37 |
|
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: 132.99 E-value: 3.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLagltHAELIQLRQRIGMIFQHFNLMSAKTVW 113
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYRRRLAYLGHADGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 114 ENVALPLKVANYKKSDIDtrVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVL 193
Cdd:COG4133 94 ENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLA 171
|
170 180
....*....|....*....|
gi 2314388301 194 SLLKEINQKLGItIVLITHE 213
Cdd:COG4133 172 ELIAAHLARGGA-VLLTTHQ 190
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-250 |
6.59e-37 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 140.38 E-value: 6.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 8 VAFSVPHIKIRNLNKYYEVQG-------KSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQ 80
Cdd:PRK10261 307 VVDGEPILQVRNLVTRFPLRSgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 81 DLAGLTHAELIQLRQRIGMIFQ--HFNLMSAKTVWENVALPLKVANYKKSD-IDTRVNEVLQLVGL-SDKAQNYPSQLSG 156
Cdd:PRK10261 387 RIDTLSPGKLQALRRDIQFIFQdpYASLDPRQTVGDSIMEPLRVHGLLPGKaAAARVAWLLERVGLlPEHAWRYPHEFSG 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 157 GQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:PRK10261 467 GQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
250
....*....|....
gi 2314388301 237 EVWSVFSNPQQQIT 250
Cdd:PRK10261 547 PRRAVFENPQHPYT 560
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
15-245 |
1.18e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 133.77 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLaglTHAELIQLR 94
Cdd:PRK13652 4 IETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFN-LMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:PRK13652 78 KFVGLVFQNPDdQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNP 245
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-238 |
2.01e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 134.06 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKS-----------------VHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHI 77
Cdd:COG4586 2 IEVENLSKTYRVYEKEpglkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 78 hqqdlAGLT-HAELIQLRQRIGMIF-Q----HFNLmsakTVWENVALpLKvANYK--KSDIDTRVNEVLQLVGLSDKAQN 149
Cdd:COG4586 82 -----LGYVpFKRRKEFARRIGVVFgQrsqlWWDL----PAIDSFRL-LK-AIYRipDAEYKKRLDELVELLDLGELLDT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 150 YPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEK 229
Cdd:COG4586 151 PVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH 230
|
....*....
gi 2314388301 230 GEIVESGEV 238
Cdd:COG4586 231 GRIIYDGSL 239
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
31-236 |
3.14e-36 |
|
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: 131.12 E-value: 3.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 31 VHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLthaELIQLRQRIGMIFQHFNLMSAk 110
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL---NLRWLRSQIGLVSQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 111 TVWENVALPlkvanyKKSDIDTRVNEVLQLVGLSDKAQNYP-----------SQLSGGQKQRVGIARALVHHPEILLCDE 179
Cdd:cd03249 92 TIAENIRYG------KPDATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 180 ATSALDPESTSVVLSLLKEInqKLGITIVLITHEMQVIREiCDQVVVIEKGEIVESG 236
Cdd:cd03249 166 ATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQG 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
13-227 |
4.68e-36 |
|
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: 137.03 E-value: 4.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEVQGKsvhALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAeliQ 92
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRP---ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD---S 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQRIGMIFQHfNLMSAKTVWENVALPLKVANykksdiDTRVNEVLQLVGLSDKAQNYP-----------SQLSGGQKQR 161
Cdd:TIGR02857 394 WRDQIAWVPQH-PFLFAGTIAENIRLARPDAS------DAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 162 VGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIREiCDQVVVI 227
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
33-246 |
1.06e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 131.08 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGL---EQISEGHIHIhqqDLAGLTHAELIQLRQRIGMIFQH-FNLMS 108
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITV---DGITLTAKTVWDIREKVGIVFQNpDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 109 AKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPES 188
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 189 TSVVLSLLKEINQKLGITIVLITHEMQVIrEICDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-250 |
1.30e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 130.54 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 12 VPHIKIRNLNKYYEVQgksvHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQIS-----EGHIHIHQQDLAGlT 86
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYE-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 87 HAELIQLRQRIGMIFQHFNLMSAkTVWENVALPLKVANYK-KSDIDTRVNEVLQLVGLSDKAQN--YPS--QLSGGQKQR 161
Cdd:PRK14258 80 RVNLNRLRRQVSMVHPKPNLFPM-SVYDNVAYGVKIVGWRpKLEIDDIVESALKDADLWDEIKHkiHKSalDLSGGQQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 162 VGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEK-----GEIVESG 236
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFG 238
|
250
....*....|....
gi 2314388301 237 EVWSVFSNPQQQIT 250
Cdd:PRK14258 239 LTKKIFNSPHDSRT 252
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-238 |
1.53e-35 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 129.82 E-value: 1.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKS------------------VHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIH 76
Cdd:COG1134 5 IEVENVSKSYRLYHEPsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 77 IHqqdlaGlTHAELIQLrqriGMIFqHFNLmsakTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSD----KAQNYPS 152
Cdd:COG1134 85 VN-----G-RVSALLEL----GAGF-HPEL----TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDfidqPVKTYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 153 qlsgGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEI 232
Cdd:COG1134 150 ----GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
....*.
gi 2314388301 233 VESGEV 238
Cdd:COG1134 225 VMDGDP 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
15-238 |
2.48e-35 |
|
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: 129.05 E-value: 2.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLE-QISEGHIHIHQQDLAGlthAELIQL 93
Cdd:COG1119 4 LELRNVTVRRG--GKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRGG---EDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 94 RQRIGMI--FQHFNLMSAKTVWENVA--------LPLKVanykkSDIDT-RVNEVLQLVGLSDKAQNYPSQLSGGQKQRV 162
Cdd:COG1119 77 RKRIGLVspALQLRFPRDETVLDVVLsgffdsigLYREP-----TDEQReRARELLELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 163 GIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEV 238
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPK 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-243 |
4.01e-35 |
|
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: 134.54 E-value: 4.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNK-YYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQ----DLAGLTH 87
Cdd:TIGR03269 278 PIIKVRNVSKrYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 88 AELIQLRQRIGMIFQHFNLMSAKTVWENVA------LPLKVANYKKSdidtrvnEVLQLVGLSD-KAQN----YPSQLSG 156
Cdd:TIGR03269 358 DGRGRAKRYIGILHQEYDLYPHRTVLDNLTeaigleLPDELARMKAV-------ITLKMVGFDEeKAEEildkYPDELSE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 157 GQKQRVGIARALVHHPEILLCDEATSALDP-ESTSVVLSLLK---EINQklgiTIVLITHEMQVIREICDQVVVIEKGEI 232
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPiTKVDVTHSILKareEMEQ----TFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
250
....*....|.
gi 2314388301 233 VESGEVWSVFS 243
Cdd:TIGR03269 507 VKIGDPEEIVE 517
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
15-245 |
1.48e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 129.20 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLN-KYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHI------HQQDLAGLTH 87
Cdd:PRK13631 22 LRVKNLYcVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 88 AELI-------QLRQRIGMIFQHFNLMSAKTVWEN------VALPLKvanykKSDIDTRVNEVLQLVGL-SDKAQNYPSQ 153
Cdd:PRK13631 102 NPYSkkiknfkELRRRVSMVFQFPEYQLFKDTIEKdimfgpVALGVK-----KSEAKKLAKFYLNKMGLdDSYLERSPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 154 LSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEiNQKLGITIVLITHEMQVIREICDQVVVIEKGEIV 233
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
250
....*....|..
gi 2314388301 234 ESGEVWSVFSNP 245
Cdd:PRK13631 256 KTGTPYEIFTDQ 267
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
16-236 |
1.56e-34 |
|
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: 126.49 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 16 KIRNLNKYYevqGKSvHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGL-THAeliqlR 94
Cdd:TIGR03410 2 EVSNLNVYY---GQS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLpPHE-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIG--------MIFQHFnlmsakTVWENVALPLKVANYKKSDIDTRVNE---VLQLVgLSDKAQNypsqLSGGQKQRVG 163
Cdd:TIGR03410 73 ARAGiayvpqgrEIFPRL------TVEENLLTGLAALPRRSRKIPDEIYElfpVLKEM-LGRRGGD----LSGGQQQQLA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 164 IARALVHHPEILLCDEATSALDPestSVVLSL---LKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:TIGR03410 142 IARALVTRPKLLLLDEPTEGIQP---SIIKDIgrvIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASG 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-236 |
1.73e-34 |
|
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: 126.11 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKS------------------VHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIH 76
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 77 IHQQ-----DLAGLTHAELiqlrqrigmifqhfnlmsakTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDkAQNYP 151
Cdd:cd03220 81 VRGRvssllGLGGGFNPEL--------------------TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGD-FIDLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 152 -SQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKG 230
Cdd:cd03220 140 vKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKG 218
|
....*.
gi 2314388301 231 EIVESG 236
Cdd:cd03220 219 KIRFDG 224
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-236 |
2.29e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 132.64 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 2 VSFG--SQVAFSVPHIKIRNLNKYYEVQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQ 79
Cdd:PRK11160 324 VTFPttSTAAADQVSLTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 80 QDLAGLTHAeliQLRQRIGMIFQHFNLMSAkTVWENVALPLKVANykksdiDTRVNEVLQLVGLSDKAQNYPS------- 152
Cdd:PRK11160 402 QPIADYSEA---ALRQAISVVSQRVHLFSA-TLRDNLLLAAPNAS------DEALIEVLQQVGLEKLLEDDKGlnawlge 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 153 ---QLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIrEICDQVVVIEK 229
Cdd:PRK11160 472 ggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGL-EQFDRICVMDN 548
|
....*..
gi 2314388301 230 GEIVESG 236
Cdd:PRK11160 549 GQIIEQG 555
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
15-237 |
6.44e-34 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 125.08 E-value: 6.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqgksvHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDlagltHAELIQLR 94
Cdd:PRK10771 2 LKLTDITWLYH------HLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-----HTTTPPSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVAL---P-LKVANYKKSdidtRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVH 170
Cdd:PRK10771 71 RPVSMLFQENNLFSHLTVAQNIGLglnPgLKLNAAQRE----KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 171 HPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGE 237
Cdd:PRK10771 147 EQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
15-249 |
8.18e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 125.98 E-value: 8.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIhqqDLAGLTHAELIQLR 94
Cdd:PRK13642 5 LEVENLVFKYEKE-SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI---DGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQH-FNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:PRK13642 81 RKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREiCDQVVVIEKGEIVESGEVWSVFSNPQQQI 249
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMV 235
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
34-232 |
1.03e-33 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 122.71 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIhqqDLAGLTHAELIQLRQRIGMIFQHFNLMSAkTVW 113
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL---DGADISQWDPNELGDHVGYLPQDDELFSG-SIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 114 ENValplkvanykksdidtrvnevlqlvglsdkaqnypsqLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVL 193
Cdd:cd03246 94 ENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 2314388301 194 SLLKEInQKLGITIVLITHEMQVIrEICDQVVVIEKGEI 232
Cdd:cd03246 137 QAIAAL-KAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-246 |
2.25e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 125.33 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYY------EVQGksvhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHA 88
Cdd:PRK13641 3 IKFENVDYIYspgtpmEKKG-----LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 89 E-LIQLRQRIGMIFQhF--NLMSAKTVWENVALPLKvaNYKKSDIDTRVNEV--LQLVGLSDKAQNY-PSQLSGGQKQRV 162
Cdd:PRK13641 78 KnLKKLRKKVSLVFQ-FpeAQLFENTVLKDVEFGPK--NFGFSEDEAKEKALkwLKKVGLSEDLISKsPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 163 GIARALVHHPEILLCDEATSALDPESTSVVLSLLKEInQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVF 242
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
....
gi 2314388301 243 SNPQ 246
Cdd:PRK13641 234 SDKE 237
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
14-236 |
2.97e-33 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 129.75 E-value: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 14 HIKIRNLNKYYevQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThaeLIQL 93
Cdd:PRK11176 341 DIEFRNVTFTY--PGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT---LASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 94 RQRIGMIFQHFNLMSaKTVWENVALPLKvANYKKSDIDT--RVNEVLQLVGLSDKA------QNYPSqLSGGQKQRVGIA 165
Cdd:PRK11176 416 RNQVALVSQNVHLFN-DTIANNIAYART-EQYSREQIEEaaRMAYAMDFINKMDNGldtvigENGVL-LSGGQRQRIAIA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 166 RALVHHPEILLCDEATSALDPESTSVVLSLLKEInQKlGITIVLITHEMQVIrEICDQVVVIEKGEIVESG 236
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDEL-QK-NRTSLVIAHRLSTI-EKADEILVVEDGEIVERG 560
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
34-236 |
3.98e-33 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 129.55 E-value: 3.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELiqlRQRIGMIFQH---FNlmsaK 110
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---RAAIGIVPQDtvlFN----D 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 111 TVWENVAlplkvanYKKSDI-DTRVNEVLQLVGLSDKAQNYPSQ-----------LSGGQKQRVGIARALVHHPEILLCD 178
Cdd:COG5265 447 TIAYNIA-------YGRPDAsEEEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFD 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 179 EATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIREiCDQVVVIEKGEIVESG 236
Cdd:COG5265 520 EATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
15-234 |
4.16e-33 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 122.97 E-value: 4.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR 94
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 -QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:PRK10584 87 aKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREiCDQVVVIEKGEIVE 234
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-236 |
4.91e-33 |
|
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: 129.07 E-value: 4.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThaeLIQLR 94
Cdd:TIGR02203 331 VEFRNVTFRY--PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSaKTVWENVAlplkvanYKKSD--IDTRVNEVLQLVGLSDKAQNYP-----------SQLSGGQKQR 161
Cdd:TIGR02203 406 RQVALVSQDVVLFN-DTIANNIA-------YGRTEqaDRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQR 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 162 VGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIrEICDQVVVIEKGEIVESG 236
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTI-EKADRIVVMDDGRIVERG 549
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-236 |
1.51e-32 |
|
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: 121.67 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGK-----------------SVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHI 77
Cdd:cd03267 1 IEVSNLSKSYRVYSKepgligslkslfkrkyrEVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 78 hqqdlAGLT-HAELIQLRQRIGMIF-QHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLS 155
Cdd:cd03267 81 -----AGLVpWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 156 GGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVES 235
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
.
gi 2314388301 236 G 236
Cdd:cd03267 236 G 236
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-242 |
1.79e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 122.92 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGK-SVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLT-HAELIQ 92
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQRIGMIFQH-FNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKA-QNYPSQLSGGQKQRVGIARALVH 170
Cdd:PRK13643 82 VRKKVGVVFQFpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 171 HPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVF 242
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-241 |
2.98e-32 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 126.44 E-value: 2.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEVqgksVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQ 92
Cdd:PRK09700 4 PYISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LrqRIGMIFQHFNLMSAKTVWENV---ALPLK------VANYKKSDIdtRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVG 163
Cdd:PRK09700 80 L--GIGIIYQELSVIDELTVLENLyigRHLTKkvcgvnIIDWREMRV--RAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 164 IARALVHHPEILLCDEATSALDPESTSVVLSLLKEInQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSV 241
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
15-245 |
5.40e-32 |
|
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: 119.96 E-value: 5.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLaglTHAELIQlR 94
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI---TKLPMHK-R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIF--QHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHP 172
Cdd:cd03218 73 ARLGIGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 173 EILLCDEATSALDPESTSVVLSLLKEINQKlGITIvLIT-HEMQVIREICDQVVVIEKGEIVESGEVWSVFSNP 245
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKDR-GIGV-LITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
33-215 |
5.93e-32 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 120.57 E-value: 5.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGlTHAELiqlrqriGMIFQHFNLMSAKTV 112
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER-------GVVFQNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 113 WENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVV 192
Cdd:PRK11248 88 QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180
....*....|....*....|...
gi 2314388301 193 LSLLKEINQKLGITIVLITHEMQ 215
Cdd:PRK11248 168 QTLLLKLWQETGKQVLLITHDIE 190
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-245 |
1.32e-31 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 121.55 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 17 IRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLE----QISEGHIHIHQQDLAGLTHAELIQ 92
Cdd:COG4170 6 IRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 L-RQRIGMIFQHFN--LMSAKTVWENV--ALP--------LKVANYKKsdidTRVNEVLQLVGLSD-KA--QNYPSQLSG 156
Cdd:COG4170 86 IiGREIAMIFQEPSscLDPSAKIGDQLieAIPswtfkgkwWQRFKWRK----KRAIELLHRVGIKDhKDimNSYPHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 157 GQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESG 241
|
....*....
gi 2314388301 237 EVWSVFSNP 245
Cdd:COG4170 242 PTEQILKSP 250
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
33-244 |
1.35e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 120.50 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDL-AGLTH-AELIQLRQRIGMIFQ--HFNLMS 108
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKiKEVKRLRKEIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 109 aKTVWENVAL-PLKVANyKKSDIDTRVNEVLQLVGL-SDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDP 186
Cdd:PRK13645 106 -ETIEKDIAFgPVNLGE-NKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 187 ESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSN 244
Cdd:PRK13645 184 KGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
33-247 |
1.45e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 120.27 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELI-QLRQRIGMIFQH-FNLMSAK 110
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIrPVRKRIGMVFQFpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 111 TVWENVALPLKVANYKKSDIDTRVNEVLQLVGLS-DKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPEST 189
Cdd:PRK13646 102 TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 190 SVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQQ 247
Cdd:PRK13646 182 RQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
15-238 |
1.82e-31 |
|
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: 118.27 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQgksvHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLaglTHAELiqlr 94
Cdd:TIGR03740 1 LETKNLSKRFGKQ----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW---TRKDL---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENvalpLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:TIGR03740 70 HKIGSLIESPPLYENLTAREN----LKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEV 238
Cdd:TIGR03740 146 LILDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLGYQGKI 208
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
15-244 |
3.91e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 119.42 E-value: 3.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvQGKSVH--ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELI- 91
Cdd:PRK13651 3 IKVKNIVKIFN-KKLPTElkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 92 --------------------QLRQRIGMIFQ--HFNLMSAkTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDK-AQ 148
Cdd:PRK13651 82 kvleklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESyLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 149 NYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIE 228
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFK 239
|
250
....*....|....*.
gi 2314388301 229 KGEIVESGEVWSVFSN 244
Cdd:PRK13651 240 DGKIIKDGDTYDILSD 255
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
11-245 |
8.11e-31 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 119.44 E-value: 8.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 11 SVPHIKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGL---EQISEGHIHIHQQDLAGLTH 87
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 88 AELIQLR-QRIGMIFQHfnlmsaktvwenvalPLKVAN-YKKsdIDTRVNEVLQLVGLSDKAQN---------------- 149
Cdd:PRK09473 89 KELNKLRaEQISMIFQD---------------PMTSLNpYMR--VGEQLMEVLMLHKGMSKAEAfeesvrmldavkmpea 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 150 ------YPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQ 223
Cdd:PRK09473 152 rkrmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDK 231
|
250 260
....*....|....*....|..
gi 2314388301 224 VVVIEKGEIVESGEVWSVFSNP 245
Cdd:PRK09473 232 VLVMYAGRTMEYGNARDVFYQP 253
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-248 |
2.54e-30 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 121.39 E-value: 2.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 14 HIKIRNLnkYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIhqqDLAGLTHAELIQL 93
Cdd:COG4618 330 RLSVENL--TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL---DGADLSQWDREEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 94 RQRIGMIFQHFNLMSAkTVWENVA-LPlkvanykksDIDT-RVNEVLQLVGLSDKAQNYP-----------SQLSGGQKQ 160
Cdd:COG4618 405 GRHIGYLPQDVELFDG-TIAENIArFG---------DADPeKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 161 RVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIReICDQVVVIEKGEIVESG---E 237
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGprdE 552
|
250
....*....|.
gi 2314388301 238 VWSVFSNPQQQ 248
Cdd:COG4618 553 VLARLARPAAA 563
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-240 |
3.59e-30 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 118.05 E-value: 3.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 36 NINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLagLTHAELIQL---RQRIGMIFQHFNLMSAKTV 112
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL--FDAEKGICLppeKRRIGYVFQDARLFPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 113 WENvaLPLKVANYKKSDIDtrvnEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVV 192
Cdd:PRK11144 94 RGN--LRYGMAKSMVAQFD----KIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 193 LSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG---EVWS 240
Cdd:PRK11144 168 LPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGpleEVWA 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-236 |
3.67e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 116.83 E-value: 3.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 11 SVPHIKIRNLNKYYevqGKSVhALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHael 90
Cdd:PRK13537 4 SVAPIDFRNVEKRY---GDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 91 iQLRQRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVH 170
Cdd:PRK13537 77 -HARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 171 HPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-250 |
1.16e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 119.04 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 11 SVPHIKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKS----SLLRTLNGLEQI-SEGHIHIHQQDLAGL 85
Cdd:PRK15134 2 TQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 86 THAELIQLR-QRIGMIFQHfnlmsaktvwENVAL-PLKvanykksDIDTRVNEVLQL-------------------VGLS 144
Cdd:PRK15134 82 SEQTLRGVRgNKIAMIFQE----------PMVSLnPLH-------TLEKQLYEVLSLhrgmrreaargeilncldrVGIR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 145 DKAQ---NYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREIC 221
Cdd:PRK15134 145 QAAKrltDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLA 224
|
250 260
....*....|....*....|....*....
gi 2314388301 222 DQVVVIEKGEIVESGEVWSVFSNPQQQIT 250
Cdd:PRK15134 225 DRVAVMQNGRCVEQNRAATLFSAPTHPYT 253
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-250 |
1.20e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 119.57 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 17 IRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQ----------DLAGLT 86
Cdd:PRK10261 15 VENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 87 HAELIQLR-QRIGMIFQH--FNLMSAKTVWENVALPLKV-ANYKKSDIDTRVNEVLQLVGLSDKAQ---NYPSQLSGGQK 159
Cdd:PRK10261 95 AAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTilsRYPHQLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 160 QRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVW 239
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVE 254
|
250
....*....|.
gi 2314388301 240 SVFSNPQQQIT 250
Cdd:PRK10261 255 QIFHAPQHPYT 265
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
33-245 |
2.05e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 113.55 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHaeliQLRQRIGMI--FQHFNLMSAK 110
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG----HQIARMGVVrtFQHVRLFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 111 TVWEN--VA---------LP--LKVANYKKSDID--TRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEIL 175
Cdd:PRK11300 96 TVIENllVAqhqqlktglFSglLKTPAFRRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 176 LCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNP 245
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
11-250 |
3.66e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 113.10 E-value: 3.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 11 SVPHIKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQ-----DLAGL 85
Cdd:PRK11701 3 DQPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 86 THAELIQL-RQRIGMIFQHF--NLMSAKTVWENVALPLKVA---NYkkSDIDTRVNEVLQLVGL-SDKAQNYPSQLSGGQ 158
Cdd:PRK11701 79 SEAERRRLlRTEWGFVHQHPrdGLRMQVSAGGNIGERLMAVgarHY--GDIRATAGDWLERVEIdAARIDDLPTTFSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 159 KQRVGIARALVHHPEILLCDEATSALDpesTSV---VLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVES 235
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLD---VSVqarLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
250
....*....|....*
gi 2314388301 236 GEVWSVFSNPQQQIT 250
Cdd:PRK11701 234 GLTDQVLDDPQHPYT 248
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
15-250 |
3.92e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 114.45 E-value: 3.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGL----EQISEGHIHIHQQDLAGLTHAEL 90
Cdd:PRK11022 4 LNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 91 IQL-RQRIGMIFQH--FNLMSAKTVWENVALPLKV--ANYKKSDIDtRVNEVLQLVGLSDKA---QNYPSQLSGGQKQRV 162
Cdd:PRK11022 84 RNLvGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhqGGNKKTRRQ-RAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 163 GIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVF 242
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
....*...
gi 2314388301 243 SNPQQQIT 250
Cdd:PRK11022 243 RAPRHPYT 250
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
34-243 |
3.94e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 113.56 E-value: 3.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIhIHQQDLAGLTHAELIQLRQRIGMIFQHFNLMSAKT-V 112
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLDYSKRGLLALRQQVATVFQDPEQQIFYTdI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 113 WENVALPLKVANYKKSDIDTRVNEVLQLVglsdKAQNYPSQ----LSGGQKQRVGIARALVHHPEILLCDEATSALDPES 188
Cdd:PRK13638 96 DSDIAFSLRNLGVPEAEITRRVDEALTLV----DAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 189 TSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFS 243
Cdd:PRK13638 172 RTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
30-236 |
4.94e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 118.29 E-value: 4.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 30 SVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAeliQLRQRIGMIFQHFNLMSa 109
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH---YLHRQVALVGQEPVLFS- 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 110 KTVWENVALPLKVANykksdiDTRVNEVLQLVGLSDKAQNYP-----------SQLSGGQKQRVGIARALVHHPEILLCD 178
Cdd:TIGR00958 569 GSVRENIAYGLTDTP------DEEIMAAAKAANAHDFIMEFPngydtevgekgSQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 179 EATSALDPESTsvvlSLLKEINQKLGITIVLITHEMQVIREiCDQVVVIEKGEIVESG 236
Cdd:TIGR00958 643 EATSALDAECE----QLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-232 |
9.77e-29 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 109.83 E-value: 9.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 25 EVQGKSVH-ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQL--------RQ 95
Cdd:cd03215 6 EVRGLSVKgAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 96 RIGmifqhfnLMSAKTVWENVALPlkvanykksdidtrvnevlqlvglsdkaqnypSQLSGGQKQRVGIARALVHHPEIL 175
Cdd:cd03215 86 REG-------LVLDLSVAENIALS--------------------------------SLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 176 LCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEI 232
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
15-236 |
1.68e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 113.39 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIhqqdLAGLTHAELIQLR 94
Cdd:PRK13536 42 IDLAGVSKSY--GDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV----LGVPVPARARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKG-EIVESG 236
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGR 255
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
15-250 |
3.24e-28 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 110.56 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNkyYEVQGKSVHalkNINLDIPEGKIFGIIGKSGAGKS----SLLRTL-NGLEQISeGHIHIHQQDLAGlthae 89
Cdd:PRK10418 5 IELRNIA--LQAAQPLVH---GVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQTA-GRVLLDGKPVAP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 90 lIQLRQR-IGMIFQhfNLMSA----KTVWENVALPLKVANykKSDIDTRVNEVLQLVGLSDKA---QNYPSQLSGGQKQR 161
Cdd:PRK10418 74 -CALRGRkIATIMQ--NPRSAfnplHTMHTHARETCLALG--KPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 162 VGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSV 241
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
....*....
gi 2314388301 242 FSNPQQQIT 250
Cdd:PRK10418 229 FNAPKHAVT 237
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
34-230 |
3.52e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 115.29 E-value: 3.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEG-KIFgIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQqdlagltHAELIQLRQR----IGmifqhfNLMS 108
Cdd:COG4178 379 LEDLSLSLKPGeRLL-ITGPSGSGKSTLLRAIAGLWPYGSGRIARPA-------GARVLFLPQRpylpLG------TLRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 109 AktvwenVALPLKVANYKksdiDTRVNEVLQLVGLS------DKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATS 182
Cdd:COG4178 445 A------LLYPATAEAFS----DAELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2314388301 183 ALDPESTSVVLSLLKEinQKLGITIVLITHEmQVIREICDQVVVIEKG 230
Cdd:COG4178 515 ALDEENEAALYQLLRE--ELPGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-250 |
8.85e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 109.80 E-value: 8.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 28 GKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAG---LTHAELIQLRQRIGMIFQHF 104
Cdd:PRK14271 33 GKTV--LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGrsiFNYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 105 NLMSAkTVWENV-----ALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDE 179
Cdd:PRK14271 111 NPFPM-SIMDNVlagvrAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 180 ATSALDPESTSVVLSLLKEINQKLgiTIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQQQIT 250
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-237 |
1.28e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 109.02 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNK-YYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAEliql 93
Cdd:COG1101 2 LELKNLSKtFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 94 R-QRIGMIFQhfNLM----SAKTVWENVAL--------PLKVANyKKSDIDtRVNEVLQLVG------LSDKAqnypSQL 154
Cdd:COG1101 78 RaKYIGRVFQ--DPMmgtaPSMTIEENLALayrrgkrrGLRRGL-TKKRRE-LFRELLATLGlglenrLDTKV----GLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 155 SGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVE 234
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIIL 229
|
....*
gi 2314388301 235 --SGE 237
Cdd:COG1101 230 dvSGE 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
15-246 |
1.72e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 108.19 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThaelIQLR 94
Cdd:COG1137 4 LEAENLVKSY--GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP----MHKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGM--------IFQhfNLmsakTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIAR 166
Cdd:COG1137 76 ARLGIgylpqeasIFR--KL----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 167 ALVHHPEILLCDEATSALDPEStsvVLSlLKEINQKL---GITiVLIT-HemQViRE---ICDQVVVIEKGEIVESGEVW 239
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIA---VAD-IQKIIRHLkerGIG-VLITdH--NV-REtlgICDRAYIISEGKVLAEGTPE 221
|
....*..
gi 2314388301 240 SVFSNPQ 246
Cdd:COG1137 222 EILNNPL 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-236 |
2.44e-27 |
|
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: 106.48 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 18 RNLNkyYEVQGKSVHA----LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGL--EQISEGHIHIHQQDLaglthaELI 91
Cdd:cd03213 7 RNLT--VTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPL------DKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 92 QLRQRIGMIFQHFNLMSAKTVWENVALPLKVanykksdidtrvnevlqlvglsdkaqnypSQLSGGQKQRVGIARALVHH 171
Cdd:cd03213 79 SFRKIIGYVPQDDILHPTLTVRETLMFAAKL-----------------------------RGLSGGERKRVSIALELVSN 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 172 PEILLCDEATSALDPESTSVVLSLLKEINQkLGITIVLITHE-MQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
35-236 |
3.46e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 108.15 E-value: 3.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 35 KNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIhqqDLAGLTHAELIQLRQRIGMIFQHFNLMSAKTVWE 114
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL---DGEHIQHYASKEVARRIGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 115 NVAL------PLkVANYKKSDIDTrVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPES 188
Cdd:PRK10253 101 LVARgryphqPL-FTRWRKEDEEA-VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2314388301 189 TSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:PRK10253 179 QIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-236 |
4.34e-27 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 112.12 E-value: 4.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 14 HIKIRNLNKYYEvQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAeliQL 93
Cdd:PRK10790 340 RIDIDNVSFAYR-DDNLV--LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---VL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 94 RQRIGMIFQHFNLMsAKTVWENVALplkvanykKSDID-TRVNEVLQLVGLSDKAQNYP-----------SQLSGGQKQR 161
Cdd:PRK10790 414 RQGVAMVQQDPVVL-ADTFLANVTL--------GRDISeEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 162 VGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlgITIVLITHEMQVIREiCDQVVVIEKGEIVESG 236
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQG 556
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-236 |
5.85e-27 |
|
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: 105.09 E-value: 5.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKsvHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAeliqLR 94
Cdd:cd03247 1 LSINNVSFSYPEQEQ--QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAkTVWENVALplkvanykksdidtrvnevlqlvglsdkaqnypsQLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03247 75 SLISVLNQRPYLFDT-TLRNNLGR----------------------------------RFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIrEICDQVVVIEKGEIVESG 236
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGI-EHMDKILFLENGKIIMQG 178
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-250 |
1.51e-26 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 107.58 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 12 VPHIKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQ----ISEGHIHIHQQDLAGLTH 87
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 88 AELIQL-RQRIGMIFQH------------FNLMSAKTVWENVALPLKVANYKKsdidTRVNEVLQLVGLSDKA---QNYP 151
Cdd:PRK15093 81 RERRKLvGHNVSMIFQEpqscldpservgRQLMQNIPGWTYKGRWWQRFGWRK----RRAIELLHRVGIKDHKdamRSFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 152 SQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGE 231
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
250
....*....|....*....
gi 2314388301 232 IVESGEVWSVFSNPQQQIT 250
Cdd:PRK15093 237 TVETAPSKELVTTPHHPYT 255
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
15-236 |
3.25e-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: 103.65 E-value: 3.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAgltHAELIQLR 94
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS---TIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAkTVWENVALplkvanYKKSDiDTRVNEVLQlvgLSDKAQNypsqLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03369 82 SSLTIIPQDPTLFSG-TIRSNLDP------FDEYS-DEEIYGALR---VSEGGLN----LSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIREiCDQVVVIEKGEIVESG 236
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-231 |
3.50e-26 |
|
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: 103.70 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYE-VQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQqdlaglthaeliql 93
Cdd:cd03250 1 ISVEDASFTWDsGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 94 rqRIGMIFQHFNLMSAkTVWENV--ALPLkvanykksDIDtRVNEVLQLVGLSDKAQNYPSQ-----------LSGGQKQ 160
Cdd:cd03250 67 --SIAYVSQEPWIQNG-TIRENIlfGKPF--------DEE-RYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 161 RVGIARALVHHPEILLCDEATSALDPES-----TSVVLSLLKeiNQKlgiTIVLITHEMQVIREiCDQVVVIEKGE 231
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLLL--NNK---TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-236 |
5.71e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.78 E-value: 5.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 14 HIKIRNLnKYYEVQGKSvhALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLeqIS-EGHIHIHQQDLAGLthaELIQ 92
Cdd:PRK11174 349 TIEAEDL-EILSPDGKT--LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF--LPyQGSLKINGIELREL---DPES 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQRIGMIFQHFNLMSAkTVWENVALplkvanyKKSDI-DTRVNEVLQLVGLSD--KAQ----NYP-----SQLSGGQKQ 160
Cdd:PRK11174 421 WRKHLSWVGQNPQLPHG-TLRDNVLL-------GNPDAsDEQLQQALENAWVSEflPLLpqglDTPigdqaAGLSVGQAQ 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 161 RVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIREiCDQVVVIEKGEIVESG 236
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
15-236 |
6.54e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 104.33 E-value: 6.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAeliQLR 94
Cdd:PRK11231 3 LRTENLTVGY--GTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR---QLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVAlplkvanYKKS-----------DIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVG 163
Cdd:PRK11231 76 RRLALLPQHHLTPEGITVRELVA-------YGRSpwlslwgrlsaEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 164 IARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-232 |
7.22e-26 |
|
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: 103.32 E-value: 7.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 14 HIKIRNLNKYYEVQgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAeliQL 93
Cdd:cd03248 11 IVKFQNVTFAYPTR-PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK---YL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 94 RQRIGMIFQHFNLmSAKTVWENVALPLK-------VANYKKSDIDTRVNEVLQlvGLSDKAQNYPSQLSGGQKQRVGIAR 166
Cdd:cd03248 87 HSKVSLVGQEPVL-FARSLQDNIAYGLQscsfecvKEAAQKAHAHSFISELAS--GYDTEVGEKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 167 ALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLgiTIVLITHEMQVIrEICDQVVVIEKGEI 232
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-236 |
7.72e-26 |
|
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: 103.12 E-value: 7.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 27 QGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQ---ISEGHIHIHQQDLagltHAELIQlrQRIGMIFQH 103
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPR----KPDQFQ--KCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 104 FNLMSAKTVWENV--ALPLKVANYKKSDIDTRVNEVLQL--VGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDE 179
Cdd:cd03234 90 DILLPGLTVRETLtyTAILRLPRKSSDAIRKKRVEDVLLrdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 180 ATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
33-236 |
1.34e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 107.74 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAeliQLRQRIGMIFQHFNLMsAKTV 112
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA---SLRRNIAVVFQDAGLF-NRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 113 WENvalpLKVAnyKKSDIDTRVNEVLQLVGLSD----KAQNYP-------SQLSGGQKQRVGIARALVHHPEILLCDEAT 181
Cdd:PRK13657 426 EDN----IRVG--RPDATDEEMRAAAERAQAHDfierKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 182 SALDPESTSVVLSLLKEINQklGITIVLITHEMQVIREiCDQVVVIEKGEIVESG 236
Cdd:PRK13657 500 SALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-234 |
3.09e-25 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 101.57 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYY--------EVQ------GKSV-----HALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEG 73
Cdd:COG2401 6 PFFVLMRVTKVYssvldlseRVAivleafGVELrvverYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 74 HIHIHQQDLaglthaeliqlrqrigmifqhfNLMSAKTVWENValplkvanYKKSDIDTRVnEVLQLVGLSDkAQNY--- 150
Cdd:COG2401 86 AGCVDVPDN----------------------QFGREASLIDAI--------GRKGDFKDAV-ELLNAVGLSD-AVLWlrr 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 151 PSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIE-K 229
Cdd:COG2401 134 FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVgY 213
|
....*
gi 2314388301 230 GEIVE 234
Cdd:COG2401 214 GGVPE 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
17-232 |
4.39e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.92 E-value: 4.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 17 IRNLNKYYEvqGKSVhaLKNINLDIPEG-KIfGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQdlaglthaeliqlrQ 95
Cdd:COG0488 1 LENLSKSFG--GRPL--LDDVSLSINPGdRI-GLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG--------------L 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 96 RIGMIFQHFNLMSAKTVWENV---------------ALPLKVANYKKS-----------------DIDTRVNEVLQLVGL 143
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVldgdaelraleaeleELEAKLAEPDEDlerlaelqeefealggwEAEARAEEILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 144 SDKAQNYP-SQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINqklgITIVLITHEMQVIREICD 222
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP----GTVLVVSHDRYFLDRVAT 217
|
250
....*....|
gi 2314388301 223 QVVVIEKGEI 232
Cdd:COG0488 218 RILELDRGKL 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
25-212 |
1.07e-24 |
|
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: 104.75 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 25 EVQGKSVH------ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELiqlRQRIG 98
Cdd:TIGR02868 336 ELRDLSAGypgappVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---RRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 99 MIFQHFNLMSAkTVWENvalpLKVANYKKSDIDtrVNEVLQLVGLSDKAQNYP-----------SQLSGGQKQRVGIARA 167
Cdd:TIGR02868 413 VCAQDAHLFDT-TVREN----LRLARPDATDEE--LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2314388301 168 LVHHPEILLCDEATSALDPESTSVVLSLLKEINQklGITIVLITH 212
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITH 528
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
34-212 |
2.01e-24 |
|
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: 97.61 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHqqdlaglTHAELIQLRQRigmifqhfNLMSAKTVW 113
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP-------EGEDLLFLPQR--------PYLPLGTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 114 ENVALPLKvanykksdidtrvnevlqlvglsdkaqnypSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVL 193
Cdd:cd03223 82 EQLIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170
....*....|....*....
gi 2314388301 194 SLLKEinqkLGITIVLITH 212
Cdd:cd03223 132 QLLKE----LGITVISVGH 146
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
13-237 |
2.82e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 103.59 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQ 92
Cdd:PRK15439 10 PLLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LrqRIGMIFQHFNLMSAKTVWENVALPLKvanyKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHP 172
Cdd:PRK15439 86 L--GIYLVPQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 173 EILLCDEATSALDPESTSVVLSLLKEInQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGE 237
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-237 |
4.18e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 99.48 E-value: 4.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 21 NKYYEVQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELI--------Q 92
Cdd:PRK10575 16 NVSFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFArkvaylpqQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQRIGMifqhfnlmsakTVWENVAL---PLKVA--NYKKSDIDtRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARA 167
Cdd:PRK10575 94 LPAAEGM-----------TVRELVAIgryPWHGAlgRFGAADRE-KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 168 LVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGE 237
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
11-235 |
8.89e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 101.91 E-value: 8.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 11 SVPHIKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAEl 90
Cdd:PRK11288 1 SSPYLSFDGIGKTF----PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 91 iQLRQRIGMIFQHFNLMSAKTVWENV---ALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARA 167
Cdd:PRK11288 76 -ALAAGVAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 168 LVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVES 235
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-234 |
1.42e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQqdlaGLTHAELIQLR 94
Cdd:COG0488 316 LELEGLSKSYG--DKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE----TVKIGYFDQHQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QrigmifqhfNLMSAKTVWENvalplkVANYKKSDIDTRVNEVLQLVGLS-DKAQNYPSQLSGGQKQRVGIARALVHHPE 173
Cdd:COG0488 388 E---------ELDPDKTVLDE------LRDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 174 ILLCDEATSALDPESTSVVLSLLKEINqklGiTIVLITHEMQVIREICDQVVVIEKGEIVE 234
Cdd:COG0488 453 VLLLDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-214 |
1.68e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 99.04 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHihihqqdlaglthAEL---------IQLRQRIGMIFQH 103
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE-------------AWLfgqpvdagdIATRRRVGYMSQA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 104 FNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSA 183
Cdd:NF033858 348 FSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSG 427
|
170 180 190
....*....|....*....|....*....|.
gi 2314388301 184 LDPESTSVVLSLLKEINQKLGITIVLITHEM 214
Cdd:NF033858 428 VDPVARDMFWRLLIELSREDGVTIFISTHFM 458
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-238 |
2.82e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.40 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 1 MVsfGSQVAFSVPH---------IKIRNLNkyyeVQGKS-VHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQI 70
Cdd:COG3845 237 MV--GREVLLRVEKapaepgevvLEVENLS----VRDDRgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPP 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 71 SEGHIHIHQQDLAGLTHAELIQL--------RQRIGMIfqhfnlmSAKTVWENVAL------PLK---VANYKKsdIDTR 133
Cdd:COG3845 311 ASGSIRLDGEDITGLSPRERRRLgvayipedRLGRGLV-------PDMSVAENLILgryrrpPFSrggFLDRKA--IRAF 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 134 VNEVLQ-----LVGLSDKAqnypSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIV 208
Cdd:COG3845 382 AEELIEefdvrTPGPDTPA----RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVL 456
|
250 260 270
....*....|....*....|....*....|
gi 2314388301 209 LITHEMQVIREICDQVVVIEKGEIVesGEV 238
Cdd:COG3845 457 LISEDLDEILALSDRIAVMYEGRIV--GEV 484
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-233 |
3.65e-22 |
|
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: 97.20 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 30 SVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQIS--EGHIHIHQQDL--AGLTHAEliqlRQRIGMIFQHFN 105
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLkaSNIRDTE----RAGIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 106 LMSAKTVWENV------ALPLKVANYkkSDIDTRVNEVLQLVGLSDKAQNYP-SQLSGGQKQRVGIARALVHHPEILLCD 178
Cdd:TIGR02633 89 LVPELSVAENIflgneiTLPGGRMAY--NAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 179 EATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIV 233
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
34-243 |
4.26e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 93.75 E-value: 4.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQiSEGHIHIHQQDLAGLTHAELIQLRqriGMIFQHFNLMSAKTVW 113
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHR---AYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 114 ENVALPLKvANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVH-HPEI------LLCDEATSALDP 186
Cdd:COG4138 88 QYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvWPTInpegqlLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 187 ESTSVVLSLLKEINQkLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFS 243
Cdd:COG4138 167 AQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-236 |
5.01e-22 |
|
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: 97.78 E-value: 5.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 12 VPHIKIRNLNKYYEVQGKSvhALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLagltHAELI 91
Cdd:TIGR01257 926 VPGVCVKNLVKIFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLD 999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 92 QLRQRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHH 171
Cdd:TIGR01257 1000 AVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 172 PEILLCDEATSALDPESTSVVLSLLkeINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:TIGR01257 1080 AKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
31-231 |
5.19e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.92 E-value: 5.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 31 VHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQIS--EGHIHIHQQDLagltHAELIQLRQRIGMIFQHFNLMS 108
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEEL----QASNIRDTERAGIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 109 AK--TVWENVAL-----PLKVANYKKsdIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEAT 181
Cdd:PRK13549 94 VKelSVLENIFLgneitPGGIMDYDA--MYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2314388301 182 SALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGE 231
Cdd:PRK13549 172 ASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
33-237 |
9.49e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 96.32 E-value: 9.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLthaELIQLRQRIGMIFQHFNLMSaKTV 112
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPFLFS-DTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 113 WENVALPLKVAnyKKSDIDtrvnEVLQLVGLSDK----AQNYPSQ-------LSGGQKQRVGIARALVHHPEILLCDEAT 181
Cdd:PRK10789 406 ANNIALGRPDA--TQQEIE----HVARLASVHDDilrlPQGYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 182 SALDPESTSVVLSLLKEINQklGITIVLITHEMQVIREiCDQVVVIEKGEIVESGE 237
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGN 532
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
33-212 |
1.52e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 90.88 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIhihqqDLAGLTHAELIQLRQRIGMIFQHFN-LMSAKT 111
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV-----RWNGTPLAEQRDEPHENILYLGHLPgLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 112 VWENvalpLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSV 191
Cdd:TIGR01189 90 ALEN----LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|.
gi 2314388301 192 VLSLLKEINQKLGITIvLITH 212
Cdd:TIGR01189 166 LAGLLRAHLARGGIVL-LTTH 185
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
15-231 |
1.64e-21 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 89.04 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQqdlaglthaeliqlR 94
Cdd:cd03221 1 IELENLSKTYG--GKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS--------------T 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGmifqhfnlmsaktvwenvalplkvanykksdidtrvnevlqlvglsdkaqnYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:cd03221 63 VKIG---------------------------------------------------YFEQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 175 LLCDEATSALDPESTSVVLSLLKEINQklgiTIVLITHEMQVIREICDQVVVIEKGE 231
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
32-238 |
1.81e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.50 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 32 HALKNINLDIPEGKIFGIIGKSGAGKSSLLrtlNGLEQISEGHIHIHQQDLAGLTHAELIQLRQRIGMIFQHFNLMSAKT 111
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 112 VWE--NVALPLKV-ANYKKSDIDTRVNEVLQLVGLSDKAQ------NYPSQLSGGQKQRVGIARALVHHPEILLCDEATS 182
Cdd:TIGR00955 116 VREhlMFQAHLRMpRRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 183 ALDPESTSVVLSLLKEINQKlGITIVLITHE-MQVIREICDQVVVIEKGEIVESGEV 238
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSP 251
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-236 |
5.34e-21 |
|
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: 89.51 E-value: 5.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLnkYYEVQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLE--QISEGHIHIHQQDLAGLThaelIQ 92
Cdd:cd03217 1 LEIKDL--HVSVGGKEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLP----PE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQR--IGMIFQhfnlmsaktvwENVALP-LKVANYKKSdidtrVNEvlqlvglsdkaqnypsQLSGGQKQRVGIARALV 169
Cdd:cd03217 73 ERARlgIFLAFQ-----------YPPEIPgVKNADFLRY-----VNE----------------GFSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 170 HHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREI-CDQVVVIEKGEIVESG 236
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-245 |
7.23e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.60 E-value: 7.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNkyyeVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAEliq 92
Cdd:PRK09536 2 PMIDVSDLS----VEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQRIGMIFQHFNL---MSAKTVWENVALPLKVANYKKSDIDTR-VNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARAL 168
Cdd:PRK09536 75 ASRRVASVPQDTSLsfeFDVRQVVEMGRTPHRSRFDTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 169 VHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNP 245
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
34-218 |
1.10e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.78 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLrqrIGmifqHFNLM-SAKTV 112
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY---LG----HRNAMkPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 113 WENVALPLKVANYKKSDIDtrvnEVLQLVGLSDKAqNYPSQ-LSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSV 191
Cdd:PRK13539 91 AENLEFWAAFLGGEELDIA----AALEAVGLAPLA-HLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180 190
....*....|....*....|....*....|...
gi 2314388301 192 VLSLLKEINQKLGItIVLITH------EMQVIR 218
Cdd:PRK13539 166 FAELIRAHLAQGGI-VIAATHiplglpGARELD 197
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
13-233 |
1.17e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 89.55 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYevqGKsVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELiq 92
Cdd:PRK11614 4 VMLSFDKVSAHY---GK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQRIGMIFQHFNLMSAKTVWENVALPLKVAnyKKSDIDTRVNEVLQLVG-LSDKAQNYPSQLSGGQKQRVGIARALVHH 171
Cdd:PRK11614 78 MREAVAIVPEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 172 PEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIV 233
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
33-237 |
1.24e-20 |
|
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: 93.27 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAeliQLRQRIGMIFQHfNLMSAKTV 112
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRH---TLRQFINYLPQE-PYIFSGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 113 WENVALPLKvANYKKSDIDtrvnEVLQLVGLSDKAQNYP-----------SQLSGGQKQRVGIARALVHHPEILLCDEAT 181
Cdd:TIGR01193 565 LENLLLGAK-ENVSQDEIW----AACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 182 SALDPESTSVVLSLLKEINQKlgiTIVLITHEMQVIREIcDQVVVIEKGEIVESGE 237
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGS 691
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-246 |
5.85e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.64 E-value: 5.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 19 NLNKYYevQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLT-HAeliQLRQRI 97
Cdd:PRK10895 8 NLAKAY--KGRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHA---RARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 98 GMIFQHFNLMSAKTVWENVALPLKV-ANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILL 176
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 177 CDEATSALDPEStsvVLSlLKEINQKL---GITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:PRK10895 161 LDEPFAGVDPIS---VID-IKRIIEHLrdsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
33-243 |
9.33e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 87.63 E-value: 9.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLRQRIGMIFQHFNLMSAKTV 112
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 113 WENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVV 192
Cdd:PRK15056 102 MMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 193 LSLLKEINQKlGITIVLITHEMQVIREICDQVVVIeKGEIVESGEVWSVFS 243
Cdd:PRK15056 182 ISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFT 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
31-235 |
1.49e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.68 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 31 VHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLA--GLTHAEliqlRQRIGMIFQHFNLMS 108
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQ----EAGIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 109 AKTVWENVAL------PLKVANYKKsdIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATS 182
Cdd:PRK10762 93 QLTIAENIFLgrefvnRFGRIDWKK--MYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 183 ALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGE-IVES 235
Cdd:PRK10762 171 ALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQfIAER 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-238 |
1.73e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.31 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 25 EVQGKSV-HALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIqlRQRIGMI--- 100
Cdd:COG1129 258 EVEGLSVgGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAI--RAGIAYVped 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 101 FQHFNLMSAKTVWENVALPL--KVANY---KKSDIDTRVNEVLQLVGLsdKAQNyPSQ----LSGGQKQRVGIARALVHH 171
Cdd:COG1129 336 RKGEGLVLDLSIRENITLASldRLSRGgllDRRRERALAEEYIKRLRI--KTPS-PEQpvgnLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 172 PEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVesGEV 238
Cdd:COG1129 413 PKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV--GEL 476
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
44-246 |
3.01e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 85.75 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 44 GKIFGIIGKSGAGKSSLLRTLNGLEQiSEGHIHIHQQDLAGLTHAELIQLRqriGMIFQHFNLMSAKTVWENVALPLKvA 123
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHR---AYLSQQQTPPFAMPVFQYLTLHQP-D 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 124 NYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVH-HPEI------LLCDEATSALDPESTSVVLSLL 196
Cdd:PRK03695 97 KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLDVAQQAALDRLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2314388301 197 KEINQkLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:PRK03695 177 SELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
12-218 |
4.14e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 88.93 E-value: 4.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 12 VPHIKIRNLNKYYEVQgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHqqDLAGLTHAELI 91
Cdd:PTZ00265 380 IKKIQFKNVRFHYDTR-KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 92 QLRQRIGMIFQ-----------------------------------------------------HFNLMSaKTVWENVAL 118
Cdd:PTZ00265 457 WWRSKIGVVSQdpllfsnsiknnikyslyslkdlealsnyynedgndsqenknkrnscrakcagDLNDMS-NTTDSNELI 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 119 PLKvANYKKSDiDTRVNEVLQLVGLSDKAQNYP-----------SQLSGGQKQRVGIARALVHHPEILLCDEATSALDPE 187
Cdd:PTZ00265 536 EMR-KNYQTIK-DSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250 260 270
....*....|....*....|....*....|....*
gi 2314388301 188 STSVVlslLKEINQKLG----ITIVlITHEMQVIR 218
Cdd:PTZ00265 614 SEYLV---QKTINNLKGnenrITII-IAHRLSTIR 644
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
31-238 |
3.06e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 85.55 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 31 VHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAEliQLRQRIGMIFQHFNLMSAK 110
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALENGISMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 111 TVWENVAL---PLK--VANYKKSDIDTRvnEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALD 185
Cdd:PRK10982 89 SVMDNMWLgryPTKgmFVDQDKMYRDTK--AIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 186 PESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEV 238
Cdd:PRK10982 167 EKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPL 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
34-225 |
1.28e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.53 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAeliQLRQRIGMIFQHFNLMsAKTVW 113
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---IYRQQVSYCAQTPTLF-GDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 114 ENVALPLKVANyKKSDIDtRVNEVLQLVGLSDKAQNYP-SQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVV 192
Cdd:PRK10247 99 DNLIFPWQIRN-QQPDPA-IFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176
|
170 180 190
....*....|....*....|....*....|...
gi 2314388301 193 LSLLKEINQKLGITIVLITHEMQVIREiCDQVV 225
Cdd:PRK10247 177 NEIIHRYVREQNIAVLWVTHDKDEINH-ADKVI 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
34-236 |
1.28e-17 |
|
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: 84.61 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThaeLIQLRQRIGMIFQHFNLMSAkTVW 113
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFKITIIPQDPVLFSG-SLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 114 ENVAlPLkvANYKKSDIDTrvneVLQLVGLSDKAQNYPSQL-----------SGGQKQRVGIARALVHHPEILLCDEATS 182
Cdd:TIGR00957 1378 MNLD-PF--SQYSDEEVWW----ALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 183 ALDPESTSVVLSLLKeiNQKLGITIVLITHEMQVIREICdQVVVIEKGEIVESG 236
Cdd:TIGR00957 1451 AVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
31-235 |
3.11e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.53 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 31 VHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQIS--EGHIHIHQQDLA--GLTHAEliqlRQRIGMIFQHFNL 106
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRfkDIRDSE----ALGIVIIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 107 MSAKTVWENVALPLKVAnyKKSDID-----TRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEAT 181
Cdd:NF040905 90 IPYLSIAENIFLGNERA--KRGVIDwnetnRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 182 SALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVES 235
Cdd:NF040905 168 AALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
28-230 |
3.23e-17 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 79.30 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 28 GKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQdLAGLTHAELIQLRQRIGMIF--QHFN 105
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNK-NESEPSFEATRSRNRYSVAYaaQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 106 LMSAkTVWENVAL--PLKVANYKKSDIDTRVNEVLQLVGLSDKAQ--NYPSQLSGGQKQRVGIARALVHHPEILLCDEAT 181
Cdd:cd03290 90 LLNA-TVEENITFgsPFNKQRYKAVTDACSLQPDIDLLPFGDQTEigERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 182 SALDPEST-----SVVLSLLKEINQklgiTIVLITHEMQVIREiCDQVVVIEKG 230
Cdd:cd03290 169 SALDIHLSdhlmqEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
34-225 |
1.21e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.62 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIhIHQQDLaglthaeliqlrqRIGMIFQHFNLmsaktvw 113
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-KRNGKL-------------RIGYVPQKLYL------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 114 eNVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQ--NYPSQ-LSGGQKQRVGIARALVHHPEILLCDEATSALDPESTS 190
Cdd:PRK09544 79 -DTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHliDAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190
....*....|....*....|....*....|....*
gi 2314388301 191 VVLSLLKEINQKLGITIVLITHEMQVIREICDQVV 225
Cdd:PRK09544 158 ALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
34-233 |
1.24e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 81.15 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIhIHQQDL----------------------AGLTH-AEL 90
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDLivarlqqdpprnvegtvydfvaEGIEEqAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 91 I----QLRQRIGMIFQHFNLMSAKTVWENvalpLKVANYKKsdIDTRVNEVLQLVGLSDKAQnyPSQLSGGQKQRVGIAR 166
Cdd:PRK11147 98 LkryhDISHLVETDPSEKNLNELAKLQEQ----LDHHNLWQ--LENRINEVLAQLGLDPDAA--LSSLSGGWLRKAALGR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 167 ALVHHPEILLCDEATSALDPESTSVVLSLLKEINQklgiTIVLITHEMQVIREICDQVVVIEKGEIV 233
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
42-250 |
1.26e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 81.56 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 42 PEGKIfGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLA--GLThaeliQLRQRIGMIFQHFNLMSAkTVWENVAlP 119
Cdd:PLN03232 1261 PSEKV-GVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfGLT-----DLRRVLSIIPQSPVLFSG-TVRFNID-P 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 120 LKVANykksdiDTRVNEVLQLVGLSDKAQNYPSQL-----------SGGQKQRVGIARALVHHPEILLCDEATSALDPES 188
Cdd:PLN03232 1333 FSEHN------DADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 189 TSVVLSLLKEinQKLGITIVLITHEMQVIREiCDQVVVIEKGEIVEsgevwsvFSNPQQQIT 250
Cdd:PLN03232 1407 DSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLE-------YDSPQELLS 1458
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-188 |
1.32e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.32 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqGKsVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQLR 94
Cdd:NF033858 2 ARLEGVSHRY---GK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 -----QRIGMifqhfNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALV 169
Cdd:NF033858 78 iaympQGLGK-----NLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALI 152
|
170
....*....|....*....
gi 2314388301 170 HHPEILLCDEATSALDPES 188
Cdd:NF033858 153 HDPDLLILDEPTTGVDPLS 171
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-213 |
1.76e-16 |
|
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: 80.36 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 28 GKSV----HALKNINLD-IPEGKIfGIIGKSGAGKSSLLRTLNGLEQISEGHIhihqqdlaglthaeLIQLRQRIGMIFQ 102
Cdd:TIGR03719 11 SKVVppkkEILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKDFNGEA--------------RPQPGIKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 103 HFNLMSAKTVWENVALPLKV------------ANYKKSDID--------TRVNEVLQLVGLSD---------KAQNYP-- 151
Cdd:TIGR03719 76 EPQLDPTKTVRENVEEGVAEikdaldrfneisAKYAEPDADfdklaaeqAELQEIIDAADAWDldsqleiamDALRCPpw 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 152 ----SQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQklgiTIVLITHE 213
Cdd:TIGR03719 156 dadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTHD 217
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
15-243 |
4.35e-16 |
|
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: 76.87 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThaeLIQLR 94
Cdd:cd03288 20 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAkTVWENValplkvaNYKKSDIDTRVNEVLQLVGLSDKAQNYPSQL-----------SGGQKQRVG 163
Cdd:cd03288 95 SRLSIILQDPILFSG-SIRFNL-------DPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 164 IARALVHHPEILLCDEATSALDPESTSVVlsllkeinQKLGI------TIVLITHEMQVIREiCDQVVVIEKGEIVESGE 237
Cdd:cd03288 167 LARAFVRKSSILIMDEATASIDMATENIL--------QKVVMtafadrTVVTIAHRVSTILD-ADLVLVLSRGILVECDT 237
|
....*.
gi 2314388301 238 VWSVFS 243
Cdd:cd03288 238 PENLLA 243
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
37-212 |
5.09e-16 |
|
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: 79.41 E-value: 5.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 37 INLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQqdlaglthaeliqlRQRIGMIFQHfNLMSAKTVWENV 116
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA--------------KGKLFYVPQR-PYMTLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 117 ALPLKVANYKKSDI-DTRVNEVLQLVGLS---------DKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDP 186
Cdd:TIGR00954 536 IYPDSSEDMKRRGLsDKDLEQILDNVQLThilereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
170 180
....*....|....*....|....*.
gi 2314388301 187 ESTSVVLSLLKEInqklGITIVLITH 212
Cdd:TIGR00954 616 DVEGYMYRLCREF----GITLFSVSH 637
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-230 |
5.86e-16 |
|
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: 79.67 E-value: 5.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEvqGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLagLTHaeLIQLR 94
Cdd:TIGR01257 1938 LRLNELTKVYS--GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTN--ISDVH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEI 174
Cdd:TIGR01257 2012 QNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 175 LLCDEATSALDPEST----SVVLSLLKEinqklGITIVLITHEMQVIREICDQVVVIEKG 230
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARrmlwNTIVSIIRE-----GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
36-217 |
2.20e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.68 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 36 NINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIH-----IHQ------QDLAGLTHAELIQlrqrigmifqhf 104
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepIRRqrdeyhQDLLYLGHQPGIK------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 105 nlmSAKTVWENVALPLKVANYKKSDidtRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSAL 184
Cdd:PRK13538 87 ---TELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180 190
....*....|....*....|....*....|....
gi 2314388301 185 DPESTSVVLSLLKEINQKLGItIVLITH-EMQVI 217
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGM-VILTTHqDLPVA 193
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-236 |
2.45e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.47 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEVQGKSvHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGleqiseghihihqqDLAGLTHAELIq 92
Cdd:PLN03130 613 PAISIKNGYFSWDSKAER-PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG--------------ELPPRSDASVV- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQRIGMIFQHFNLMSAkTVWENV--ALPLKVANYKKSdID-TRVNEVLQLVGLSDKAQ--NYPSQLSGGQKQRVGIARA 167
Cdd:PLN03130 677 IRGTVAYVPQVSWIFNA-TVRDNIlfGSPFDPERYERA-IDvTALQHDLDLLPGGDLTEigERGVNISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 168 LVHHPEILLCDEATSALDPESTSVVLS--LLKEINQKlgiTIVLITHEMQVIREIcDQVVVIEKGEIVESG 236
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGK---TRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
44-220 |
3.30e-15 |
|
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: 73.30 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 44 GKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLA---GLTHAELIQLRQRIGMifqhfnlMSAKTVWENVALpl 120
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDfqrDSIARGLLYLGHAPGI-------KTTLSVLENLRF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 121 kvanYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEIN 200
Cdd:cd03231 97 ----WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHC 172
|
170 180
....*....|....*....|....*
gi 2314388301 201 QKLGItIVLITH-----EMQVIREI 220
Cdd:cd03231 173 ARGGM-VVLTTHqdlglSEAGAREL 196
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-212 |
6.30e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.54 E-value: 6.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLD-IPEGKIfGIIGKSGAGKSSLLRTLNGLEQISEGHIHIhqqdLAGLThaeliqlrqrIGMIFQHFNLMSAKTV 112
Cdd:PRK11819 23 LKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKEFEGEARP----APGIK----------VGYLPQEPQLDPEKTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 113 WENV--ALPLKV----------ANYKKSDID--------TRVNEVLQLVGLSD---------KAQNYP------SQLSGG 157
Cdd:PRK11819 88 RENVeeGVAEVKaaldrfneiyAAYAEPDADfdalaaeqGELQEIIDAADAWDldsqleiamDALRCPpwdakvTKLSGG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 158 QKQRVGIARALVHHPEILLCDEATSALDPEStsvVLSLLKEINQKLGiTIVLITH 212
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLHDYPG-TVVAVTH 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
150-226 |
2.06e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 74.68 E-value: 2.06e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 150 YPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREiCDQVVV 226
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1430
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-237 |
2.06e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.82 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 21 NKYYEVQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIhihqqdlagltHAEliqlrQRIGMI 100
Cdd:PTZ00243 665 DDFFELEPKVL--LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------WAE-----RSIAYV 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 101 FQHFNLMSAkTVWENVAL--PLKVANYKKSdidTRVNE----VLQLVG-----LSDKAQNypsqLSGGQKQRVGIARALV 169
Cdd:PTZ00243 727 PQQAWIMNA-TVRGNILFfdEEDAARLADA---VRVSQleadLAQLGGgleteIGEKGVN----LSGGQKARVSLARAVY 798
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2314388301 170 HHPEILLCDEATSALDPE-STSVVLSLLkeINQKLGITIVLITHEMQVIrEICDQVVVIEKGEIVESGE 237
Cdd:PTZ00243 799 ANRDVYLLDDPLSALDAHvGERVVEECF--LGALAGKTRVLATHQVHVV-PRADYVVALGDGRVEFSGS 864
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-234 |
2.78e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 24 YEVQ---GKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAglTHAELIQLRQRIGMI 100
Cdd:PRK09700 266 FEVRnvtSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVKKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 101 ---------FQHFNLMsaktvwENVALP--LKVANYKKS----------DIDTRVNEVLQLvGLSDKAQNYpSQLSGGQK 159
Cdd:PRK09700 344 tesrrdngfFPNFSIA------QNMAISrsLKDGGYKGAmglfhevdeqRTAENQRELLAL-KCHSVNQNI-TELSGGNQ 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 160 QRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVE 234
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-213 |
2.85e-14 |
|
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: 73.82 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqGKSVhALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIhqqdlaglthAELIQLr 94
Cdd:TIGR03719 323 IEAENLTKAF---GDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI----------GETVKL- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 qriGMIFQ-HFNLMSAKTVWENVALPLKVANYKKSDIDTRvnevlQLVGL-----SDKaQNYPSQLSGGQKQRVGIARAL 168
Cdd:TIGR03719 388 ---AYVDQsRDALDPNKTVWEEISGGLDIIKLGKREIPSR-----AYVGRfnfkgSDQ-QKKVGQLSGGERNRVHLAKTL 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2314388301 169 VHHPEILLCDEATSALDPEStsvvLSLLKEINQKLGITIVLITHE 213
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVET----LRALEEALLNFAGCAVVISHD 499
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
34-236 |
3.18e-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: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIhQQDLAGLTHAELIQ---LRQRIgmIFQH-FNLMSA 109
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-KGSVAYVPQQAWIQndsLRENI--LFGKaLNEKYY 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 110 KTVWENVALPLKVANYKKSDiDTRVNEvlqlvglsdKAQNypsqLSGGQKQRVGIARALVHHPEILLCDEATSALDpesT 189
Cdd:TIGR00957 731 QQVLEACALLPDLEILPSGD-RTEIGE---------KGVN----LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD---A 793
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 190 SVVLSLLKEINQKLGI----TIVLITHEMQVIREIcDQVVVIEKGEIVESG 236
Cdd:TIGR00957 794 HVGKHIFEHVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
32-244 |
5.46e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 73.00 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 32 HALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIhihqqDLAGltHAELIQLRQrigmifqhfNLMSAKT 111
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKG--SAALIAISS---------GLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 112 VWENVALPLKVANYKKSDIDTRVNEVLQLVGLSdKAQNYPSQ-LSGGQKQRVGIARALVHHPEILLCDEATSALDPESTS 190
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKIKEIIPEIIEFADIG-KFIYQPVKtYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 191 VVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVFSN 244
Cdd:PRK13545 181 KCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
15-232 |
5.49e-14 |
|
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: 71.42 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEVQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQIsEGHIHIhqqDLAGLTHAELIQLR 94
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQI---DGVSWNSVPLQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 95 QRIGMIFQHFNLMSAktvwenvALPLKVANYKKSDiDTRVNEVLQLVGLSDKAQNYPSQL-----------SGGQKQRVG 163
Cdd:cd03289 77 KAFGVIPQKVFIFSG-------TFRKNLDPYGKWS-DEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMC 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2314388301 164 IARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIREiCDQVVVIEKGEI 232
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
13-238 |
7.13e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.44 E-value: 7.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLnkyyEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLE--QISEGHIHIHQQDLAGLTHAEl 90
Cdd:CHL00131 6 PILEIKNL----HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 91 iqlRQRIGmIFQHFNLMSAKTVWEN-----VALPLKVANYKKSDID-----TRVNEVLQLVGLSDK--AQNYPSQLSGGQ 158
Cdd:CHL00131 81 ---RAHLG-IFLAFQYPIEIPGVSNadflrLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPSflSRNVNEGFSGGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 159 KQRVGIARALVHHPEILLCDEATSALDPESTSVVlslLKEINQ--KLGITIVLITHEMQVIREIC-DQVVVIEKGEIVES 235
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKII---AEGINKlmTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKT 233
|
...
gi 2314388301 236 GEV 238
Cdd:CHL00131 234 GDA 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-228 |
7.31e-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: 73.02 E-value: 7.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 14 HIKIRNLNKYYEVQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQiSEGHIHIhqqDLAGLTHAELIQL 93
Cdd:TIGR01271 1217 QMDVQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQI---DGVSWNSVTLQTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 94 RQRIGMIFQHFNLMSAkTVWENVAlplKVANYKksdiDTRVNEVLQLVGLSDKAQNYPSQL-----------SGGQKQRV 162
Cdd:TIGR01271 1291 RKAFGVIPQKVFIFSG-TFRKNLD---PYEQWS----DEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLM 1362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 163 GIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlgITIVLITHEMQVIREiCDQVVVIE 228
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN--CTVILSEHRVEALLE-CQQFLVIE 1425
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
34-234 |
7.50e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.85 E-value: 7.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThaeLIQLRQRIGMIFQHFNLMSAkTVW 113
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKVLGIIPQAPVLFSG-TVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 114 ENVAlPLKVANykksdiDTRVNEVLQLVGLSDKAQNYPSQL-----------SGGQKQRVGIARALVHHPEILLCDEATS 182
Cdd:PLN03130 1331 FNLD-PFNEHN------DADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 183 ALDPESTSVVLSLLKEinQKLGITIVLITHEMQVIREiCDQVVVIEKGEIVE 234
Cdd:PLN03130 1404 AVDVRTDALIQKTIRE--EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-244 |
1.09e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.32 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 12 VPHIKIRNLNKYYEVQgKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLngleqiseghihihqqdLAGLTHAEL- 90
Cdd:PLN03232 612 APAISIKNGYFSWDSK-TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM-----------------LGELSHAETs 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 91 -IQLRQRIGMIFQHFNLMSAkTVWENVAL--PLKVANYKKSDIDTRVNEVLQLVGLSDKAQ--NYPSQLSGGQKQRVGIA 165
Cdd:PLN03232 674 sVVIRGSVAYVPQVSWIFNA-TVRENILFgsDFESERYWRAIDVTALQHDLDLLPGRDLTEigERGVNISGGQKQRVSMA 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 166 RALVHHPEILLCDEATSALDPESTSVVL-SLLKEINQklGITIVLITHEMQVIREIcDQVVVIEKGEIVESGEVWSVFSN 244
Cdd:PLN03232 753 RAVYSNSDIYIFDDPLSALDAHVAHQVFdSCMKDELK--GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
15-238 |
1.87e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 70.53 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYevqgKSVHALKNINLDIPEGKIFGIIGKSGAGKSsllrtlngleqisEGHI--HIHQQDlAGLTH----- 87
Cdd:NF000106 14 VEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**-------------RGALpaHV*GPD-AGRRPwrf*t 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 88 --AELIQLRQRIGMifqHFNLMSAK----TVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQR 161
Cdd:NF000106 76 wcANRRALRRTIG*---HRPVR*GRresfSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 162 VGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEV 238
Cdd:NF000106 153 LDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
15-247 |
2.29e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 69.46 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYYEV----------------QGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIH 78
Cdd:PRK13546 5 VNIKNVTKEYRIyrtnkermkdalipkhKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 79 QQdlaglthaeliqlrqrIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQ 158
Cdd:PRK13546 85 GE----------------VSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 159 KQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGEV 238
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGEL 227
|
....*....
gi 2314388301 239 WSVFSNPQQ 247
Cdd:PRK13546 228 DDVLPKYEA 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
35-232 |
2.31e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.85 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 35 KNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIQL--------RQRIGMifqhfnL 106
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARglvylpedRQSSGL------Y 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 107 MSAKTVWENVAL-----PLKVANYKKSDIDTRVNEVLQlVGLSDKAQNYPSqLSGGQKQRVGIARALVHHPEILLCDEAT 181
Cdd:PRK15439 354 LDAPLAWNVCALthnrrGFWIKPARENAVLERYRRALN-IKFNHAEQAART-LSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 182 SALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEI 232
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-213 |
7.41e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.23 E-value: 7.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 10 FSVPH-------IKIRNLNKYYEVQGKSVhalKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIhqqDL 82
Cdd:PRK10522 311 FPRPQafpdwqtLELRNVTFAYQDNGFSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL---DG 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 83 AGLTHAELIQLRQRIGMIFQHFNLMSAKTVWEN-VALPLKVANYkksdidtrvnevLQLVGLSDKAQ---NYPS--QLSG 156
Cdd:PRK10522 385 KPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPEGkPANPALVEKW------------LERLKMAHKLEledGRISnlKLSK 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 157 GQKQRVGIARALVHHPEILLCDEATSALDP----ESTSVVLSLLKEinqkLGITIVLITHE 213
Cdd:PRK10522 453 GQKKRLALLLALAEERDILLLDEWAADQDPhfrrEFYQVLLPLLQE----MGKTIFAISHD 509
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
13-237 |
1.09e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 13 PHIKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLA------GLT 86
Cdd:PRK10762 247 PRLDKAPGEVRLKVDNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspqdGLA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 87 H--AELIQLRQRIGMIFQhfnlMSAKtvwENVALP-LKVANYKKSDIDTR-----VNEVLQLVGLSDKAQNYP-SQLSGG 157
Cdd:PRK10762 327 NgiVYISEDRKRDGLVLG----MSVK---ENMSLTaLRYFSRAGGSLKHAdeqqaVSDFIRLFNIKTPSMEQAiGLLSGG 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 158 QKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLlkeINQ--KLGITIVLITHEMQVIREICDQVVVIEKGEIveS 235
Cdd:PRK10762 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQL---INQfkAEGLSIILVSSEMPEVLGMSDRILVMHEGRI--S 474
|
..
gi 2314388301 236 GE 237
Cdd:PRK10762 475 GE 476
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
33-237 |
2.45e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.75 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 33 ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAE-------LIQLRQRIGMIFQHFN 105
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfaLVTEERRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 106 LmsaktvwENVALPLKVANYKKSD---IDTRVNEVLQLVGLSDKAQNyPSQ------LSGGQKQRVGIARALVHHPEILL 176
Cdd:PRK10982 343 I-------GFNSLISNIRNYKNKVgllDNSRMKSDTQWVIDSMRVKT-PGHrtqigsLSGGNQQKVIIGRWLLTQPEILM 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 177 CDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGE---IVESGE 237
Cdd:PRK10982 415 LDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLvagIVDTKT 477
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-232 |
4.74e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.69 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKYyEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGL-EQISEGHIHIHQQDLAGLTHAELIql 93
Cdd:TIGR02633 258 LEARNLTCW-DVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQAI-- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 94 RQRIGMI---FQHFNLMSAKTVWENVALPLKVANYKKSDIDTR-----VNEVLQLVGLSDKAQNYP-SQLSGGQKQRVGI 164
Cdd:TIGR02633 335 RAGIAMVpedRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAaelqiIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVL 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 165 ARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEI 232
Cdd:TIGR02633 415 AKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
34-246 |
5.29e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.03 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThaeLIQLRQRIGMIFQH---------- 103
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG---LRELRRQFSMIPQDpvlfdgtvrq 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 104 ----FNLMSAKTVW---ENVALPLKVANyKKSDIDTRVNEvlqlvGLSdkaqNYpsqlSGGQKQRVGIARALVHHPE-IL 175
Cdd:PTZ00243 1403 nvdpFLEASSAEVWaalELVGLRERVAS-ESEGIDSRVLE-----GGS----NY----SVGQRQLMCMARALLKKGSgFI 1468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 176 LCDEATSALDPestsvvlSLLKEINQKL-----GITIVLITHEMQVIREiCDQVVVIEKGEIVESGEVWSVFSNPQ 246
Cdd:PTZ00243 1469 LMDEATANIDP-------ALDRQIQATVmsafsAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
24-244 |
8.20e-11 |
|
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: 60.03 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 24 YEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLrtlngleqiseghihihQQDLAGLTHAELIQLRQRigmiFQH 103
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV-----------------NEGLYASGKARLISFLPK----FSR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 104 FNLMSaktvwenvalplkvanykksdIDtrvnevlQLVGLSDKAQNY------PSQLSGGQKQRVGIARALVHHPE--IL 175
Cdd:cd03238 60 NKLIF---------------------ID-------QLQFLIDVGLGYltlgqkLSTLSGGELQRVKLASELFSEPPgtLF 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2314388301 176 LCDEATSALDPESTSVVLSLLKEINQkLGITIVLITHEMQVIREiCDQVVVIEKGEIVESGEVwsVFSN 244
Cdd:cd03238 112 ILDEPSTGLHQQDINQLLEVIKGLID-LGNTVILIEHNLDVLSS-ADWIIDFGPGSGKSGGKV--VFSG 176
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
40-228 |
9.82e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 61.27 E-value: 9.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 40 DIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAglTHAELIQLRQRI---GMIFQHFNLMSAKTVWEN- 115
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS--YKPQYIKADYEGtvrDLLSSITKDFYTHPYFKTe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 116 VALPLKVanykKSDIDTRVNEvlqlvglsdkaqnypsqLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSL 195
Cdd:cd03237 99 IAKPLQI----EQILDREVPE-----------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180 190
....*....|....*....|....*....|...
gi 2314388301 196 LKEINQKLGITIVLITHEMQVIREICDQVVVIE 228
Cdd:cd03237 158 IRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-187 |
9.87e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.83 E-value: 9.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 35 KNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIhqqdlaGLThaeliqlrQRIGMIFQ-HFNLMSAKTVW 113
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------GET--------VKLAYVDQsRDALDPNKTVW 406
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2314388301 114 ENVALPLKVANYKKSDIDTRvnevlQLVGL-----SDKaQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPE 187
Cdd:PRK11819 407 EEISGGLDIIKVGNREIPSR-----AYVGRfnfkgGDQ-QKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
15-237 |
1.07e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 61.35 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNkyYEVQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLE--QISEGHIHIHQQDLAGLTHAEliQ 92
Cdd:PRK09580 2 LSIKDLH--VSVEDKAI--LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED--R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 93 LRQRIGMIFQHfnlmsaktvweNVALPlKVANykKSDIDTRVNEVLQLVG------------LSDKAQ--NYPSQL---- 154
Cdd:PRK09580 76 AGEGIFMAFQY-----------PVEIP-GVSN--QFFLQTALNAVRSYRGqepldrfdfqdlMEEKIAllKMPEDLltrs 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 155 -----SGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEI-NQKLGITIVliTHEMQVIREI-CDQVVVI 227
Cdd:PRK09580 142 vnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLrDGKRSFIIV--THYQRILDYIkPDYVHVL 219
|
250
....*....|
gi 2314388301 228 EKGEIVESGE 237
Cdd:PRK09580 220 YQGRIVKSGD 229
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
51-192 |
2.60e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.48 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 51 GKSGAGKSSLLRTLNGLEQISEGHIHIHqqdlaglTHAELIQLRQRIGMIFQHFNLMSAK-TVWENVALPLKVANYKKSD 129
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQID-------GKTATRGDRSRFMAYLGHLPGLKADlSTLENLHFLCGLHGRRAKQ 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 130 IDtrvNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVV 192
Cdd:PRK13543 117 MP---GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLV 176
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
34-213 |
3.45e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLagltHAELIQLRQRIGMIFQHFNLMSAKTVW 113
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 114 ENVALPLKVanykkSDIDTRVNEVLQLVGLsDKAQNYP-SQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVV 192
Cdd:PRK13540 93 ENCLYDIHF-----SPGAVGITELCRLFSL-EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|.
gi 2314388301 193 LSLLKEiNQKLGITIVLITHE 213
Cdd:PRK13540 167 ITKIQE-HRAKGGAVLLTSHQ 186
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
34-236 |
3.93e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 58.81 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGL--EQIS-EGHIHihqqdLAGLTHAELIQLRQR-IGMIFQHFNLMSA 109
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRteGNVSvEGDIH-----YNGIPYKEFAEKYPGeIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 110 KTVWENvalplkvanykksdIDTRvnevlqlvgLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPEST 189
Cdd:cd03233 98 LTVRET--------------LDFA---------LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2314388301 190 SVVLSLLKEINQKLGIT-IVLITHEMQVIREICDQVVVIEKGEIVESG 236
Cdd:cd03233 155 LEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
36-232 |
4.25e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 36 NINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQ-ISEGHIHIHQQDLAGLTHAELIqlRQRIGMIFQ---HFNLMSAKT 111
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAI--AQGIAMVPEdrkRDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 112 VWENVALplkvANYKKSDIDTRVNEVLQLVGLSDKAQNY----PS------QLSGGQKQRVGIARALVHHPEILLCDEAT 181
Cdd:PRK13549 358 VGKNITL----AALDRFTGGSRIDDAAELKTILESIQRLkvktASpelaiaRLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 182 SALDPESTSVVLSLlkeINQ--KLGITIVLITHEMQVIREICDQVVVIEKGEI 232
Cdd:PRK13549 434 RGIDVGAKYEIYKL---INQlvQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-234 |
6.76e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.20 E-value: 6.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 23 YYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIhqqDLAGLTHAELIQLRQRIGMIFQ 102
Cdd:COG4615 337 YPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL---DGQPVTADNREAYRQLFSAVFS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 103 HFNLMSaktvwenvalplKVANYKKSDIDTRVNEVLQLVGLSDK---AQNYPS--QLSGGQKQRVGIARALVHHPEILLC 177
Cdd:COG4615 414 DFHLFD------------RLLGLDGEADPARARELLERLELDHKvsvEDGRFSttDLSQGQRKRLALLVALLEDRPILVF 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 178 DEATSALDPESTSV----VLSLLKeinqKLGITIVLITHEMQVIrEICDQVVVIEKGEIVE 234
Cdd:COG4615 482 DEWAADQDPEFRRVfyteLLPELK----ARGKTVIAISHDDRYF-DLADRVLKMDYGKLVE 537
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
38-237 |
8.46e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 38 NLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHihiHQQDLAGLTHAELIQLRQRIGMIFQHFN--LMSA------ 109
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE---RQSQFSHITRLSFEQLQKLVSDEWQRNNtdMLSPgeddtg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 110 KTVWENVALPLKVANykksdidtRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPEST 189
Cdd:PRK10938 100 RTTAEIIQDEVKDPA--------RCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2314388301 190 SVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIVESGE 237
Cdd:PRK10938 172 QQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGE 218
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-230 |
8.47e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 57.64 E-value: 8.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 18 RNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQIS--EGHIHIHQQDLAglthaelIQLRQ 95
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLD-------KNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 96 RIGMIFQHFNLMSAKTVWEnvalPLKVANYkksdidtrvnevlqLVGLSDKaqnypsqlsggQKQRVGIARALVHHPEIL 175
Cdd:cd03232 80 STGYVEQQDVHSPNLTVRE----ALRFSAL--------------LRGLSVE-----------QRKRLTIGVELAAKPSIL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2314388301 176 LCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHE-MQVIREICDQVVVIEKG 230
Cdd:cd03232 131 FLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQpSASIFEKFDRLLLLKRG 185
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
34-231 |
8.96e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 58.71 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHihqqdlagltHAELIQLRQRIGMIFqhfnlmsAKTVW 113
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK----------HSGRISFSSQFSWIM-------PGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 114 ENVALPLKVANYkksdidtRVNEVLQLVGLSDKAQNYPSQ-----------LSGGQKQRVGIARALVHHPEILLCDEATS 182
Cdd:cd03291 116 ENIIFGVSYDEY-------RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 183 ALDPESTSVVLS--LLKEINQKlgiTIVLITHEMQVIReICDQVVVIEKGE 231
Cdd:cd03291 189 YLDVFTEKEIFEscVCKLMANK---TRILVTSKMEHLK-KADKILILHEGS 235
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-236 |
1.60e-09 |
|
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: 57.27 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 25 EVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSL----------LRTLNGLEQISEGHIHIHQQD----LAGLTHAel 90
Cdd:cd03270 2 IVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAYARQFLGQMDKPdvdsIEGLSPA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 91 IQLRQRIGMIFQHFNLMSAKTVWENVALPlkvanYKKSDIDTRVNeVLQLVGLS----DKAQNypsQLSGGQKQRVGIAR 166
Cdd:cd03270 80 IAIDQKTTSRNPRSTVGTVTEIYDYLRLL-----FARVGIRERLG-FLVDVGLGyltlSRSAP---TLSGGEAQRIRLAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 167 ----ALVHHPEILlcDEATSALDPESTSVVLSLLKEInQKLGITIVLITHEMQVIREiCDQVVVI------EKGEIVESG 236
Cdd:cd03270 151 qigsGLTGVLYVL--DEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA-ADHVIDIgpgagvHGGEIVAQG 226
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
34-241 |
2.74e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.14 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGleQISE----------GHIHIHQQDLAGLTHAELIQLRQRIGMIFQH 103
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGggaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 104 FNLMSAKtvwENVAL---PLKVANYKKSDIDTRV-NEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVH--------- 170
Cdd:PRK13547 95 AFAFSAR---EIVLLgryPHARRAGALTHRDGEIaWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 171 HPEILLCDEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSV 241
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
44-236 |
4.02e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.32 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 44 GKIFGIIGKSGAGKSSLLRTLNGLEQ--ISEGHIHI-----HQQDLAGLT--------HAELIQLRQriGMIFQHFnlms 108
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRIsgfpkKQETFARISgyceqndiHSPQVTVRE--SLIYSAF---- 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 109 aktvwenVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYP--SQLSGGQKQRVGIARALVHHPEILLCDEATSALDP 186
Cdd:PLN03140 980 -------LRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2314388301 187 ESTSVVLSLLKEiNQKLGITIVLITHEMQV-IREICDQVVVIEK-GEIVESG 236
Cdd:PLN03140 1053 RAAAIVMRTVRN-TVDTGRTVVCTIHQPSIdIFEAFDELLLMKRgGQVIYSG 1103
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
34-230 |
2.04e-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: 56.07 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHihqqdlagltHAELIQLRQRIGMIFqhfnlmsAKTVW 113
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK----------HSGRISFSPQTSWIM-------PGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 114 ENVALPLKVANYkksdidtRVNEVLQLVGLSDKAQNYPSQ-----------LSGGQKQRVGIARALVHHPEILLCDEATS 182
Cdd:TIGR01271 505 DNIIFGLSYDEY-------RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2314388301 183 ALDPESTSVVLS--LLKEINQKlgiTIVLITHEMQVIREiCDQVVVIEKG 230
Cdd:TIGR01271 578 HLDVVTEKEIFEscLCKLMSNK---TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-238 |
2.51e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 25 EVQGKSVHALKN-INLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLTHAELIqlrqRIGMIF-- 101
Cdd:PRK11288 259 RLDGLKGPGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAI----RAGIMLcp 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 102 -----------------------QHFN----LMSAKTVWENVALPLKVANYKKSDIDtrvnevlQLVGlsdkaqnypsQL 154
Cdd:PRK11288 335 edrkaegiipvhsvadninisarRHHLragcLINNRWEAENADRFIRSLNIKTPSRE-------QLIM----------NL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 155 SGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVIEKGEIve 234
Cdd:PRK11288 398 SGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI-- 474
|
....
gi 2314388301 235 SGEV 238
Cdd:PRK11288 475 AGEL 478
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
41-231 |
3.33e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 41 IPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIhihqqdlaglthaeLIQLR-----QRIG----MIFQHFnLMSAKT 111
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------------DPELKisykpQYIKpdydGTVEDL-LRSITD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 112 VWENvalplkvaNYKKSDIdtrvNEVLQLVGLSDKaqnYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSV 191
Cdd:PRK13409 427 DLGS--------SYYKSEI----IKPLQLERLLDK---NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2314388301 192 VLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEkGE 231
Cdd:PRK13409 492 VAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFE-GE 530
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
40-231 |
3.91e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.79 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 40 DIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGhihihqqdlaglthaeliqlrqrigmifqhfnlmsaktvweNVALP 119
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG-----------------------------------------EVDED 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 120 LKVAnYK----KSDIDTRV------------------NEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLC 177
Cdd:COG1245 401 LKIS-YKpqyiSPDYDGTVeeflrsantddfgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 178 DEATSALDPESTSVVLSLLKEINQKLGITIVLITHEMQVIREICDQVVVIEkGE 231
Cdd:COG1245 480 DEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE-GE 532
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
44-231 |
4.46e-08 |
|
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: 51.61 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 44 GKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHqqDLAGLTHAELIQLRQRIGMIFQHfnlmsaktvwenvalplkva 123
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYI--DGEDILEEVLDQLLLIIVGGKKA-------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 124 nykksdidtrvnevlqlvglsdkaqnypsQLSGGQKQRVGIARALVHHPEILLCDEATSALDPEST-----SVVLSLLKE 198
Cdd:smart00382 60 -----------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELRLLLL 110
|
170 180 190
....*....|....*....|....*....|....*...
gi 2314388301 199 INQKLGITIVLITHEMQVIREIC-----DQVVVIEKGE 231
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGPALlrrrfDRRIVLLLIL 148
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-236 |
4.58e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 2 VSFGSQVAFSVPHIKIRNLNKYY-EVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLLRTL----NGLEQISEGHIH 76
Cdd:TIGR00956 44 SDYQPTFPNALLKILTRGFRKLKkFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVIT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 77 IHqqdlaGLTHAElIQLRQRIGMIFQ-----HFNLMSAKTVWENVALPLKVAN-YKKSDIDTRVNEVLQLV----GLS-- 144
Cdd:TIGR00956 124 YD-----GITPEE-IKKHYRGDVVYNaetdvHFPHLTVGETLDFAARCKTPQNrPDGVSREEYAKHIADVYmatyGLSht 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 145 --DKAQN-YPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKLGIT-IVLITHEMQVIREI 220
Cdd:TIGR00956 198 rnTKVGNdFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTpLVAIYQCSQDAYEL 277
|
250
....*....|....*.
gi 2314388301 221 CDQVVVIEKGEIVESG 236
Cdd:TIGR00956 278 FDKVIVLYEGYQIYFG 293
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
25-225 |
6.44e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 53.00 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 25 EVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLL---------RTLNGLEQISEGH------------IHIhQQDLA 83
Cdd:cd03271 2 TLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLKKEQPGNHdrieglehidkvIVI-DQSPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 84 GLT----------------------------HAELIQLRQRIGMIFQHFNlMS---AKTVWENVAlplKVANYKKsdidt 132
Cdd:cd03271 81 GRTprsnpatytgvfdeirelfcevckgkryNRETLEVRYKGKSIADVLD-MTveeALEFFENIP---KIARKLQ----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 133 rvneVLQLVGLS--DKAQNYPSqLSGGQKQRVGIARALVH---HPEILLCDEATSALDPESTSVVLSLLKEINQKlGITI 207
Cdd:cd03271 152 ----TLCDVGLGyiKLGQPATT-LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTV 225
|
250
....*....|....*...
gi 2314388301 208 VLITHEMQVIReICDQVV 225
Cdd:cd03271 226 VVIEHNLDVIK-CADWII 242
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-238 |
8.97e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 8.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 21 NKYYEVQGKSVH--------ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGL---EQISeGHIHIHQQDL------- 82
Cdd:NF040905 255 EVVFEVKNWTVYhplhperkVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRsygRNIS-GTVFKDGKEVdvstvsd 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 83 ---AGLthAELIQLRQRIGMifqhfNLMsaKTVWENVALP----------------LKVANYKKSDIDTRVNEVLQLVGl 143
Cdd:NF040905 334 aidAGL--AYVTEDRKGYGL-----NLI--DDIKRNITLAnlgkvsrrgvideneeIKVAEEYRKKMNIKTPSVFQKVG- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 144 sdkaqnypsQLSGGQKQRVGIARALVHHPEILLCDEATSALDP----ESTSVVLSLLKEinqklGITIVLITHEMQVIRE 219
Cdd:NF040905 404 ---------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIINELAAE-----GKGVIVISSELPELLG 469
|
250
....*....|....*....
gi 2314388301 220 ICDQVVVIEKGEIVesGEV 238
Cdd:NF040905 470 MCDRIYVMNEGRIT--GEL 486
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
15-245 |
1.04e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKyyEVQGKSVH-----ALKNINLDIP-EGKIFGIIGKSGAGKSSLLRTLNG------------------LEQI 70
Cdd:PRK13409 66 ISIVNLPE--ELEEEPVHrygvnGFKLYGLPIPkEGKVTGILGPNGIGKTTAVKILSGelipnlgdyeeepswdevLKRF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 71 SEGHIHIHQQDLAG--LTHAELIQLRQRIGMIFQhfnlmsaKTVWENValplkvanyKKSDIDTRVNEVLQLVGLSDKAQ 148
Cdd:PRK13409 144 RGTELQNYFKKLYNgeIKVVHKPQYVDLIPKVFK-------GKVRELL---------KKVDERGKLDEVVERLGLENILD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 149 NYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQklGITIVLITHEMQVIREICDQVVVI- 227
Cdd:PRK13409 208 RDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAy 285
|
250
....*....|....*....
gi 2314388301 228 -EKGeivesgeVWSVFSNP 245
Cdd:PRK13409 286 gEPG-------AYGVVSKP 297
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
40-246 |
1.39e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.03 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 40 DIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEghihihqqdlaglthaeliqlrqrigmifqhfnlmsaktvwENVALP 119
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNG-----------------------------------------DNDEWD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 120 LKVANYKKSDIDtrvnevlqlvglsdkaqnypsqLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEI 199
Cdd:cd03222 60 GITPVYKPQYID----------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2314388301 200 NQKLGITIVLITHEMQVIREICDQVVVIEkgeivesGE--VWSVFSNPQ 246
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIHVFE-------GEpgVYGIASQPK 159
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-230 |
1.67e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 18 RNLNkyYEVQGKSVH--ALKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGL---------EQISEGHI----------H 76
Cdd:TIGR00956 763 RNLT--YEVKIKKEKrvILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERvttgvitggDRLVNGRPldssfqrsigY 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 77 IHQQDLagltHAELIQLRQriGMIFQHFnlmsaktvwenVALPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYPSQ-LS 155
Cdd:TIGR00956 841 VQQQDL----HLPTSTVRE--SLRFSAY-----------LRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEgLN 903
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2314388301 156 GGQKQRVGIARALVHHPEILL-CDEATSALDPESTSVVLSLLKEInQKLGITIVLITHEMQ-VIREICDQVVVIEKG 230
Cdd:TIGR00956 904 VEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPSaILFEEFDRLLLLQKG 979
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
36-232 |
1.92e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 36 NINLDIPEGKIFGIIGKSGAGKSSLLRTLNG-LEQiSEGHIHIH--------QQD-------------LAGltHAEL--- 90
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGdLEP-SAGNVSLDpnerlgklRQDqfafeeftvldtvIMG--HTELwev 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 91 IQLRQRI----------GMifqhfnlmsaktvweNVA-LPLKVANYKKSDIDTRVNEVLQLVGLSDKAQNYP-SQLSGGQ 158
Cdd:PRK15064 96 KQERDRIyalpemseedGM---------------KVAdLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLmSEVAPGW 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 159 KQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQklgiTIVLITHEMQVIREICDQVVVIEKGEI 232
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNS----TMIIISHDRHFLNSVCTHMADLDYGEL 230
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
15-245 |
2.24e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.48 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 15 IKIRNLNKyyEVQGKSVH-----ALKNINLDIP-EGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHihqqdlAGLTHA 88
Cdd:COG1245 66 ISIVNLPE--ELEEDPVHrygenGFRLYGLPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD------EEPSWD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 89 ELIQlRQRIGMIFQHFNLMSAKTVweNVA--------LPlKVANYKKSDIDTRVNE------VLQLVGLSDKAQNYPSQL 154
Cdd:COG1245 138 EVLK-RFRGTELQDYFKKLANGEI--KVAhkpqyvdlIP-KVFKGTVRELLEKVDErgkldeLAEKLGLENILDRDISEL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 155 SGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVI--EKGei 232
Cdd:COG1245 214 SGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILygEPG-- 290
|
250
....*....|...
gi 2314388301 233 vesgeVWSVFSNP 245
Cdd:COG1245 291 -----VYGVVSKP 298
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
49-196 |
1.10e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 49 IIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQDLAGLThaeliqlRQRIGMIFQHFNLMSAKTVWENVALPLKVANYKks 128
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-------KPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSA-- 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 129 didTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTSVVLSLL 196
Cdd:PRK13541 102 ---ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
34-242 |
1.13e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIH---------IHQQDLAGLTHA---------ELIQLRQ 95
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgnwqlawVNQETPALPQPAleyvidgdrEYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 96 RIGMIFQHFNLMSAKTVWEnvalplKVANYKKSDIDTRVNEVLQLVGLSDKAQNYP-SQLSGGQKQRVGIARALVHHPEI 174
Cdd:PRK10636 97 QLHDANERNDGHAIATIHG------KLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2314388301 175 LLCDEATSALDPEStsvVLSLLKEINQKLGiTIVLITHEMQVIREICDQVVVIEKGEIVESGEVWSVF 242
Cdd:PRK10636 171 LLLDEPTNHLDLDA---VIWLEKWLKSYQG-TLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSF 234
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
26-60 |
1.25e-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: 50.40 E-value: 1.25e-06
10 20 30
....*....|....*....|....*....|....*
gi 2314388301 26 VQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSL 60
Cdd:TIGR00630 4 VRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
21-60 |
1.44e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.02 E-value: 1.44e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2314388301 21 NKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSL 60
Cdd:COG0178 3 MDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
21-60 |
2.58e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 49.30 E-value: 2.58e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2314388301 21 NKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSL 60
Cdd:PRK00349 3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-217 |
3.58e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 17 IRNLNkyYEVQGKSVhaLKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIHIHQQdlagLTHAELIQLRQr 96
Cdd:PRK11147 322 MENVN--YQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFDQHRA- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 97 igmifqhfNLMSAKTVWENVAlplkvanYKKSDIDtrVNEV-------LQLVGLSDKAQNYPSQ-LSGGQKQRVGIARAL 168
Cdd:PRK11147 393 --------ELDPEKTVMDNLA-------EGKQEVM--VNGRprhvlgyLQDFLFHPKRAMTPVKaLSGGERNRLLLARLF 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2314388301 169 VHHPEILLCDEATSALDPEStsvvLSLLKEINQKLGITIVLITHEMQVI 217
Cdd:PRK11147 456 LKPSNLLILDEPTNDLDVET----LELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
134-186 |
7.46e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 7.46e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2314388301 134 VNEVLQLVGLSDKAQNYPSQ-LSGGQKQRVGIARALVHHPEILLCDEATSALDP 186
Cdd:PRK10938 381 AQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
11-61 |
8.05e-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: 47.70 E-value: 8.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 11 SVPHIKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLL 61
Cdd:TIGR00630 601 EVPAERRPGNGKFLTLKGARENNLKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
14-231 |
1.61e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 45.34 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 14 HIKIRNLNKYYEVQGKSVHALKNINldipegkIFGIIGKSGAGKSSLL---------RTLNGLEQISEGHIHIHQQDLAG 84
Cdd:cd03279 5 KLELKNFGPFREEQVIDFTGLDNNG-------LFLICGPTGAGKSTILdaityalygKTPRYGRQENLRSVFAPGEDTAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 85 LTHAelIQLRQRIGMIFQHFNLmSAKTVWENVALPL-KVANYKKSDIDT-------RVNEVLQLvGLSDKAQNypsqlSG 156
Cdd:cd03279 78 VSFT--FQLGGKKYRVERSRGL-DYDQFTRIVLLPQgEFDRFLARPVSTlsggetfLASLSLAL-ALSEVLQN-----RG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 157 GqkqrvgiARAlvhhpEILLCDEATSALDPESTSVVLSLLKEINQkLGITIVLITHeMQVIREICDQVVVIEKGE 231
Cdd:cd03279 149 G-------ARL-----EALFIDEGFGTLDPEALEAVATALELIRT-ENRMVGVISH-VEELKERIPQRLEVIKTP 209
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
12-61 |
2.07e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.60 E-value: 2.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2314388301 12 VPHIKIRNLNKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSLL 61
Cdd:PRK00349 603 VPKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
44-185 |
2.59e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 44 GKIFGIIGKSGAGKSSLLR--TLNGLEQISEGH--IHIHQQ----DLAGL-----THAELIQLRQRIGMIFQHFNLMSAK 110
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRymAMHAIDGIPKNCqiLHVEQEvvgdDTTALqcvlnTDIERTQLLEEEAQLVAQQRELEFE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 111 TVWENVALPLKvANYKKSDIDTRVNEVLQ-----------------LVGLS---DKAQNYPSQLSGGQKQRVGIARALVH 170
Cdd:PLN03073 283 TETGKGKGANK-DGVDKDAVSQRLEEIYKrlelidaytaearaasiLAGLSftpEMQVKATKTFSGGWRMRIALARALFI 361
|
170
....*....|....*
gi 2314388301 171 HPEILLCDEATSALD 185
Cdd:PLN03073 362 EPDLLLLDEPTNHLD 376
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-227 |
2.79e-05 |
|
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: 45.05 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 39 LDIP-EGKIFGIIGKSGAGKSSLLRTLNGlEQISEGHIHIHQQDLAG-LTH---AEL----IQLRQ---RIGMIFQHFNL 106
Cdd:cd03236 20 LPVPrEGQVLGLVGPNGIGKSTALKILAG-KLKPNLGKFDDPPDWDEiLDEfrgSELqnyfTKLLEgdvKVIVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 107 MSaKTVWENVALPLKvanykKSDIDTRVNEVLQLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDP 186
Cdd:cd03236 99 IP-KAVKGKVGELLK-----KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2314388301 187 ESTSVVLSLLKEINQKlGITIVLITHEMQVIREICDQVVVI 227
Cdd:cd03236 173 KQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
30-225 |
3.38e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 30 SVHALKNINLDIPEGKIFGIIGKSGAGKSSLLR-TL-----NGLEQISEGHIHIHQQDLAGLTHA--------------- 88
Cdd:PRK00635 607 TKHNLKDLTISLPLGRLTVVTGVSGSGKSSLINdTLvpaveEFIEQGFCSNLSIQWGAISRLVHItrdlpgrsqrsiplt 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 89 ------ELIQL------RQRIGMIFQHFNL------------MSAKTVWEN---------------------------VA 117
Cdd:PRK00635 687 yikafdDLRELfaeqprSKRLGLTKSHFSFntplgacaecqgLGSITTTDNrtsipcpsclgkrflpqvlevrykgknIA 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 118 LPLKVANY--KKSDIDT-RVNEVLQLV---GLSDKAQNYP-SQLSGGQKQRVGIARAL---VHHPEILLCDEATSALDPE 187
Cdd:PRK00635 767 DILEMTAYeaEKFFLDEpSIHEKIHALcslGLDYLPLGRPlSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTH 846
|
250 260 270
....*....|....*....|....*....|....*...
gi 2314388301 188 STSVVLSLLKEINQkLGITIVLITHEMQVIReICDQVV 225
Cdd:PRK00635 847 DIKALIYVLQSLTH-QGHTVVIIEHNMHVVK-VADYVL 882
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
14-212 |
3.46e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 14 HIKIRNLNKYYEVQgksvhalkniNLDIPEGkIFGIIGKSGAGKSSLLRTL--------NGLEQISEGHIHI-------- 77
Cdd:COG0419 4 RLRLENFRSYRDTE----------TIDFDDG-LNLIVGPNGAGKSTILEAIryalygkaRSRSKLRSDLINVgseeasve 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 78 --------------HQQDLAGLTHAeliQLRQRIGMIFQHFNLMSAKTVWENVALPLKVANYKKSDID--TRVNEVL--Q 139
Cdd:COG0419 73 lefehggkryrierRQGEFAEFLEA---KPSERKEALKRLLGLEIYEELKERLKELEEALESALEELAelQKLKQEIlaQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2314388301 140 LVGLSDkaqnyPSQLSGGQKQRVGIARALVhhpeiLLCDeaTSALDPESTSVVLSLLKEinqklgitIVLITH 212
Cdd:COG0419 150 LSGLDP-----IETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEE--------LAIITH 202
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
34-188 |
6.74e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 34 LKNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIH--------IHQQDlagltHAELIQlrqrigmifQHFN 105
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwsenanigYYAQD-----HAYDFE---------NDLT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 106 LMSAKTVWEnvalplkvanyKKSDIDTRVNEVL-QLVGLSDKAQNYPSQLSGGQKQRVGIARALVHHPEILLCDEATSAL 184
Cdd:PRK15064 401 LFDWMSQWR-----------QEGDDEQAVRGTLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHM 469
|
....
gi 2314388301 185 DPES 188
Cdd:PRK15064 470 DMES 473
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
152-198 |
2.22e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 39.53 E-value: 2.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 152 SQLSGGQKQ-------------RVGIARALVHHPEILLCDEATSALDPESTSVVLSLLKE 198
Cdd:pfam13558 31 GGLSGGEKQllaylplaaalaaQYGSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
21-60 |
7.28e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 7.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2314388301 21 NKYYEVQGKSVHALKNINLDIPEGKIFGIIGKSGAGKSSL 60
Cdd:COG0178 608 GKFLTIKGARENNLKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-232 |
1.51e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 35 KNINLDIPEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIhihqqdlaglthaeLIQLRQRIGMIFQH----FNLMSAK 110
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAKVRMAVFSQHhvdgLDLSSNP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 111 TVWENVALPlkvanykkSDIDTRVNEVLQLVGLSDKAQNYPS-QLSGGQKQRVGIARALVHHPEILLCDEATSALDpest 189
Cdd:PLN03073 592 LLYMMRCFP--------GVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD---- 659
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2314388301 190 svvLSLLKEINQKLGI---TIVLITHEMQVIREICDQVVVIEKGEI 232
Cdd:PLN03073 660 ---LDAVEALIQGLVLfqgGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
153-217 |
2.28e-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: 38.11 E-value: 2.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2314388301 153 QLSGGQKQRVGIARALVHH---PEILLC-DEATSALDPESTSVVLSLLKEINQKLGITIVlITHEMQVI 217
Cdd:cd03227 77 QLSGGEKELSALALILALAslkPRPLYIlDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELA 144
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| NIL |
smart00930 |
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ... |
277-347 |
2.44e-03 |
|
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: 36.33 E-value: 2.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2314388301 277 IIKLRYASSVQYSPDLKVIFEQFEHPVHLYQSHIDSIQNHLVGSLIVAVADLNLDTDLLQQKLKQHIAQIE 347
Cdd:smart00930 4 LVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGDEEDIEAALAYLREQGVEVE 74
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|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
26-93 |
6.49e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.38 E-value: 6.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314388301 26 VQGKSVHALKNInLdipEGKIFGIIGKSGAGKSSLLRTLNGLEQISEGHIhihqqdLAGL-------THAELIQL 93
Cdd:cd01854 71 KTGEGLDELREL-L---KGKTSVLVGQSGVGKSTLLNALLPELVLATGEI------SEKLgrgrhttTHRELFPL 135
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|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
154-249 |
7.95e-03 |
|
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: 38.07 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314388301 154 LSGGQKQRVGIAR----ALVHHPEILlcDEATSALDPESTSVVLSLLKEInQKLGITIVLITHEMQVIREiCDQVVVIEK 229
Cdd:TIGR00630 489 LSGGEAQRIRLATqigsGLTGVLYVL--DEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTIRA-ADYVIDIGP 564
|
90 100
....*....|....*....|
gi 2314388301 230 GEIVESGEVwsVFSNPQQQI 249
Cdd:TIGR00630 565 GAGEHGGEV--VASGTPEEI 582
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