|
Name |
Accession |
Description |
Interval |
E-value |
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-318 |
4.88e-173 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 483.04 E-value: 4.88e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY----GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDL 76
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQ 156
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 157 VLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLRNTKGL-RKL 235
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELtRRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 236 IGE-ESIILP------------KGTNIKILFPKDISNEAIITTMARELNIDVSIIFGKLEQFKDDILGSLIINIS--DKS 300
Cdd:COG1135 241 LPTvLNDELPeellarlreaagGGRLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEgdDAA 320
|
330
....*....|....*...
gi 497582239 301 GEQVKQYLTSKGIRWEEM 318
Cdd:COG1135 321 IDAALAYLREQGVVVEVL 338
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-318 |
1.27e-142 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 406.11 E-value: 1.27e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY----GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDL 76
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQ 156
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 157 VLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLR-NTKGLRKL 235
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHpKHPLTREF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 236 IGE-ESIILPK--------------GTNIKILFPKDISNEAIITTMARELNIDVSIIFGKLEQFKDDILGSLIINISDKS 300
Cdd:PRK11153 241 IQStLHLDLPEdylarlqaepttgsGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGDP 320
|
330 340
....*....|....*....|
gi 497582239 301 G--EQVKQYLTSKGIRWEEM 318
Cdd:PRK11153 321 GdiQAAIAYLQEHGVKVEVL 340
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-227 |
2.74e-132 |
|
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: 375.77 E-value: 2.74e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYG----KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDL 76
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQ 156
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497582239 157 VLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLR 227
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-225 |
1.48e-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: 300.37 E-value: 1.48e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVkSLNEKQMRDLRKEL 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVAL-PLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLL 159
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 160 CDEATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG1126 160 FDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
1-316 |
6.14e-97 |
|
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: 289.86 E-value: 6.14e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY----GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDL 76
Cdd:TIGR02314 1 MIKLSNITKVFhqgtKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQ 156
Cdd:TIGR02314 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 157 VLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI-----------F 225
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIfshpktplaqkF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 226 LRNTKGLRklIGEESIILPKGTN-------IKILFPKDISNEAIITTMARELNIDVSIIFGKLEQFKDDILGSLIINI-- 296
Cdd:TIGR02314 241 IRSTLHLS--IPEDYQERLQATPfadsvpmVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMhg 318
|
330 340
....*....|....*....|
gi 497582239 297 SDKSGEQVKQYLTSKGIRWE 316
Cdd:TIGR02314 319 TQQDTQAAIAYLQEHNVKVE 338
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
2.34e-94 |
|
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: 289.11 E-value: 2.34e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY-----GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRD 75
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 76 LRKELGMIFQH-F-SLLERKTVFDNVALPLECFG-YSKAEIKKRVLELLEVVGISEKKNDK-PRNLSGGQKQRVAIARAL 151
Cdd:COG1123 340 LRRRVQMVFQDpYsSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497582239 152 ALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
2.65e-91 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 271.53 E-value: 2.65e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYG----KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDL 76
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 R-KELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNP 155
Cdd:COG1136 84 RrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497582239 156 QVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKqICGRVAIMENGEVLE 217
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVS 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-219 |
2.58e-89 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 266.15 E-value: 2.58e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY-GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRKE 79
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLL 159
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 160 CDEATSALDPNTTKSILSLLEDINkKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVG 219
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-225 |
3.17e-89 |
|
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: 266.46 E-value: 3.17e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRKEL 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQH---FSLLerkTVFDNVALPL-ECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQ 156
Cdd:COG1127 85 GMLFQGgalFDSL---TVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 157 VLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-215 |
3.61e-87 |
|
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: 260.54 E-value: 3.61e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVkSLNEKQMRDLRKELG 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVAL-PLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 161 DEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEV 215
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-225 |
5.98e-86 |
|
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: 257.65 E-value: 5.98e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVN-KYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKslnEKQMRDLRKEL 80
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQH-----FSllerKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNP 155
Cdd:COG1122 78 GLVFQNpddqlFA----PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 156 QVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-215 |
1.02e-85 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 258.06 E-value: 1.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNK-YYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRKE 79
Cdd:COG3638 2 MLELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHFSLLERKTVFDNV-------------ALPLecfgYSKAEiKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVA 146
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagrlgrtstwrsLLGL----FPPED-RERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 147 IARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEV 215
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-215 |
1.38e-84 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 253.95 E-value: 1.38e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYG----KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLR 77
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 78 -KELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQ 156
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 157 VLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKqICGRVAIMENGEV 215
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-242 |
1.01e-83 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 256.56 E-value: 1.01e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLN-EKqmRDLrke 79
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPpEK--RNV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 lGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLL 159
Cdd:COG3842 80 -GMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 160 CDEATSALDPNTTKSILSLLEDINKKLGITIIVVTH-QMEVIkQICGRVAIMENGEVLEVGDTEEIFLR-NTKGLRKLIG 237
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLQRELGITFIYVTHdQEEAL-ALADRIAVMNDGRIEQVGTPEEIYERpATRFVADFIG 237
|
....*
gi 497582239 238 EESII 242
Cdd:COG3842 238 EANLL 242
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-225 |
7.40e-83 |
|
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: 250.49 E-value: 7.40e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGK----IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKslnEKQMRDL 76
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT---RRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKELGMIFQHF--SLLERKTVFDNVALPLECFGysKAEIKKRVLELLEVVGISEKKNDK-PRNLSGGQKQRVAIARALAL 153
Cdd:COG1124 78 RRRVQMVFQDPyaSLHPRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497582239 154 NPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-225 |
1.81e-82 |
|
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: 249.34 E-value: 1.81e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRKELG 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPL-ECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 161 DEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-232 |
1.19e-78 |
|
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: 242.27 E-value: 1.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY----GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEE---YQEGSVLVSDKEVKSLNEKQM 73
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 74 RDLR-KELGMIFQHF--SLLERKTVFDNVALPLECF-GYSKAEIKKRVLELLEVVGISEKK---NDKPRNLSGGQKQRVA 146
Cdd:COG0444 81 RKIRgREIQMIFQDPmtSLNPVMTVGDQIAEPLRIHgGLSKAEARERAIELLERVGLPDPErrlDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 147 IARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFl 226
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF- 239
|
250
....*....|.
gi 497582239 227 RN-----TKGL 232
Cdd:COG0444 240 ENprhpyTRAL 250
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-224 |
1.39e-78 |
|
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: 239.39 E-value: 1.39e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYG-KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRKEL 80
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVALPL--------ECFG-YSKAEiKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARAL 151
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGlFPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 152 ALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-224 |
1.68e-78 |
|
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: 238.62 E-value: 1.68e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQ-----EGSVLVSDKEVKSLNEKQMRdL 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDVLE-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKELGMIFQHFSLLeRKTVFDNVALPLECFGY-SKAEIKKRVLELLEVVGISEKKNDK--PRNLSGGQKQRVAIARALAL 153
Cdd:cd03260 80 RRRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497582239 154 NPQVLLCDEATSALDPNTTKSILSLLEDINKKlgITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-224 |
2.47e-77 |
|
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: 236.43 E-value: 2.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGK-IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRKE 79
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHFSLLERKTVFDNVALPL--------ECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARAL 151
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRlgykptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 152 ALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-231 |
8.63e-77 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 234.57 E-value: 8.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKslneKQMRDLRKELG 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDT--------EEIFLRNTKG 231
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPdelkarllEDVFLELTGE 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-219 |
8.23e-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: 232.01 E-value: 8.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY----GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDL 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKELGMIFQH--FSLLERKTVFDNVALPLECFG--YSKAEIKKRVLELLEVVGISEK-KNDKPRNLSGGQKQRVAIARAL 151
Cdd:cd03257 81 RKEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 152 ALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVG 219
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-219 |
1.24e-75 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 230.87 E-value: 1.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmRDLrkelG 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER-RNI----G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVG 219
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-224 |
2.41e-75 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 231.14 E-value: 2.41e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSlNEKQMRDLRKEL 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVAL-PLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLL 159
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 160 CDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-227 |
2.65e-75 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 234.97 E-value: 2.65e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmRDLrkel 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RNI---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 161 DEATSALDPNTTKSILSLLEDINKKLGITIIVVTH-QMEVIkQICGRVAIMENGEVLEVGDTEEIFLR 227
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHdQVEAM-TLADRIAVMNDGRIQQVGTPEELYDR 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-195 |
2.80e-75 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 231.90 E-value: 2.80e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY----GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVkslnekqmRDL 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV--------TGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQ 156
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 497582239 157 VLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTH 195
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTH 197
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-214 |
1.59e-74 |
|
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: 227.07 E-value: 1.59e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNeKQMRDLRKELG 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE-DELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLecfgyskaeikkrvlellevvgisekkndkprnlSGGQKQRVAIARALALNPQVLLCD 161
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGE 214
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-225 |
1.69e-74 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 232.73 E-value: 1.69e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSlnEKQMRDLRkeLG 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT--NLPPRERR--VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-235 |
1.48e-73 |
|
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: 228.10 E-value: 1.48e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGK-----IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDL 76
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKELGMIFQhFS---LLERkTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDK-PRNLSGGQKQRVAIARALA 152
Cdd:TIGR04521 81 RKKVGLVFQ-FPehqLFEE-TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERsPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 153 LNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFlRNTKGL 232
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF-SDVDEL 237
|
...
gi 497582239 233 RKL 235
Cdd:TIGR04521 238 EKI 240
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-214 |
3.12e-72 |
|
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: 222.34 E-value: 3.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 3 SIKNVNKYY--GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRKEL 80
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSL-LERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLL 159
Cdd:cd03225 78 GLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 160 CDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGE 214
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-225 |
1.04e-71 |
|
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: 222.90 E-value: 1.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYG---------------KIQVLK---------DVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGS 57
Cdd:cd03294 1 IKIKGLYKIFGknpqkafkllakgksKEEILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 58 VLVSDKEVKSLNEKQMRDLR-KELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRN 136
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRrKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 137 LSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVL 216
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
....*....
gi 497582239 217 EVGDTEEIF 225
Cdd:cd03294 241 QVGTPEEIL 249
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-227 |
3.20e-71 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 225.75 E-value: 3.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYG---------------KIQVLK---------DVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEG 56
Cdd:COG4175 3 KIEVRNLYKIFGkrperalklldqgksKDEILEktgqtvgvnDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 57 SVLVSDKEVKSLNEKQMRDLR-KELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPR 135
Cdd:COG4175 83 EVLIDGEDITKLSKKELRELRrKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 136 NLSGGQKQRVAIARALALNPQVLLCDEATSALDPnttksilsL--------LEDINKKLGITIIVVTHQM-EVIKqICGR 206
Cdd:COG4175 163 ELSGGMQQRVGLARALATDPDILLMDEAFSALDP--------LirremqdeLLELQAKLKKTIVFITHDLdEALR-LGDR 233
|
250 260
....*....|....*....|.
gi 497582239 207 VAIMENGEVLEVGDTEEIFLR 227
Cdd:COG4175 234 IAIMKDGRIVQIGTPEEILTN 254
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-222 |
1.74e-70 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 218.73 E-value: 1.74e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEV---KSLNEKQMRDLRK 78
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 79 ELGMIFQHFSLLERKTVFDN-VALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQV 157
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 158 LLCDEATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTE 222
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-222 |
1.66e-69 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 216.42 E-value: 1.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEV---KSLNEKQMRDLRK 78
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 79 ELGMIFQHFSLLERKTVFDN-VALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQV 157
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 158 LLCDEATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTE 222
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
3.29e-69 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 224.01 E-value: 3.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY--GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQ---EGSVLVSDKEVKSLNEkqmRD 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE---AL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 76 LRKELGMIFQHF-SLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALN 154
Cdd:COG1123 81 RGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497582239 155 PQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-225 |
7.05e-69 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 215.29 E-value: 7.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQ-----EGSVLVSDKEVkslNEKQMR-- 74
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDI---YDPDVDvv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 75 DLRKELGMIFQH---FSllerKTVFDNVALPLECFGY-SKAEIKKRVLELLEVVGI-SEKK---NDKPRNLSGGQKQRVA 146
Cdd:COG1117 89 ELRRRVGMVFQKpnpFP----KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwDEVKdrlKKSALGLSGGQQQRLC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 147 IARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLgiTIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-225 |
1.17e-68 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 217.29 E-value: 1.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYY--------GKIQVLK---DVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNE 70
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 71 KQMRDLRKELGMIFQ--HFSLLERKTVFDNVALPLECFG-YSKAEIKKRVLELLEVVGISEKKNDK-PRNLSGGQKQRVA 146
Cdd:COG4608 88 RELRPLRRRMQMVFQdpYASLNPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPEHADRyPHEFSGGQRQRIG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 147 IARALALNPQVLLCDEATSALDpnttKSI----LSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTE 222
Cdd:COG4608 168 IARALALNPKLIVCDEPVSALD----VSIqaqvLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRD 243
|
...
gi 497582239 223 EIF 225
Cdd:COG4608 244 ELY 246
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-198 |
1.59e-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: 213.10 E-value: 1.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYG----KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVkslnekqmRDLR 77
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV--------TGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 78 KELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQV 157
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 497582239 158 LLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQME 198
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDID 193
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-225 |
2.54e-68 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 213.89 E-value: 2.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVK----------SLNE 70
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelvPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 71 KQMRDLRKELGMIFQHFSLLERKTVFDNVAL-PLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIAR 149
Cdd:COG4598 88 RQLQRIRTRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 150 ALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVF 242
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-235 |
6.71e-68 |
|
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: 213.06 E-value: 6.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYY--GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVksLNEKQMRDLRKE 79
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQH----FSlleRKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNP 155
Cdd:TIGR04520 79 VGMVFQNpdnqFV---GATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 156 QVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQM-EVIKqiCGRVAIMENGEVLEVGDTEEIFLRNTKgLRK 234
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMeEAVL--ADRVIVMNKGKIVAEGTPREIFSQVEL-LKE 232
|
.
gi 497582239 235 L 235
Cdd:TIGR04520 233 I 233
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-225 |
1.69e-66 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 208.24 E-value: 1.69e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSL--NEKQMrdlrke 79
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLppHKRPV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 lGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLL 159
Cdd:cd03300 75 -NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 160 CDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-225 |
8.11e-66 |
|
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: 207.20 E-value: 8.11e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEkqmRDLRKEL 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR---RELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVAL---P-LECFGYSKAEIKKRVLELLEVVGISEKKnDKP-RNLSGGQKQRVAIARALALNP 155
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVALgryPhLGLFGRPSAEDREAVEEALERTGLEHLA-DRPvDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 156 QVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-215 |
1.64e-65 |
|
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: 205.33 E-value: 1.64e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYY-GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRKEL 80
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 161 DEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEV 215
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-225 |
1.14e-63 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 201.41 E-value: 1.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdlrKELG 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLE----CFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQV 157
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 158 LLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-219 |
4.52e-63 |
|
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: 199.02 E-value: 4.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmRDLrkelG 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RDI----A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKLGITIIVVTH-QMEVIkQICGRVAIMENGEVLEVG 219
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHdQVEAM-TMADRIAVMNDGQIQQIG 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-258 |
8.04e-63 |
|
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: 199.31 E-value: 8.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKqmrdLRKEL 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE----ARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 161 DEATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIflrntkglRKLIGEES 240
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL--------REEIGEEN 227
|
250
....*....|....*...
gi 497582239 241 IilpKGTNIKILFPKDIS 258
Cdd:COG4555 228 L---EDAFVALIGSEEGE 242
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-225 |
3.10e-62 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 198.27 E-value: 3.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEV----------KSLNEK 71
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 72 QMRDLRKELGMIFQHFSLLERKTVFDNV-ALPLECFGYSKAEIKKRVLELLEVVGISEKKNDK-PRNLSGGQKQRVAIAR 149
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 150 ALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-217 |
5.81e-61 |
|
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: 194.19 E-value: 5.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY----GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDL 76
Cdd:COG4181 8 IIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKE-LGMIFQHFSLLERKTVFDNVALPLECFGYSKAEikKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNP 155
Cdd:COG4181 88 RARhVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497582239 156 QVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQiCGRVAIMENGEVLE 217
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-224 |
8.51e-61 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 197.61 E-value: 8.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRdlrkeLG 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK-----VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVAlplecFGY---------SKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALA 152
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIA-----FGLtvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497582239 153 LNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-225 |
1.26e-60 |
|
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: 201.84 E-value: 1.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 12 GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEyQEGSVLVSDKEVKSLNEKQMRDLRKELGMIFQH-F-SL 89
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpFgSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 90 LERKTVFDNVALPLE--CFGYSKAEIKKRVLELLEVVGISEKKNDK-PRNLSGGQKQRVAIARALALNPQVLLCDEATSA 166
Cdd:COG4172 376 SPRMTVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 167 LDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVF 514
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-225 |
2.46e-60 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 193.00 E-value: 2.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVkslnekqmRDLRKEL 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--------RRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLlERK---TVFDNVAL----PLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALAL 153
Cdd:COG1121 78 GYVPQRAEV-DWDfpiTVRDVVLMgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497582239 154 NPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMeNGEVLEVGDTEEIF 225
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVL 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-224 |
9.87e-60 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 191.79 E-value: 9.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdlRKEL 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR----IARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMI--FQHFSLLERKTVFDNVALPLEC---------------FGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQ 143
Cdd:COG0411 80 GIArtFQNPRLFPELTVLENVLVAAHArlgrgllaallrlprARREEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 144 RVAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEE 223
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
.
gi 497582239 224 I 224
Cdd:COG0411 240 V 240
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-227 |
1.01e-59 |
|
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: 191.36 E-value: 1.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQ-VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdLRKEL 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKK--NDKPRNLSGGQKQRVAIARALALNPQVL 158
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 159 LCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLR 227
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-215 |
5.06e-59 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 188.49 E-value: 5.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRKELG 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLErKTVFDNVALPlecFGYSKAEI-KKRVLELLEVVGISEKKNDKP-RNLSGGQKQRVAIARALALNPQVLL 159
Cdd:COG4619 78 YVPQEPALWG-GTVRDNLPFP---FQLRERKFdRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 160 CDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEV 215
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-225 |
1.61e-58 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 188.42 E-value: 1.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEV---KSLNEKQ--MRD 75
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQKglIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 76 LRKELGMIFQHFSLLERKTVFDNVAL-PLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALN 154
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497582239 155 PQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-224 |
7.19e-58 |
|
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: 186.49 E-value: 7.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEkqmrDLRKELG 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP----HEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MI--FQHFSLLERKTVFDNVALPLEC----------FGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIAR 149
Cdd:cd03219 77 IGrtFQIPRLFPELTVLENVMVAAQArtgsglllarARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 150 ALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-215 |
6.31e-57 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 181.83 E-value: 6.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKslneKQMRDLRKELG 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNValplecfgyskaeikkrvlellevvgisekkndkprNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:cd03230 77 YLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEV 215
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-225 |
1.93e-56 |
|
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: 182.54 E-value: 1.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQvLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNeKQMRDLrkelG 81
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP-PEKRDI----S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:cd03299 75 YVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-225 |
1.41e-55 |
|
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: 188.74 E-value: 1.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 12 GKIQVLKDVSIEIESGEIFGIIGHSGAGKS----TLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLR-KELGMIFQH 86
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRgNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 87 --FSLLERKTVFDNVALPLEC-FGYSKAEIKKRVLELLEVVGISEKK---NDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:COG4172 101 pmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQRVMIAMALANEPDLLIA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 161 DEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG4172 181 DEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELF 245
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-238 |
2.29e-54 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 177.25 E-value: 2.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGkiQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdlRKeL 80
Cdd:COG3840 1 MLRLDDLTYRYG--DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE----RP-V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVALplecfG------YSKAEiKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALN 154
Cdd:COG3840 74 SMLFQENNLFPHLTVAQNIGL-----GlrpglkLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 155 PQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF-LRNTKGLR 233
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLdGEPPPALA 227
|
....*
gi 497582239 234 KLIGE 238
Cdd:COG3840 228 AYLGI 232
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-232 |
5.16e-54 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 187.35 E-value: 5.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYG--KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRKE 79
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHFSLLERkTVFDNVALplecfGYSKAEIKkRVLELLEVVGISEKKNDKP-----------RNLSGGQKQRVAIA 148
Cdd:COG2274 551 IGVVLQDVFLFSG-TIRENITL-----GDPDATDE-EIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 149 RALALNPQVLLCDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEifLRN 228
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEE--LLA 698
|
....
gi 497582239 229 TKGL 232
Cdd:COG2274 699 RKGL 702
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-219 |
5.95e-54 |
|
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: 175.77 E-value: 5.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQ--VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSlnekQMRDLRKE 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLL 159
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 160 CDEATSALDPNTTKSILSLLEDInkKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVG 219
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-225 |
6.35e-54 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 180.53 E-value: 6.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdlrKELG 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-----RHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIY 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-233 |
9.30e-54 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 177.13 E-value: 9.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYY--GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEvksLNEKQMRDLRKE 79
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQH----FSlleRKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNP 155
Cdd:PRK13635 83 VGMVFQNpdnqFV---GATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 156 QVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEIFLRNTKGLR 233
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQE 236
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-216 |
2.59e-53 |
|
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: 173.87 E-value: 2.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 3 SIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVkslnekqmRDLRKELGM 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--------EKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 83 IFQHFSLlERK---TVFDNVALPLE-----CFGYSKAEiKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALN 154
Cdd:cd03235 73 VPQRRSI-DRDfpiSVRDVVLMGLYghkglFRRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497582239 155 PQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMeNGEVL 216
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-227 |
6.94e-53 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 175.21 E-value: 6.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 17 LKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKS-LNEKQMRDLRKELGMIFQ--HFSLLErK 93
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgKKNKKLKPLRKKVGIVFQfpEHQLFE-E 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 94 TVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDK-PRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTT 172
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 173 KSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLR 227
Cdd:PRK13634 182 KEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-219 |
5.31e-52 |
|
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: 169.15 E-value: 5.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 3 SIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRkelgm 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 83 ifqhfsllerktvfdnvalplecfGYskaeikkrVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDE 162
Cdd:cd03214 76 ------------------------AY--------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 163 ATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVG 219
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-225 |
6.34e-52 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 174.12 E-value: 6.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 3 SIKNVNKY-YGKIQVLK---DVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRK 78
Cdd:PRK15079 19 DIKDGKQWfWQPPKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 79 ELGMIFQH--FSLLERKTVFDNVALPLECF--GYSKAEIKKRVLELLEVVGISEKK-NDKPRNLSGGQKQRVAIARALAL 153
Cdd:PRK15079 99 DIQMIFQDplASLNPRMTIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497582239 154 NPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVY 250
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-165 |
6.61e-52 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 168.21 E-value: 6.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 17 LKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEvksLNEKQMRDLRKELGMIFQHFSLLERKTVF 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 97 DNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDK----PRNLSGGQKQRVAIARALALNPQVLLCDEATS 165
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-224 |
3.13e-51 |
|
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: 168.70 E-value: 3.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKslneKQMRDLRKELG 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-225 |
4.74e-51 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 170.61 E-value: 4.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGK-----IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKqMRDL 76
Cdd:PRK13637 3 IKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKELGMIFQH--FSLLErKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGIS-EKKNDK-PRNLSGGQKQRVAIARALA 152
Cdd:PRK13637 82 RKKVGLVFQYpeYQLFE-ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKsPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 153 LNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-221 |
1.72e-50 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 168.33 E-value: 1.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY---------GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEK 71
Cdd:PRK10419 3 LLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 72 QMRDLRKELGMIFQH-FSLLE-RKTVFDNVALPLE-CFGYSKAEIKKRVLELLEVVGISEKKNDK-PRNLSGGQKQRVAI 147
Cdd:PRK10419 83 QRKAFRRDIQMVFQDsISAVNpRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVLDKrPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 148 ARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLE---VGDT 221
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqpVGDK 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-225 |
2.77e-50 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 171.17 E-value: 2.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKslnekQMRDLRKEL 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 161 DEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-213 |
4.69e-50 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 165.82 E-value: 4.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNK-YYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRKE 79
Cdd:PRK10908 1 MIRFEHVSKaYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLL 159
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497582239 160 CDEATSALDPNTTKSILSLLEDINkKLGITIIVVTHQMEVIKQICGRVAIMENG 213
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-214 |
7.74e-50 |
|
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: 163.18 E-value: 7.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 3 SIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdLRKELGM 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---LRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 83 IFQhfsllerktvfdnvalplecfgyskaeikkrvlellevvgisekkndkprnLSGGQKQRVAIARALALNPQVLLCDE 162
Cdd:cd00267 78 VPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497582239 163 ATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGE 214
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-224 |
8.70e-50 |
|
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: 164.91 E-value: 8.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMrdLRKELG 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLECFGYSK-AEIKKRVLELLEVvgISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARRRAKrKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497582239 161 DEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-227 |
9.81e-50 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 166.83 E-value: 9.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQ---VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEvksLNEKQMRDLR 77
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 78 KELGMIFQH-FSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQ 156
Cdd:PRK13650 81 HKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497582239 157 VLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKqICGRVAIMENGEVLEVGDTEEIFLR 227
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-213 |
1.04e-49 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 165.37 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 6 NVNKYY--GKIQ--VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLR-KEL 80
Cdd:PRK11629 10 NLCKRYqeGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497582239 161 DEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQIcGRVAIMENG 213
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDG 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-236 |
3.79e-49 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 165.67 E-value: 3.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSlnekqmRDLRK-- 78
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP------EDRRRig 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 79 ----ELGmifqhfsLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALN 154
Cdd:COG4152 75 ylpeERG-------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 155 PQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIflRNTKGLRK 234
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI--RRQFGRNT 224
|
..
gi 497582239 235 LI 236
Cdd:COG4152 225 LR 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-227 |
6.10e-49 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 166.81 E-value: 6.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIkNVNKYYGKIQVlkDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVksLNEKQMRDL---R 77
Cdd:COG4148 2 MLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGIFLpphR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 78 KELGMIFQHFSLLERKTVFDNValpleCFGYSKAEIKKRVLELLEVV---GISEKKNDKPRNLSGGQKQRVAIARALALN 154
Cdd:COG4148 77 RRIGYVFQEARLFPHLSVRGNL-----LYGRKRAPRAERRISFDEVVellGIGHLLDRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 155 PQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLR 227
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-232 |
9.04e-49 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 171.50 E-value: 9.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVN-KYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRKEL 80
Cdd:COG1132 340 IEFENVSfSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERkTVFDNVALPLEcfGYSKAEIKkrvlELLEVVGISEKKNDKP-----------RNLSGGQKQRVAIAR 149
Cdd:COG1132 417 GVVPQDTFLFSG-TIRENIRYGRP--DATDEEVE----EAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 150 ALALNPQVLLCDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEifLRNT 229
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE--LLAR 564
|
...
gi 497582239 230 KGL 232
Cdd:COG1132 565 GGL 567
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-224 |
1.12e-48 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 169.43 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRkeL 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG--I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVALPLEC--FG-YSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQV 157
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPrrGGlIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 158 LLCDEATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-214 |
2.57e-48 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 159.47 E-value: 2.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYG--KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRKE 79
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHFSLLERkTVFDNValplecfgyskaeikkrvlellevvgisekkndkprnLSGGQKQRVAIARALALNPQVLL 159
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 160 CDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQiCGRVAIMENGE 214
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
3.92e-48 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 162.47 E-value: 3.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYG--KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRK 78
Cdd:PRK13632 7 MIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN---LKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 79 ELGMIFQH----FSLLerkTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALN 154
Cdd:PRK13632 84 KIGIIFQNpdnqFIGA---TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497582239 155 PQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQM-EVIKqiCGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMdEAIL--ADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-219 |
7.70e-48 |
|
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: 159.67 E-value: 7.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGeIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKslneKQMRDLRKELG 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:cd03264 76 YLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 162 EATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQICGRVAIMENGEVLEVG 219
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-225 |
9.36e-48 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 161.79 E-value: 9.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGK------IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKslNEKQMR 74
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS--DEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 75 DLRKELGMIFQH-FSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALAL 153
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497582239 154 NPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-241 |
1.17e-47 |
|
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: 167.29 E-value: 1.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQ--EGSVL-------------------- 59
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 60 ---VSDKEVKS-------LNEKQMRDLRKELGMIFQH-FSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISE 128
Cdd:TIGR03269 81 pcpVCGGTLEPeevdfwnLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 129 KKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVA 208
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 497582239 209 IMENGEVLEVGDTEEI---FLRNTKGLRK----LIGEESI 241
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVvavFMEGVSEVEKecevEVGEPII 280
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-223 |
2.22e-46 |
|
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: 164.55 E-value: 2.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVN-KYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKqmrDLRKEL 80
Cdd:COG4988 337 IELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPA---SWRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHfSLLERKTVFDNVAL--PlecfGYSKAEIKkRVLE---LLEVV-----GISEKKNDKPRNLSGGQKQRVAIARA 150
Cdd:COG4988 414 AWVPQN-PYLFAGTIRENLRLgrP----DASDEELE-AALEaagLDEFVaalpdGLDTPLGEGGRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 151 LALNPQVLLCDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEE 223
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-234 |
3.01e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 157.55 E-value: 3.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVN-KYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKsLNEKQMRDLRKE 79
Cdd:PRK13639 1 ILETRDLKySYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHF-SLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVL 158
Cdd:PRK13639 80 VGIVFQNPdDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 159 LCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFlRNTKGLRK 234
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF-SDIETIRK 233
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-225 |
5.37e-46 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 159.42 E-value: 5.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVsdkevkslNEKQMRDL---RK 78
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI--------GEKRMNDVppaER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 79 ELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVL 158
Cdd:PRK11000 76 GVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 159 LCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTH-QMEVIkQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK11000 156 LLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHdQVEAM-TLADKIVVLDAGRVAQVGKPLELY 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-225 |
6.60e-46 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 160.20 E-value: 6.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 17 LKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLR-KELGMIFQHFSLLERKTV 95
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 96 FDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSI 175
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497582239 176 LSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-225 |
8.15e-46 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 156.15 E-value: 8.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYY---------GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQ 72
Cdd:COG4167 5 LEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 73 M-RDLRkelgMIFQH--FSLLERKTVFDNVALPLEC-FGYSKAEIKKRVLELLEVVGIS-EKKNDKPRNLSGGQKQRVAI 147
Cdd:COG4167 85 RcKHIR----MIFQDpnTSLNPRLNIGQILEEPLRLnTDLTAEEREERIFATLRLVGLLpEHANFYPHMLSSGQKQRVAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 148 ARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVF 238
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-225 |
2.19e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 155.67 E-value: 2.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYG-----KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNE-KQMRD 75
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 76 LRKELGMIFQhF--SLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDK-PRNLSGGQKQRVAIARALA 152
Cdd:PRK13649 83 IRKKVGLVFQ-FpeSQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 153 LNPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-223 |
7.95e-45 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 159.42 E-value: 7.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRkeL 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALG--I 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVAL---PLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQV 157
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 158 LLCDEATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEE 223
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-241 |
9.04e-45 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 156.03 E-value: 9.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 4 IKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSlNEKQMRDLrkelGMI 83
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH-RSIQQRDI----CMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 84 FQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVV---GISEKKNDKprnLSGGQKQRVAIARALALNPQVLLC 160
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVdlaGFEDRYVDQ---ISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 161 DEATSALDPNTTKSILSLLEDINKKLGITIIVVTH-QMEVIKqICGRVAIMENGEVLEVGDTEEIFLR-NTKGLRKLIGE 238
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHdQSEAFA-VSDTVIVMNKGKIMQIGSPQELYRQpASRFMASFMGD 239
|
...
gi 497582239 239 ESI 241
Cdd:PRK11432 240 ANI 242
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-215 |
9.48e-45 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 153.29 E-value: 9.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEvkslnekqMRDLRKELG 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP--------LAEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLecfgysKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEV 215
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-235 |
1.20e-44 |
|
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: 152.06 E-value: 1.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLN-EKQMRdlrke 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIAR----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIF-----QHFSLLerkTVFDNVALPLECFGySKAEIKK---RVLELLEVVGisEKKNDKPRNLSGGQKQRVAIARAL 151
Cdd:COG0410 78 LGIGYvpegrRIFPSL---TVEENLLLGAYARR-DRAEVRAdleRVYELFPRLK--ERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 152 ALNPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEifLRNTKG 231
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAE--LLADPE 228
|
....
gi 497582239 232 LRKL 235
Cdd:COG0410 229 VREA 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-198 |
1.22e-44 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 153.09 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGK----IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqmrdl 76
Cdd:COG4525 3 MLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 rKELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQ 156
Cdd:COG4525 76 -ADRGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 497582239 157 VLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQME 198
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVE 196
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
1.57e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 152.98 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVN-KYYGKIQ-VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRK 78
Cdd:PRK13648 7 IIVFKNVSfQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN---FEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 79 ELGMIFQH-FSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQV 157
Cdd:PRK13648 84 HIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 158 LLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQM-EVIKQicGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLsEAMEA--DHVIVMNKGTVYKEGTPTEIF 230
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-225 |
1.84e-44 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 152.30 E-value: 1.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQ-----EGSVLVSDKEVKSLNEKQMRdL 76
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIE-V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKELGMIFQHFSLLERKTVFDNVALPLECFGY--SKAEIKKRVLELLEVVG----ISEKKNDKPRNLSGGQKQRVAIARA 150
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAAlwdeVKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 151 LALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLgiTIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
2.92e-44 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 148.73 E-value: 2.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRkeLG 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAG--IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQhfsllerktvfdnvalplecfgyskaeikkrvlellevvgisekkndkprnLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:cd03216 79 MVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497582239 162 EATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEV 215
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-224 |
3.62e-44 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 150.95 E-value: 3.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMrDLRKEL 80
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP---M-HKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIF--QHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVL 158
Cdd:COG1137 79 GIGYlpQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 159 LCDEATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:COG1137 159 LLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-219 |
4.93e-44 |
|
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: 149.74 E-value: 4.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRKELG 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 mifqhfsLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:cd03269 81 -------LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVG 219
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-224 |
6.62e-44 |
|
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: 149.98 E-value: 6.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 3 SIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdlRKELGM 82
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE----RARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 83 IF-----QHFSLLerkTVFDNVALPLECFGYSKAEIKKRVLELLEVvgISEKKNDKPRNLSGGQKQRVAIARALALNPQV 157
Cdd:TIGR03410 78 AYvpqgrEIFPRL---TVEENLLTGLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 158 LLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:TIGR03410 153 LLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
5-227 |
1.04e-43 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 152.43 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 5 KNVNKYY----------GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMR 74
Cdd:PRK11308 9 IDLKKHYpvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 75 DLRKELGMIFQ--HFSLLERKTVFDNVALPLEC-FGYSKAEIKKRVLELLEVVGI-SEKKNDKPRNLSGGQKQRVAIARA 150
Cdd:PRK11308 89 LLRQKIQIVFQnpYGSLNPRKKVGQILEEPLLInTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 151 LALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLR 227
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
17-219 |
1.32e-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: 148.98 E-value: 1.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 17 LKDVSIEIE---SGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSlNEKQMrDL---RKELGMIFQHFSLL 90
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD-SRKKI-NLppqQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 91 ERKTVFDNValpleCFGY---SKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSAL 167
Cdd:cd03297 88 PHLNVRENL-----AFGLkrkRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497582239 168 DPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVG 219
Cdd:cd03297 163 DRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-225 |
2.28e-43 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 157.32 E-value: 2.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 8 NKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRKELGMIFQ-- 85
Cdd:PRK10261 331 NRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQdp 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 86 HFSLLERKTVFDNVALPLECFGYSKAE-IKKRVLELLEVVGI-SEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEA 163
Cdd:PRK10261 411 YASLDPRQTVGDSIMEPLRVHGLLPGKaAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497582239 164 TSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF 552
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-227 |
4.52e-43 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 151.53 E-value: 4.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNK-YYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmRDlrke 79
Cdd:PRK11650 3 GLKLQAVRKsYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-RD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLL 159
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 160 CDEATSALDPNTTKSILSLLEDINKKLGITIIVVTH-QMEVIkQICGRVAIMENGEVLEVGDTEEIFLR 227
Cdd:PRK11650 158 FDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHdQVEAM-TLADRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-224 |
5.42e-43 |
|
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: 148.00 E-value: 5.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 17 LKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMrdlrkelgMIFQHFSLLERKTVF 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 97 DNVALPLECF--GYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKS 174
Cdd:TIGR01184 73 ENIALAVDRVlpDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497582239 175 ILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-226 |
8.08e-43 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 148.00 E-value: 8.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGL-----EEYQEGSVLVSDKEVKSLNEKQMrD 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTV-D 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 76 LRKELGMIFQH---FSLlerkTVFDNVALPLECFG-YSKAEIKKRVLELLEVVGISEKKNDKPRN----LSGGQKQRVAI 147
Cdd:PRK14239 84 LRKEIGMVFQQpnpFPM----SIYENVVYGLRLKGiKDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 148 ARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLgiTIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFL 226
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFM 236
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
1.14e-42 |
|
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: 146.81 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY------GK-IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGleEY--QEGSVLVSDKE----VKS 67
Cdd:COG4778 4 LLEVENLSKTFtlhlqgGKrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG--NYlpDSGSILVRHDGgwvdLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 68 LNEKQMRDLRK-ELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKND-KPRNLSGGQKQRV 145
Cdd:COG4778 82 ASPREILALRRrTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDlPPATFSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 146 AIARALALNPQVLLCDEATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENG 213
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-222 |
1.18e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 148.34 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGK-IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdLRKEL 80
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---VRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQH-----FSllerKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNP 155
Cdd:PRK13647 82 GLVFQDpddqvFS----STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 156 QVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTE 222
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-219 |
1.71e-42 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 145.82 E-value: 1.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKqmrdlRKELG 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA-----LRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLECFGYSKAEIKkrvlELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:cd03268 76 ALIEAPGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVG 219
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-227 |
2.81e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 146.60 E-value: 2.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGL-EEYQE----GSVLVSDKEVKSLNekqMRDL 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLiELYPEarvsGEVYLDGQDIFKMD---VIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKELGMIFQHFSLLERKTVFDNVALPLEC--FGYSKAEIKKRVLELLEVVGISEKKNDK----PRNLSGGQKQRVAIARA 150
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 151 LALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLgiTIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLR 227
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-223 |
2.95e-42 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 147.08 E-value: 2.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLeeyqegsvLVSDKEVKSLNE---------- 70
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--------ITGDKSAGSHIEllgrtvqreg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 71 KQMRDLRK---ELGMIFQHFSLLERKTVFDNVAL------PL--ECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSG 139
Cdd:PRK09984 76 RLARDIRKsraNTGYIFQQFNLVNRLSVLENVLIgalgstPFwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 140 GQKQRVAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVG 219
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
....
gi 497582239 220 DTEE 223
Cdd:PRK09984 236 SSQQ 239
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-225 |
5.92e-42 |
|
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: 144.99 E-value: 5.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdlRKELG 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK----RARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIF--QHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLL 159
Cdd:cd03218 77 IGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 160 CDEATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-225 |
7.08e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 146.48 E-value: 7.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYY--GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGL---EEYQEGSVLVSDKEvksLNEKQMRDL 76
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGIT---LTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKELGMIFQH-FSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNP 155
Cdd:PRK13640 83 REKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 156 QVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIF 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-224 |
8.73e-42 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 145.22 E-value: 8.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY----------------------GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSV 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 59 LVsDKEVKSLnekqmrdLrkELGMIFqHFSLlerkTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKnDKP-RNL 137
Cdd:COG1134 84 EV-NGRVSAL-------L--ELGAGF-HPEL----TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFI-DQPvKTY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 138 SGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLE 217
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
....*..
gi 497582239 218 VGDTEEI 224
Cdd:COG1134 227 DGDPEEV 233
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-225 |
9.46e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 146.42 E-value: 9.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYG-----KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLN-EKQMR 74
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 75 DLRKELGMIFQH-FSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDK-PRNLSGGQKQRVAIARALA 152
Cdd:PRK13643 81 PVRKKVGVVFQFpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKsPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 153 LNPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-196 |
1.89e-41 |
|
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: 143.00 E-value: 1.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVkslnEKQMRDLRKEL 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVALPLECFGYSKAEIkkRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 497582239 161 DEATSALDPNTTKSILSLLEDiNKKLGITIIVVTHQ 196
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-219 |
3.19e-41 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 142.89 E-value: 3.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGK----IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVkslnEKQMRDL 76
Cdd:cd03266 1 MITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV----VKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQ 156
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 157 VLLCDEATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVG 219
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-232 |
4.85e-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: 151.65 E-value: 4.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGK--IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRKE 79
Cdd:TIGR03797 452 IEVDRVTFRYRPdgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLD---VQAVRRQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHfSLLERKTVFDNVA----LPLEcfgyskaeikkRVLELLEVVGISEKKNDKP-----------RNLSGGQKQR 144
Cdd:TIGR03797 529 LGVVLQN-GRLMSGSIFENIAggapLTLD-----------EAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQR 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 145 VAIARALALNPQVLLCDEATSALDpNTTKSILSllEDINkKLGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEi 224
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALD-NRTQAIVS--ESLE-RLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE- 670
|
....*...
gi 497582239 225 fLRNTKGL 232
Cdd:TIGR03797 671 -LMAREGL 677
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
10-227 |
6.98e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 143.79 E-value: 6.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 10 YYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRKELGMIFQH--- 86
Cdd:PRK13652 13 YSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN---IREVRKFVGLVFQNpdd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 87 --FSllerKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEAT 164
Cdd:PRK13652 90 qiFS----PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 165 SALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLR 227
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-256 |
1.34e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 143.06 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGK-IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVkSLNEKQMRDLRKE 79
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQH-FSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVL 158
Cdd:PRK13636 84 VGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 159 LCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLRntkglRKLIGE 238
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE-----KEMLRK 238
|
250
....*....|....*....
gi 497582239 239 ESIILPK-GTNIKILFPKD 256
Cdd:PRK13636 239 VNLRLPRiGHLMEILKEKD 257
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-219 |
1.47e-40 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 141.09 E-value: 1.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVlkDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKqmrdlRKELG 81
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-----DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:cd03298 74 MLFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVG 219
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-215 |
2.24e-40 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 140.08 E-value: 2.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 3 SIKNVN-KYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSlnekqmRDLRKELG 81
Cdd:cd03226 1 RIENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHF-SLLERKTVFDNVALPLEcfgySKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:cd03226 75 YVMQDVdYQLFTDSVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 161 DEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEV 215
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-272 |
3.36e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 142.53 E-value: 3.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGK-----IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSV--LVSDKEVKSLNE---- 70
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 71 ---------------KQMRDLRKELGMIFQ--HFSLLErKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDK 133
Cdd:PRK13651 83 vleklviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFE-QTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 134 -PRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMEN 212
Cdd:PRK13651 162 sPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 213 GEVLEVGDTEEIfLRNTKGLRkligEESIILPKGTNIKILFPK---DISNEAIITTMARELNI 272
Cdd:PRK13651 241 GKIIKDGDTYDI-LSDNKFLI----ENNMEPPKLLNFVNKLEKkgiDVPKVTSIEELASEINM 298
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-225 |
3.42e-40 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 147.54 E-value: 3.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 15 QVLKDVSIEIESGEIFGIIGHSGAGKST----LLRCINgleeyQEGSVLVSDKEVKSLNEKQMRDLRKELGMIFQ--HFS 88
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 89 LLERKTVFDNVALPLECF--GYSKAEIKKRVLELLEVVGIS-EKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATS 165
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVHqpTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 166 ALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVF 514
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-234 |
3.83e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 142.28 E-value: 3.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYG-----KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKS-LNEKQMRD 75
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 76 LRKELGMIFQhFS---LLErKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDK-PRNLSGGQKQRVAIARAL 151
Cdd:PRK13641 83 LRKKVSLVFQ-FPeaqLFE-NTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKsPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 152 ALNPQVLLCDEATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFlRNTKG 231
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF-SDKEW 238
|
...
gi 497582239 232 LRK 234
Cdd:PRK13641 239 LKK 241
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-225 |
3.96e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 141.34 E-value: 3.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 6 NVNKYYGKIQ---VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEV---KSLNEKQMRDLRKE 79
Cdd:PRK14246 12 NISRLYLYINdkaILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHFSLLERKTVFDNVALPLECFGYS-KAEIKKRVLELLEVVG----ISEKKNDKPRNLSGGQKQRVAIARALALN 154
Cdd:PRK14246 92 VGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497582239 155 PQVLLCDEATSALDPNTTKSILSLLEDINKKlgITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-225 |
4.62e-40 |
|
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: 140.60 E-value: 4.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGlEEYQegsvlVSDKEVKSLNEK----QMRDL 76
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-DLPP-----TYGNDVRLFGERrggeDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKELGMI--FQHFSLLERKTV--------FDNVALPLEcfgYSKAEIKkRVLELLEVVGISEKKNDKPRNLSGGQKQRVA 146
Cdd:COG1119 77 RKRIGLVspALQLRFPRDETVldvvlsgfFDSIGLYRE---PTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 147 IARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-216 |
5.20e-40 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 148.33 E-value: 5.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY----GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDL 76
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKE-LGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNP 155
Cdd:PRK10535 84 RREhFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497582239 156 QVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQiCGRVAIMENGEVL 216
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-198 |
9.74e-40 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 140.22 E-value: 9.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVlvsdkevkSLNEKQMRDLRKEL 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI--------TLDGKPVEGPGAER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 497582239 161 DEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQME 198
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIE 190
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-217 |
2.46e-39 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 138.37 E-value: 2.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYG----KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDL 76
Cdd:PRK10584 6 IVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 R-KELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNP 155
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497582239 156 QVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQiCGRVAIMENGEVLE 217
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-224 |
2.62e-39 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 141.79 E-value: 2.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 19 DVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEK-QMRDLRKELGMIFQHFSLLERKTVFD 97
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 98 NVAlplecFGYSKAEIKKRVL---ELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKS 174
Cdd:TIGR02142 95 NLR-----YGMKRARPSERRIsfeRVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497582239 175 ILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-224 |
9.95e-39 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 137.97 E-value: 9.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRKEL 80
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVALPL-ECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLL 159
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 160 CDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-215 |
1.08e-38 |
|
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: 136.18 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYY--GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRKE 79
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHFSLLeRKTVFDNVALplecfGYSKAEiKKRVLELLEVVGISEKKNDKP-----------RNLSGGQKQRVAIA 148
Cdd:cd03245 80 IGYVPQDVTLF-YGTLRDNITL-----GAPLAD-DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 149 RALALNPQVLLCDEATSALDPNTTKSILSLLedinKKL--GITIIVVTHQMEVIkQICGRVAIMENGEV 215
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERL----RQLlgDKTLIIITHRPSLL-DLVDRIIVMDSGRI 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-235 |
1.39e-38 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 143.37 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVN-KYYGKIQ-VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKqmrDLRKE 79
Cdd:COG4987 334 LELEDVSfRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED---DLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQH---FSllerKTVFDN--VALPlecfGYSKAEikkrVLELLEVVGISEKKNDKP-----------RNLSGGQKQ 143
Cdd:COG4987 411 IAVVPQRphlFD----TTLRENlrLARP----DATDEE----LWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 144 RVAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEE 223
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEE 555
|
250
....*....|..
gi 497582239 224 IfLRNTKGLRKL 235
Cdd:COG4987 556 L-LAQNGRYRQL 566
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-224 |
7.75e-38 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 140.71 E-value: 7.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY-----GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGS--VLVSDKEVKSLNEKQM 73
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 74 RDLR--KELGMIFQHFSLLERKTVFDNVA------LPLEcFGYSKAEIkkrvleLLEVVGISEKK-----NDKPRNLSGG 140
Cdd:TIGR03269 359 GRGRakRYIGILHQEYDLYPHRTVLDNLTeaigleLPDE-LARMKAVI------TLKMVGFDEEKaeeilDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 141 QKQRVAIARALALNPQVLLCDEATSALDPNT----TKSILSLLEDINKklgiTIIVVTHQMEVIKQICGRVAIMENGEVL 216
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITkvdvTHSILKAREEMEQ----TFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
....*...
gi 497582239 217 EVGDTEEI 224
Cdd:TIGR03269 508 KIGDPEEI 515
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-225 |
1.61e-37 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 134.52 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 5 KNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEY-----QEGSVLVSDKEvksLNEKQMR--DLR 77
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKN---LYAPDVDpvEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 78 KELGMIFQH---FSllerKTVFDNVALPLECFGYsKAEIKKRVLELLEVVGISEKKNDKPR----NLSGGQKQRVAIARA 150
Cdd:PRK14243 91 RRIGMVFQKpnpFP----KSIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKqsglSLSGGQQQRLCIARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 151 LALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLgiTIIVVTHQMevikQICGRVAIM-------------ENGEVLE 217
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNM----QQAARVSDMtaffnveltegggRYGYLVE 239
|
....*...
gi 497582239 218 VGDTEEIF 225
Cdd:PRK14243 240 FDRTEKIF 247
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-228 |
2.36e-37 |
|
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: 133.12 E-value: 2.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVN-KYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLnekQMRDLRKEL 80
Cdd:cd03253 1 IEFENVTfAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV---TLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHfSLLERKTVFDNV------ALPLECFGYSK-AEIKKRVLELLEvvGISEKKNDKPRNLSGGQKQRVAIARALAL 153
Cdd:cd03253 78 GVVPQD-TVLFNDTIGYNIrygrpdATDEEVIEAAKaAQIHDKIMRFPD--GYDTIVGERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 154 NPQVLLCDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEIFLRN 228
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKG 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-215 |
2.94e-37 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 131.18 E-value: 2.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQ--VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLrke 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHFSLLErKTVFDNValplecfgyskaeikkrvlellevvgisekkndkprnLSGGQKQRVAIARALALNPQVLL 159
Cdd:cd03246 78 VGYLPQDDELFS-GSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 160 CDEATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQiCGRVAIMENGEV 215
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-228 |
1.17e-36 |
|
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: 131.19 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVN-KYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdLRKEL 80
Cdd:cd03254 3 IEFENVNfSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS---LRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERkTVFDNVALplecfGYSKAEiKKRVLELLEVVGISEKKNDKPR-----------NLSGGQKQRVAIAR 149
Cdd:cd03254 80 GVVLQDTFLFSG-TIMENIRL-----GRPNAT-DEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 150 ALALNPQVLLCDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEIFLRN 228
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-225 |
1.37e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 132.82 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGK-----IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKS--LNEKQMR 74
Cdd:PRK13645 7 IILDNVSYTYAKktpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 75 DLRKELGMIFQ--HFSLLErKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDK-PRNLSGGQKQRVAIARAL 151
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQ-ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497582239 152 ALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-225 |
1.68e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 132.03 E-value: 1.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVN-KYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVsdKEVKSLNEKQMRDLRKE 79
Cdd:PRK13644 1 MIRLENVSySYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV--SGIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQH-FSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVL 158
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 159 LCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIkQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-223 |
1.98e-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: 130.74 E-value: 1.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYY---GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTllrCINGLEEY---QEGSVLVSDKEVKSLNekqMRD 75
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERFydpTSGEILLDGVDIRDLN---LRW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 76 LRKELGMIFQHFSLLERkTVFDNVALPLE----------CfgySKAEIKKRVLELLE----VVGisekknDKPRNLSGGQ 141
Cdd:cd03249 75 LRSQIGLVSQEPVLFDG-TIAENIRYGKPdatdeeveeaA---KKANIHDFIMSLPDgydtLVG------ERGSQLSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 142 KQRVAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDT 221
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTH 221
|
..
gi 497582239 222 EE 223
Cdd:cd03249 222 DE 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-219 |
2.12e-36 |
|
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: 130.35 E-value: 2.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYY----------------------GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVL 59
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 60 VsDKEVKSLnekqmrdlrKELGMIFQhfsllERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSG 139
Cdd:cd03220 81 V-RGRVSSL---------LGLGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 140 GQKQRVAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVG 219
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-228 |
4.81e-36 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 129.66 E-value: 4.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGK--IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLnekQMRDLRKE 79
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY---TLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHfSLLERKTVFDNVALPLEcfGYSKAEIKK--RVLELLEVV-----GISEKKNDKPRNLSGGQKQRVAIARALA 152
Cdd:cd03251 78 IGLVSQD-VFLFNDTVAENIAYGRP--GATREEVEEaaRAANAHEFImelpeGYDTVIGERGVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 153 LNPQVLLCDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQIcGRVAIMENGEVLEVGDTEEIFLRN 228
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELLAQG 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-224 |
5.31e-36 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 130.20 E-value: 5.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEkqmRDLRKEL 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS---RELAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQ--HFSLleRKTVFDNVAlplecFG---YSK----AEIKKRV---LELLEVVGISEKKNDkprNLSGGQKQRVAIA 148
Cdd:COG4604 78 AILRQenHINS--RLTVRELVA-----FGrfpYSKgrltAEDREIIdeaIAYLDLEDLADRYLD---ELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 149 RALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
13-245 |
5.37e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 131.90 E-value: 5.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 13 KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSD----------KEVKSLNEKQMRD---LRKE 79
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhELITNPYSKKIKNfkeLRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQ--HFSL----LERKTVFDNVALplecfGYSKAEIKKRVLELLEVVGISEKKNDK-PRNLSGGQKQRVAIARALA 152
Cdd:PRK13631 118 VSMVFQfpEYQLfkdtIEKDIMFGPVAL-----GVKKSEAKKLAKFYLNKMGLDDSYLERsPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 153 LNPQVLLCDEATSALDPNTTKSILSLLEDiNKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLRNTkgl 232
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH--- 268
|
250
....*....|...
gi 497582239 233 rkLIGEESIILPK 245
Cdd:PRK13631 269 --IINSTSIQVPR 279
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-228 |
7.01e-36 |
|
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: 129.53 E-value: 7.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdLRKELGMIFQHFSLLERkTV 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW---LRRQVGVVLQENVLFNR-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 96 FDNVALPLECFGYSKAEIKKR-------VLELLEvvGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALD 168
Cdd:cd03252 93 RDNIALADPGMSMERVIEAAKlagahdfISELPE--GYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 169 PNTTKSILSLLEDINKklGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEIFLRN 228
Cdd:cd03252 171 YESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-225 |
1.85e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 129.00 E-value: 1.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYqEGSVLVSDKeVKSLNEK------QMRD 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGR-VEFFNQNiyerrvNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 76 LRKELGMIFQHFSLLErKTVFDNVALPLECFGYS-KAEIKKRVLELLEVVG----ISEKKNDKPRNLSGGQKQRVAIARA 150
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRpKLEIDDIVESALKDADlwdeIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 151 LALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMEN-----GEVLEVGDTEEIF 225
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIF 244
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-269 |
2.34e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 129.51 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGK-----IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKS-LNEKQMRD 75
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 76 LRKELGMIFQhfsLLERKTVFDNVALPLEC----FGYSKAEIKKRVLELLEVVGISEKKNDK-PRNLSGGQKQRVAIARA 150
Cdd:PRK13646 83 VRKRIGMVFQ---FPESQLFEDTVEREIIFgpknFKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 151 LALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLRNTK 230
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 497582239 231 GLRKLIGEESII-LPKGTNIK--ILFPKDISNEAIITTMARE 269
Cdd:PRK13646 240 LADWHIGLPEIVqLQYDFEQKyqTKLKDIALTEEEFVSLYKE 281
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-224 |
5.46e-35 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 127.73 E-value: 5.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDK-----EVKSLNEKQMRD 75
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 76 L-RKELGMIFQHFSLLERKTVF--DNVALPLECFG---YskAEIKKRVLELLEVVGISEKK-NDKPRNLSGGQKQRVAIA 148
Cdd:PRK11701 86 LlRTEWGFVHQHPRDGLRMQVSagGNIGERLMAVGarhY--GDIRATAGDWLERVEIDAARiDDLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 149 RALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQV 239
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-229 |
1.10e-34 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 128.69 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 12 GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQ---EGSVLVSDKEVKSLNEKQMRDLR-KELGMIFQH- 86
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKLRaEQISMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 87 -FSLLERKTVFDNVALPLECF-GYSKAEIKKRVLELLEVVGISEKK---NDKPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:PRK09473 107 mTSLNPYMRVGEQLMEVLMLHkGMSKAEAFEESVRMLDAVKMPEARkrmKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLRNT 229
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-200 |
1.46e-34 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 132.03 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVN-KYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKqmrDLRKEL 80
Cdd:TIGR02857 322 LEFSGVSvAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD---SWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLErKTVFDNVAlpLECFGYSKAEIkKRVLE---LLEVV-----GISEKKNDKPRNLSGGQKQRVAIARALA 152
Cdd:TIGR02857 399 AWVPQHPFLFA-GTIAENIR--LARPDASDAEI-REALEragLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 497582239 153 LNPQVLLCDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVI 200
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA 520
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-223 |
1.70e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 126.42 E-value: 1.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCING-LEEYQeGSVLVSDKEVKSLnekQMRDLRKE 79
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDS-GEVRLNGRPLADW---SPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALA------L 153
Cdd:PRK13548 78 RAVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 154 NPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEE 223
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
1.75e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 127.61 E-value: 1.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSlnekQMRDLRKELG 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS----RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-213 |
2.84e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 128.02 E-value: 2.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSlnekQMRDLRKELG 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA----RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQhFSLLERK-TVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:PRK13536 118 VVPQ-FDNLDLEfTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497582239 161 DEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENG 213
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-219 |
1.21e-33 |
|
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: 122.27 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 15 QVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQ--EGSVLVSDKEVKslnekqMRDLRKELGMIFQHFSLLER 92
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLD------KRSFRKIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 93 KTVFDNVALPLECfgyskaeikkrvlellevvgisekkndkpRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTT 172
Cdd:cd03213 97 LTVRETLMFAAKL-----------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497582239 173 KSILSLLEDInKKLGITIIVVTHQ--MEVIKQiCGRVAIMENGEVLEVG 219
Cdd:cd03213 148 LQVMSLLRRL-ADTGRTIICSIHQpsSEIFEL-FDKLLLLSQGRVIYFG 194
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-228 |
4.07e-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: 128.30 E-value: 4.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYG--KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLnekQMRDLRKE 79
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY---TLASLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHFSLLErKTVFDNVALPlECFGYSKAEIKkRVLE---LLEVV-----GISEKKNDKPRNLSGGQKQRVAIARAL 151
Cdd:TIGR02203 408 VALVSQDVVLFN-DTIANNIAYG-RTEQADRAEIE-RALAaayAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 152 ALNPQVLLCDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEIFLRN 228
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLARN 558
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
14-225 |
4.63e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 123.28 E-value: 4.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 14 IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRKELGMIFQH-FSLLER 92
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN---VWNLRRKIGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 93 KTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTT 172
Cdd:PRK13642 97 ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497582239 173 KSILSLLEDINKKLGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
14-224 |
1.15e-32 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 121.82 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 14 IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVkSLNEKQMRDLRkeLGMIFQ--HFSLLE 91
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSQR--IRMIFQdpSTSLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 92 RKTVFDNVALPLEC-FGYSKAEIKKRVLELLEVVGI-SEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDP 169
Cdd:PRK15112 103 RQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 170 NTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:PRK15112 183 SMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-219 |
1.50e-32 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 120.29 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYY--GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRKE 79
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHfSLLERKTVFDNVAlPLEcfGYSKAEIkKRVLE---LLEVVGISEKKNDKP-----RNLSGGQKQRVAIARAL 151
Cdd:cd03244 80 ISIIPQD-PVLFSGTIRSNLD-PFG--EYSDEEL-WQALErvgLKEFVESLPGGLDTVveeggENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 152 ALNPQVLLCDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVG 219
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-225 |
2.24e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 122.54 E-value: 2.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 20 VSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYqEGSVLV-----SDKEVKSLNEKQMRDL-RKELGMIFQH--FSLLE 91
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMAeklefNGQDLQRISEKERRNLvGAEVAMIFQDpmTSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 92 RKTVFDNVALPLECF-GYSKAEIKKRVLELLEVVGI---SEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSAL 167
Cdd:PRK11022 105 CYTVGFQIMEAIKVHqGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTAL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 168 DPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK11022 185 DVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-225 |
2.90e-32 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 126.12 E-value: 2.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY----GKIQVLKDVSIEIESGEIFGIIGHSGAGKS----TLLRCINgleeyQEGSVLVSDK--------E 64
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLE-----QAGGLVQCDKmllrrrsrQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 65 VKSLNE---KQMRDLR-KELGMIFQH--FSLLERKTVFDNVALPLECF-GYSKAEIKKRVLELLEVVGISEKK---NDKP 134
Cdd:PRK10261 87 VIELSEqsaAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHqGASREEAMVEAKRMLDQVRIPEAQtilSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 135 RNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGE 214
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250
....*....|.
gi 497582239 215 VLEVGDTEEIF 225
Cdd:PRK10261 247 AVETGSVEQIF 257
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-223 |
2.95e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 119.12 E-value: 2.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGL--EEYQ-EGSVLvsdkevksLNEKQMRDL- 76
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSaSGEVL--------LNGRRLTALp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 --RKELGMIFQ------HFSllerktVFDNV--ALPLecfGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVA 146
Cdd:COG4136 73 aeQRRIGILFQddllfpHLS------VGENLafALPP---TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 147 IARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEvikqicgrvAIMENGEVLEVGDTEE 223
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE---------DAPAAGRVLDLGNWQH 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-225 |
4.76e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 119.84 E-value: 4.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEkqmRDLRKEL 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSP---WELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQH----FSLlerkTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALA---- 152
Cdd:COG4559 78 AVLPQHsslaFPF----TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwe 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 153 ---LNPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG4559 154 pvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-225 |
8.86e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 124.05 E-value: 8.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 15 QVLKDVSIEIESGEIFGIIGHSGAGKS-TLLRCINGLE----EYQEGSVLVSDKEVKSLNEKQMRDLR-KELGMIFQH-- 86
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPsppvVYPSGDIRFHGESLLHASEQTLRGVRgNKIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 87 FSL-----LErKTVFDNVALPLecfGYSKAEIKKRVLELLEVVGISEKK---NDKPRNLSGGQKQRVAIARALALNPQVL 158
Cdd:PRK15134 103 VSLnplhtLE-KQLYEVLSLHR---GMRREAARGEILNCLDRVGIRQAAkrlTDYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 159 LCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLF 245
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-239 |
1.34e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 118.46 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 5 KNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVK--SLNEKQmrdlRKELGM 82
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARA----RRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 83 IFQHFSLLERKTVFDNVALPLECF-GYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 162 EATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIfLRNTKGLRKLIGEE 239
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI-LQDEHVKRVYLGED 238
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-276 |
2.14e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 119.81 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYY-------G--------------KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVL 59
Cdd:COG4586 1 IIEVENLSKTYrvyekepGlkgalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 60 VSDKEVKslneKQMRDLRKELGMIF-QHFSLLerktvFDnvaLPL--------ECFGYSKAEIKKRVLELLEVVGISEKK 130
Cdd:COG4586 81 VLGYVPF----KRRKEFARRIGVVFgQRSQLW-----WD---LPAidsfrllkAIYRIPDAEYKKRLDELVELLDLGELL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 131 NdKP-RNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAI 209
Cdd:COG4586 149 D-TPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 210 MENGEVLEVGDTEEifLRNTKGLRKLI------GEESIILPKGT--------NIKILFPKDISNEAIITTMARELNI-DV 274
Cdd:COG4586 228 IDHGRIIYDGSLEE--LKERFGPYKTIvlelaePVPPLELPRGGevieregnRVRLEVDPRESLAEVLARLLARYPVrDL 305
|
..
gi 497582239 275 SI 276
Cdd:COG4586 306 TI 307
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-225 |
2.47e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 117.81 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdLRKEL 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ---LARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVA------LPLecFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALN 154
Cdd:PRK11231 79 ALLPQHHLTPEGITVRELVAygrspwLSL--WGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497582239 155 PQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-198 |
3.55e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 117.88 E-value: 3.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGK-----IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrd 75
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 76 lR-KELGMIFQHFSL--LERKTVFDNVALPL---ECFGYSKAEIKKR---VLELLEVVGIS-EKK-NDKPRNLSGGQKQR 144
Cdd:COG1101 78 -RaKYIGRVFQDPMMgtAPSMTIEENLALAYrrgKRRGLRRGLTKKRrelFRELLATLGLGlENRlDTKVGLLSGGQRQA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497582239 145 VAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQME 198
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNME 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-225 |
5.19e-31 |
|
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: 122.16 E-value: 5.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEkqmRDLRKELGMIFQHFSLLErKTV 95
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR---EELGRHIGYLPQDVELFD-GTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 96 FDNVAlpleCFGYSKAEikkRVLELLEVVGISE-----------KKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEAT 164
Cdd:COG4618 423 AENIA----RFGDADPE---KVVAAAKLAGVHEmilrlpdgydtRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497582239 165 SALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIkQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG4618 496 SNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLL-AAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-227 |
9.16e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 117.03 E-value: 9.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVkSLNEKQMRDLRKEL 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFD-NVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLL 159
Cdd:PRK13638 80 ATVFQDPEQQIFYTDIDsDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 160 CDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLR 227
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-225 |
1.06e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 118.08 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 12 GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLeeyQEGSVLVS-------DKEVKSLNEKQMRDL-RKELGMI 83
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI---TKDNWHVTadrfrwnGIDLLKLSPRERRKIiGREIAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 84 FQH--FSLLERKTVFDNV--ALPLECFGYS----KAEIKKRVLELLEVVGISEKK---NDKPRNLSGGQKQRVAIARALA 152
Cdd:COG4170 95 FQEpsSCLDPSAKIGDQLieAIPSWTFKGKwwqrFKWRKKRAIELLHRVGIKDHKdimNSYPHELTEGECQKVMIAMAIA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 153 LNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQIL 247
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-239 |
1.15e-30 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 121.04 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLrkEL 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL--GI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNV---ALPL-ECFGYSK---AEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALAL 153
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLyigRHLTkKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 154 NPQVLLCDEATSALdpnTTKSILSLLEDIN--KKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIflRNTKG 231
Cdd:PRK09700 163 DAKVIIMDEPTSSL---TNKEVDYLFLIMNqlRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV--SNDDI 237
|
....*...
gi 497582239 232 LRKLIGEE 239
Cdd:PRK09700 238 VRLMVGRE 245
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-216 |
1.28e-30 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 115.51 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 7 VNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDkEVKSlneKQMRDLRKELGMIF-Q 85
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPW---KRRKKFLRRIGVVFgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 86 HFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATS 165
Cdd:cd03267 103 KTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497582239 166 ALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVL 216
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-215 |
2.51e-29 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 111.79 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 15 QVLKDVSIEIESGEIFGIIGHSGAGKSTllrCINGLEEY---QEGSVLVSDKevkSLNEKQMRDLRKELGMIFQHFSLLE 91
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENFyqpQGGQVLLDGK---PISQYEHKYLHSKVSLVGQEPVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 92 RkTVFDNVA-----LPLECF--GYSKAEIKKRVLELLEvvGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEAT 164
Cdd:cd03248 102 R-SLQDNIAyglqsCSFECVkeAAQKAHAHSFISELAS--GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497582239 165 SALDPNTTKSILSLLEDINKKLgiTIIVVTHQMEVIKQiCGRVAIMENGEV 215
Cdd:cd03248 179 SALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-219 |
4.94e-29 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 116.84 E-value: 4.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 15 QVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKqmrDLRKELGMIFQHfSLLERKT 94
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQA---SLRAAIGIVPQD-TVLFNDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 95 VFDNVAlplecfgY-----SKAEIKK--RVLELLE-----------VVGisEK--KndkprnLSGGQKQRVAIARALALN 154
Cdd:COG5265 448 IAYNIA-------YgrpdaSEEEVEAaaRAAQIHDfieslpdgydtRVG--ERglK------LSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 155 PQVLLCDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVI---KQIcgrvAIMENGEVLEVG 219
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIvdaDEI----LVLEAGRIVERG 574
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-225 |
5.22e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 112.50 E-value: 5.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEE----YQ-EGSVLVSDKEVksLNEKQMRDLRKELGMIFQHFSLL 90
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgYRySGDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 91 ERkTVFDNVA--------LPLECFgysKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDE 162
Cdd:PRK14271 114 PM-SIMDNVLagvrahklVPRKEF---RGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 163 ATSALDPNTTKSILSLLEDINKKLgiTIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-228 |
6.56e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 111.62 E-value: 6.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRdlRKEL 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA--RMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDN--VA-------------LPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRV 145
Cdd:PRK11300 83 VRTFQHVRLFREMTVIENllVAqhqqlktglfsglLKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 146 AIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIf 225
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI- 241
|
...
gi 497582239 226 lRN 228
Cdd:PRK11300 242 -RN 243
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
5-219 |
9.69e-29 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 110.44 E-value: 9.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 5 KNVNKYygkIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQE---GSVLVSDKEVKSlneKQMRdlrKELG 81
Cdd:cd03234 14 KNWNKY---ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP---DQFQ---KCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFD------NVALPlECFgySKAEIKKRV-LELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALN 154
Cdd:cd03234 85 YVRQDDILLPGLTVREtltytaILRLP-RKS--SDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 155 PQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEV-IKQICGRVAIMENGEVLEVG 219
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQPRSdLFRLFDRILLLSSGEIVYSG 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-201 |
1.47e-28 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 109.66 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQ--VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKqmrdlrk 78
Cdd:COG2401 28 AIVLEAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREA------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 79 elgmifqhfsllerkTVFDNVALPLEcfgyskaeiKKRVLELLEVVGISEKKN--DKPRNLSGGQKQRVAIARALALNPQ 156
Cdd:COG2401 101 ---------------SLIDAIGRKGD---------FKDAVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 497582239 157 VLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIK 201
Cdd:COG2401 157 LLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVID 201
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-228 |
1.54e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.44 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVN-KYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRKEL 80
Cdd:PRK13657 335 VEFDDVSfSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERkTVFDNVALPLEcfGYSKAEIKkRVLELLEVVGISEKKNDK--------PRNLSGGQKQRVAIARALA 152
Cdd:PRK13657 412 AVVFQDAGLFNR-SIEDNIRVGRP--DATDEEMR-AAAERAQAHDFIERKPDGydtvvgerGRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 153 LNPQVLLCDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEIFLRN 228
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVARG 560
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-241 |
2.41e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 113.01 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEK----QMRDL 76
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARaasrRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 77 RKELGMIFQhFSLleRKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQ 156
Cdd:PRK09536 83 PQDTSLSFE-FDV--RQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 157 VLLCDEATSALDPN----TTKSILSLLEDinkklGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF----LRN 228
Cdd:PRK09536 160 VLLLDEPTASLDINhqvrTLELVRRLVDD-----GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLtadtLRA 234
|
250
....*....|...
gi 497582239 229 TKGLRKLIGEESI 241
Cdd:PRK09536 235 AFDARTAVGTDPA 247
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-228 |
2.52e-28 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 109.58 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKslNEKQMRDLRKEL 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT--DWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVAlpLECFGYSKAEIKKRVLELLEVVG-ISEKKNDKPRNLSGGQKQRVAIARALALNPQVLL 159
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLA--MGGFFAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 160 CDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLeVGDTEEIFLRN 228
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV-LEDTGDALLAN 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-224 |
3.36e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.90 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEieSGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKevkslNEKQMRDLRKEL 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTPPSRRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:PRK10771 74 SMLFQENNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497582239 161 DEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:PRK10771 154 DEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-228 |
7.17e-28 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 113.58 E-value: 7.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYY-GK-IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEvksLNEKQMRDLRKE 79
Cdd:PRK11176 342 IEFRNVTFTYpGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHFSLLErKTVFDNVALPLECFgYSKAEIKK--RVLELLEVVGISEKKND-----KPRNLSGGQKQRVAIARALA 152
Cdd:PRK11176 419 VALVSQNVHLFN-DTIANNIAYARTEQ-YSREQIEEaaRMAYAMDFINKMDNGLDtvigeNGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 153 LNPQVLLCDEATSALDPNTTKSILSLLEDINKKLgiTIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEIFLRN 228
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQN 569
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-224 |
1.19e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 112.63 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKN--VNKYYGKiQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQeGSVLVSDKEVKSLNEKQmrdLRKE 79
Cdd:PRK11174 350 IEAEDleILSPDGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPES---WRKH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHFSLLErKTVFDNVALplecfGYSKAEiKKRVLELLEVVGISEKKNDKPRNL-----------SGGQKQRVAIA 148
Cdd:PRK11174 425 LSWVGQNPQLPH-GTLRDNVLL-----GNPDAS-DEQLQQALENAWVSEFLPLLPQGLdtpigdqaaglSVGQAQRLALA 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 149 RALALNPQVLLCDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEI 224
Cdd:PRK11174 498 RALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAEL 570
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-230 |
1.53e-27 |
|
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: 107.10 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 4 IKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSlnekqmRDLRKeLGMI 83
Cdd:TIGR03740 3 TKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR------KDLHK-IGSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 84 FQHFSLLERKTVFDNVALPLECFGYSKAEIkkrvLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEA 163
Cdd:TIGR03740 76 IESPPLYENLTARENLKVHTTLLGLPDSRI----DEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 164 TSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVG------DTEEIFLRNTK 230
Cdd:TIGR03740 152 TNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLGYQGkinkseNLEKLFVEVVK 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-231 |
1.55e-27 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 113.18 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKY---YGKIQVLKdVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVkslnEKQMRDLRK 78
Cdd:TIGR01257 929 VCVKNLVKIfepSGRPAVDR-LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQ 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 79 ELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVL 158
Cdd:TIGR01257 1004 SLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 159 LCDEATSALDPNTTKSILSLLedINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGdtEEIFLRNTKG 231
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG--TPLFLKNCFG 1152
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-215 |
2.53e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.31 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 4 IKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSdkevkslnekqmRDLRkeLGMI 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------------KGLR--IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 84 FQHFSLLERKTVFDNV--------------ALPLECFGYSKAEIKK------------------RVLELLEVVGISEKKN 131
Cdd:COG0488 67 PQEPPLDDDLTVLDTVldgdaelraleaelEELEAKLAEPDEDLERlaelqeefealggweaeaRAEEILSGLGFPEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 132 DKP-RNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTksilSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIM 210
Cdd:COG0488 147 DRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESI----EWLEEFLKNYPGTVLVVSHDRYFLDRVATRILEL 222
|
....*
gi 497582239 211 ENGEV 215
Cdd:COG0488 223 DRGKL 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-223 |
3.70e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.46 E-value: 3.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYY--GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRdlrke 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR----- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 lgmifQHFSLL-ERKTVF-----DNVALPlecfgySKAEIKKRVLELLEVVGIsEK--KNDKP---------RNLSGGQK 142
Cdd:PRK11160 414 -----QAISVVsQRVHLFsatlrDNLLLA------APNASDEALIEVLQQVGL-EKllEDDKGlnawlgeggRQLSGGEQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 143 QRVAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQ---MEVIKQICgrvaIMENGEVLEVG 219
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRltgLEQFDRIC----VMDNGQIIEQG 555
|
....
gi 497582239 220 DTEE 223
Cdd:PRK11160 556 THQE 559
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-223 |
6.37e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.15 E-value: 6.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKeVKslnekqmrdlrkeL 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET-VK-------------I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLL-ERKTVFDNV--ALP----------LECFGYSKAEIKKRVlellevvgisekkndkpRNLSGGQKQRVAI 147
Cdd:COG0488 381 GYFDQHQEELdPDKTVLDELrdGAPggteqevrgyLGRFLFSGDDAFKPV-----------------GVLSGGEKARLAL 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 148 ARALALNPQVLLCDEATSALDPNTTKSILSLLEDINkklGiTIIVVTHQMEVIKQICGRVAIMENGEVLE-VGDTEE 223
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHDRYFLDRVATRILEFEDGGVREyPGGYDD 516
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-215 |
1.45e-26 |
|
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: 103.28 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDL--------RKELGmifqhf 87
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedRKREG------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 88 sLLERKTVFDNVALPlecfgyskaeikkrvlellevvgisekkndkpRNLSGGQKQRVAIARALALNPQVLLCDEATSAL 167
Cdd:cd03215 89 -LVLDLSVAENIALS--------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 497582239 168 DPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEV 215
Cdd:cd03215 136 DVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-219 |
2.15e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 109.43 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 13 KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdLRKELGMIFQHfSLLER 92
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHY---LHRQVALVGQE-PVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 93 KTVFDNVALPLEcfGYSKAEIKKRVLELLEVVGISEKKND-------KPRNLSGGQKQRVAIARALALNPQVLLCDEATS 165
Cdd:TIGR00958 569 GSVRENIAYGLT--DTPDEEIMAAAKAANAHDFIMEFPNGydtevgeKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497582239 166 ALDpnttKSILSLLEDINKKLGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVG 219
Cdd:TIGR00958 647 ALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-219 |
2.70e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 102.39 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYG--KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLnEKQMRDLrke 79
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQhfslleRKTVFDNValplecfgyskaeikkrvleLLEVVGisekkndkpRNLSGGQKQRVAIARALALNPQVLL 159
Cdd:cd03247 77 ISVLNQ------RPYLFDTT--------------------LRNNLG---------RRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 160 CDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQIcGRVAIMENGEVLEVG 219
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-202 |
3.70e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 103.26 E-value: 3.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRdlrKEL 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR---QQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLErKTVFDNVALPLECFGysKAEIKKRVLELLEVVGISEKKNDKPRN-LSGGQKQRVAIARALALNPQVLL 159
Cdd:PRK10247 84 SYCAQTPTLFG-DTVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 497582239 160 CDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQ 202
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH 203
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-244 |
1.67e-25 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.56 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdLRKELGMIFQHFSLLERKTV 95
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA---FARKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 96 FDNVAL-------PLECFGyskAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALD 168
Cdd:PRK10575 103 RELVAIgrypwhgALGRFG---AADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 169 PNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLRNTkgLRKLIGEESIILP 244
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET--LEQIYGIPMGILP 253
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-224 |
2.34e-25 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 103.80 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 19 DVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVlvsdkevkSLNEKQMRDLRKEL---------GMIFQHFSL 89
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRI--------VLNGRVLFDAEKGIclppekrriGYVFQDARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 90 LERKTVFDNValpleCFGYSKAEIKK--RVLELLevvGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSAL 167
Cdd:PRK11144 88 FPHYKVRGNL-----RYGMAKSMVAQfdKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 168 DPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:PRK11144 160 DLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-224 |
4.37e-25 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 105.59 E-value: 4.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 19 DVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSlnekqmRDL--RKELGMIFQHFSLLERKTVF 96
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA------GDIatRRRVGYMSQAFSLYGELTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 97 DNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSIL 176
Cdd:NF033858 358 QNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFW 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497582239 177 SLLEDINKKLGITIIVVTHQM-EVikQICGRVAIMENGEVLEVGDTEEI 224
Cdd:NF033858 438 RLLIELSREDGVTIFISTHFMnEA--ERCDRISLMHAGRVLASDTPAAL 484
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-215 |
5.13e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.72 E-value: 5.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDL--------RKELGmIFQHF 87
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAgiayvpedRKGEG-LVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 88 SllerktVFDNVALP----LECFGY-SKAEIKKRVLELLEVVGISEKKNDKP-RNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:COG1129 346 S------IRENITLAsldrLSRGGLlDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEV 215
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-219 |
6.07e-25 |
|
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: 99.79 E-value: 6.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGK--IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRKE 79
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMIFQHFSLLErKTVFDNvalpLECFG-YSKAEIkkrvlelLEVVGISEKKNdkprNLSGGQKQRVAIARALALNPQVL 158
Cdd:cd03369 84 LTIIPQDPTLFS-GTIRSN----LDPFDeYSDEEI-------YGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497582239 159 LCDEATSALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVG 219
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-196 |
1.23e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.12 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEvkslnekqmrdlrkelGMIFqhfslLERK-- 93
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA----------------RVLF-----LPQRpy 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 94 ----TVFDNVALPLECFGYSKAEIKkrvlELLEVVGIS------EKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEA 163
Cdd:COG4178 437 lplgTLREALLYPATAEAFSDAELR----EALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190
....*....|....*....|....*....|...
gi 497582239 164 TSALDPNTTKSILSLLEDINKklGITIIVVTHQ 196
Cdd:COG4178 513 TSALDEENEAALYQLLREELP--GTTVISVGHR 543
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-213 |
1.93e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 103.07 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 3 SIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRD-LRKELG 81
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAS---TTAaLAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNV---ALPlECFGY-SKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQV 157
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLylgQLP-HKGGIvNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 158 LLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENG 213
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-214 |
2.16e-24 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 102.89 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 4 IKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMrdLRKELGMI 83
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA--LENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 84 FQHFSLLERKTVFDNVAL---PLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 161 DEATSALdpnTTKSILSLLEDINK--KLGITIIVVTHQMEVIKQICGRVAIMENGE 214
Cdd:PRK10982 159 DEPTSSL---TEKEVNHLFTIIRKlkERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-225 |
3.05e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 102.87 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQ-VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEkqmRDLRKEL 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLErKTVFDNVALPLECfgyskaeIKKRVLELLEVV-----------GISEKKNDKPRNLSGGQKQRVAIAR 149
Cdd:PRK10790 418 AMVQQDPVVLA-DTFLANVTLGRDI-------SEEQVWQALETVqlaelarslpdGLYTPLGEQGNNLSVGQKQLLALAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 150 ALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKlgITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-214 |
3.83e-24 |
|
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: 97.54 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSdkevkslnekqmrdlrkelGMIF---QhFSLLER 92
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP-------------------GSIAyvsQ-EPWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 93 KTVFDNValpleCFG-------YSKAeIK----KRVLELLE-----VVGisekknDKPRNLSGGQKQRVAIARALALNPQ 156
Cdd:cd03250 80 GTIRENI-----LFGkpfdeerYEKV-IKacalEPDLEILPdgdltEIG------EKGINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 157 VLLCDEATSALDPNTTKSILSLLedINKKL--GITIIVVTHQMEVIKQiCGRVAIMENGE 214
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFENC--ILGLLlnNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-241 |
1.07e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 97.75 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 11 YGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdLRKELGMIFQHFSLL 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE---VARRIGLLAQNATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 91 ERKTVFDNVA------LPLecFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEAT 164
Cdd:PRK10253 94 GDITVQELVArgryphQPL--FTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 165 SALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI----FLRNTKGLRKLIGEES 240
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIvtaeLIERIYGLRCMIIDDP 251
|
.
gi 497582239 241 I 241
Cdd:PRK10253 252 V 252
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-224 |
1.85e-23 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 98.34 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 12 GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEE----YQEGSVLVSDKEVKSLNEKQMRDL-RKELGMIFQh 86
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERRKLvGHNVSMIFQ- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 87 fsllERKTVFDnvalPLECFGYSKAEI-----------------KKRVLELLEVVGISEKKN---DKPRNLSGGQKQRVA 146
Cdd:PRK15093 97 ----EPQSCLD----PSERVGRQLMQNipgwtykgrwwqrfgwrKRRAIELLHRVGIKDHKDamrSFPYELTEGECQKVM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 147 IARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:PRK15093 169 IAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-214 |
3.61e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 99.62 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 5 KNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEY--QEGSVLVSDKEVKSLNekqMRDL-RKELG 81
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIFEGEELQASN---IRDTeRAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLEC--FGYSK-AEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVL 158
Cdd:PRK13549 86 IIHQELALVKELSVLENIFLGNEItpGGIMDyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 159 LCDEATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGE 214
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-210 |
4.92e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 99.35 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 15 QVLKDVSIEIESGEIFGIIGHSGAGKSTLLrciNGLEEYQEGSVLVSDKEV---KSLNEKQMRDLR---KELGMIFQHFS 88
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGSGSVLlngMPIDAKEMRAISayvQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 89 LLERKTVFDNVALPLEcfgYSKAEIKKRVLELLEVVGISEKKN------DKPRNLSGGQKQRVAIARALALNPQVLLCDE 162
Cdd:TIGR00955 116 VREHLMFQAHLRMPRR---VTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 163 ATSALDPNTTKSILSLLEDINKKlGITIIVVTHQ-----MEVIKQIC----GRVAIM 210
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpsselFELFDKIIlmaeGRVAYL 248
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-196 |
9.40e-23 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 98.20 E-value: 9.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 10 YYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKqmrDLRKELGMIFQHFSL 89
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD---EVRRRVSVCAQDAHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 90 LErKTVFDNVALPleCFGYSKAEikkrVLELLEVVGISEKKNDKP-----------RNLSGGQKQRVAIARALALNPQVL 158
Cdd:TIGR02868 421 FD-TTVRENLRLA--RPDATDEE----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPIL 493
|
170 180 190
....*....|....*....|....*....|....*....
gi 497582239 159 LCDEATSALDPNTTKsilSLLEDINKKL-GITIIVVTHQ 196
Cdd:TIGR02868 494 LLDEPTEHLDAETAD---ELLEDLLAALsGRTVVLITHH 529
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-256 |
1.36e-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: 97.59 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEY--QEGSVLVSDKEVKSLNekqMRDL-R 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgtWDGEIYWSGSPLKASN---IRDTeR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 78 KELGMIFQHFSLLERKTVFDNVALPLEC----FGYSKAEIKKRVLELLEVVGISEKKNDKP-RNLSGGQKQRVAIARALA 152
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 153 LNPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEvlEVGdteeiflrnTKGL 232
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ--HVA---------TKDM 225
|
250 260
....*....|....*....|....
gi 497582239 233 RKLIGEESIILPKGTNIKILFPKD 256
Cdd:TIGR02633 226 STMSEDDIITMMVGREITSLYPHE 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-224 |
1.52e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.81 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLrkEL 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL--GI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNValpleCFGYSK-AEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLL 159
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENI-----LFGLPKrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 160 CDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-228 |
2.42e-22 |
|
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: 97.50 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRdlrkelgmifQHFSLLERK-- 93
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR----------QFINYLPQEpy 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 94 ----TVFDNVALplecfgysKAEIKKRVLELLEVVGISEKKNDKPR--------------NLSGGQKQRVAIARALALNP 155
Cdd:TIGR01193 559 ifsgSILENLLL--------GAKENVSQDEIWAACEIAEIKDDIENmplgyqtelseegsSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 156 QVLLCDEATSALDPNTTKSILSLLEDINKKlgiTIIVVTHQMEVIKQIcGRVAIMENGEVLEVGDTEEIFLRN 228
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLDRN 699
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-214 |
6.34e-22 |
|
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: 89.82 E-value: 6.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVkslnekqmrdlrkelg 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 miFQHFSllerktvfdnvalplecfgyskaeikkrvlellevvgisekkndkprNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:cd03221 65 --IGYFE-----------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497582239 162 EATSALDpntTKSILSLLEDINKKLGiTIIVVTHQMEVIKQICGRVAIMENGE 214
Cdd:cd03221 96 EPTNHLD---LESIEALEEALKEYPG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-196 |
3.63e-21 |
|
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: 88.36 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVlvsdkevkslnekqMRDLRKELGMIFQHfSLLERKTV 95
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------------GMPEGEDLLFLPQR-PYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 96 FDNVALPLEcfgyskaeikkrvlellevvgisekkndkpRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSI 175
Cdd:cd03223 81 REQLIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL 130
|
170 180
....*....|....*....|.
gi 497582239 176 LSLLedinKKLGITIIVVTHQ 196
Cdd:cd03223 131 YQLL----KELGITVISVGHR 147
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-225 |
5.84e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 90.14 E-value: 5.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 18 KDVSIEIESGEIFGIIGHSGAGKStlLRCINGLE------EYQEGSVLVSDKEVKSlnekqmRDLR-KELGMIFQH---- 86
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVAP------CALRgRKIATIMQNprsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 87 FSLLerKTVFDNVALPLECFGysKAEIKKRVLELLEVVGISEKK---NDKPRNLSGGQKQRVAIARALALNPQVLLCDEA 163
Cdd:PRK10418 92 FNPL--HTMHTHARETCLALG--KPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497582239 164 TSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-200 |
1.18e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 89.02 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKevkslnekqmrdLRkeL 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LR--I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLlerktvfdNVALPL--ECFGYSKAEIKKR-VLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQV 157
Cdd:PRK09544 70 GYVPQKLYL--------DTTLPLtvNRFLRLRPGTKKEdILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 497582239 158 LLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVI 200
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-224 |
1.57e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 92.08 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLnekQMRDLRKELGMIFQH---FSller 92
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTpflFS---- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 93 KTVFDNVALPleCFGYSKAEIKkRVLELLEV--------VGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEAT 164
Cdd:PRK10789 403 DTVANNIALG--RPDATQQEIE-HVARLASVhddilrlpQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 165 SALDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEI 224
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQL 536
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-224 |
3.10e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.86 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRdlrkELGMIF-----QHFSLL 90
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERR----RLGVAYipedrLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 91 ERKTVFDNVAL------PLECFG-YSKAEIKKRVLELLE---VVGISEkkNDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:COG3845 349 PDMSVAENLILgryrrpPFSRGGfLDRKAIRAFAEELIEefdVRTPGP--DTPARSLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497582239 161 DEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:COG3845 427 AQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-225 |
1.13e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.86 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 17 LKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRKELGMIFQHFSLLERKTVF 96
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 97 DNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSIL 176
Cdd:PRK15056 103 MGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARII 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497582239 177 SLLEDINKKlGITIIVVTHQMEVIKQICGrVAIMENGEVLEVGDTEEIF 225
Cdd:PRK15056 183 SLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTF 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-222 |
2.28e-19 |
|
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: 84.50 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQ--EGSVLVSDKEVKSL--NEKQmrdlR 77
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLppEERA----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 78 KELGMIFQHfsllerktvfdnvalPLECFGYskaeikkRVLELLEVVGIsekkndkprNLSGGQKQRVAIARALALNPQV 157
Cdd:cd03217 77 LGIFLAFQY---------------PPEIPGV-------KNADFLRYVNE---------GFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 158 LLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICG-RVAIMENGEVLEVGDTE 222
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIKPdRVHVLYDGRIVKSGDKE 190
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
2.85e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.16 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVK-SLNEKQM-----R 74
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEAChylghR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 75 D-LRKELgmifqhfsllerkTVFDNVALPLECFGYSKAEIkkrvLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALAL 153
Cdd:PRK13539 82 NaMKPAL-------------TVAENLEFWAAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 497582239 154 NPQVLLCDEATSALDPNTTKSILSLLEDINKKLGItIIVVTHQ 196
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAVALFAELIRAHLAQGGI-VIAATHI 186
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-225 |
3.18e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.89 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 17 LKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQeGSVLVSDKEVKSLNEKQMRDLRkelGMIFQHFSLLERKTVF 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDWSAAELARHR---AYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 97 DNVAL--PLECfgySKAEIKKRVLELLEVVGIsekkNDK-PRN---LSGGQKQRVAIARAL-----ALNP--QVLLCDEA 163
Cdd:COG4138 88 QYLALhqPAGA---SSEAVEQLLAQLAEALGL----EDKlSRPltqLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497582239 164 TSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIF 225
Cdd:COG4138 161 MNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-224 |
3.77e-19 |
|
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: 88.46 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRKELGMIFQHFSLLErktv 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFKITIIPQDPVLFS---- 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 96 fDNVALPLECFG-YSKAEIKKrVLELLEVVGISEKKNDK--------PRNLSGGQKQRVAIARALALNPQVLLCDEATSA 166
Cdd:TIGR00957 1374 -GSLRMNLDPFSqYSDEEVWW-ALELAHLKTFVSALPDKldhecaegGENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497582239 167 LDPNTTKSILSLL----EDinkklgITIIVVTHQMEVIKQICgRVAIMENGEVLEVGDTEEI 224
Cdd:TIGR00957 1452 VDLETDNLIQSTIrtqfED------CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-224 |
8.34e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.10 E-value: 8.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQ--------M 73
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRavcpriayM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 74 -----RDLRKELgmifqhfsllerkTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKnDKP-RNLSGGQKQRVAI 147
Cdd:NF033858 82 pqglgKNLYPTL-------------SVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFA-DRPaGKLSGGMKQKLGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 148 ARALALNPQVLLCDEATSALDPnttksiLS------LLEDINKKL-GITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGD 220
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDP------LSrrqfweLIDRIRAERpGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGT 220
|
....
gi 497582239 221 TEEI 224
Cdd:NF033858 221 PAEL 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-234 |
5.55e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 84.70 E-value: 5.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVL---------------KDVSIEIESGEIFGIIGHSGAGKSTLLRCI------------------- 47
Cdd:PTZ00265 1154 IRIKNKNDIKGKIEIMdvnfryisrpnvpiyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneht 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 48 ---NGLEEYQ--------------------------------EGSVLVSDKEVKSLNekqMRDLRKELGMIFQHfSLLER 92
Cdd:PTZ00265 1234 ndmTNEQDYQgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYN---LKDLRNLFSIVSQE-PMLFN 1309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 93 KTVFDNVAlplecFGYSKA--EIKKRVL------ELLEVVGISEKKNDKP--RNLSGGQKQRVAIARALALNPQVLLCDE 162
Cdd:PTZ00265 1310 MSIYENIK-----FGKEDAtrEDVKRACkfaaidEFIESLPNKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDE 1384
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 163 ATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQiCGRVAIMEN----GEVLEVGDTEEIFLRNTKGLRK 234
Cdd:PTZ00265 1385 ATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQAHGTHEELLSVQDGVYK 1459
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-236 |
1.15e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 83.87 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRKELGMIFQHFSLLERKTV 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRRVLSIIPQSPVLFSGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 96 FD-------NVALPLECFgySKAEIKKRVLEllEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALD 168
Cdd:PLN03232 1328 FNidpfsehNDADLWEAL--ERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 169 PNTTKSILSLLEDINKKlgITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEIFLRNTKGLRKLI 236
Cdd:PLN03232 1404 VRTDSLIQRTIREEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMV 1468
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-224 |
1.19e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.75 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 20 VSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYqEGSVLVSDkevKSLNEKQMRDLRKELGMIFQHFSLLERKTVFDNV 99
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAG---QPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 100 ALPLECfGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARAL-----ALNP--QVLLCDEATSALDPnTT 172
Cdd:PRK03695 91 TLHQPD-KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDV-AQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497582239 173 KSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:PRK03695 169 QAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-227 |
1.58e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 83.29 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRKELGMIFQHFSLLErKTV 95
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG---LRELRRQFSMIPQDPVLFD-GTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 96 FDNVALPLECfgySKAEikkrVLELLEVVGI-----SEKKNDKPR------NLSGGQKQRVAIARA-LALNPQVLLCDEA 163
Cdd:PTZ00243 1401 RQNVDPFLEA---SSAE----VWAALELVGLrervaSESEGIDSRvleggsNYSVGQRQLMCMARAlLKKGSGFILMDEA 1473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497582239 164 TSALDP-------NTTKSILSlledinkklGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEIFLR 227
Cdd:PTZ00243 1474 TANIDPaldrqiqATVMSAFS---------AYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGSPRELVMN 1534
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-228 |
1.93e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 83.25 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqMRDLRKELGMIFQHFSLLERKTV 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKVLGIIPQAPVLFSGTVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 96 FDnvalpLECFG-YSKAEIKKrVLE---LLEVV-----GISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSA 166
Cdd:PLN03130 1331 FN-----LDPFNeHNDADLWE-SLErahLKDVIrrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497582239 167 LDPNTTKSILSLLEDINKklGITIIVVTHQMEVIKQiCGRVAIMENGEVLEVgDTEEIFLRN 228
Cdd:PLN03130 1405 VDVRTDALIQKTIREEFK--SCTMLIIAHRLNTIID-CDRILVLDAGRVVEF-DTPENLLSN 1462
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-195 |
2.65e-17 |
|
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: 82.29 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKeVKSLNEKQMRDlrkelg 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET-VKLAYVDQSRD------ 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 mifqhfSLLERKTVFDNVALPLECFGYSKAEIKKRV-LELLEVVGISEKKndKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:TIGR03719 396 ------ALDPNKTVWEEISGGLDIIKLGKREIPSRAyVGRFNFKGSDQQK--KVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
170 180 190
....*....|....*....|....*....|....*
gi 497582239 161 DEATSALDPNTtksiLSLLEDINKKLGITIIVVTH 195
Cdd:TIGR03719 468 DEPTNDLDVET----LRALEEALLNFAGCAVVISH 498
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-215 |
3.54e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.02 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 18 KDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdlRKELGMIF------QHFSLLE 91
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RLARGLVYlpedrqSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 92 RKTVFDNVALPLECFGY---SKAEikKRVLE-LLEVVGISEKKNDKP-RNLSGGQKQRVAIARALALNPQVLLCDEATSA 166
Cdd:PRK15439 356 APLAWNVCALTHNRRGFwikPARE--NAVLErYRRALNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497582239 167 LDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEV 215
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-196 |
7.42e-17 |
|
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: 77.69 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 13 KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCING-LEEYQ--EGSVLVSDKEVKSLNEKQMRDLrkelgmIF----- 84
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrTEGNVsvEGDIHYNGIPYKEFAEKYPGEI------IYvseed 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 85 QHFSLLerkTVFDNVALPLECFGyskaeikkrvlellevvgisekkNDKPRNLSGGQKQRVAIARALALNPQVLLCDEAT 164
Cdd:cd03233 93 VHFPTL---TVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190
....*....|....*....|....*....|..
gi 497582239 165 SALDPNTTKSILSLLEDINKKLGITIIVVTHQ 196
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVLKTTTFVSLYQ 178
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-196 |
1.27e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 76.63 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKslnekQMRDLRKELGMIFQHFSLLE-RKT 94
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHENILYLGHLPGLKpELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 95 VFDNVALPLECFGYSKAEIkkrvLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKS 174
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|..
gi 497582239 175 ILSLLEDINKKLGITIIvVTHQ 196
Cdd:TIGR01189 166 LAGLLRAHLARGGIVLL-TTHQ 186
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-224 |
1.60e-16 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 79.93 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 17 LKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVlvsdkevkslnekqmrDLRKELGMIFQHFSLLERKTVF 96
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV----------------DIKGSAALIAISSGLNGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 97 DNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSIL 176
Cdd:PRK13545 104 ENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 497582239 177 SLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:PRK13545 184 DKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-195 |
4.09e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 78.69 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 20 VSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVkslNEKQMRDLRkelgmifQHFSllerkTVFDNV 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAYR-------QLFS-----AVFSDF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 100 ALPLECFGYSKAEIKKRVLELLEVVGISEK---KNDK--PRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPN---- 170
Cdd:COG4615 416 HLFDRLLGLDGEADPARARELLERLELDHKvsvEDGRfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrv 495
|
170 180
....*....|....*....|....*..
gi 497582239 171 --TTksILSLLedinKKLGITIIVVTH 195
Cdd:COG4615 496 fyTE--LLPEL----KARGKTVIAISH 516
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-223 |
5.64e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 78.29 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 5 KNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEY--QEGSVLVSDKEVkslnekQMRDLR--KEL 80
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGEVC------RFKDIRdsEAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GM--IFQHFSLLERKTVFDNVALPLEC--FGY-SKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNP 155
Cdd:NF040905 79 GIviIHQELALIPYLSIAENIFLGNERakRGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 156 QVLLCDEATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEE 223
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRA 225
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-224 |
8.69e-16 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 76.01 E-value: 8.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 17 LKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVlvsdkevkslnekqmrDLRKELGMIFQHFSLLERKTVF 96
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV----------------DRNGEVSVIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 97 DNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSIL 176
Cdd:PRK13546 104 ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 497582239 177 SLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:PRK13546 184 DKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-248 |
1.08e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.15 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGK---IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEvkSLNEKQMRDLRK 78
Cdd:PTZ00265 383 IQFKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 79 ELGMIFQHfSLLERKTVFDNVALPL--------------------------------ECFGYSK-----------AEIKK 115
Cdd:PTZ00265 461 KIGVVSQD-PLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscraKCAGDLNdmsnttdsnelIEMRK 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 116 --RVLELLEVVGISEKK-----------------NDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNT----T 172
Cdd:PTZ00265 540 nyQTIKDSEVVDVSKKVlihdfvsalpdkyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSeylvQ 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 173 KSILSLLEDINKklgITIIvVTHQMEVIK-------------------QICGRVAIMENGEVLEVGDTEEIFLRNTKGLR 233
Cdd:PTZ00265 620 KTINNLKGNENR---ITII-IAHRLSTIRyantifvlsnrergstvdvDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNN 695
|
330
....*....|....*
gi 497582239 234 KLIGEESIILPKGTN 248
Cdd:PTZ00265 696 KINNAGSYIIEQGTH 710
|
|
| NIL |
smart00930 |
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ... |
246-317 |
1.65e-15 |
|
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins; This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.
Pssm-ID: 197998 [Multi-domain] Cd Length: 76 Bit Score: 70.23 E-value: 1.65e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497582239 246 GTNIKILFPKDISNEAIITTMARELNIDVSIIFGKLEQFKDDILGSLI--INISDKSGEQVKQYLTSKGIRWEE 317
Cdd:smart00930 2 GRLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVveLTGDEEDIEAALAYLREQGVEVEV 75
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-215 |
1.83e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 17 LKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQ--------MRDLRKE----LGMif 84
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDRKRdglvLGM-- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 85 qhfsllerkTVFDNVALP-LECFGYSKAEIKKR-----VLELLEVVGISEKKNDKP-RNLSGGQKQRVAIARALALNPQV 157
Cdd:PRK10762 346 ---------SVKENMSLTaLRYFSRAGGSLKHAdeqqaVSDFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 158 LLCDEATSALDPNTTKSILSLledIN--KKLGITIIVVTHQMEVIKQICGRVAIMENGEV 215
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQL---INqfKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-256 |
2.14e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 76.98 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 22 IEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSlnekQMRDLRKELGMIFQHFSLLERKTVFDNVAL 101
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDVHQNMGYCPQFDAIDDLLTGREHLYL 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 102 PLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSILSLLED 181
Cdd:TIGR01257 2036 YARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 182 INKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEiflrntkgLRKLIGEESIIlpkgtNIKILFPKD 256
Cdd:TIGR01257 2116 IIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQH--------LKSKFGDGYIV-----TMKIKSPKD 2176
|
|
| NIL |
pfam09383 |
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ... |
247-317 |
5.13e-15 |
|
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins. This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.
Pssm-ID: 462781 [Multi-domain] Cd Length: 73 Bit Score: 68.63 E-value: 5.13e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 247 TNIKILFPKDISNEAIITTMARELNIDVSIIFGKLEQFKDDILGSLIINISDKSG--EQVKQYLTSKGIRWEE 317
Cdd:pfam09383 1 RLVRLTFPGESADEPVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELPGDPEqiEAALAYLREQGVEVEV 73
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-195 |
6.74e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.01 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQV-LKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVkslNEKQMRDLRKEL 80
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLlerktvFDNValpLECFGYSKAEikKRVLELLEVVGISEK---KNDKPRN--LSGGQKQRVAIARALALNP 155
Cdd:PRK10522 400 SAVFTDFHL------FDQL---LGPEGKPANP--ALVEKWLERLKMAHKlelEDGRISNlkLSKGQKKRLALLLALAEER 468
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 497582239 156 QVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTH 195
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISH 508
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-222 |
8.01e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 72.75 E-value: 8.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQ--EGSVLVSDKEVKSLNEkqmrDLRK 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEP----EERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 79 ELGMI--FQH-----------FSLL----ERKTVFDNVALPLECFGYskaeikkrVLELLEVVGISEKKNDKPRN--LSG 139
Cdd:CHL00131 83 HLGIFlaFQYpieipgvsnadFLRLaynsKRKFQGLPELDPLEFLEI--------INEKLKLVGMDPSFLSRNVNegFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 140 GQKQRVAIARALALNPQVLLCDEATSALDPNTTKSIlslLEDINK--KLGITIIVVTHQMEVIKQIC-GRVAIMENGEVL 216
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKII---AEGINKlmTSENSIILITHYQRLLDYIKpDYVHVMQNGKII 231
|
....*.
gi 497582239 217 EVGDTE 222
Cdd:CHL00131 232 KTGDAE 237
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-223 |
1.08e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDlrKEL 80
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQE--AGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVALPLE---CFG-------YSKAEikkrvlELLEVVGISEKKNDKPRNLSGGQKQRVAIARA 150
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGREfvnRFGridwkkmYAEAD------KLLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 151 LALNPQVLLCDEATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIKQICGRVAIMENGEVL---EVGDTEE 223
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIaerEVADLTE 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-196 |
1.26e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.37 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 19 DVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLvsdkevksLNEKQMRDLRKELgmifqHFSLL-------- 90
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL--------WQGEPIRRQRDEY-----HQDLLylghqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 91 -ERKTVFDNVALPLECFGYSKAEikkRVLELLEVVGISEKKnDKP-RNLSGGQKQRVAIARaLALNPQVL-LCDEATSAL 167
Cdd:PRK13538 86 kTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFE-DVPvRQLSAGQQRRVALAR-LWLTRAPLwILDEPFTAI 160
|
170 180
....*....|....*....|....*....
gi 497582239 168 DPNTTKSILSLLEDINKKLGItIIVVTHQ 196
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGM-VILTTHQ 188
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-198 |
3.11e-14 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 70.44 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 14 IQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRKELGMIFQHFSLLERK 93
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 94 TVFDNVAlplecFG--YSKAEIKKRV--------LELLEVvGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEA 163
Cdd:cd03290 94 TVEENIT-----FGspFNKQRYKAVTdacslqpdIDLLPF-GDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 497582239 164 TSALDPNTT-----KSILSLLEDINKklgiTIIVVTHQME 198
Cdd:cd03290 168 FSALDIHLSdhlmqEGILKFLQDDKR----TLVLVTHKLQ 203
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-181 |
9.16e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 71.69 E-value: 9.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKeVKSLNEKQMRDlrkelg 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET-VKLAYVDQSRD------ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 mifqhfSLLERKTVFDNVALPLECFGYSKAEIKKRVLelleVVGISEKKND---KPRNLSGGQKQRVAIARALALNPQVL 158
Cdd:PRK11819 398 ------ALDPNKTVWEEISGGLDIIKVGNREIPSRAY----VGRFNFKGGDqqkKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
170 180
....*....|....*....|...
gi 497582239 159 LCDEATSALDPNTtksiLSLLED 181
Cdd:PRK11819 468 LLDEPTNDLDVET----LRALEE 486
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-228 |
2.51e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 70.74 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 17 LKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVlvsdkevkslnekqmrDLRKELGMIFQHfSLLERKTVF 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV----------------HMKGSVAYVPQQ-AWIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 97 DNVAL--PLECFGYSKAEIKKRVLELLEVV--GISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTT 172
Cdd:TIGR00957 717 ENILFgkALNEKYYQQVLEACALLPDLEILpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 173 KSIlslLEDINKKLGI----TIIVVTHQMEVIKQIcGRVAIMENGEVLEVGDTEEIFLRN 228
Cdd:TIGR00957 797 KHI---FEHVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRD 852
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-215 |
4.11e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.47 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 13 KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQ-EGSVLVSDKEVKSLNEKQ--------MRDLRKELGMI 83
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQairagiamVPEDRKRHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 84 FQ-------HFSLLER---KTVFDNVAlPLECFGYSKAEIKKRVLELLEVVGisekkndkprNLSGGQKQRVAIARALAL 153
Cdd:TIGR02633 352 PIlgvgkniTLSVLKSfcfKMRIDAAA-ELQIIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLT 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497582239 154 NPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEV 215
Cdd:TIGR02633 421 NPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-218 |
1.05e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 4 IKNVNKYygKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEkqMRDLRKELGMI 83
Cdd:PRK09700 268 VRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 84 ---------FQHFSLLErktvfdNVALP--LECFGYSKA----------EIKKRVLELLEVVGISEKKNDKprNLSGGQK 142
Cdd:PRK09700 344 tesrrdngfFPNFSIAQ------NMAISrsLKDGGYKGAmglfhevdeqRTAENQRELLALKCHSVNQNIT--ELSGGNQ 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 143 QRVAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEV 218
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-219 |
1.39e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQ--EGSVLVSDKevkslneKQMRDLRKELGMIFQ------HF 87
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNR-------KPTKQILKRTGFVTQddilypHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 88 SLLERKTVFDNVALPLECFGYSKAEIKKRVLELL-------EVVGisekkNDKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:PLN03211 156 TVRETLVFCSLLRLPKSLTKQEKILVAESVISELgltkcenTIIG-----NSFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 161 DEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQ-MEVIKQICGRVAIMENGEVLEVG 219
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-224 |
1.51e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.61 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYY---GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCING-LEEYQEGSVLvsdkevkslnekqmrdLR 77
Cdd:PLN03130 615 ISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVV----------------IR 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 78 KELGMIFQhFSLLERKTVFDNV--ALPLECFGYSKAeIK----KRVLELL---EVVGISEKKndkpRNLSGGQKQRVAIA 148
Cdd:PLN03130 679 GTVAYVPQ-VSWIFNATVRDNIlfGSPFDPERYERA-IDvtalQHDLDLLpggDLTEIGERG----VNISGGQKQRVSMA 752
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 149 RALALNPQVLLCDEATSALDPNTTKSILS--LLEDINKKlgiTIIVVTHQMEVIKQIcGRVAIMENGEVLEVGDTEEI 224
Cdd:PLN03130 753 RAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGK---TRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEEL 826
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-223 |
1.84e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.45 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 17 LKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQ--------MRDLRKELGmIFQHFS 88
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfalVTEERRSTG-IYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 89 LlERKTVFDNVALPLECFGY-SKAEIKKR---VLELLEVVGISEKKNDKprNLSGGQKQRVAIARALALNPQVLLCDEAT 164
Cdd:PRK10982 343 I-GFNSLISNIRNYKNKVGLlDNSRMKSDtqwVIDSMRVKTPGHRTQIG--SLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 165 SALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEE 223
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKT 477
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-235 |
2.33e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 66.68 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAG--KSTLLRCINGLEEYQEGSVLVSDKEVKslnekqmRDLRKE 79
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANR-------RALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 LGMifqHFSL-LERKTVF---DNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNP 155
Cdd:NF000106 87 IG*---HRPVr*GRRESFsgrENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 156 QVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEifLRNTKGLRKL 235
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDE--LKTKVGGRTL 240
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-215 |
3.27e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.86 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 20 VSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQM---------RDlRKELGMIFQHfsll 90
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAiragimlcpED-RKAEGIIPVH---- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 91 erkTVFDNVA-------LPLECFGYSKAEIK--KRVLELLEVVGISEKKndKPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:PRK11288 347 ---SVADNINisarrhhLRAGCLINNRWEAEnaDRFIRSLNIKTPSREQ--LIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 162 EATSALDPNTTKSILSLLEDINKKlGITIIVVTHQ-MEVIKqICGRVAIMENGEV 215
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDlPEVLG-VADRIVVMREGRI 474
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-195 |
3.61e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.88 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 3 SIKNVNKYY-GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKevkslnekqmrdlrKELG 81
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPG--------------IKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLecfgyskAEIKKRVLELLEvvgISEKKNDKP--------------------------- 134
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEEGV-------AEIKDALDRFNE---ISAKYAEPDadfdklaaeqaelqeiidaadawdlds 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 135 ------------------RNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTksilSLLEDINKKLGITIIVVTH 195
Cdd:TIGR03719 142 qleiamdalrcppwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV----AWLERHLQEYPGTVVAVTH 216
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-196 |
5.17e-12 |
|
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: 63.80 E-value: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNkYY-----GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEE--YQEGSVLVSDKEVKSlnekqmr 74
Cdd:cd03232 4 LTWKNLN-YTvpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 75 DLRKELGMIFQHFSLLERKTVfdnvalpLECFGYSkAEIkkrvlellevvgisekkndkpRNLSGGQKQRVAIARALALN 154
Cdd:cd03232 76 NFQRSTGYVEQQDVHSPNLTV-------REALRFS-ALL---------------------RGLSVEQRKRLTIGVELAAK 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 497582239 155 PQVLLCDEATSALDPNTTKSILSLLedinKKL---GITIIVVTHQ 196
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFL----KKLadsGQAILCTIHQ 167
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-215 |
5.72e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.11 E-value: 5.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 13 KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLeeYQ---EGSVLVSDKEVKSLNEKQMRDL--------RKELG 81
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGA--YPgrwEGEIFIDGKPVKIRNPQQAIAQgiamvpedRKRDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MI----------------FQHFSLLerktvfdNVALPLECFGYSKAEIKKRVLELLEVVGisekkndkprNLSGGQKQRV 145
Cdd:PRK13549 352 IVpvmgvgknitlaaldrFTGGSRI-------DDAAELKTILESIQRLKVKTASPELAIA----------RLSGGNQQKA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 146 AIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEV 215
Cdd:PRK13549 415 VLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-196 |
9.37e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.90 E-value: 9.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 13 KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCING-LEEYQEGSVLVSDKEVKSLNEkQMRDLRKELGMIFQ---HFS 88
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFHIGVEGVITYDGITPEE-IKKHYRGDVVYNAEtdvHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 89 LLerkTVFDNVALPLEC-------FGYSKAEIKKRVLEL-LEVVGISEKKNDKP-----RNLSGGQKQRVAIARALALNP 155
Cdd:TIGR00956 152 HL---TVGETLDFAARCktpqnrpDGVSREEYAKHIADVyMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGA 228
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 497582239 156 QVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQ 196
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQ 269
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-227 |
9.52e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 9.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSdkevkslnekqmrdlrKELGMIFQHfSLLERKTV 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE----------------RSIAYVPQQ-AWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 96 FDNVALPLEcfgyskaeikKRVLELLEVVGISEKKND--------------KPRNLSGGQKQRVAIARALALNPQVLLCD 161
Cdd:PTZ00243 738 RGNILFFDE----------EDAARLADAVRVSQLEADlaqlgggleteigeKGVNLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 162 EATSALDPNTTKSILSllEDINKKL-GITIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEiFLR 227
Cdd:PTZ00243 808 DPLSALDAHVGERVVE--ECFLGALaGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSAD-FMR 870
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-266 |
1.03e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.77 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVN-KYYGKIQ--VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVsdkevkslnekqmrdLRK 78
Cdd:PLN03232 615 ISIKNGYfSWDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV---------------IRG 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 79 ELGMIFQhFSLLERKTVFDNVAL--PLECFGYSKA---EIKKRVLELLEVVGISEKkNDKPRNLSGGQKQRVAIARALAL 153
Cdd:PLN03232 680 SVAYVPQ-VSWIFNATVRENILFgsDFESERYWRAidvTALQHDLDLLPGRDLTEI-GERGVNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 154 NPQVLLCDEATSALDPNTTKSIL-SLLEDINKklGITIIVVTHQMEVIKQIcGRVAIMENGEVLEVGDTEEIFlRNTKGL 232
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQVFdSCMKDELK--GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS-KSGSLF 833
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 497582239 233 RKL------IGEESIILPKGTNIKILFPK---DISNEAIITTM 266
Cdd:PLN03232 834 KKLmenagkMDATQEVNTNDENILKLGPTvtiDVSERNLGSTK 876
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-214 |
1.04e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.30 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKE-VKSLNEKQM--RDLR 77
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNErLGKLRQDQFafEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 78 KELGMIFQHFSLLERKTVFDNV-ALP------------LEC-F----GYSkAEikKRVLELLEVVGISEKKNDKP-RNLS 138
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQERDRIyALPemseedgmkvadLEVkFaemdGYT-AE--ARAGELLLGVGIPEEQHYGLmSEVA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 139 GGQKQRVAIARALALNPQVLLCDEATSALDPNTtksiLSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGE 214
Cdd:PRK15064 158 PGWKLRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGE 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-196 |
1.23e-11 |
|
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: 62.90 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVkslnEKQMRDLRKELGMIFQHFSLLERKTV 95
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL----DFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 96 FDNVALplecfgYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSI 175
Cdd:cd03231 91 LENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|.
gi 497582239 176 LSLLEDINKKLGItIIVVTHQ 196
Cdd:cd03231 165 AEAMAGHCARGGM-VVLTTHQ 184
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-219 |
1.70e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.69 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGleEYQE----------GSVLVSDKEVKSLNEKQMRDLRKELGMIFQ 85
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGggaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 86 H-FSLLERKTVFdnvalpLECFGYSKA---------EIKKRVLELlevVGISEKKNDKPRNLSGGQKQRVAIARALA--- 152
Cdd:PRK13547 94 PaFAFSAREIVL------LGRYPHARRagalthrdgEIAWQALAL---AGATALVGRDVTTLSGGELARVQFARVLAqlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 153 ------LNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVG 219
Cdd:PRK13547 165 pphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-169 |
1.70e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.65 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCING-----------LEEYQEGSvlvsdkevkslnE 70
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGS------------G 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 71 KQMRDLRKELGMIFQHFSLLER-----KTV-----FDNVALplecfgYSKAEIKKRVL--ELLEVVGISEKKNDKP-RNL 137
Cdd:PRK10938 329 ETIWDIKKHIGYVSSSLHLDYRvstsvRNVilsgfFDSIGI------YQAVSDRQQKLaqQWLDILGIDKRTADAPfHSL 402
|
170 180 190
....*....|....*....|....*....|..
gi 497582239 138 SGGQKQRVAIARALALNPQVLLCDEATSALDP 169
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-240 |
2.82e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.55 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVlvsdkevkslnekqmrdlrKELGMI--FQHFSLLERK 93
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------------------KHSGRIsfSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 94 TVFDNValpleCFGYSKAEIKKRVL----ELLEVVGISEKKNDKPR-----NLSGGQKQRVAIARALALNPQVLLCDEAT 164
Cdd:TIGR01271 502 TIKDNI-----IFGLSYDEYRYTSVikacQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 165 SALDPNTTKSILS--LLEDINKKlgiTIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEIFLRNTKGLRKLIGEES 240
Cdd:TIGR01271 577 THLDVVTEKEIFEscLCKLMSNK---TRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEA 650
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-215 |
5.45e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLV-SDKEVKSLNEKQMRDlrke 79
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIVARLQQDPPRN---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 80 lgmifqhfsllERKTVFDNVALPLECFG----------------YSKAEIKK------------------RVLELLEVVG 125
Cdd:PRK11147 79 -----------VEGTVYDFVAEGIEEQAeylkryhdishlvetdPSEKNLNElaklqeqldhhnlwqlenRINEVLAQLG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 126 ISEkknDKPRN-LSGGQKQRVAIARALALNPQVLLCDEATSALDPNTtksiLSLLEDINKKLGITIIVVTHQMEVIKQIC 204
Cdd:PRK11147 148 LDP---DAALSsLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQGSIIFISHDRSFIRNMA 220
|
250
....*....|.
gi 497582239 205 GRVAIMENGEV 215
Cdd:PRK11147 221 TRIVDLDRGKL 231
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-203 |
7.02e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.96 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLR-----CINGL---------EEYQEGS-------VLV 60
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGIpkncqilhvEQEVVGDdttalqcVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 61 SDKEVKSLNEKQMRDLRKELGMIFQhfSLLERKTVFDNVALPLECFGYSKAEIKKRvLELLE-----------VVGIS-- 127
Cdd:PLN03073 258 TDIERTQLLEEEAQLVAQQRELEFE--TETGKGKGANKDGVDKDAVSQRLEEIYKR-LELIDaytaearaasiLAGLSft 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 128 -EKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDpntTKSILsLLEDINKKLGITIIVVTHQMEVIKQI 203
Cdd:PLN03073 335 pEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVL-WLETYLLKWPKTFIVVSHAREFLNTV 407
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-201 |
1.24e-10 |
|
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: 62.07 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQeGSVLVSDKEVKSLNEKQmrdlRKELGmifqhfslleRKTV 95
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVY-GGRLTKPAKGKLFYVPQ----RPYMT----------LGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 96 FDNVALPLECF-----GYSKAEIKKrVLELLEVVGISEKK------NDKPRNLSGGQKQRVAIARALALNPQVLLCDEAT 164
Cdd:TIGR00954 532 RDQIIYPDSSEdmkrrGLSDKDLEQ-ILDNVQLTHILEREggwsavQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|....*..
gi 497582239 165 SALDPNTTKSILSLLedinKKLGITIIVVTHQMEVIK 201
Cdd:TIGR00954 611 SAVSVDVEGYMYRLC----REFGITLFSVSHRKSLWK 643
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-242 |
1.41e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 61.02 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYY--GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTL----LRCINGLEEYQEGSVlvsdkevkSLNEKQMRD 75
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNTEGDIQIDGV--------SWNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 76 LRKELGMIFQH---FSLLERKTvfdnvalpLECFGYSKAEIKKRVLELLEVVGISEKKNDKPR--------NLSGGQKQR 144
Cdd:cd03289 75 WRKAFGVIPQKvfiFSGTFRKN--------LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDfvlvdggcVLSHGHKQL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 145 VAIARALALNPQVLLCDEATSALDPNTTKSILSLLEdiNKKLGITIIVVTHQMEVIKQiCGRVAIMENGEVlevgdteei 224
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIEENKV--------- 214
|
250
....*....|....*...
gi 497582239 225 flRNTKGLRKLIGEESII 242
Cdd:cd03289 215 --RQYDSIQKLLNEKSHF 230
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
3.48e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKslnekqmrdlrKEL 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-----------KDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKT-VFDNVALPLECfgYSKAEIKKRVLELLEVVGISEKKN--DKPRN-LSGGQKQRVAIARALALNPQ 156
Cdd:PRK13540 70 CTYQKQLCFVGHRSgINPYLTLRENC--LYDIHFSPGAVGITELCRLFSLEHliDYPCGlLSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 497582239 157 VLLCDEATSALDPNTTKSILSLLEDiNKKLGITIIVVTHQ 196
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSHQ 186
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-228 |
3.79e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.68 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 4 IKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDK---------------EVKSL 68
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENanigyyaqdhaydfeNDLTL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 69 NE-----KQMRD----LRKELG-MIFqhfsllerktvfdnvalplecfgySKAEIKKRVlellevvgisekkndkpRNLS 138
Cdd:PRK15064 402 FDwmsqwRQEGDdeqaVRGTLGrLLF------------------------SQDDIKKSV-----------------KVLS 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 139 GGQKQRVAIARALALNPQVLLCDEATSALDpntTKSILSLLEDINKKLGiTIIVVTHQMEVIKQICGRVAIMENGEVLEV 218
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMD---MESIESLNMALEKYEG-TLIFVSHDREFVSSLATRIIEITPDGVVDF 516
|
250
....*....|
gi 497582239 219 GDTEEIFLRN 228
Cdd:PRK15064 517 SGTYEEYLRS 526
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-214 |
5.13e-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: 59.10 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSlnekqmrdlrkelgmifQHFSLLERKTV 95
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFS-----------------SQFSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 96 FDNVALPLECFGYS-KAEIKKRVLElLEVVGISEKKN----DKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPN 170
Cdd:cd03291 115 KENIIFGVSYDEYRyKSVVKACQLE-EDITKFPEKDNtvlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497582239 171 TTKSIlslLEDINKKL--GITIIVVTHQMEVIKqICGRVAIMENGE 214
Cdd:cd03291 194 TEKEI---FESCVCKLmaNKTRILVTSKMEHLK-KADKILILHEGS 235
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-224 |
5.50e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 21 SIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQmrdLRKELGMIFQHfslleRKTvfDNVA 100
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQ---LQKLVSDEWQR-----NNT--DMLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 101 LPLECFGYSKAEI-------KKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTK 173
Cdd:PRK10938 93 PGEDDTGRTTAEIiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497582239 174 SILSLLEDINKKlGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEI 224
Cdd:PRK10938 173 QLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-195 |
6.03e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 4 IKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDK-EVKSLNekqmrdlrkelgm 82
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFD------------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 83 ifQHFSLLE-RKTVFDNVAlplecfgYSKAEI-----KKRVLELLEVVGISEKKNDKP-RNLSGGQKQRVAIARaLALNP 155
Cdd:PRK11147 389 --QHRAELDpEKTVMDNLA-------EGKQEVmvngrPRHVLGYLQDFLFHPKRAMTPvKALSGGERNRLLLAR-LFLKP 458
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 497582239 156 QVLLC-DEATSALDPNTtksiLSLLEDINKKLGITIIVVTH 195
Cdd:PRK11147 459 SNLLIlDEPTNDLDVET----LELLEELLDSYQGTVLLVSH 495
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
9-211 |
6.96e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.57 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 9 KYYGKIQVLKDVSIEIESG-----EIFGIIGHSGAGKSTLLRCINGLEEYQEGSVlvsDKEVKSLNEKQMRDLRKELGMI 83
Cdd:cd03237 2 TYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKPQYIKADYEGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 84 FQhfsLLERKTvfDNValplecfgYSKAEIKKRVLELLEVVGISEKKndkPRNLSGGQKQRVAIARALALNPQVLLCDEA 163
Cdd:cd03237 79 RD---LLSSIT--KDF--------YTHPYFKTEIAKPLQIEQILDRE---VPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497582239 164 TSALDPN----TTKSILSLLEDINKklgiTIIVVTHQMEVIKQICGRVAIME 211
Cdd:cd03237 143 SAYLDVEqrlmASKVIRRFAENNEK----TAFVVEHDIIMIDYLADRLIVFE 190
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-220 |
1.41e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.49 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQ--EGSVLVSDKEVKSLNEKQmrdlRK 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLELSPED----RA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 79 ELG--MIFQHfsllerktvfdnvalPLECFGYS---------KAEIKKRVLELLEVVGISEKKNDK------PRNL---- 137
Cdd:PRK09580 77 GEGifMAFQY---------------PVEIPGVSnqfflqtalNAVRSYRGQEPLDRFDFQDLMEEKiallkmPEDLltrs 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 138 -----SGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSI---LSLLEDINKklgiTIIVVTHQMEVIKQI-CGRVA 208
Cdd:PRK09580 142 vnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVadgVNSLRDGKR----SFIIVTHYQRILDYIkPDYVH 217
|
250
....*....|..
gi 497582239 209 IMENGEVLEVGD 220
Cdd:PRK09580 218 VLYQGRIVKSGD 229
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-242 |
1.57e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.15 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLeeyqegsvLVSDKEVK----SLNEKQMRDLRKELGMIFQHFSLLe 91
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL--------LSTEGEIQidgvSWNSVTLQTWRKAFGVIPQKVFIF- 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 92 rKTVFDNVALPLEcfGYSKAEIKKrVLELLEVVGISEKKNDKPR--------NLSGGQKQRVAIARALALNPQVLLCDEA 163
Cdd:TIGR01271 1305 -SGTFRKNLDPYE--QWSDEEIWK-VAEEVGLKSVIEQFPDKLDfvlvdggyVLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 164 TSALDPNTTKSILSLLEDINKKlgITIIVVTHQMEvikqicgrvAIMENGEVLEVgdtEEIFLRNTKGLRKLIGEESII 242
Cdd:TIGR01271 1381 SAHLDPVTLQIIRKTLKQSFSN--CTVILSEHRVE---------ALLECQQFLVI---EGSSVKQYDSIQKLLNETSLF 1445
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-195 |
2.39e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 3 SIKNVNKYYG-KIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDkevkslnekqmrDLRkeLG 81
Cdd:PRK11819 8 TMNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAP------------GIK--VG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 82 MIFQHFSLLERKTVFDNVALPLecfgyskAEIKKRVLELLEvvgISEK------KNDK---------------------- 133
Cdd:PRK11819 74 YLPQEPQLDPEKTVRENVEEGV-------AEVKAALDRFNE---IYAAyaepdaDFDAlaaeqgelqeiidaadawdlds 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497582239 134 -----------P------RNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTksilSLLEDINKKLGITIIVVTH 195
Cdd:PRK11819 144 qleiamdalrcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV----AWLEQFLHDYPGTVVAVTH 218
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-200 |
1.17e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.07 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 25 ESGEIFGIIGHSGAGKSTLLRCING------------------LEEYQeGSVLvsDKEVKSLNEKQMRDLRKElgmifQH 86
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdwdeiLDEFR-GSEL--QNYFTKLLEGDVKVIVKP-----QY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 87 FSLLErKTVFDNVALPLEcfGYSKAEIKKRVLELLEVVGISEKKNDkprNLSGGQKQRVAIARALALNPQVLLCDEATSA 166
Cdd:cd03236 96 VDLIP-KAVKGKVGELLK--KKDERGKLDELVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 497582239 167 LDP----NTTKSILSLLEDINkklgiTIIVVTHQMEVI 200
Cdd:cd03236 170 LDIkqrlNAARLIRELAEDDN-----YVLVVEHDLAVL 202
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-170 |
1.56e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRKELGMIFQHFSLLERktv 95
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLEN--- 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497582239 96 fdnvaLPLECfGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARaLALNPQVL-LCDEATSALDPN 170
Cdd:PRK13543 103 -----LHFLC-GLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDLE 171
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-200 |
1.77e-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: 52.76 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 26 SGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEvkslnekqmrdlrkelgmifqhfsllerktvfdnvalplec 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 106 fgyskaEIKKRVLELLEVVGISEKKndkpRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSILSLLED---- 181
Cdd:smart00382 40 ------DILEEVLDQLLLIIVGGKK----ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrlll 109
|
170 180
....*....|....*....|
gi 497582239 182 -INKKLGITIIVVTHQMEVI 200
Cdd:smart00382 110 lLKSEKNLTVILTTNDEKDL 129
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
16-227 |
3.03e-08 |
|
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: 53.76 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 16 VLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLnekQMRDLRKELGMIFQHFSLL----- 90
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSRLSIILQDPILFsgsir 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 91 -----ERKTVFDNVALPLECfgyskAEIKKRVLELLEvvGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATS 165
Cdd:cd03288 113 fnldpECKCTDDRLWEALEI-----AQLKNMVKSLPG--GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 166 ALDPNTtksilsllEDINKKLGI------TIIVVTHQMEVIKQiCGRVAIMENGEVLEVGDTEEIFLR 227
Cdd:cd03288 186 SIDMAT--------ENILQKVVMtafadrTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
17-195 |
3.18e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 17 LKDVSIEIESGEIF-----GIIGHSGAGKSTLLRCINGLEEYQEGSVL----VSDK--EVKSLNEKQMRDLrkeLGMIfq 85
Cdd:PRK13409 350 LGDFSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpelkISYKpqYIKPDYDGTVEDL---LRSI-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 86 hfsllerKTVFDNvalplecfGYSKAEIKKRvLELlevvgisEKKNDKP-RNLSGGQKQRVAIARALALNPQVLLCDEAT 164
Cdd:PRK13409 425 -------TDDLGS--------SYYKSEIIKP-LQL-------ERLLDKNvKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180 190
....*....|....*....|....*....|....*
gi 497582239 165 SALDP----NTTKSILSLLEDINKklgiTIIVVTH 195
Cdd:PRK13409 482 AHLDVeqrlAVAKAIRRIAEEREA----TALVVDH 512
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
12-196 |
4.35e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 12 GKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEE---YQEGSVLVSDKEVKSlnekqmrDLRKELGMIFQHFS 88
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDS-------SFQRSIGYVQQQDL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 89 LLERKTVFDNVA------LPLECFGYSKAEIKKRVLELLE-------VVGISEKkndkprNLSGGQKQRVAIARALALNP 155
Cdd:TIGR00956 847 HLPTSTVRESLRfsaylrQPKSVSKSEKMEYVEEVIKLLEmesyadaVVGVPGE------GLNVEQRKRLTIGVELVAKP 920
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 497582239 156 QVLL-CDEATSALDPNTTKSILSLLedinKKL---GITIIVVTHQ 196
Cdd:TIGR00956 921 KLLLfLDEPTSGLDSQTAWSICKLM----RKLadhGQAILCTIHQ 961
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-214 |
4.51e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.41 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 23 EIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVL----VSDK--EVKSLNEKQMRD-LRKELGMIFQHfsllerktv 95
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkISYKpqYISPDYDGTVEEfLRSANTDDFGS--------- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 96 fdnvalplecfGYSKAEIKKRvLELlevvgisEKKNDKP-RNLSGGQKQRVAIARALALNPQVLLCDEATSALDP----N 170
Cdd:COG1245 433 -----------SYYKTEIIKP-LGL-------EKLLDKNvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlA 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 497582239 171 TTKSILSLLEDiNKKlgiTIIVVTHQMEVIKQICGRVAIMEnGE 214
Cdd:COG1245 494 VAKAIRRFAEN-RGK---TAMVVDHDIYLIDYISDRLMVFE-GE 532
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-195 |
5.16e-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: 54.02 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 25 ESGEIFGIIGHSGAGKSTLLRCING------------------LEEYQeGSVL------VSDKEVKSLNEKQMRDlrkel 80
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGelkpnlgdydeepswdevLKRFR-GTELqdyfkkLANGEIKVAHKPQYVD----- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 gMIFQHFS-----LLErktvfdnvalplecfgysKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNP 155
Cdd:COG1245 171 -LIPKVFKgtvreLLE------------------KVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 497582239 156 QVLLCDEATSALDP----NTTKSILSLLEDinkklGITIIVVTH 195
Cdd:COG1245 232 DFYFFDEPSSYLDIyqrlNVARLIRELAEE-----GKYVLVVEH 270
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-215 |
7.82e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSdKEVK--SLNEKQMRDLRK 78
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA-KGIKlgYFAQHQLEFLRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 79 ELGMIfQHFSLLERKTVFDNVALPLECFGYSkaeikkrvlellevvgiSEKKNDKPRNLSGGQKQRVAIARALALNPQVL 158
Cdd:PRK10636 391 DESPL-QHLARLAPQELEQKLRDYLGGFGFQ-----------------GDKVTEETRRFSGGEKARLVLALIVWQRPNLL 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497582239 159 LCDEATSALDPNTTKSILSLLEDINKKLgitiIVVTHQMEVIKQICGRVAIMENGEV 215
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
2-203 |
8.52e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.84 E-value: 8.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYgkiqvlKDVSIEIESGeIFGIIGHSGAGKSTLLRCIngleeyqegsvLVSDKEVKSLNEKQMRDLRK--- 78
Cdd:cd03240 4 LSIRNIRSFH------ERSEIEFFSP-LTLIVGQNGAGKTTIIEAL-----------KYALTGELPPNSKGGAHDPKlir 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 79 ---ELGMIFQHFSLLERKT--------VFDNVALpleCfgySKAEIKKRVLELLEvvgisekkndkprNLSGGQKQ---- 143
Cdd:cd03240 66 egeVRAQVKLAFENANGKKytitrslaILENVIF---C---HQGESNWPLLDMRG-------------RCSGGEKVlasl 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497582239 144 --RVAIARALALNPQVLLCDEATSALDP-NTTKSILSLLEDINKKLGITIIVVTHQMEVIKQI 203
Cdd:cd03240 127 iiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-202 |
1.17e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.78 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 17 LKDVSIEIESGEIFGIIGHSGAGKSTLlrCINGLEEyQEGSVLVSDKEVKSlnekqmrdlrkelgmifqhfsllERKTVF 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYA-SGKARLISFLPKFS-----------------------RNKLIF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 97 dnvalplecfgyskaeIKKrvLELLEVVGISEKKNDKPRN-LSGGQKQRVAIARALALNPQ--VLLCDEATSALDPNTTK 173
Cdd:cd03238 65 ----------------IDQ--LQFLIDVGLGYLTLGQKLStLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180
....*....|....*....|....*....
gi 497582239 174 SILSLLEDInKKLGITIIVVTHQMEVIKQ 202
Cdd:cd03238 127 QLLEVIKGL-IDLGNTVILIEHNLDVLSS 154
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-195 |
2.58e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 27 GEIFGIIGHSGAGKSTLLRCING-----LEEYQE------------GSVL------VSDKEVKSLNEKQMRDLRKElgmi 83
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGelipnLGDYEEepswdevlkrfrGTELqnyfkkLYNGEIKVVHKPQYVDLIPK---- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 84 fqhfsllerktVFD-NVALPLEcfgysKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDE 162
Cdd:PRK13409 175 -----------VFKgKVRELLK-----KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....*..
gi 497582239 163 ATSALDP----NTTKSILSLLEdinkklGITIIVVTH 195
Cdd:PRK13409 239 PTSYLDIrqrlNVARLIRELAE------GKYVLVVEH 269
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-195 |
1.07e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.47 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 2 ISIKNVNKYYGKiqvlkdVSIEIESGeIFGIIGHSGAGKSTLLRCI--------NGLEEYQEGSVLVSDKEVK-----SL 68
Cdd:COG0419 5 LRLENFRSYRDT------ETIDFDDG-LNLIVGPNGAGKSTILEAIryalygkaRSRSKLRSDLINVGSEEASvelefEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 69 NEKQMRDLRKELGMI-FQHFSLLERKTVFDNVaLPLECFGYS-------KAEIKKRVLELLEVVGISEK------KNDKP 134
Cdd:COG0419 78 GGKRYRIERRQGEFAeFLEAKPSERKEALKRL-LGLEIYEELkerlkelEEALESALEELAELQKLKQEilaqlsGLDPI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497582239 135 RNLSGGQKQRVAIARALAlnpqvLLCDeaTSALDPNTTKSILSLLEDINkklgitiiVVTH 195
Cdd:COG0419 157 ETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA--------IITH 202
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-201 |
1.97e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.02 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 17 LKDVSIEIESGEIFGIIGHSGAGKSTL----------LRCINGLEEYQ---------------EG-SVLVSDKEvKSLNe 70
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAYArqflgqmdkpdvdsiEGlSPAIAIDQ-KTTS- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 71 kqmRDLRKELGMIFQHFSLLerktvfdnvalpleCFGYSKAEIKKRvLELLEVVGISEKKNDKPRN-LSGGQKQRVAIAR 149
Cdd:cd03270 89 ---RNPRSTVGTVTEIYDYL--------------RLLFARVGIRER-LGFLVDVGLGYLTLSRSAPtLSGGEAQRIRLAT 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497582239 150 AL--ALNPQVLLCDEATSALDPNTTKSILSLLEDInKKLGITIIVVTHQMEVIK 201
Cdd:cd03270 151 QIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIR 203
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
9-211 |
7.60e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.64 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 9 KYYGKIQVLKDVSiEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEgsvlvsdkevkslnekqmrdlrkelgmifqhfs 88
Cdd:cd03222 8 KRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNG--------------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 89 llerktvfDNVALPLECFGYSKAEIKkrvlellevvgisekkndkprnLSGGQKQRVAIARALALNPQVLLCDEATSALD 168
Cdd:cd03222 54 --------DNDEWDGITPVYKPQYID----------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497582239 169 P----NTTKSILSLLEDINKklgiTIIVVTHQMEVIKQICGRVAIME 211
Cdd:cd03222 104 IeqrlNAARAIRRLSEEGKK----TALVVEHDLAVLDYLSDRIHVFE 146
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-215 |
8.19e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 15 QVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLE--EYQEGSVLVSDKEVKSLNEKQMRDL--------RKELGMIf 84
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVSTVSDAIDAglayvtedRKGYGLN- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 85 qhfsLLErkTVFDNVALPlecfgySKAEIKKR-VLELLEVVGISEKKNDKPR-----------NLSGGQKQRVAIARALA 152
Cdd:NF040905 353 ----LID--DIKRNITLA------NLGKVSRRgVIDENEEIKVAEEYRKKMNiktpsvfqkvgNLSGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 153 LNPQVLLCDEATSALDPNTTKSILSLledINK--KLGITIIVVTHQMEVIKQICGRVAIMENGEV 215
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTI---INElaAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-201 |
3.36e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.09 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 1 MISIKNVnKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNekqmrdlRKEL 80
Cdd:PRK13541 1 MLSLHQL-QFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-------KPYC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 81 GMIFQHFSLLERKTVFDNVALPLECfgYSKAEIKKRVLELLEVVGISEKkndKPRNLSGGQKQRVAIARALALNPQVLLC 160
Cdd:PRK13541 73 TYIGHNLGLKLEMTVFENLKFWSEI--YNSAETLYAAIHYFKLHDLLDE---KCYSLSSGMQKIVAIARLIACQSDLWLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 497582239 161 DEATSALDpNTTKSILSLLEDINKKLGITIIVVTHQMEVIK 201
Cdd:PRK13541 148 DEVETNLS-KENRDLLNNLIVMKANSGGIVLLSSHLESSIK 187
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
3-201 |
7.56e-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: 43.03 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 3 SIKNVNKYYGKiQVLkDVSiEIESGEIFGIIGHSGAGKSTLLRCI---------NGLEEYQEGSVLVS-DKEVK-----S 67
Cdd:cd03279 7 ELKNFGPFREE-QVI-DFT-GLDNNGLFLICGPTGAGKSTILDAItyalygktpRYGRQENLRSVFAPgEDTAEvsftfQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 68 LNEKQMRdLRKELGMIFQHFslleRKTVFdnvaLPlecfgysKAEIKkrvlELLEvvgisekkndKP-RNLSGGQKQRVA 146
Cdd:cd03279 84 LGGKKYR-VERSRGLDYDQF----TRIVL----LP-------QGEFD----RFLA----------RPvSTLSGGETFLAS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497582239 147 IARALALNPQV----------LLCDEATSALDPNTTKSILSLLEDInKKLGITIIVVTHqMEVIK 201
Cdd:cd03279 134 LSLALALSEVLqnrggarleaLFIDEGFGTLDPEALEAVATALELI-RTENRMVGVISH-VEELK 196
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
21-201 |
1.96e-04 |
|
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: 41.19 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 21 SIEIESGEIFGIIGHSGAGKSTLLRCInGLEEYQEGSVLVSDKEVKSlnekqmrdlrkelgmifQHFSllerktvfdnva 100
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDAI-GLALGGAQSATRRRSGVKA-----------------GCIV------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 101 lplecfGYSKAEIkkrvleLLEVVGisekkndkprnLSGGQKQRVAIARALAL---NPQVLLC-DEATSALDPNTTKSIL 176
Cdd:cd03227 65 ------AAVSAEL------IFTRLQ-----------LSGGEKELSALALILALaslKPRPLYIlDEIDRGLDPRDGQALA 121
|
170 180
....*....|....*....|....*
gi 497582239 177 SLLEDINKKlGITIIVVTHQMEVIK 201
Cdd:cd03227 122 EAILEHLVK-GAQVIVITHLPELAE 145
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
112-281 |
3.58e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 112 EIKKRvLELLEVVGISEKKNDKP-RNLSGGQKQRVAIARAL--ALNPQVLLCDEATSALDPNTTKSILSLLEDInKKLGI 188
Cdd:TIGR00630 464 EIRER-LGFLIDVGLDYLSLSRAaGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRL-RDLGN 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 189 TIIVVTHQMEVIKQI-----CGRVAIMENGEVLEVGDTEEIfLRNTKGL--RKLIGEESIILPKgtnikilFPKDISNEA 261
Cdd:TIGR00630 542 TLIVVEHDEDTIRAAdyvidIGPGAGEHGGEVVASGTPEEI-LANPDSLtgQYLSGRKKIEVPA-------ERRPGNGKF 613
|
170 180
....*....|....*....|...
gi 497582239 262 IITTMARELN---IDVSIIFGKL 281
Cdd:TIGR00630 614 LTLKGARENNlknITVSIPLGLF 636
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
17-276 |
5.39e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 17 LKDVSIEIESGEIFGIIGHSGAGKS-----TLLRCINGLEE--------YQEGSV--LV---------SDKEVKSLNEKQ 72
Cdd:PRK00635 611 LKDLTISLPLGRLTVVTGVSGSGKSslindTLVPAVEEFIEqgfcsnlsIQWGAIsrLVhitrdlpgrSQRSIPLTYIKA 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 73 MRDLR---------KELGMIFQHFSL------------LERKTVFDN---VALPLeCFGY----SKAEIK---KRVLELL 121
Cdd:PRK00635 691 FDDLRelfaeqprsKRLGLTKSHFSFntplgacaecqgLGSITTTDNrtsIPCPS-CLGKrflpQVLEVRykgKNIADIL 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 122 EVVGISEKK--NDKPR-----------------------NLSGGQKQRVAIARAL---ALNPQVLLCDEATSALDPNTTK 173
Cdd:PRK00635 770 EMTAYEAEKffLDEPSihekihalcslgldylplgrplsSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIK 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 174 SILSLLEDINKkLGITIIVVTHQMEVIKqICGRVAIM------ENGEVLEVGDTEEIFLRNT---KGLRKLIgEESIILP 244
Cdd:PRK00635 850 ALIYVLQSLTH-QGHTVVIIEHNMHVVK-VADYVLELgpeggnLGGYLLASCSPEELIHLHTptaKALRPYL-SSPQELP 926
|
330 340 350
....*....|....*....|....*....|....*
gi 497582239 245 KgtnIKILFPKDISNEAIITTMARELN---IDVSI 276
Cdd:PRK00635 927 Y---LPDPSPKPPVPADITIKNAYQHNlkhIDLSL 958
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
116-202 |
5.60e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 116 RVLELLEVVGISEKKNDKP-RNLSGGQKQRVAIARAL---ALNPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITII 191
Cdd:TIGR00630 808 RKLQTLCDVGLGYIRLGQPaTTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDK-GNTVV 886
|
90
....*....|.
gi 497582239 192 VVTHQMEVIKQ 202
Cdd:TIGR00630 887 VIEHNLDVIKT 897
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
10-168 |
8.22e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 10 YYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDlrkelGMIFQHFSL 89
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVD-----GLDLSSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 90 LERKTVFDNVAlplecfgyskaeiKKRVLELLEVVGISEKKNDKPR-NLSGGQKQRVAIARALALNPQVLLCDEATSALD 168
Cdd:PLN03073 593 LYMMRCFPGVP-------------EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
115-201 |
1.02e-03 |
|
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: 39.91 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 115 KRVLELLEVVGISEKKNDKP-RNLSGGQKQRVAIARAL---ALNPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITI 190
Cdd:cd03271 147 ARKLQTLCDVGLGYIKLGQPaTTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTV 225
|
90
....*....|.
gi 497582239 191 IVVTHQMEVIK 201
Cdd:cd03271 226 VVIEHNLDVIK 236
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
137-181 |
2.53e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.44 E-value: 2.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 497582239 137 LSGGQKQR-VAIARALAL------------NPQVLLCDEATSALDPNTTKSILSLLED 181
Cdd:pfam13558 33 LSGGEKQLlAYLPLAAALaaqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-244 |
2.71e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497582239 137 LSGGQKQRVAIARALA--LNPQVLLCDEATSALDPNTTKSILSLLEDINKKlGITIIVVTHQMEVIkQICGRV------A 208
Cdd:PRK00635 477 LSGGEQERTALAKHLGaeLIGITYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDEQMI-SLADRIidigpgA 554
|
90 100 110
....*....|....*....|....*....|....*...
gi 497582239 209 IMENGEVLEVGDTEEiFLRNTKGL--RKLIGEESIILP 244
Cdd:PRK00635 555 GIFGGEVLFNGSPRE-FLAKSDSLtaKYLRQELTIPIP 591
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
135-182 |
8.60e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.90 E-value: 8.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 497582239 135 RNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDI 182
Cdd:PLN03140 335 RGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQI 382
|
|
| |
