|
Name |
Accession |
Description |
Interval |
E-value |
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-226 |
1.12e-151 |
|
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: 421.07 E-value: 1.12e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTFVLYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERWVDIV 80
Cdd:COG4778 1 MTTLLEVENLSKTFTLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 NADARHVLEIRRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLAPATFSGGEQQR 160
Cdd:COG4778 81 QASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLPPATFSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404648 161 INIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSMA 226
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
5-229 |
1.80e-128 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 362.09 E-value: 1.80e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFVLYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERWVDIVNADA 84
Cdd:TIGR02324 2 LEVEDLSKTFTLHQQGGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEGAWVDLAQASP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLAPATFSGGEQQRINIA 164
Cdd:TIGR02324 82 REVLEVRRKTIGYVSQFLRVIPRVSALEVVAEPLLERGVPREAARARARELLARLNIPERLWHLPPATFSGGEQQRVNIA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLysMAMTS 229
Cdd:TIGR02324 162 RGFIADYPILLLDEPTASLDAANRQVVVELIAEAKARGAALIGIFHDEEVRELVADRV--MDVTP 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-225 |
4.99e-53 |
|
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: 170.36 E-value: 4.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTfvlYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADA 84
Cdd:cd03255 1 IELKNLSKT---YGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGT----DISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLwSLAPATFSGGEQQRINIA 164
Cdd:cd03255 74 KELAAFRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRL-NHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHvADRLYSM 225
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRElNKEAGTTIVVVTHDPELAEY-ADRIIEL 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-225 |
1.99e-52 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 169.07 E-value: 1.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTfvlYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIV 80
Cdd:COG1136 1 MSPLLELRNLTKS---YGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQ----DIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 NADARHVLEIRRETVGWVSQFLRVIPRISTL-NVVIqPLLERGMSRQESEIRGGELLTHLNVPERLWSLaPATFSGGEQQ 159
Cdd:COG1136 74 SLSERELARLRRRHIGFVFQFFNLLPELTALeNVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHR-PSQLSGGQQQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 160 RINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHvADRLYSM 225
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVTHDPELAAR-ADRVIRL 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-181 |
8.45e-44 |
|
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: 144.71 E-value: 8.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 27 FHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERWVDIvnadarhvLEIRRETVGWVSQFLRVIP 106
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE--------RKSLRKEIGYVFQDPQLFP 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404648 107 RISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPE---RLWSLAPATFSGGEQQRINIARGFIGDYPILLLDEPTA 181
Cdd:pfam00005 73 RLTVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-225 |
1.68e-43 |
|
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: 146.11 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFVLynqQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADA 84
Cdd:cd03257 2 LEVKNLSVSFPT---GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGK----DLLKLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RhVLEIRRETVGWVSQ--FLRVIPRISTLNVVIQPLLERGMSRQESEIR--GGELLTHLNVPERLWSLAPATFSGGEQQR 160
Cdd:cd03257 75 R-LRKIRRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKeaVLLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404648 161 INIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-226 |
6.21e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 139.18 E-value: 6.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVdktfvlyNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERwvdivnaDA 84
Cdd:COG4619 1 LELEGL-------SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-------SA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRREtVGWVSQflrvIPRI---STLNVVIQPLLERGMSRQESEIRggELLTHLNVPERLWSLAPATFSGGEQQRI 161
Cdd:COG4619 67 MPPPEWRRQ-VAYVPQ----EPALwggTVRDNLPFPFQLRERKFDRERAL--ELLERLGLPPDILDKPVERLSGGERQRL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404648 162 NIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADRLYSMA 226
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLE 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-206 |
3.44e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.48 E-value: 3.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADA 84
Cdd:COG2884 2 IRFENVSKRY------PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQ----DLSRLKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRReTVGWVSQFLRVIPRISTL-NVVIqPLLERGMSRQESEIRGGELLTHLNVPERLWSLaPATFSGGEQQRINI 163
Cdd:COG2884 72 REIPYLRR-RIGVVFQDFRLLPDRTVYeNVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKAL-PHELSGGEQQRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499404648 164 ARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVV 206
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVL 191
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-226 |
3.75e-38 |
|
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: 131.88 E-value: 3.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTrLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiVNADA 84
Cdd:cd03262 1 IEIKNLHKSF------GD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLK-----LTDDK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRREtVGWVSQFLRVIPRISTL-NVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLaPATFSGGEQQRINI 163
Cdd:cd03262 69 KNINELRQK-VGMVFQQFNLFPHLTVLeNITLAPIKVKGMSKAEAEERALELLEKVGLADKADAY-PAQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499404648 164 ARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSMA 226
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMD 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-225 |
2.20e-37 |
|
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: 136.57 E-value: 2.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFVLynQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADA 84
Cdd:COG1123 261 LEVRNLSKRYPV--RGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGK----DLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRREtVGWVSQ--FLRVIPRISTLNVVIQPLLERG-MSRQESEIRGGELLTHLNVPERLWSLAPATFSGGEQQRI 161
Cdd:COG1123 335 RSLRELRRR-VQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 162 NIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlQRELGLTYLFISHDLAVVRYIADRVAVM 478
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-226 |
6.28e-37 |
|
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: 129.92 E-value: 6.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTfvlYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdIVNADA 84
Cdd:COG1124 2 LEVRNLSVS---YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRP----VTRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHvleiRRETVGWVSQ--FLRVIPRISTLNVVIQPLLERGMSRQESEIRggELLTHLNVPERLWSLAPATFSGGEQQRIN 162
Cdd:COG1124 75 KA----FRRRVQMVFQdpYASLHPRHTVDRILAEPLRIHGLPDREERIA--ELLEQVGLPPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 163 IARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAK-SKGCAVVGIFHDDEVRQHVADRLYSMA 226
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQ 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
17-225 |
3.76e-35 |
|
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: 124.12 E-value: 3.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 17 YNQQGTrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvdivNADARHVLEIRREtVG 96
Cdd:cd03225 9 YPDGAR--PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGK-------DLTKLSLKELRRK-VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 97 WVSQFlrviPR--ISTLNV---VIQPLLERGMSRQESEIRGGELLTHLNvperLWSLA---PATFSGGEQQRINIARGFI 168
Cdd:cd03225 79 LVFQN----PDdqFFGPTVeeeVAFGLENLGLPEEEIEERVEEALELVG----LEGLRdrsPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 169 GDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-184 |
2.06e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 123.18 E-value: 2.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTrLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLygNY--RPDGGHIWVRHRErwvdiVNA 82
Cdd:COG1126 2 IEIENLHKSF------GD-LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI--NLleEPDSGTITVDGED-----LTD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 83 DARHVLEIRREtVGWVSQ----FlrviPRISTL-NVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLaPATFSGGE 157
Cdd:COG1126 68 SKKDINKLRRK-VGMVFQqfnlF----PHLTVLeNVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAY-PAQLSGGQ 141
|
170 180
....*....|....*....|....*..
gi 499404648 158 QQRINIARGFIGDYPILLLDEPTASLD 184
Cdd:COG1126 142 QQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-195 |
3.77e-34 |
|
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: 122.16 E-value: 3.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTfvlYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVDIVNADA 84
Cdd:COG4181 9 IELRGLTKT---VGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD--LFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RhvLEIRRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSrqESEIRGGELLTHLNVPERLwSLAPATFSGGEQQRINIA 164
Cdd:COG4181 84 R--ARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRL-DHYPAQLSGGEQQRVALA 158
|
170 180 190
....*....|....*....|....*....|.
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQLI 195
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLL 189
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-222 |
4.29e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 122.09 E-value: 4.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIvnadA 84
Cdd:COG1131 1 IEVRGLTKRY------GDK-TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE----DV----A 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRREtVGWVSQFLRVIPRIStlnvVIQpLLE-----RGMSRQESEIRGGELLTHLNVPERLWSLApATFSGGEQQ 159
Cdd:COG1131 66 RDPAEVRRR-IGYVPQEPALYPDLT----VRE-NLRffarlYGLPRKEARERIDELLELFGLTDAADRKV-GTLSGGMKQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404648 160 RINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVvgIF--HD-DEVrQHVADRL 222
Cdd:COG1131 139 RLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTV--LLstHYlEEA-ERLCDRV 201
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-222 |
1.37e-33 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 120.43 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADA 84
Cdd:TIGR02673 2 IEFHNVSKAY------PGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGE----DVNRLRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRREtVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLaPATFSGGEQQRINIA 164
Cdd:TIGR02673 72 RQLPLLRRR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAF-PEQLSGGEQQRVAIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRL 222
Cdd:TIGR02673 150 RAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRV 207
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
9-222 |
2.20e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.58 E-value: 2.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 9 NVDKTFvlynqqgTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiVNADARHVL 88
Cdd:PRK09493 6 NVSKHF-------GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLK-----VNDPKVDER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 89 EIRRETvGWVSQFLRVIPRISTL-NVVIQPLLERGMSRQESEIRGGELLTHLNVPERLwSLAPATFSGGEQQRINIARGF 167
Cdd:PRK09493 74 LIRQEA-GMVFQQFYLFPHLTALeNVMFGPLRVRGASKEEAEKQARELLAKVGLAERA-HHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 168 IGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRL 222
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRL 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-225 |
3.52e-33 |
|
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: 117.88 E-value: 3.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIvnadA 84
Cdd:cd03230 1 IEVRNLSKRY------GKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG----KDI----K 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRREtVGWVSQFLRVIPRIStlnvviqpllergmsrqeseirGGELLthlnvperlwslapaTFSGGEQQRINIA 164
Cdd:cd03230 66 KEPEEVKRR-IGYLPEEPSLYENLT----------------------VRENL---------------KLSGGMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAIL 168
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
1.05e-32 |
|
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: 123.86 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTFvlynqQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGnYRPDGGHIWVRHRERWVDIV 80
Cdd:COG1123 1 MTPLLEVRDLSVRY-----PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRISGEVLLDGRDLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 NADARhvleIRRETVGWVSQ-FLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSlAPATFSGGEQQ 159
Cdd:COG1123 75 ELSEA----LRGRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDR-YPHQLSGGQRQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 160 RINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLGVVAEIADRVVVM 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-206 |
1.11e-32 |
|
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: 117.58 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 4 QLRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRhrerwvdivNAD 83
Cdd:COG4133 2 MLEAENLSCRR------GER-LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN---------GEP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 84 ARHVLEIRRETVGWVSQFLRVIPRIStlnvviqpLLE--------RGMSRQESEIRggELLTHLNVpERLWSLAPATFSG 155
Cdd:COG4133 66 IRDAREDYRRRLAYLGHADGLKPELT--------VREnlrfwaalYGLRADREAID--EALEAVGL-AGLADLPVRQLSA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499404648 156 GEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVV 206
Cdd:COG4133 135 GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVL 185
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-230 |
2.51e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 118.27 E-value: 2.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTfvlYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrhrerwvdiv 80
Cdd:COG1116 4 AAPALELRGVSKR---FPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 naDARHVLEIRREtVGWVSQFLRVIPRISTL-NVVIqPLLERGMSRQESEIRGGELLTHLNVPERLWSLaPATFSGGEQQ 159
Cdd:COG1116 71 --DGKPVTGPGPD-RGVVFQEPALLPWLTVLdNVAL-GLELRGVPKAERRERARELLELVGLAGFEDAY-PHQLSGGMRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499404648 160 RINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHD-DE-VRqhVADRLYsmAMTSR 230
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRlWQETGKTVLFVTHDvDEaVF--LADRVV--VLSAR 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
25-211 |
2.93e-32 |
|
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: 116.00 E-value: 2.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrhrerwvDIVNADARHVLEIRREtVGWVSQFLRV 104
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL-------DGKDLASLSPKELARK-IAYVPQALEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 ipristlnVVIQPLLERGMSrqeseirggellthlnvperlwslapaTFSGGEQQRINIARGFIGDYPILLLDEPTASLD 184
Cdd:cd03214 85 --------LGLAHLADRPFN---------------------------ELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180
....*....|....*....|....*...
gi 499404648 185 AKNRLAVTQLIDD-AKSKGCAVVGIFHD 211
Cdd:cd03214 130 IAHQIELLELLRRlARERGKTVVMVLHD 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-211 |
1.37e-31 |
|
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: 116.30 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDktfVLYNQQgtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADA 84
Cdd:COG1120 2 LEAENLS---VGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGR----DLASLSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RhvlEIRReTVGWVSQFLRVIPRISTLNVVI------QPLLERGMSRQESEIRggELLTHLNvperLWSLAP---ATFSG 155
Cdd:COG1120 71 R---ELAR-RIAYVPQEPPAPFGLTVRELVAlgryphLGLFGRPSAEDREAVE--EALERTG----LEHLADrpvDELSG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 156 GEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHD 211
Cdd:COG1120 141 GERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlARERGRTVVMVLHD 197
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-226 |
5.75e-31 |
|
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: 114.32 E-value: 5.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 4 QLRIENVDKTFvlynqqGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNAD 83
Cdd:TIGR02315 1 MLEVENLSKVY------PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGT----DITKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 84 ARHVLEIRRETvGWVSQFLRVIPRISTLNVVIQPLLE-----RGMSRQESE---IRGGELLTHLNVPERLWSLApATFSG 155
Cdd:TIGR02315 71 GKKLRKLRRRI-GMIFQHYNLIERLTVLENVLHGRLGykptwRSLLGRFSEedkERALSALERVGLADKAYQRA-DQLSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 156 GEQQRINIARGFIGDYPILLLDEPTASLDAKNrlaVTQLIDD----AKSKGCAVVGIFHDDEVRQHVADRLYSMA 226
Cdd:TIGR02315 149 GQQQRVAIARALAQQPDLILADEPIASLDPKT---SKQVMDYlkriNKEDGITVIINLHQVDLAKKYADRIVGLK 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-225 |
1.10e-30 |
|
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: 111.18 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 6 RIENVDKTfvlYNQQgtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERWvdivnadaR 85
Cdd:cd00267 1 EIENLSFR---YGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA--------K 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 86 HVLEIRRETVGWVSQFlrvipristlnvviqpllergmsrqeseirggellthlnvperlwslapatfSGGEQQRINIAR 165
Cdd:cd00267 66 LPLEELRRRIGYVPQL----------------------------------------------------SGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 166 GFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-222 |
1.66e-30 |
|
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: 113.05 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTfvlYNQQGTRLpvfHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiVNADA 84
Cdd:cd03256 1 IEVENLSKT---YPNGKKAL---KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTD-----INKLK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRRETVGWVSQFLRVIPRISTLNVVIQPLLE-----RGMSRQESEI---RGGELLTHLNVPERLWSLApATFSGG 156
Cdd:cd03256 70 GKALRQLRRQIGMIFQQFNLIERLSVLENVLSGRLGrrstwRSLFGLFPKEekqRALAALERVGLLDKAYQRA-DQLSGG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 157 EQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLI-DDAKSKGCAVVGIFHDDEVRQHVADRL 222
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREEGITVIVSLHQVDLAREYADRI 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-221 |
2.05e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 112.84 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADA 84
Cdd:COG3638 3 LELRNLSKRY------PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQ----DVTALRG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRREtVGWVSQFLRVIPRISTL-NVVI-----QPLLeRGMSRQ--ESEIRGG-ELLTHLNVPERLWSLApATFSG 155
Cdd:COG3638 73 RALRRLRRR-IGMIFQQFNLVPRLSVLtNVLAgrlgrTSTW-RSLLGLfpPEDRERAlEALERVGLADKAYQRA-DQLSG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404648 156 GEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLI-DDAKSKGCAVVGIFHD-DEVRQHvADR 221
Cdd:COG3638 150 GQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREDGITVVVNLHQvDLARRY-ADR 216
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-223 |
3.43e-30 |
|
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: 112.00 E-value: 3.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIV 80
Cdd:COG1127 2 SEPMIEVRNLTKSF------GDR-VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQ----DIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 NADARHVLEIRREtVGWVSQF--LrviprISTLNV---VIQPLLER-GMSRQESEIRGGELLTHLNVPErLWSLAPATFS 154
Cdd:COG1127 71 GLSEKELYELRRR-IGMLFQGgaL-----FDSLTVfenVAFPLREHtDLSEAEIRELVLEKLELVGLPG-AADKMPSELS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404648 155 GGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHD-DEVRQhVADRLY 223
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDlDSAFA-IADRVA 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-226 |
5.51e-30 |
|
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: 111.27 E-value: 5.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVdkTFVlYNQQGtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADA 84
Cdd:COG1122 1 IELENL--SFS-YPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGK----DITKKNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RhvlEIRREtVGWV-----SQFLRvipriSTlnV---VIQPLLERGMSRQESEIRGGELLTHLNVpERLWSLAPATFSGG 156
Cdd:COG1122 71 R---ELRRK-VGLVfqnpdDQLFA-----PT--VeedVAFGPENLGLPREEIRERVEEALELVGL-EHLADRPPHELSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404648 157 EQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD-DEVRQhVADRLYSMA 226
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDlDLVAE-LADRVIVLD 208
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-223 |
7.49e-30 |
|
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: 109.39 E-value: 7.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNADa 84
Cdd:cd03228 1 IEFKNVSFSY-----PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG----VDLRDLD- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 rhvLEIRRETVGWVSQflrvipristlnvviQPLLERGmsrqeseirggellthlnvperlwSLAPATFSGGEQQRINIA 164
Cdd:cd03228 71 ---LESLRKNIAYVPQ---------------DPFLFSG------------------------TIRENILSGGQRQRIAIA 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAkSKGCAVVGIFHDDEVRQHvADRLY 223
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRD-ADRII 165
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-223 |
8.62e-30 |
|
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: 111.05 E-value: 8.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNADA 84
Cdd:cd03261 1 IELRGLTKSF------GGR-TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDG----EDISGLSE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRREtVGWVSQF--LrviprISTLNV---VIQPLLERG-MSRQESEIRGGELLTHLNVPERLwSLAPATFSGGEQ 158
Cdd:cd03261 70 AELYRLRRR-MGMLFQSgaL-----FDSLTVfenVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 159 QRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHD-DEVRQhVADRLY 223
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlKKELGLTSIMVTHDlDTAFA-IADRIA 208
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-225 |
2.37e-29 |
|
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: 109.15 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqQGTRlpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrhrerwvdivnaDA 84
Cdd:cd03259 1 LELKGLSKTY-----GSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI------------DG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHV--LEIRRETVGWVSQFLRVIPRISTL-NVVIqPLLERGMSRQESEIRGGELLTHLNVPERLwSLAPATFSGGEQQRI 161
Cdd:cd03259 62 RDVtgVPPERRNIGMVFQDYALFPHLTVAeNIAF-GLKLRGVPKAEIRARVRELLELVGLEGLL-NRYPHELSGGQQQRV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 162 NIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDA-KSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVM 204
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-221 |
3.07e-29 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 108.86 E-value: 3.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 7 IENVDKTFvlynqqGTRLpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdIVNADARH 86
Cdd:TIGR03608 1 LKNISKKF------GDKV-ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQE----TPPLNSKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 87 VLEIRRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLwSLAPATFSGGEQQRINIARG 166
Cdd:TIGR03608 70 ASKFRREKLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKL-KQKIYELSGGEQQRVALARA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 167 FIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQhVADR 221
Cdd:TIGR03608 149 ILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK-QADR 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
3.19e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 109.79 E-value: 3.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDktfVLYNQQgtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiv 80
Cdd:COG1121 3 MMPAIELENLT---VSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 nadarhvLEIRRETVGWVSQFLRVIPR--ISTLNVVIQPL-----LERGMSRQESEiRGGELLTHLNvperLWSLAPATF 153
Cdd:COG1121 70 -------PRRARRRIGYVPQRAEVDWDfpITVRDVVLMGRygrrgLFRRPSRADRE-AVDEALERVG----LEDLADRPI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499404648 154 ---SGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD-DEVRQHVaDRL 222
Cdd:COG1121 138 gelSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDlGAVREYF-DRV 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-214 |
9.16e-29 |
|
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: 107.88 E-value: 9.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 8 ENVDKTFvlynqqGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNADARHV 87
Cdd:cd03292 4 INVTKTY------PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNG----QDVSDLRGRAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 88 LEIRREtVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLaPATFSGGEQQRINIARGF 167
Cdd:cd03292 74 PYLRRK-IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRAL-PAELSGGEQQRVAIARAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499404648 168 IGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEV 214
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKEL 198
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-230 |
1.71e-28 |
|
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: 107.17 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTfvlYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrhrerwvdivnaDA 84
Cdd:cd03293 1 LEVRNVSKT---YGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLV------------DG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRREtVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELL--THLNVPERLWslaPATFSGGEQQRIN 162
Cdd:cd03293 66 EPVTGPGPD-RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLelVGLSGFENAY---PHQLSGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404648 163 IARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHD-DE-VrqHVADRLYsmAMTSR 230
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDiDEaV--FLADRVV--VLSAR 208
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-213 |
2.84e-28 |
|
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: 107.48 E-value: 2.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDktfVLYNQQgtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRP-DGGHIWVRHRERW-VDIvna 82
Cdd:COG1119 4 LELRNVT---VRRGGK----TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGERRGgEDV--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 83 darhvLEIRREtVGWVSQFL--RVIPRISTLNVV-------IqpllerGMSRQESEI---RGGELLTHLnvpeRLWSLAP 150
Cdd:COG1119 74 -----WELRKR-IGLVSPALqlRFPRDETVLDVVlsgffdsI------GLYREPTDEqreRARELLELL----GLAHLAD 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 151 ATF---SGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDE 213
Cdd:COG1119 138 RPFgtlSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVLVTHHVE 204
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-225 |
4.27e-28 |
|
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: 111.40 E-value: 4.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVDIVNADA 84
Cdd:COG4987 334 LELEDVSFRY-----PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD--LRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RhvleirRETVGWVSQ----FLrvipriSTL--NVviqpLLERGMSrQESEIRG-------GELLTHLnvPERLWSL--- 148
Cdd:COG4987 407 L------RRRIAVVPQrphlFD------TTLreNL----RLARPDA-TDEELWAalervglGDWLAAL--PDGLDTWlge 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 149 APATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAkSKGCAVVGIFHDDEVRQHvADRLYSM 225
Cdd:COG4987 468 GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLER-MDRILVL 542
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-226 |
9.15e-28 |
|
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: 104.19 E-value: 9.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTfvlYNQQgtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRhrerwvDIVNADA 84
Cdd:cd03229 1 LELKNVSKR---YGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID------GEDLTDL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRRETVGWVSQFLRVIPRISTLNVVIQPLlergmsrqeseirggellthlnvperlwslapatfSGGEQQRINIA 164
Cdd:cd03229 68 EDELPPLRRRIGMVFQDFALFPHLTVLENIALGL-----------------------------------SGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADRLYSMA 226
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-223 |
1.32e-27 |
|
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: 105.32 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRhrerwvdivNADA 84
Cdd:COG4555 2 IEVENLSKKY------GKV-PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID---------GEDV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRRETVGWVSQFLRVIPRISTL-NVVIQPLLeRGMSRQESEIRGGELLTHLNVPE---RLWSlapaTFSGGEQQR 160
Cdd:COG4555 66 RKEPREARRQIGVLPDERGLYDRLTVReNIRYFAEL-YGLFDEELKKRIEELIELLGLEEfldRRVG----ELSTGMKKK 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 161 INIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVvgIF--HDDEVRQHVADRLY 223
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTV--LFssHIMQEVEALCDRVV 203
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-225 |
2.61e-27 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 105.27 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 3 TQLRIENVDKTFV--LYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhRERWVDIV 80
Cdd:TIGR02769 1 SLLEVRDVTHTYRtgGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTV----SFRGQDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 NADARHVLEIRREtVGWVSQ--FLRVIPRISTLNVVIQPL--LERgMSRQESEIRGGELLTHLNVPERLWSLAPATFSGG 156
Cdd:TIGR02769 77 QLDRKQRRAFRRD-VQLVFQdsPSAVNPRMTVRQIIGEPLrhLTS-LDESEQKARIAELLDMVGLRSEDADKLPRQLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 157 EQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVM 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-225 |
6.60e-27 |
|
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: 107.92 E-value: 6.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 4 QLRIENVDktfVLYNQqgtRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNAD 83
Cdd:COG4988 336 SIELEDVS---FSYPG---GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING----VDLSDLD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 84 ARHvleiRRETVGWVSQflrvipristlnvviQPLLERG-------MSRQ---ESEIRggELLTHLNVPERLWSLaP--- 150
Cdd:COG4988 406 PAS----WRRQIAWVPQ---------------NPYLFAGtirenlrLGRPdasDEELE--AALEAAGLDEFVAAL-Pdgl 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 151 --------ATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAkSKGCAVVGIFHDDEVRQHvADRL 222
Cdd:COG4988 464 dtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQ-ADRI 541
|
...
gi 499404648 223 YSM 225
Cdd:COG4988 542 LVL 544
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-186 |
1.49e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 102.55 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 23 RLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGnyRPDGGHIWVRHRERWVDIVNADARhvLEIRRETVGWVSQFL 102
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAG--LDDGSSGEVSLVGQPLHQMDEEAR--AKLRAKHVGFVFQSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 103 RVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLaPATFSGGEQQRINIARGFIGDYPILLLDEPTAS 182
Cdd:PRK10584 98 MLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHL-PAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
....
gi 499404648 183 LDAK 186
Cdd:PRK10584 177 LDRQ 180
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-191 |
1.51e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 104.79 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIV 80
Cdd:COG3842 2 AMPALELENVSKRY------GDV-TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR----DVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 N--ADARHvleirretVGWVSQ----FlrviPRistLNV---VIQPLLERGMSRQESEIRGGELLTHLNVPErlwsLA-- 149
Cdd:COG3842 71 GlpPEKRN--------VGMVFQdyalF----PH---LTVaenVAFGLRMRGVPKAEIRARVAELLELVGLEG----LAdr 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499404648 150 -PATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAV 191
Cdd:COG3842 132 yPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEM 174
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-221 |
4.57e-26 |
|
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: 101.12 E-value: 4.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlyNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADA 84
Cdd:cd03258 2 IELKNVSKVF---GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGT----DLTLLSG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRREtVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLaPATFSGGEQQRINIA 164
Cdd:cd03258 75 KELRKARRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAY-PAQLSGGQKQRVGIA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADR 221
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDR 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-211 |
5.21e-26 |
|
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: 100.69 E-value: 5.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 6 RIENVdkTFVLYNQqgtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrhrerwvdivnaDAR 85
Cdd:cd03235 1 EVEDL--TVSYGGH-----PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV------------FGK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 86 HVLEIRREtVGWVSQFlRVIPR---ISTLNVVIQPL-----LERGMSRQESEI------RGGelLTHLnVPERLWSLapa 151
Cdd:cd03235 62 PLEKERKR-IGYVPQR-RSIDRdfpISVRDVVLMGLyghkgLFRRLSKADKAKvdealeRVG--LSEL-ADRQIGEL--- 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 152 tfSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD 211
Cdd:cd03235 134 --SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHD 191
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-221 |
5.57e-26 |
|
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: 102.82 E-value: 5.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFVLYNQqgtRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRP---DGGHIWVRHRerwvDIVN 81
Cdd:COG0444 2 LEVRNLKVYFPTRRG---VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGE----DLLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 82 ADARHVLEIRRETVGWVSQflr--viPRISTLNVVIQPLLE-RGMSRQESEIRGGELLT--HLNVPERLWSLAPATFSGG 156
Cdd:COG0444 75 LSEKELRKIRGREIQMIFQdpmtslnPVMTVGDQIAEPLRIhGGLSKAEARERAIELLErvGLPDPERRLDRYPHELSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404648 157 EQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADR 221
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDlQRELGLAILFITHDLGVVAEIADR 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
26-225 |
9.56e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 100.47 E-value: 9.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhrerwvDIVN--------ADARHVLEIRREtVGW 97
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL---------NIAGnhfdfsktPSDKAIRELRRN-VGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 98 VSQFLRVIPRIStlnvVIQPLLE-----RGMSRQESEIRGGELLTHLnvpeRLWSLA---PATFSGGEQQRINIARGFIG 169
Cdd:PRK11124 87 VFQQYNLWPHLT----VQQNLIEapcrvLGLSKDQALARAEKLLERL----RLKPYAdrfPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499404648 170 DYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYM 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-226 |
1.26e-25 |
|
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: 98.44 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVdkTFVLynqQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNADa 84
Cdd:cd03246 1 LEVENV--SFRY---PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG----ADISQWD- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 rhvLEIRRETVGWVSQflrvipristlnvviqpllergmsrqESEIRGGellthlnvperlwSLAPATFSGGEQQRINIA 164
Cdd:cd03246 71 ---PNELGDHVGYLPQ--------------------------DDELFSG-------------SIAENILSGGQRQRLGLA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQhVADRLYSMA 226
Cdd:cd03246 109 RALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLE 169
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-222 |
1.36e-25 |
|
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: 99.50 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdivnaDA 84
Cdd:cd03263 1 LQIRNLTKTY-----KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS--------IR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRREtVGWVSQFlRVIPriSTLNV----VIQPLLeRGMSRQ------ESEIRGGELLTHLNVPERlwslapaTFS 154
Cdd:cd03263 68 TDRKAARQS-LGYCPQF-DALF--DELTVrehlRFYARL-KGLPKSeikeevELLLRVLGLTDKANKRAR-------TLS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404648 155 GGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKsKGCAVVGIFHDDEVRQHVADRL 222
Cdd:cd03263 136 GGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRI 202
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-225 |
3.51e-25 |
|
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: 103.38 E-value: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVdkTFVlYNQQGTrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNADA 84
Cdd:COG2274 474 IELENV--SFR-YPGDSP--PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG----IDLRQIDP 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVleirRETVGWVSQ--FL-------------------RVIP--RISTLNVVIQpLLERGMSRQESEirGGellthlnv 141
Cdd:COG2274 545 ASL----RRQIGVVLQdvFLfsgtirenitlgdpdatdeEIIEaaRLAGLHDFIE-ALPMGYDTVVGE--GG-------- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 142 perlwslapATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKsKGCAVVGIFHDDEVRQHvADR 221
Cdd:COG2274 610 ---------SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRL-ADR 678
|
....
gi 499404648 222 LYSM 225
Cdd:COG2274 679 IIVL 682
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
26-221 |
5.69e-25 |
|
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: 98.02 E-value: 5.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLRSLYG-----NYRPDGGHIWVRHRERWVDIVNadarhVLEIRReTVGWVSQ 100
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVD-----VLELRR-RVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 101 FLRVIPRISTLNVVIQPLLeRGM-SRQESEIRGGELLTHLNVPERLW-SLAPATFSGGEQQRINIARGFIGDYPILLLDE 178
Cdd:cd03260 89 KPNPFPGSIYDNVAYGLRL-HGIkLKEELDERVEEALRKAALWDEVKdRLHALGLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499404648 179 PTASLDAKNRLAVTQLIDDAKsKGCAVVGIFHDDEVRQHVADR 221
Cdd:cd03260 168 PTSALDPISTAKIEELIAELK-KEYTIVIVTHNMQQAARVADR 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
25-225 |
8.66e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.16 E-value: 8.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVDIVN-ADARHVLEIRREtVGWVSQFLR 103
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQ--FDFSQkPSEKAIRLLRQK-VGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 104 VIPRIStlnvVIQPLLER-----GMSRQESEIRGGELLTHLnvpeRLWSLA---PATFSGGEQQRINIARGFIGDYPILL 175
Cdd:COG4161 93 LWPHLT----VMENLIEApckvlGLSKEQAREKAMKLLARL----RLTDKAdrfPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499404648 176 LDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:COG4161 165 FDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYM 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
28-225 |
8.76e-25 |
|
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: 98.48 E-value: 8.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 28 HDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADARHVLEIRRETVGWVSQFLRVIPR 107
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQ----DIAAMSRKELRELRRKKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 108 ISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLaPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKN 187
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKY-PDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499404648 188 RLAV-TQLIDDAKSKGCAVVGIFHD-DE-VRqhVADRLYSM 225
Cdd:cd03294 196 RREMqDELLRLQAELQKTIVFITHDlDEaLR--LGDRIAIM 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
26-222 |
1.26e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 97.58 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHiwVRHRERWVDIVNADARhvLEIRRETVGWVSQFLRVI 105
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGD--VIFNGQPMSKLSSAAK--AELRNQKLGFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 106 PRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSlAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDA 185
Cdd:PRK11629 100 PDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANH-RPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 499404648 186 KNRLAVTQLIDDA-KSKGCAVVGIFHDdevrQHVADRL 222
Cdd:PRK11629 179 RNADSIFQLLGELnRLQGTAFLVVTHD----LQLAKRM 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-225 |
1.32e-24 |
|
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: 97.76 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADa 84
Cdd:cd03295 1 IEFENVTKRY------GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE----DIREQD- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 rhVLEIRREtVGWVSQFLRVIPRISTL-NVVIQPLLErGMSRQESEIRGGELLTHLNVPERlwSLA---PATFSGGEQQR 160
Cdd:cd03295 70 --PVELRRK-IGYVIQQIGLFPHMTVEeNIALVPKLL-KWPKEKIRERADELLALVGLDPA--EFAdryPHELSGGQQQR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404648 161 INIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIM 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-225 |
1.50e-24 |
|
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: 101.21 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 4 QLRIENVDktfVLYNqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNAD 83
Cdd:TIGR02857 321 SLEFSGVS---VAYP--GRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG----VPLADAD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 84 ARHvleiRRETVGWVSQFLRVIPRISTLNVVI-QPLLERGMSRQESEIRG-GELLTHLnvPERLWSLA---PATFSGGEQ 158
Cdd:TIGR02857 391 ADS----WRDQIAWVPQHPFLFAGTIAENIRLaRPDASDAEIREALERAGlDEFVAAL--PQGLDTPIgegGAGLSGGQA 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 159 QRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAkSKGCAVVGIFHDDEVRqHVADRLYSM 225
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-221 |
1.54e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.86 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFVlynqqGTRlpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVDIvnada 84
Cdd:COG1129 5 LEMRGISKSFG-----GVK--ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEP--VRF----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRRETVGWVSQFLRVIPRISTL-NVVIQPLLERG--MSRQESEIRGGELLTHLNVPERLWSLApATFSGGEQQRI 161
Cdd:COG1129 71 RSPRDAQAAGIAIIHQELNLVPNLSVAeNIFLGREPRRGglIDWRAMRRRARELLARLGLDIDPDTPV-GDLSVAQQQLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404648 162 NIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD-DEVRQhVADR 221
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRlDEVFE-IADR 209
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
26-222 |
1.94e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.34 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVDIVNADARHVLeiRRETVGWVSQFLRVI 105
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQD--VATLDADALAQL--RREHFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 106 PRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLwSLAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDA 185
Cdd:PRK10535 99 SHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRV-EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 499404648 186 KNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHvADRL 222
Cdd:PRK10535 178 HSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERV 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-184 |
4.09e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 96.36 E-value: 4.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 7 IENVDKTFvlYNQQgtrlpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRhrerwvDIVNADARH 86
Cdd:PRK11264 6 VKNLVKKF--HGQT-----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG------DITIDTARS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 87 VLE----IR--RETVGWVSQFLRVIPRISTLNVVIQ-PLLERGMSRQESEIRGGELLTHLNV-------PERLwslapat 152
Cdd:PRK11264 73 LSQqkglIRqlRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLagketsyPRRL------- 145
|
170 180 190
....*....|....*....|....*....|..
gi 499404648 153 fSGGEQQRINIARGFIGDYPILLLDEPTASLD 184
Cdd:PRK11264 146 -SGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-225 |
4.42e-24 |
|
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: 94.03 E-value: 4.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqgTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVDIVN-AD 83
Cdd:cd03216 1 LELRGITKRF-------GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE--VSFASpRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 84 ARhvleirRETVGWVSQFlrvipristlnvviqpllergmsrqeseirggellthlnvperlwslapatfSGGEQQRINI 163
Cdd:cd03216 72 AR------RAGIAMVYQL----------------------------------------------------SVGERQMVEI 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499404648 164 ARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD-DEVRQhVADRLYSM 225
Cdd:cd03216 94 ARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRlDEVFE-IADRVTVL 155
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-225 |
6.40e-24 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 97.80 E-value: 6.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTFvlynQQGTRLpvfHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIV 80
Cdd:TIGR03265 1 SSPYLSIDNIRKRF----GAFTAL---KDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGR----DIT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 NadarhvLEIRRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVP--ERLWslaPATFSGGEQ 158
Cdd:TIGR03265 70 R------LPPQKRDYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPgsERKY---PGQLSGGQQ 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404648 159 QRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:TIGR03265 141 QRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVM 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-225 |
9.51e-24 |
|
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: 95.10 E-value: 9.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqgTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWvrhrerwvdIVNADA 84
Cdd:cd03296 3 IEVRNVSKRF-------GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIL---------FGGEDA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVlEIRRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQ--ESEIRG--GELLTHLNVpERLWSLAPATFSGGEQQR 160
Cdd:cd03296 67 TDV-PVQERNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERppEAEIRAkvHELLKLVQL-DWLADRYPAQLSGGQRQR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499404648 161 INIARGFIGDYPILLLDEPTASLDAKNRLA----VTQLIDDAkskGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDAKVRKElrrwLRRLHDEL---HVTTVFVTHDQEEALEVADRVVVM 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
29-226 |
1.11e-23 |
|
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: 94.25 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhrerwvdIVNADARHVLEiRRETVGWVSQFLRvipRI 108
Cdd:cd03226 18 DLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSI----------LLNGKPIKAKE-RRKSIGYVMQDVD---YQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 109 STLNVVIQPLLERGMSRQESEIRGGELLTHLNvperLWSLA---PATFSGGEQQRINIARGFIGDYPILLLDEPTASLDA 185
Cdd:cd03226 84 LFTDSVREELLLGLKELDAGNEQAETVLKDLD----LYALKerhPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499404648 186 KNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSMA 226
Cdd:cd03226 160 KNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
5-223 |
2.14e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.57 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFVLYNQQGTRlpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhreRWVDIVNADA 84
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASR--ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV------TVGDIVVSST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIR--RETVGWVSQF--LRVIPRISTLNVVIQPLlERGMSRQESEIRGGELLTHLNVPERLWSLAPATFSGGEQQR 160
Cdd:PRK13643 74 SKQKEIKpvRKKVGVVFQFpeSQLFEETVLKDVAFGPQ-NFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499404648 161 INIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFH-DDEVRQHvADRLY 223
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHlMDDVADY-ADYVY 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-226 |
4.89e-23 |
|
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: 92.70 E-value: 4.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADA 84
Cdd:cd03301 1 VELENVTKRF------GNV-TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR----DVTDLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHvleirrETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVpERLWSLAPATFSGGEQQRINIA 164
Cdd:cd03301 70 KD------RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQI-EHLLDRKPKQLSGGQRQRVALG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAV-TQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSMA 226
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQMrAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMN 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-225 |
1.20e-22 |
|
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: 92.40 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKT---FVLYNqqgtrlpvfhdINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVN 81
Cdd:cd03299 1 LKVENLSKDwkeFKLKN-----------VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG----KDITN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 82 adarhvLEIRRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVpERLWSLAPATFSGGEQQRI 161
Cdd:cd03299 66 ------LPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRV 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 162 NIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIM 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-220 |
1.59e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 7 IENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRhrerwvdivnadarh 86
Cdd:COG0488 1 LENLSKSF------GGR-PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP--------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 87 vleiRRETVGWVSQFLRVIPRISTLNVVIQPLLERG-------------------MSRQ---------------ESEIRg 132
Cdd:COG0488 59 ----KGLRIGYLPQEPPLDDDLTVLDTVLDGDAELRaleaeleeleaklaepdedLERLaelqeefealggweaEARAE- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 133 gELLTHLNVPERLWSLAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKnrlAVTQLIDDAKSKGCAVVGIFHD- 211
Cdd:COG0488 134 -EILSGLGFPEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE---SIEWLEEFLKNYPGTVLVVSHDr 209
|
250
....*....|..
gi 499404648 212 ---DEVRQHVAD 220
Cdd:COG0488 210 yflDRVATRILE 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-225 |
2.21e-22 |
|
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: 91.53 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTfvlYNQQgtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNada 84
Cdd:cd03300 1 IELENVSKF---YGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK----DITN--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 rhvLEIRRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLtHLNVPERLWSLAPATFSGGEQQRINIA 164
Cdd:cd03300 67 ---LPPHKRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEAL-DLVQLEGYANRKPSQLSGGQQQRVAIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDLKLRKDMQLELKRlQKELGITFVFVTHDQEEALTMSDRIAVM 204
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
25-222 |
2.96e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.76 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRE--RWvdivnadARHVLEIRREtvgwvsqfl 102
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPlaDW-------SPAELARRRA--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 103 rVIPRISTLN-------VViqpllerGMSR---QESEIRGGEL---------LTHLNvpERLWslapATFSGGEQQRINI 163
Cdd:PRK13548 80 -VLPQHSSLSfpftveeVV-------AMGRaphGLSRAEDDALvaaalaqvdLAHLA--GRDY----PQLSGGEQQRVQL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404648 164 AR------GFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADRL 222
Cdd:PRK13548 146 ARvlaqlwEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQlAHERGLAVIVVLHDLNLAARYADRI 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-222 |
3.47e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 92.90 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVDIvnadA 84
Cdd:COG1118 3 IEVRNISKRF------GSF-TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD--LFT----N 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEiRRetVGWVSQ----------------FLRVIPRistlnvviqpllergmSRQESEIRGGELLTHLNVPErlwsL 148
Cdd:COG1118 70 LPPRE-RR--VGFVFQhyalfphmtvaeniafGLRVRPP----------------SKAEIRARVEELLELVQLEG----L 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 149 A---PATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAV----TQLIDDAKskgcaVVGIF--HD-DEVRQhV 218
Cdd:COG1118 127 AdryPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELrrwlRRLHDELG-----GTTVFvtHDqEEALE-L 200
|
....
gi 499404648 219 ADRL 222
Cdd:COG1118 201 ADRV 204
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-225 |
8.37e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 90.84 E-value: 8.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDktfvlYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiv 80
Cdd:PRK13635 2 KEEIIRVEHIS-----FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 nADARHVLEIRREtVGWV-----SQFLRvipriSTLNVVIQPLLE-RGMSRQESEIRGGELLTHLNVPERLwSLAPATFS 154
Cdd:PRK13635 71 -LSEETVWDVRRQ-VGMVfqnpdNQFVG-----ATVQDDVAFGLEnIGVPREEMVERVDQALRQVGMEDFL-NREPHRLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499404648 155 GGEQQRINIArGFIGDYP-ILLLDEPTASLDAKNRLAVTQLIDDAK-SKGCAVVGIFHD-DEVRQhvADRLYSM 225
Cdd:PRK13635 143 GGQKQRVAIA-GVLALQPdIIILDEATSMLDPRGRREVLETVRQLKeQKGITVLSITHDlDEAAQ--ADRVIVM 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-225 |
1.01e-21 |
|
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: 89.80 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqgTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADA 84
Cdd:cd03219 1 LEVRGLTKRF-------GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGE----DITGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RhvlEIRRETVGWVSQFLRVIPRISTL-NVVI-------QPLLERGMSRQESEIRG--GELLTHLNVPERLWSLApATFS 154
Cdd:cd03219 70 H---EIARLGIGRTFQIPRLFPELTVLeNVMVaaqartgSGLLLARARREEREAREraEELLERVGLADLADRPA-GELS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404648 155 GGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVL 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
25-226 |
1.57e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 89.79 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWV--RHRERWvdivnadARHVLEIRREtvgwvsqfl 102
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLngRPLAAW-------SPWELARRRA--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 103 rVIPRISTLN-------VVIQPLLERGMSRQESEIRGGELLTHLNVP---ERLWSlapaTFSGGEQQRINIAR------- 165
Cdd:COG4559 79 -VLPQHSSLAfpftveeVVALGRAPHGSSAAQDRQIVREALALVGLAhlaGRSYQ----TLSGGEQQRVQLARvlaqlwe 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404648 166 GFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSMA 226
Cdd:COG4559 154 PVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLH 214
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
7-225 |
1.66e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.19 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 7 IENVDKTFvlynQQGTRL--PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERWVDIVNADA 84
Cdd:PRK13649 5 LQNVSYTY----QAGTPFegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVleirRETVGWVSQF--LRVIPRISTLNVVIQPlLERGMSRQESEIRGGELLTHLNVPERLWSLAPATFSGGEQQRIN 162
Cdd:PRK13649 81 KQI----RKKVGLVFQFpeSQLFEETVLKDVAFGP-QNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 163 IArGFIGDYP-ILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFH-DDEVRQHvADRLYSM 225
Cdd:PRK13649 156 IA-GILAMEPkILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlMDDVANY-ADFVYVL 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-225 |
2.51e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 89.36 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFVLYNQQGTR--LPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhRERWVDIVNA 82
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSGKHqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV----SWRGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 83 DARHVLEIRReTVGWVSQ--FLRVIPRISTLNVVIQPLLE-RGMSRQESEIRGGELLTHLNVPERLWSLAPATFSGGEQQ 159
Cdd:PRK10419 80 NRAQRKAFRR-DIQMVFQdsISAVNPRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 160 RINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVM 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-221 |
4.72e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 89.75 E-value: 4.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlyNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNADA 84
Cdd:COG1135 2 IELENLSKTF---PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDG----VDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRREtVGWVSQ-F-LrviprISTLNV---VIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLaPATFSGGEQQ 159
Cdd:COG1135 75 RELRAARRK-IGMIFQhFnL-----LSSRTVaenVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAY-PSQLSGGQKQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499404648 160 RINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADR 221
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDR 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
29-225 |
7.43e-21 |
|
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: 89.40 E-value: 7.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErWVDivnADARHVLEIRRETVGWVSQFLRVIPRI 108
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRT-LFD---SRKGIFLPPEKRRIGYVFQEARLFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 109 StlnvvIQPLLERGMSR---QESEIRGGELLTHLNVpERLWSLAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDA 185
Cdd:TIGR02142 91 S-----VRGNLRYGMKRarpSERRISFERVIELLGI-GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499404648 186 KNRLAVTQLIDD-AKSKGCAVVGIFHD-DEVrQHVADRLYSM 225
Cdd:TIGR02142 165 PRKYEILPYLERlHAEFGIPILYVSHSlQEV-LRLADRVVVL 205
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-210 |
1.23e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 87.38 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTFvlynQQGTRLpvfHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPD---GGHIwvrhrERWV 77
Cdd:PRK09984 1 MQTIIRVEKLAKTF----NQHQAL---HAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHI-----ELLG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 78 DIVNADARHVLEIR--RETVGWVSQFLRVIPRISTL-NVVIQPL--------LERGMSRQESEiRGGELLTHLNVPERLW 146
Cdd:PRK09984 69 RTVQREGRLARDIRksRANTGYIFQQFNLVNRLSVLeNVLIGALgstpfwrtCFSWFTREQKQ-RALQALTRVGMVHFAH 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 147 SLApATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKN-RLAVTQLIDDAKSKGCAVVGIFH 210
Cdd:PRK09984 148 QRV-STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESaRIVMDTLRDINQNDGITVVVTLH 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-195 |
1.46e-20 |
|
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: 86.09 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqgTRLPVFHDINLSVKCGeCVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdivnaDA 84
Cdd:cd03264 1 LQLENLTKRY-------GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD--------VL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRReTVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLwSLAPATFSGGEQQRINIA 164
Cdd:cd03264 65 KQPQKLRR-RIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIA 142
|
170 180 190
....*....|....*....|....*....|.
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQLI 195
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLL 173
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-186 |
1.56e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 88.59 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 3 TQLRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrhrerwvdivna 82
Cdd:COG3839 2 ASLELENVSKSY------GGV-EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 83 DARHV--LEIRRETVGWVSQFLRVIPrisTLNV---VIQPLLERGMSRQESEIRGGELLTHLNVPE---RLwslaPATFS 154
Cdd:COG3839 63 GGRDVtdLPPKDRNIAMVFQSYALYP---HMTVyenIAFPLKLRKVPKAEIDRRVREAAELLGLEDlldRK----PKQLS 135
|
170 180 190
....*....|....*....|....*....|..
gi 499404648 155 GGEQQRINIARGFIGDYPILLLDEPTASLDAK 186
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
25-214 |
1.60e-20 |
|
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: 85.06 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWvrhrerwvdIVNADARHVLEIRRETVGWVSQflrv 104
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT---------LDGVPVSDLEKALSSLISVLNQ---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 ipristlnvviQPLLERGMSRQeseirggellthlNVPERlwslapatFSGGEQQRINIARGFIGDYPILLLDEPTASLD 184
Cdd:cd03247 83 -----------RPYLFDTTLRN-------------NLGRR--------FSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190
....*....|....*....|....*....|....*.
gi 499404648 185 AKNRLAVTQLI-DDAKSKGCAVV-----GIFHDDEV 214
Cdd:cd03247 131 PITERQLLSLIfEVLKDKTLIWIthhltGIEHMDKI 166
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
29-222 |
1.91e-20 |
|
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: 85.88 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNaDARHVleirRETVGWVSQFLRVIPRI 108
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG----HDVVR-EPREV----RRRIGIVFQDLSVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 109 S-TLNVVIQPLLErGMSRQESEIRGGELLTHLNVPERLWSLApATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKN 187
Cdd:cd03265 89 TgWENLYIHARLY-GVPGAERRERIDELLDFVGLLEAADRLV-KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 499404648 188 RLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADRL 222
Cdd:cd03265 167 RAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRV 202
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-184 |
2.30e-20 |
|
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: 85.72 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 6 RIENVDKTFVLYNQQGtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhrerWVDIVNADAR 85
Cdd:cd03245 2 RIEFRNVSFSYPNQEI---PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV-------LLDGTDIRQL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 86 HVLEIRREtVGWVSQ------------------------FLRVIpRISTLNVVIQpLLERGMSRQESEirGGELLthlnv 141
Cdd:cd03245 72 DPADLRRN-IGYVPQdvtlfygtlrdnitlgapladderILRAA-ELAGVTDFVN-KHPNGLDLQIGE--RGRGL----- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499404648 142 perlwslapatfSGGEQQRINIARGFIGDYPILLLDEPTASLD 184
Cdd:cd03245 142 ------------SGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
26-219 |
3.19e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.18 E-value: 3.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVDIV-NADA------RHVLEIRRETVGWV 98
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQT--INLVrDKDGqlkvadKNQLRLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 99 SQFLRVIPRISTL-NVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLAPATFSGGEQQRINIARGFIGDYPILLLD 177
Cdd:PRK10619 98 FQHFNLWSHMTVLeNVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499404648 178 EPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVA 219
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVS 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-213 |
3.66e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.07 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 3 TQLRIENVDktfVLYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVDIVNA 82
Cdd:COG4525 2 SMLTVRHVS---VRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP--VTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 83 DaRHVleirretvgwVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPE----RLWSLapatfSGGEQ 158
Cdd:COG4525 77 D-RGV----------VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADfarrRIWQL-----SGGMR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499404648 159 QRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDE 213
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVE 196
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-211 |
4.83e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.93 E-value: 4.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvLYNQQGTRLPVFHdinlsVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADA 84
Cdd:PRK10908 2 IRFEHVSKAY-LGGRQALQGVTFH-----MRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH----DITRLKN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRREtVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLaPATFSGGEQQRINIA 164
Cdd:PRK10908 72 REVPFLRRQ-IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNF-PIQLSGGEQQRVGIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD 211
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHD 196
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-225 |
4.91e-20 |
|
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: 84.79 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDktfVLYnqqgTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADA 84
Cdd:cd03224 1 LEVENLN---AGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGR----DITGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RhvlEIRRETVGWVSQFLRVIPRIS---TLNVVIQPLLERGMSRQESEIRggELLTHLnvPERLWSLApATFSGGEQQRI 161
Cdd:cd03224 70 H---ERARAGIGYVPEGRRIFPELTveeNLLLGAYARRRAKRKARLERVY--ELFPRL--KERRKQLA-GTLSGGEQQML 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499404648 162 NIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVL 205
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
25-217 |
9.60e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.44 E-value: 9.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERwvdivnadarhvleirretVGWVSQFLRV 104
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGAR-------------------VAYVPQRSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 IPrisTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLAPATF--------SGGEQQRINIARGFIGDYPILLL 176
Cdd:NF040873 67 PD---SLPLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLagrqlgelSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499404648 177 DEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD-DEVRQH 217
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGATVVVVTHDlELVRRA 185
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-225 |
1.15e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 86.29 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 7 IENVDKTFvlynqqgTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHI--------WVRHRERWVD 78
Cdd:PRK10851 5 IANIKKSF-------GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrfhgtdvsRLHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 79 IVnadARHVLEIRRETVGWVSQF-LRVIPRISTLNVVIqplLERGMSRQESEIRggelLTHLnvPERLwslaPATFSGGE 157
Cdd:PRK10851 78 FV---FQHYALFRHMTVFDNIAFgLTVLPRRERPNAAA---IKAKVTQLLEMVQ----LAHL--ADRY----PAQLSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404648 158 QQRINIARGFIGDYPILLLDEPTASLDAKNRLA----VTQLIDDAKSKGcavVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK10851 142 KQRVALARALAVEPQILLLDEPFGALDAQVRKElrrwLRQLHEELKFTS---VFVTHDQEEAMEVADRVVVM 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
29-222 |
1.78e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.88 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhrerwvDIV------NADARHVLEIRREtVGWVSQFl 102
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI---------TIAgyhitpETGNKNLKKLRKK-VSLVFQF- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 103 rviPRISTL-NVVIQPL----LERGMSRQESEIRGGELLTHLNVPERLWSLAPATFSGGEQQRINIArGFIGDYP-ILLL 176
Cdd:PRK13641 94 ---PEAQLFeNTVLKDVefgpKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIA-GVMAYEPeILCL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499404648 177 DEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD-DEVRQHVADRL 222
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNmDDVAEYADDVL 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-221 |
1.97e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.23 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTF--VLYNQqgtrlpvfhDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVD 78
Cdd:COG3845 2 MPPALELRGITKRFggVVAND---------DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP--VR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 79 IVN-ADArhvleiRRETVGWVSQFLRVIPRISTL-NVVI----QPLLERGMSRQESEIRggELL--THLNV-PERL-WSL 148
Cdd:COG3845 71 IRSpRDA------IALGIGMVHQHFMLVPNLTVAeNIVLglepTKGGRLDRKAARARIR--ELSerYGLDVdPDAKvEDL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404648 149 apatfSGGEQQRINIARGFIGDYPILLLDEPTASL--DAKNRLAVTqlIDDAKSKGCAVVGIFHD-DEVRQhVADR 221
Cdd:COG3845 143 -----SVGEQQRVEILKALYRGARILILDEPTAVLtpQEADELFEI--LRRLAAEGKSIIFITHKlREVMA-IADR 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
29-221 |
3.30e-19 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 84.40 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADARHVLEIRREtvgwvsqfLRVI--- 105
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ----DITGLSGRELRPLRRR--------MQMVfqd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 106 ------PRISTLNVVIQPLLERGM-SRQESEIRGGELLT-------HLNvpeRLwslaPATFSGGEQQRINIARGFIGDY 171
Cdd:COG4608 104 pyaslnPRMTVGDIIAEPLRIHGLaSKAERRERVAELLElvglrpeHAD---RY----PHEFSGGQRQRIGIARALALNP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499404648 172 PILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADR 221
Cdd:COG4608 177 KLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDR 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
25-211 |
6.13e-19 |
|
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: 85.10 E-value: 6.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrhrerwvDIVNADARHVLEIRReTVGWVSQFLRV 104
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTL-------DGVPVSSLDQDEVRR-RVSVCAQDAHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 IPriSTL--NVviqpLLERG------MSRQESEIRGGELLTHLnvPERLWSL---APATFSGGEQQRINIARGFIGDYPI 173
Cdd:TIGR02868 421 FD--TTVreNL----RLARPdatdeeLWAALERVGLADWLRAL--PDGLDTVlgeGGARLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*...
gi 499404648 174 LLLDEPTASLDAKNRLAVTQLIDDAKSkGCAVVGIFHD 211
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHH 529
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-226 |
6.56e-19 |
|
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: 82.03 E-value: 6.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlyNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNADA 84
Cdd:cd03266 2 ITADALTKRF---RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG----FDVVKEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 rhvlEIRREtVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLApATFSGGEQQRINIA 164
Cdd:cd03266 75 ----EARRR-LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRV-GGFSTGMRQKVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSMA 226
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLH 210
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-226 |
7.55e-19 |
|
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: 80.94 E-value: 7.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdivnADARHVLEIRRETVGWVSqflrvi 105
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP-------VTRRSPRDAIRAGIAYVP------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 106 pristlnvviqpllergmsrqesEIRGGE-LLTHLNVPERLwsLAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLD 184
Cdd:cd03215 82 -----------------------EDRKREgLVLDLSVAENI--ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499404648 185 AKNRLAVTQLIDDAKSKGCAVVGIFHD-DEVRqHVADRLYSMA 226
Cdd:cd03215 137 VGAKAEIYRLIRELADAGKAVLLISSElDELL-GLCDRILVMY 178
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
1.29e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 82.38 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDtqLRIENVDKTFvlynQQGT---RLPVFhDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwv 77
Cdd:PRK13634 1 MD--ITFQKVEHRY----QYKTpfeRRALY-DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERV--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 78 dIVNADARHVLEIRRETVGWVSQFlrviPRISTLNVVIQ------PLlERGMSRQESEIRGGELLTHLNVPERLWSLAPA 151
Cdd:PRK13634 71 -ITAGKKNKKLKPLRKKVGIVFQF----PEHQLFEETVEkdicfgPM-NFGVSEEDAKQKAREMIELVGLPEELLARSPF 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404648 152 TFSGGEQQRINIArGFIGDYP-ILLLDEPTASLDAKNRLAVTQLIDDA-KSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK13634 145 ELSGGQMRRVAIA-GVLAMEPeVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVM 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-225 |
1.35e-18 |
|
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: 80.80 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 23 RLPvFHDINLSVKC-GECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErWVDivnADARHVLEIRRETVGWVSQF 101
Cdd:cd03297 9 RLP-DFTLKIDFDLnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV-LFD---SRKKINLPPQQRKIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 102 LRVIPRIStlnvVIQPLL--ERGMSRQESEIRGGELLTHLNVpERLWSLAPATFSGGEQQRINIARGFIGDYPILLLDEP 179
Cdd:cd03297 84 YALFPHLN----VRENLAfgLKRKRNREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499404648 180 TASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:cd03297 159 FSALDRALRLQLLPELKQiKKNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
30-226 |
1.50e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.05 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 30 INLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiVNADARHVLEIRReTVGWVSQ------Flr 103
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP-----IKYDKKSLLEVRK-TVGIVFQnpddqlF-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 104 vIPRISTlNVVIQPlLERGMSRQESEIRGGELLTHLNVpERLWSLAPATFSGGEQQRINIArGFIGDYP-ILLLDEPTAS 182
Cdd:PRK13639 93 -APTVEE-DVAFGP-LNLGLSKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIA-GILAMKPeIIVLDEPTSG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499404648 183 LDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSMA 226
Cdd:PRK13639 168 LDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMS 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
25-187 |
2.46e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 83.29 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIvnadaRHV-LEIRRETVGWVSQ--F 101
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG----VDI-----RDLtLESLRRQIGVVPQdtF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 102 L-------------------RVIP--RISTLNVVIQpLLERGMsrqESEI--RGGELlthlnvperlwslapatfSGGEQ 158
Cdd:COG1132 425 LfsgtirenirygrpdatdeEVEEaaKAAQAHEFIE-ALPDGY---DTVVgeRGVNL------------------SGGQR 482
|
170 180
....*....|....*....|....*....
gi 499404648 159 QRINIARGFIGDYPILLLDEPTASLDAKN 187
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTET 511
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-225 |
2.66e-18 |
|
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: 83.20 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQ--LRIENVDKTFvlyNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKS----TLLRSLYGNYRPDGGHIWVRHRe 74
Cdd:COG4172 1 MMSMplLSVEDLSVAF---GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQ- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 75 rwvDIVNADARHVLEIRRETVGWVSQflrvIPrISTLNvviqPL------------LERGMSRQESEIRGGELLTHLNVP 142
Cdd:COG4172 77 ---DLLGLSERELRRIRGNRIAMIFQ----EP-MTSLN----PLhtigkqiaevlrLHRGLSGAAARARALELLERVGIP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 143 E---RLWSLaPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDaknrlaVT------QLIDDAKSK-GCAVVGIFHDD 212
Cdd:COG4172 145 DperRLDAY-PHQLSGGQRQRVMIAMALANEPDLLIADEPTTALD------VTvqaqilDLLKDLQRElGMALLLITHDL 217
|
250
....*....|...
gi 499404648 213 EVRQHVADRLYSM 225
Cdd:COG4172 218 GVVRRFADRVAVM 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
27-225 |
2.88e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 80.74 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 27 FHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRE-RWVDIV---NADARHVLeirRETVGWVSQF- 101
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgQLRDLYalsEAERRRLL---RTEWGFVHQHp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 102 ---LRviPRISTLNVVIQPLLERGMsRQESEIR--GGELLTHLNVPERLWSLAPATFSGGEQQRINIARGFIGDYPILLL 176
Cdd:PRK11701 99 rdgLR--MQVSAGGNIGERLMAVGA-RHYGDIRatAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499404648 177 DEPTASLD--AKNRL--AVTQLIDDAkskGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK11701 176 DEPTGGLDvsVQARLldLLRGLVREL---GLAVVIVTHDLAVARLLAHRLLVM 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
25-211 |
3.06e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.58 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADARHVleirretvgwvSQFLRV 104
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGD----DVEALSARAA-----------SRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 IPRISTL--NVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLAPATF--------SGGEQQRINIARGFIGDYPIL 174
Cdd:PRK09536 82 VPQDTSLsfEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFadrpvtslSGGERQRVLLARALAQATPVL 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 499404648 175 LLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD 211
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHD 198
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
5-210 |
3.42e-18 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 82.78 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDktfvlYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhRERWVDIVNADA 84
Cdd:TIGR01842 317 LSVENVT-----IVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV----RLDGADLKQWDR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVleirRETVGWVSQFLRVIPriSTLNVVIQPLLERGMSRQ--ESEIRGG--ELLthLNVPERLWS-LAP--ATFSGGE 157
Cdd:TIGR01842 388 ETF----GKHIGYLPQDVELFP--GTVAENIARFGENADPEKiiEAAKLAGvhELI--LRLPDGYDTvIGPggATLSGGQ 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499404648 158 QQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFH 210
Cdd:TIGR01842 460 RQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITH 512
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-210 |
3.98e-18 |
|
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: 80.28 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNADARHVleirRETVGWVSQ---- 100
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG----VDIRDLNLRWL----RSQIGLVSQepvl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 101 FLRVIprisTLNVviqpLLERGMSRQESEIRGGELLTHLNV----PERLWSLAPA---TFSGGEQQRINIARGFIGDYPI 173
Cdd:cd03249 89 FDGTI----AENI----RYGKPDATDEEVEEAAKKANIHDFimslPDGYDTLVGErgsQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 499404648 174 LLLDEPTASLDAKNRLAVTQLIDDAKsKGCAVVGIFH 210
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAH 196
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-183 |
4.35e-18 |
|
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: 80.03 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDktfVLYNQqgtrLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADA 84
Cdd:COG0410 4 LEVENLH---AGYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGE----DITGLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RhvlEIRRETVGWVSQFLRVIPRISTL-NVVIQPLLERGMSRQESEIrggELLTHL--NVPERLWSLApATFSGGEQQRI 161
Cdd:COG0410 73 H---RIARLGIGYVPEGRRIFPSLTVEeNLLLGAYARRDRAEVRADL---ERVYELfpRLKERRRQRA-GTLSGGEQQML 145
|
170 180
....*....|....*....|..
gi 499404648 162 NIARGFIGDYPILLLDEPTASL 183
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGL 167
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
25-186 |
5.83e-18 |
|
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: 79.58 E-value: 5.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiVNADARHVLeirRETVGWVSQFLRV 104
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGID-----IRDISRKSL---RSMIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 IPRISTLNVviqpLLERGMSRQESEIRGGELLTHLNVPERL-----WSLAPA--TFSGGEQQRINIARGFIGDYPILLLD 177
Cdd:cd03254 89 FSGTIMENI----RLGRPNATDEEVIEAAKEAGAHDFIMKLpngydTVLGENggNLSQGERQLLAIARAMLRDPKILILD 164
|
....*....
gi 499404648 178 EPTASLDAK 186
Cdd:cd03254 165 EATSNIDTE 173
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
26-211 |
6.31e-18 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 78.62 E-value: 6.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiVNADARHVLEIRReTVGWVSQ----- 100
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEP-----LDYSRKGLLERRQ-RVGLVFQdpddq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 101 -FlrvIPRISTlNVVIQPLlERGMSRQESEIRGGELLTHLNVpERLWSLAPATFSGGEQQRINIARGFIGDYPILLLDEP 179
Cdd:TIGR01166 81 lF---AADVDQ-DVAFGPL-NLGLSEAEVERRVREALTAVGA-SGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 499404648 180 TASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD 211
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-225 |
7.21e-18 |
|
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: 77.10 E-value: 7.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrhrerwvdivnada 84
Cdd:cd03221 1 IELENLSKTY------GGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 rhvleIRRETVGWVSQFlrvipristlnvviqpllergmsrqeseirggellthlnvperlwslapatfSGGEQQRINIA 164
Cdd:cd03221 60 -----GSTVKIGYFEQL----------------------------------------------------SGGEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKnrlAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLE---SIEALEEALKEYPGTVILVSHDRYFLDQVATKIIEL 140
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-221 |
7.66e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.00 E-value: 7.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 6 RIENVDKTFvlynQQGTR-LPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNADA 84
Cdd:PRK11153 3 ELKNISKVF----PQGGRtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDG----QDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRREtVGWVSQFLRViprISTLNV---VIQPLLERGMSRQESEIRGGELLThlnvperLWSLA------PATFSG 155
Cdd:PRK11153 75 KELRKARRQ-IGMIFQHFNL---LSSRTVfdnVALPLELAGTPKAEIKARVTELLE-------LVGLSdkadryPAQLSG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 156 GEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADR 221
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDR 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-221 |
9.55e-18 |
|
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: 81.41 E-value: 9.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqgTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYrPDG---GHIWVRHRErwvdivn 81
Cdd:TIGR02633 2 LEMKGIVKTF-------GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSP------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 82 ADARHVLEIRRETVGWVSQFLRVIPRISTL-NVVI-QPLLERG--MSRQESEIRGGELLTHLNVPERLWSLAPATFSGGE 157
Cdd:TIGR02633 67 LKASNIRDTERAGIVIIHQELTLVPELSVAeNIFLgNEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 158 QQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD-DEVR------------QHVADR 221
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKlNEVKavcdticvirdgQHVATK 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-221 |
9.58e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.34 E-value: 9.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 3 TQLRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWvrhrerwvdivnA 82
Cdd:PRK11247 11 TPLLLNAVSKRY------GER-TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL------------A 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 83 DARHVLEIRRETvGWVSQFLRVIPRISTLNVVIQPLleRGMSRQESEirggELLTHLNVPERL--WslaPATFSGGEQQR 160
Cdd:PRK11247 72 GTAPLAEAREDT-RLMFQDARLLPWKKVIDNVGLGL--KGQWRDAAL----QALAAVGLADRAneW---PAALSGGQKQR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404648 161 INIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDA-KSKGCAVVGIFHDDEVRQHVADR 221
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADR 203
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-217 |
1.05e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.39 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 2 DTQLRIENVDktfvLYNQQGTRLpvFHDINLSVKCGECVALHGHSGTGKSTLLRSLYG--NY------RPDGGHiwvrhr 73
Cdd:COG4178 360 DGALALEDLT----LRTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwPYgsgriaRPAGAR------ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 74 erwvdivnadarhVLeirretvgWVSQflRV-IPRISTLNVVIQPLLERGMSRQE-----SEIRGGELLTHLNVpERLWS 147
Cdd:COG4178 428 -------------VL--------FLPQ--RPyLPLGTLREALLYPATAEAFSDAElrealEAVGLGHLAERLDE-EADWD 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 148 lapATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAkSKGCAVVGIFHDDEVRQH 217
Cdd:COG4178 484 ---QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE-LPGTTVISVGHRSTLAAF 549
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-223 |
1.08e-17 |
|
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: 78.74 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNAda 84
Cdd:cd03218 1 LRAENLSKRY------GKR-KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ----DITKL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 rHVLEIRRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLApATFSGGEQQRINIA 164
Cdd:cd03218 68 -PMHKRARLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKA-SSLSGGERRRVEIA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGcavVGIF-HDDEVRQ--HVADRLY 223
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRG---IGVLiTDHNVREtlSITDRAY 204
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
5-201 |
1.33e-17 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 78.88 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDktfVLYNQQgtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSL------YGNYRPDGgHIWVRHRErwvd 78
Cdd:TIGR00972 2 IEIENLN---LFYGEK----EALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmndlVPGVRIEG-KVLFDGQD---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 79 iVNADARHVLEIRREtVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHL----NVPERLwSLAPATFS 154
Cdd:TIGR00972 70 -IYDKKIDVVELRRR-VGMVFQKPNPFPMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAalwdEVKDRL-HDSALGLS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499404648 155 GGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK 201
Cdd:TIGR00972 147 GGQQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK 193
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-211 |
1.99e-17 |
|
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: 80.56 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 4 QLRIENVdkTFVLynqQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHiwVRhrerwVDivNAD 83
Cdd:COG4618 330 RLSVENL--TVVP---PGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGS--VR-----LD--GAD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 84 ARHvleIRRET----VGWVSQflRV----------IPRISTLN---VV-----------IQpLLERGMsrqESEI-RGGE 134
Cdd:COG4618 396 LSQ---WDREElgrhIGYLPQ--DVelfdgtiaenIARFGDADpekVVaaaklagvhemIL-RLPDGY---DTRIgEGGA 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 135 LLthlnvperlwslapatfSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD 211
Cdd:COG4618 467 RL-----------------SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHR 526
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-225 |
2.26e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.98 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 18 NQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRhrerwvDIVNADARHVLEIRRETvGW 97
Cdd:PRK13633 17 NEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVD------GLDTSDEENLWDIRNKA-GM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 98 VSQFL--RVIPRISTLNVVIQPllER-GMSRQESEIRGGELLTHLNVPErLWSLAPATFSGGEQQRINIArGFIGDYP-I 173
Cdd:PRK13633 90 VFQNPdnQIVATIVEEDVAFGP--ENlGIPPEEIRERVDESLKKVGMYE-YRRHAPHLLSGGQKQRVAIA-GILAMRPeC 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499404648 174 LLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFH-DDEVRQhvADRLYSM 225
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHyMEEAVE--ADRIIVM 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-225 |
4.68e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.17 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVdkTFVlYNQqGTrlP----VFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIV 80
Cdd:PRK13637 3 IKIENL--THI-YME-GT--PfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG----VDIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 NADARhVLEIRREtVGWVSQFlrviPRISTLNVVIQPLLE-----RGMSRQESEIRGGELLTHLNVP-ERLWSLAPATFS 154
Cdd:PRK13637 73 DKKVK-LSDIRKK-VGLVFQY----PEYQLFEETIEKDIAfgpinLGLSEEEIENRVKRAMNIVGLDyEDYKDKSPFELS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499404648 155 GGEQQRINIArGFIGDYP-ILLLDEPTASLDAKNRLAVTQLIDDA-KSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK13637 147 GGQKRRVAIA-GVVAMEPkILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVM 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-222 |
6.25e-17 |
|
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: 76.49 E-value: 6.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHI------WVRHRERWVD 78
Cdd:cd03268 1 LKTNDLTKTY------GKK-RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItfdgksYQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 79 I----------VNADARHVLEIrretvgwvsqfLRVIPRIStlNVVIQPLLER-GMSRQEseirggelltHLNVperlws 147
Cdd:cd03268 74 IgalieapgfyPNLTARENLRL-----------LARLLGIR--KKRIDEVLDVvGLKDSA----------KKKV------ 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 148 lapATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRL 222
Cdd:cd03268 125 ---KGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRI 196
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-226 |
6.93e-17 |
|
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: 77.00 E-value: 6.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTFvlynqqGTrLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIV 80
Cdd:COG0411 1 SDPLLEVRGLTKRF------GG-LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGR----DIT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 NADARhvlEIRRETVGWVSQFLRVIPRISTL-NVVIQPLLERGMS------------RQESEIRG--GELLTHLNVpERL 145
Cdd:COG0411 70 GLPPH---RIARLGIARTFQNPRLFPELTVLeNVLVAAHARLGRGllaallrlprarREEREAREraEELLERVGL-ADR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 146 WSLAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHD-DEVRQhVADRLY 223
Cdd:COG0411 146 ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRlRDERGITILLIEHDmDLVMG-LADRIV 224
|
...
gi 499404648 224 SMA 226
Cdd:COG0411 225 VLD 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-211 |
7.03e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.53 E-value: 7.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 22 TRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHiwvrHRERWVDIVNADARHVLEIrRETVGWV--- 98
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNP----NSKITVDGITLTAKTVWDI-REKVGIVfqn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 99 --SQFL--------------RVIPRISTLNVVIQPLLERGMSR-QESEirggellthlnvperlwslaPATFSGGEQQRI 161
Cdd:PRK13640 93 pdNQFVgatvgddvafglenRAVPRPEMIKIVRDVLADVGMLDyIDSE--------------------PANLSGGQKQRV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499404648 162 NIArGFIGDYP-ILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHD 211
Cdd:PRK13640 153 AIA-GILAVEPkIIILDESTSMLDPAGKEQILKLIRKlKKKNNLTVISITHD 203
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
42-225 |
1.55e-16 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 77.15 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 42 LHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVDIVNADARHVleirretvGWVSQFLRVIPRISTLNVVIQPLLER 121
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGED--VTNVPPHLRHI--------NMVFQSYALFPHMTVEENVAFGLKMR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 122 GMSRQESEIRGGELLTHLNVPERLwSLAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK 201
Cdd:TIGR01187 71 KVPRAEIKPRVLEALRLVQLEEFA-DRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
|
170 180
....*....|....*....|....*
gi 499404648 202 -GCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:TIGR01187 150 lGITFVFVTHDQEEAMTMSDRIAIM 174
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
22-210 |
1.60e-16 |
|
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: 75.73 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 22 TRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWvrhrerwvdIVNADARHV-LEIRRETVGwvsq 100
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIL---------IDGQDIREVtLDSLRRAIG---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 101 flrVIPRISTL-NVVIQPLLERG-MSRQESEIRGGELLTHLN-------------VPERLWSLapatfSGGEQQRINIAR 165
Cdd:cd03253 79 ---VVPQDTVLfNDTIGYNIRYGrPDATDEEVIEAAKAAQIHdkimrfpdgydtiVGERGLKL-----SGGEKQRVAIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499404648 166 GFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAkSKGCAVVGIFH 210
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAH 194
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-196 |
1.97e-16 |
|
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: 77.83 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIvnadA 84
Cdd:TIGR02203 331 VEFRNVTFRY-----PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG----HDL----A 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLN-VPERLWSLA---PATFSGGEQQR 160
Cdd:TIGR02203 398 DYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDkLPLGLDTPIgenGVLLSGGQRQR 477
|
170 180 190
....*....|....*....|....*....|....*.
gi 499404648 161 INIARGFIGDYPILLLDEPTASLDAKNRLAVTQLID 196
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALE 513
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-186 |
2.17e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.56 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTfvlYNQQGtrLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiVNADA 84
Cdd:PRK11160 339 LTLNNVSFT---YPDQP--QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP-----IADYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLeirRETVGWVSQflRV--------------IPRIS--TLNVVIQPLlergmsrqeseirggELLTHLNVPERL--W 146
Cdd:PRK11160 409 EAAL---RQAISVVSQ--RVhlfsatlrdnlllaAPNASdeALIEVLQQV---------------GLEKLLEDDKGLnaW 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499404648 147 ------SLapatfSGGEQQRINIARGFIGDYPILLLDEPTASLDAK 186
Cdd:PRK11160 469 lgeggrQL-----SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE 509
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-225 |
2.19e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 76.67 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 19 QQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHI-WVRHrerwvDIVNADARHVLEIRREtvgw 97
Cdd:PRK15079 29 QPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLGK-----DLLGMKDDEWRAVRSD---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 98 vsqfLRVI---------PRISTLNVVIQPL--LERGMSRQESEIRGGELLTHLNVPERLWSLAPATFSGGEQQRINIARG 166
Cdd:PRK15079 100 ----IQMIfqdplaslnPRMTIGEIIAEPLrtYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 167 FIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK15079 176 LILEPKLIICDEPVSALDVSIQAQVVNLLQQlQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-201 |
2.54e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 75.46 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDktfVLYNQQgtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRS------LYGNYRPDgGHIWVRHRe 74
Cdd:COG1117 8 LEPKIEVRNLN---VYYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndLIPGARVE-GEILLDGE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 75 rwvDIVNADARhVLEIRREtVGWVSQ----FLRVIPRistlNVVIQPLLERGMSRQESEIRGGELLTHLN----VPERLW 146
Cdd:COG1117 79 ---DIYDPDVD-VVELRRR-VGMVFQkpnpFPKSIYD----NVAYGLRLHGIKSKSELDEIVEESLRKAAlwdeVKDRLK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 147 SLApATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK 201
Cdd:COG1117 150 KSA-LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD 203
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-218 |
3.26e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.59 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 19 QQGT--RLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNADARHVLEIRRETVG 96
Cdd:PRK13646 13 QKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDD----ITITHKTKDKYIRPVRKRIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 97 WVSQFlrviPRISTLNVVIQPLLERG-----MSRQESEIRGGELLTHLNVPERLWSLAPATFSGGEQQRINIARGFIGDY 171
Cdd:PRK13646 89 MVFQF----PESQLFEDTVEREIIFGpknfkMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499404648 172 PILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHD-DEVRQHV 218
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDmNEVARYA 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-210 |
3.68e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.95 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLR------SLYGNYRPDGghiwvrhrERWVDIVNADARHVLEIRREtVGWVS 99
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrliELYPEARVSG--------EVYLDGQDIFKMDVIELRRR-VQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 100 QFLRVIPRISTL-NVVIQPLLERGM-SRQESEIRGGELLTHLN----VPERLWslAPA-TFSGGEQQRINIARGFIGDYP 172
Cdd:PRK14247 89 QIPNPIPNLSIFeNVALGLKLNRLVkSKKELQERVRWALEKAQlwdeVKDRLD--APAgKLSGGQQQRLCIARALAFQPE 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 499404648 173 ILLLDEPTASLDAKNRLAVTQLIDDAKsKGCAVVGIFH 210
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLFLELK-KDMTIVLVTH 203
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-180 |
4.03e-16 |
|
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: 74.48 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDktfVLYNQQgtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhreRW--VDIvNA 82
Cdd:TIGR03410 1 LEVSNLN---VYYGQS----HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSI------RLdgEDI-TK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 83 DARHvlEIRRETVGWVSQFLRVIPRISTL-NvviqplLERGMSRQESEIRGgellthlnVPERLWSLAPATF-------- 153
Cdd:TIGR03410 67 LPPH--ERARAGIAYVPQGREIFPRLTVEeN------LLTGLAALPRRSRK--------IPDEIYELFPVLKemlgrrgg 130
|
170 180
....*....|....*....|....*....
gi 499404648 154 --SGGEQQRINIARGFIGDYPILLLDEPT 180
Cdd:TIGR03410 131 dlSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-220 |
4.05e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.89 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTFvlynqQGTRlpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYrPDG---GHIWVRHRERwv 77
Cdd:PRK13549 2 MEYLLEMKNITKTF-----GGVK--ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEEL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 78 divnaDARHVLEIRRETVGWVSQFLRVIPRISTL-NVVIQPLLERG--MSRQESEIRGGELLTHLNVperlwSLAPAT-- 152
Cdd:PRK13549 72 -----QASNIRDTERAGIAIIHQELALVKELSVLeNIFLGNEITPGgiMDYDAMYLRAQKLLAQLKL-----DINPATpv 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404648 153 --FSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD-DEVRQhVAD 220
Cdd:PRK13549 142 gnLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKlNEVKA-ISD 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-225 |
4.26e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.41 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlyNQQgtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRhrerwvdivNADA 84
Cdd:PRK11607 20 LEIRNLTKSF---DGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD---------GVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRReTVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPErLWSLAPATFSGGEQQRINIA 164
Cdd:PRK11607 84 SHVPPYQR-PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQE-FAKRKPHQLSGGQRQRVALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVT-QLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQlEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIM 223
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-188 |
4.48e-16 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 75.51 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 6 RIENVDKTFvlynqqGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLygN--YRPDGGHIWVRHRerwvDIVNAD 83
Cdd:COG1125 3 EFENVTKRY------PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMI--NrlIEPTSGRILIDGE----DIRDLD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 84 ARhvlEIRREtVGWVSQ----F--LRVIPristlNVVIQPLLeRGMSRQESEIRGGELLT--HLNvPERLWSLAPATFSG 155
Cdd:COG1125 71 PV---ELRRR-IGYVIQqiglFphMTVAE-----NIATVPRL-LGWDKERIRARVDELLElvGLD-PEEYRDRYPHELSG 139
|
170 180 190
....*....|....*....|....*....|...
gi 499404648 156 GEQQRINIARGFIGDYPILLLDEPTASLDAKNR 188
Cdd:COG1125 140 GQQQRVGVARALAADPPILLMDEPFGALDPITR 172
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-223 |
4.98e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvdivnada 84
Cdd:COG0488 316 LELEGLSKSY------GDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET----------- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 rhvLEIrretvGWVSQFLRVIPriSTLNVV--IQPLLERGmsrQESEIRGgeLLTHLN-VPERLWSLApATFSGGEQQRI 161
Cdd:COG0488 378 ---VKI-----GYFDQHQEELD--PDKTVLdeLRDGAPGG---TEQEVRG--YLGRFLfSGDDAFKPV-GVLSGGEKARL 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404648 162 NIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAksKGCAVVgIFHDDEVRQHVADRLY 223
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PGTVLL-VSHDRYFLDRVATRIL 500
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-222 |
6.48e-16 |
|
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: 73.47 E-value: 6.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFVLYNqqgtrlpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrhrerwvdivnaDA 84
Cdd:cd03269 1 LEVENVTKRFGRVT-------ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF------------DG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERlWSLAPATFSGGEQQRINIA 164
Cdd:cd03269 62 KPLDIAARNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEY-ANKRVEELSKGNQQKVQFI 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRL 222
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRV 198
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-71 |
8.97e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.96 E-value: 8.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTFVLYNQQGTRL---------------PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDG 65
Cdd:COG1134 1 MSSMIEVENVSKSYRLYHEPSRSLkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
....*.
gi 499404648 66 GHIWVR 71
Cdd:COG1134 81 GRVEVN 86
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-188 |
1.17e-15 |
|
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: 74.75 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 23 RLPVFH-DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrERWVDivnADARHVLEIRRETVGWVSQF 101
Cdd:COG4148 10 RRGGFTlDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVLQD---SARGIFLPPHRRRIGYVFQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 102 LRVIPRistLNVviQPLLERGMSRQESEIRGGEL--------LTHLnvperlwsLA--PATFSGGEQQRINIARGFIGDY 171
Cdd:COG4148 86 ARLFPH---LSV--RGNLLYGRKRAPRAERRISFdevvellgIGHL--------LDrrPATLSGGERQRVAIGRALLSSP 152
|
170
....*....|....*..
gi 499404648 172 PILLLDEPTASLDAKNR 188
Cdd:COG4148 153 RLLLMDEPLAALDLARK 169
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
1.69e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.12 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 2 DTQLRIENVdkTFVLYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVR------HRER 75
Cdd:PRK13631 19 DIILRVKNL--YCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 76 WVDIVNADARHVLEIR--RETVGWVSQFlrviPRISTLNVVIQ------PLlERGMSRQESEIRGGELLTHLNVPERLWS 147
Cdd:PRK13631 97 HELITNPYSKKIKNFKelRRRVSMVFQF----PEYQLFKDTIEkdimfgPV-ALGVKKSEAKKLAKFYLNKMGLDDSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 148 LAPATFSGGEQQRINIArGFIGDYP-ILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSMA 226
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIA-GILAIQPeILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
27-225 |
1.86e-15 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 73.33 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 27 FHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERW-VDIV---NADARHVLeirRETVGWVSQF- 101
Cdd:TIGR02323 19 CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAeLELYqlsEAERRRLM---RTEWGFVHQNp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 102 ---LRVipRISTLNVVIQPLLERGmSRQESEIR--GGELLTHLNVPERLWSLAPATFSGGEQQRINIARGFIGDYPILLL 176
Cdd:TIGR02323 96 rdgLRM--RVSAGANIGERLMAIG-ARHYGNIRatAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499404648 177 DEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:TIGR02323 173 DEPTGGLDVSVQARLLDLLRGlVRDLGLAVIIVTHDLGVARLLAQRLLVM 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-222 |
3.08e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 72.09 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVdktfvLYNQQGTRLpvfhDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRhrerwvdivNADA 84
Cdd:COG3840 2 LRLDDL-----TYRYGDFPL----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN---------GQDL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRRetvgwvsqflrviPrISTL--------------NVV--IQPLLeRGMSRQESEIRG-------GELLthlnv 141
Cdd:COG3840 64 TALPPAER-------------P-VSMLfqennlfphltvaqNIGlgLRPGL-KLTAEQRAQVEQalervglAGLL----- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 142 pERLwslaPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHD-DEVRqHVA 219
Cdd:COG3840 124 -DRL----PGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDElCRERGLTVLMVTHDpEDAA-RIA 197
|
...
gi 499404648 220 DRL 222
Cdd:COG3840 198 DRV 200
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
26-225 |
3.25e-15 |
|
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: 72.13 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNADarhvLEIRRETVGWVSQFLRVI 105
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG----HDLALAD----PAWLRRQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 106 PRISTLNVViqpLLERGMSRQESEIRGGELLTH---LNVPERLWSLA---PATFSGGEQQRINIARGFIGDYPILLLDEP 179
Cdd:cd03252 89 NRSIRDNIA---LADPGMSMERVIEAAKLAGAHdfiSELPEGYDTIVgeqGAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499404648 180 TASLDAKNRLAVTQLIDDAkSKGCAVVGIFHD-DEVRQhvADRLYSM 225
Cdd:cd03252 166 TSALDYESEHAIMRNMHDI-CAGRTVIIIAHRlSTVKN--ADRIIVM 209
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-223 |
3.38e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.23 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqQGTRlpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVDIVNADA 84
Cdd:PRK10895 4 LTAKNLAKAY-----KGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDED--ISLLPLHA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RhvleiRRETVGWVSQFLRVIPRISTLNVVIQPL-LERGMSRQESEIRGGELLTHLNVPERLWSLAPAtFSGGEQQRINI 163
Cdd:PRK10895 75 R-----ARRGIGYLPQEASIFRRLSVYDNLMAVLqIRDDLSAEQREDRANELMEEFHIEHLRDSMGQS-LSGGERRRVEI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 164 ARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLY 223
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAY 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-222 |
4.04e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 73.33 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiVNADARhvleIRRETVGWVSQFLRV 104
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP-----VPARAR----LARARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 IPRIStlnvVIQPLLERG----MSRQESEIRGGELLTHlnvpERLWSLAP---ATFSGGEQQRINIARGFIGDYPILLLD 177
Cdd:PRK13536 126 DLEFT----VRENLLVFGryfgMSTREIEAVIPSLLEF----ARLESKADarvSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499404648 178 EPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRL 222
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRL 242
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-188 |
6.10e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.06 E-value: 6.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqQGTrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVDIVNADA 84
Cdd:PRK09452 15 VELRGISKSF-----DGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD--ITHVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVleirrETVgwvSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLnvpeRLWSLA---PATFSGGEQQRI 161
Cdd:PRK09452 86 RHV-----NTV---FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMV----QLEEFAqrkPHQLSGGQQQRV 153
|
170 180
....*....|....*....|....*..
gi 499404648 162 NIARGFIGDYPILLLDEPTASLDAKNR 188
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLR 180
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-225 |
6.18e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 72.07 E-value: 6.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 17 YNQQGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERWVDivnadarHVLEIRREtVG 96
Cdd:PRK13650 14 YKEDQEK-YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEE-------NVWDIRHK-IG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 97 WV-----SQFLRVipriSTLNVVIQPLLERGMSRQESEIRGGE---LLTHLNVPERlwslAPATFSGGEQQRINIArGFI 168
Cdd:PRK13650 85 MVfqnpdNQFVGA----TVEDDVAFGLENKGIPHEEMKERVNEaleLVGMQDFKER----EPARLSGGQKQRVAIA-GAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 169 GDYP-ILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHD-DEVRqhVADRLYSM 225
Cdd:PRK13650 156 AMRPkIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDlDEVA--LSDRVLVM 213
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-222 |
6.25e-15 |
|
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: 71.67 E-value: 6.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 37 GECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhrERWVDIVNADARhvlEIRRETVGWVSQFLRVIPRISTL----- 111
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-----EIELDTVSYKPQ---YIKADYEGTVRDLLSSITKDFYThpyfk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 112 NVVIQPL-LERGMSRQeseirggellthlnVPErlwslapatFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLA 190
Cdd:cd03237 97 TEIAKPLqIEQILDRE--------------VPE---------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190
....*....|....*....|....*....|....*
gi 499404648 191 VTQLID---DAKSKGCAVVGifHDDEVRQHVADRL 222
Cdd:cd03237 154 ASKVIRrfaENNEKTAFVVE--HDIIMIDYLADRL 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-214 |
6.46e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.41 E-value: 6.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTFvlynqQGTRlpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERwvdiV 80
Cdd:PRK11288 1 SSPYLSFDGIGKTF-----PGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM----R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 NADARHVLEirrETVGWVSQFLRVIPRISTL-NVVIQPLLERG--MSRQESEIRGGELLTHLNVperlwSLAPAT----F 153
Cdd:PRK11288 70 FASTTAALA---AGVAIIYQELHLVPEMTVAeNLYLGQLPHKGgiVNRRLLNYEAREQLEHLGV-----DIDPDTplkyL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404648 154 SGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD-DEV 214
Cdd:PRK11288 142 SIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRmEEI 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-221 |
7.15e-15 |
|
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: 73.30 E-value: 7.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqQGTRlpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYG--NYRPDGGHI-----------WVR 71
Cdd:TIGR03269 1 IEVKNLTKKF-----DGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgYVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 72 HRERW---------------VDIVNADARHVLEIRRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELL 136
Cdd:TIGR03269 74 RPSKVgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 137 THLNVPERLWSLApATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKN-RLAVTQLIDDAKSKGCAVVGIFHDDEVR 215
Cdd:TIGR03269 154 EMVQLSHRITHIA-RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTaKLVHNALEEAVKASGISMVLTSHWPEVI 232
|
....*.
gi 499404648 216 QHVADR 221
Cdd:TIGR03269 233 EDLSDK 238
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
28-197 |
8.49e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.07 E-value: 8.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 28 HDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhrerwvDIVNADARHV-LEIRRETVGWVSQ----FL 102
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI---------LIDGTDIRTVtRASLRRNIAVVFQdaglFN 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 103 RVIP------RISTLNVVIQPLLERGMSRQESEIRGGELLThlNVPERLWSLapatfSGGEQQRINIARGFIGDYPILLL 176
Cdd:PRK13657 423 RSIEdnirvgRPDATDEEMRAAAERAQAHDFIERKPDGYDT--VVGERGRQL-----SGGERQRLAIARALLKDPPILIL 495
|
170 180
....*....|....*....|.
gi 499404648 177 DEPTASLDAKNRLAVTQLIDD 197
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDE 516
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
25-184 |
8.60e-15 |
|
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: 73.24 E-value: 8.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNADaRHVLeirRETVGWVSQflrv 104
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNG----FSLKDID-RHTL---RQFINYLPQ---- 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 IPRISTLNVVIQPLL--ERGMSRQE-------SEIRGGELLTHLNVPERLwSLAPATFSGGEQQRINIARGFIGDYPILL 175
Cdd:TIGR01193 556 EPYIFSGSILENLLLgaKENVSQDEiwaaceiAEIKDDIENMPLGYQTEL-SEEGSSISGGQKQRIALARALLTDSKVLI 634
|
....*....
gi 499404648 176 LDEPTASLD 184
Cdd:TIGR01193 635 LDESTSNLD 643
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
29-225 |
8.76e-15 |
|
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: 70.96 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRE-------RWVDIVNADARHVLEIRRETVGWVSQF 101
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQitepgpdRMVVFQNYSLLPWLTVRENIALAVDRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 102 LRVIPRISTLNVVIQPLLERGMsRQESEIRGGELlthlnvperlwslapatfSGGEQQRINIARGFIGDYPILLLDEPTA 181
Cdd:TIGR01184 83 LPDLSKSERRAIVEEHIALVGL-TEAADKRPGQL------------------SGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499404648 182 SLDAKNRLAVT-QLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:TIGR01184 144 ALDALTRGNLQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVML 188
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
28-184 |
9.33e-15 |
|
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: 72.79 E-value: 9.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 28 HDINLSVKCGECVALHGHSGTGKSTLLRSLYGnYRPDGGHIWVRHRerwvDIVNADARHVLEIRREtvgwvsqfLRVI-- 105
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQ----DLDGLSRRALRPLRRR--------MQVVfq 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 106 -------PRISTLNVVIQPL--LERGMSRQESEIRGGELLTHLNVPERLWSLAPATFSGGEQQRINIARGFIGDYPILLL 176
Cdd:COG4172 370 dpfgslsPRMTVGQIIAEGLrvHGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
....*...
gi 499404648 177 DEPTASLD 184
Cdd:COG4172 450 DEPTSALD 457
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-223 |
9.99e-15 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 70.77 E-value: 9.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhrerwvDIVNADA 84
Cdd:TIGR04406 2 LVAENLIKSY------KKR-KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKI---------LIDGQDI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHV-LEIR-RETVGWVSQFLRVIPRISTLNVVIQPLLERG-MSRQESEIRGGELLTHLNVpERLWSLAPATFSGGEQQRI 161
Cdd:TIGR04406 66 THLpMHERaRLGIGYLPQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQI-SHLRDNKAMSLSGGERRRV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499404648 162 NIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVvgIFHDDEVRQ--HVADRLY 223
Cdd:TIGR04406 145 EIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGV--LITDHNVREtlDICDRAY 206
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
25-213 |
1.09e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.88 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvRHRERWVDIVNADArhvleirretvGWVSQFLRV 104
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI--TLDGKPVEGPGAER-----------GVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 IPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPE----RLWSLapatfSGGEQQRINIARGFIGDYPILLLDEPT 180
Cdd:PRK11248 82 LPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGaekrYIWQL-----SGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 499404648 181 ASLDAKNRLAVTQLI-----DDAKSkgcaVVGIFHDDE 213
Cdd:PRK11248 157 GALDAFTREQMQTLLlklwqETGKQ----VLLITHDIE 190
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-196 |
1.13e-14 |
|
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: 70.72 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhrerwvDIVNADA 84
Cdd:cd03251 1 VEFKNVTFRY-----PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRI---------LIDGHDV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHV-LEIRRETVGWVSQflRVIPRISTL--NVVIQpllERGMSRQESE-----------IRGGELLTHLNVPERLWSLap 150
Cdd:cd03251 67 RDYtLASLRRQIGLVSQ--DVFLFNDTVaeNIAYG---RPGATREEVEeaaraanahefIMELPEGYDTVIGERGVKL-- 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499404648 151 atfSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLID 196
Cdd:cd03251 140 ---SGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALE 182
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
10-222 |
1.17e-14 |
|
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: 70.21 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 10 VDKTFVLYNQQGTRLpvfhdiNLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNAD--ARHV 87
Cdd:cd03298 3 LDKIRFSYGEQPMHF------DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING----VDVTAAPpaDRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 88 LEIRRET-----------VGwvsqfLRVIPRIStLNVVIQPLLERGMSRqeSEIRGGELlthlnvpeRLwslaPATFSGG 156
Cdd:cd03298 73 SMLFQENnlfahltveqnVG-----LGLSPGLK-LTAEDRQAIEVALAR--VGLAGLEK--------RL----PGELSGG 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 157 EQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDA-KSKGCAVVGIFHDDEVRQHVADRL 222
Cdd:cd03298 133 ERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRV 199
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-211 |
1.33e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.66 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 4 QLRIENVDKTFvlyNQQ-GTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHI-WV------RHRER 75
Cdd:PRK13651 2 QIKVKNIVKIF---NKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIfkdeknKKKTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 76 WVDIVNAD----------ARHVLEIRREtVGWVSQFLRVIPRISTL--NVVIQPlLERGMSRQESEIRGGELLTHLNVPE 143
Cdd:PRK13651 79 EKEKVLEKlviqktrfkkIKKIKEIRRR-VGVVFQFAEYQLFEQTIekDIIFGP-VSMGVSKEEAKKRAAKYIELVGLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499404648 144 RLWSLAPATFSGGEQQRINIArGFIGDYP-ILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD 211
Cdd:PRK13651 157 SYLQRSPFELSGGQKRRVALA-GILAMEPdFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-225 |
1.38e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.17 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynQQGTrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRhrerwvDIVNADA 84
Cdd:PRK13644 2 IRLENVSYSY----PDGT--PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVS------GIDTGDF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRReTVGWV-----SQFL-RVIPR---ISTLNVVIQPL-LERGMSRQESEIRGGELLTHlnvperlwslAPATFS 154
Cdd:PRK13644 70 SKLQGIRK-LVGIVfqnpeTQFVgRTVEEdlaFGPENLCLPPIeIRKRVDRALAEIGLEKYRHR----------SPKTLS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404648 155 GGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEvRQHVADRLYSM 225
Cdd:PRK13644 139 GGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVM 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-225 |
1.42e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.36 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 22 TRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVDIVN-ADA-RH----VLEIRRETv 95
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKP--VRIRSpRDAiRAgiayVPEDRKGE- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 96 GWVSQF-------LRVIPRISTLnvviqPLLERGMSRQESEirggELLTHLNVpeRLWSL-APA-TFSGGEQQRINIARG 166
Cdd:COG1129 340 GLVLDLsirenitLASLDRLSRG-----GLLDRRRERALAE----EYIKRLRI--KTPSPeQPVgNLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 167 FIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD-DEVRqHVADRLYSM 225
Cdd:COG1129 409 LATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSElPELL-GLSDRILVM 467
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-188 |
2.65e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.60 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRLpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwvDIVNADA 84
Cdd:PRK13537 8 IDFRNVEKRY------GDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-----EPVPSRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVleirRETVGWVSQFLRVIPRIStlnvVIQPLL----ERGMSRQESEIRGGELLTHlnvpERLWSLAPA---TFSGGE 157
Cdd:PRK13537 76 RHA----RQRVGVVPQFDNLDPDFT----VRENLLvfgrYFGLSAAAARALVPPLLEF----AKLENKADAkvgELSGGM 143
|
170 180 190
....*....|....*....|....*....|.
gi 499404648 158 QQRINIARGFIGDYPILLLDEPTASLDAKNR 188
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
29-227 |
4.47e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.99 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNADaRHVLEIRRETVGWVSQ--FLRVIP 106
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG----QDLLKAD-PEAQKLLRQKIQIVFQnpYGSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 107 RISTLNVVIQPLL-ERGMSRQESEIRGGELLTHLNV-PERlWSLAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLD 184
Cdd:PRK11308 108 RKKVGQILEEPLLiNTSLSAAERREKALAMMAKVGLrPEH-YDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499404648 185 AKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADRLysMAM 227
Cdd:PRK11308 187 VSVQAQVLNLMMDlQQELGLSYVFISHDLSVVEHIADEV--MVM 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-225 |
5.49e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.46 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrHRERWVDIVNADArHVLEIRretvgWVSQFLRV 104
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEI-GGNPCARLTPAKA-HQLGIY-----LVPQEPLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 IPRIStlnvVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLApATFSGGEQQRINIARGFIGDYPILLLDEPTASLD 184
Cdd:PRK15439 98 FPNLS----VKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSA-GSLEVADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499404648 185 AKNRLAVTQLIDDAKSKGCAVVGIFHD-DEVRQhVADRLYSM 225
Cdd:PRK15439 173 PAETERLFSRIRELLAQGVGIVFISHKlPEIRQ-LADRISVM 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-77 |
6.13e-14 |
|
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: 68.33 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFVLYNQQGTRL---------------PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIW 69
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLkklgilgrkgevgefWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
....*...
gi 499404648 70 VRHRERWV 77
Cdd:cd03220 81 VRGRVSSL 88
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-226 |
6.56e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.46 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 27 FHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRE-RWVDIVNADAR---HVLEIRRET-------V 95
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEiNALSTAQRLARglvYLPEDRQSSglyldapL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 96 GWVSQFLRVipriSTLNVVIQP-----LLERgmSRQESEIRggelLTHLNVPERlwslapaTFSGGEQQRINIARGFIGD 170
Cdd:PRK15439 359 AWNVCALTH----NRRGFWIKParenaVLER--YRRALNIK----FNHAEQAAR-------TLSGGNQQKVLIAKCLEAS 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 171 YPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD-DEVRQhVADRLYSMA 226
Cdd:PRK15439 422 PQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDlEEIEQ-MADRVLVMH 477
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-211 |
8.55e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 8.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRER--WV- 77
Cdd:PRK09544 1 MTSLVSLENVSVSF------GQR-RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRigYVp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 78 DIVNADARHVLEirretvgwVSQFLRVIPRISTLNvvIQPLLERgmsrqeseIRGGELLThlnvperlwslAP-ATFSGG 156
Cdd:PRK09544 74 QKLYLDTTLPLT--------VNRFLRLRPGTKKED--ILPALKR--------VQAGHLID-----------APmQKLSGG 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499404648 157 EQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHD 211
Cdd:PRK09544 125 ETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHD 180
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-220 |
9.15e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.54 E-value: 9.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 9 NVDKTFVLYNQQGtrlpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLY-------GNYRPDGGHIWVRHrerwvDIVN 81
Cdd:PRK14246 12 NISRLYLYINDKA----ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGK-----DIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 82 ADArhvLEIRREtVGWVSQFLRVIPRISTLNVVIQPLLERGMsRQESEIRG--GELLTHL----NVPERLWSLApATFSG 155
Cdd:PRK14246 83 IDA---IKLRKE-VGMVFQQPNPFPHLSIYDNIAYPLKSHGI-KEKREIKKivEECLRKVglwkEVYDRLNSPA-SQLSG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 156 GEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKsKGCAVVGIFHDDEVRQHVAD 220
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELK-NEIAIVIVSHNPQQVARVAD 220
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-213 |
1.46e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 67.12 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPD---GGHIWVRHRErwVDIVNADARHVleirretvGWVSQF 101
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRR--LTALPAEQRRI--------GILFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 102 LRVIPRIStlnvVIQPL---LERGMSRQESEIRGGELLTHLNVP---ERlwslAPATFSGGEQQRINIARGFIGDYPILL 175
Cdd:COG4136 85 DLLFPHLS----VGENLafaLPPTIGRAQRRARVEQALEEAGLAgfaDR----DPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 499404648 176 LDEPTASLDAKNRLAVTQLI-DDAKSKGCAVVGIFHDDE 213
Cdd:COG4136 157 LDEPFSKLDAALRAQFREFVfEQIRQRGIPALLVTHDEE 195
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
26-211 |
1.55e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.09 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrhrerwvdivnaDARHVL-----EIRREtVGWVSQ 100
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL------------DGEHIQhyaskEVARR-IGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 101 FLRVIPRISTLNVVI------QPLLERGMSRQESEIRGGELLTHLNvpeRLWSLAPATFSGGEQQRINIARGFIGDYPIL 174
Cdd:PRK10253 89 NATTPGDITVQELVArgryphQPLFTRWRKEDEEAVTKAMQATGIT---HLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 499404648 175 LLDEPTASLDAKNRLAVTQLIDDA-KSKGCAVVGIFHD 211
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHD 203
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-226 |
1.59e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.87 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 16 LYNQQGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwvDIVNADARHVLEIRRETV 95
Cdd:PRK11831 13 VSFTRGNR-CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG-----ENIPAMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 96 GWVSQFLRVIPRISTLNVVIQPLLErgmsrqesEIRGGELLTHLNVPERL--------WSLAPATFSGGEQQRINIARGF 167
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLRE--------HTQLPAPLLHSTVMMKLeavglrgaAKLMPSELSGGMARRAALARAI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 168 IGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADRLYSMA 226
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVA 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-210 |
1.69e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 69.37 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 24 LPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNADA----RHVLEIRRETVGWVS 99
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG----VPLVQYDHhylhRQVALVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 100 QF-------LRVIPRISTLNVVIqpllergMSRQESEIRGGELLTHLNVPERLWSLapatfSGGEQQRINIARGFIGDYP 172
Cdd:TIGR00958 570 SVreniaygLTDTPDEEIMAAAK-------AANAHDFIMEFPNGYDTEVGEKGSQL-----SGGQKQRIAIARALVRKPR 637
|
170 180 190
....*....|....*....|....*....|....*...
gi 499404648 173 ILLLDEPTASLDAKNRLAVTQlidDAKSKGCAVVGIFH 210
Cdd:TIGR00958 638 VLILDEATSALDAECEQLLQE---SRSRASRTVLLIAH 672
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
24-226 |
1.69e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 68.09 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 24 LPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhrerWVDIVNADARHVLEIrRETVGWV----- 98
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI-------KIDGITISKENLKEI-RKKIGIIfqnpd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 99 SQFLRvipriSTLNVVIQPLLE-RGMSRQESEIRGGELLTHLNVPERLwSLAPATFSGGEQQRINIARGFIGDYPILLLD 177
Cdd:PRK13632 94 NQFIG-----ATVEDDIAFGLEnKKVPPKKMKDIIDDLAKKVGMEDYL-DKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499404648 178 EPTASLDAKNRLAVTQLIDDAKSKGC-AVVGIFHD-DEVRQhvADRLYSMA 226
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDmDEAIL--ADKVIVFS 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
29-210 |
2.69e-13 |
|
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: 66.91 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDG---GHIWVRHRERWVDIVnadarhvleirRETVGWVSQFLRVI 105
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQF-----------QKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 106 PrisTLNV-------VIQPLLERGMSRQESEIRGGELLTHLNVpERLWSLAPATFSGGEQQRINIARGFIGDYPILLLDE 178
Cdd:cd03234 94 P---GLTVretltytAILRLPRKSSDAIRKKRVEDVLLRDLAL-TRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|..
gi 499404648 179 PTASLDAKNRLAVTQLIDDAKSKGCAVVGIFH 210
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-197 |
3.22e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.53 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 31 NLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWvrhrerwvdIVNADARHVLEIRREtvgwVSQF--------- 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLT---------LNGQDHTTTPPSRRP----VSMLfqennlfsh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 102 LRVIPRIS-------TLNVVIQPLLERgMSRQESeirggeLLTHLnvpERLwslaPATFSGGEQQRINIARGFIGDYPIL 174
Cdd:PRK10771 86 LTVAQNIGlglnpglKLNAAQREKLHA-IARQMG------IEDLL---ARL----PGQLSGGQRQRVALARCLVREQPIL 151
|
170 180
....*....|....*....|...
gi 499404648 175 LLDEPTASLDAKNRLAVTQLIDD 197
Cdd:PRK10771 152 LLDEPFSALDPALRQEMLTLVSQ 174
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
26-225 |
4.36e-13 |
|
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: 65.63 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGN--YRPDGGHIWVRHRerwvDIVNAdarhvleirretvgwvsqflr 103
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGE----DITDL--------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 104 vipristlnvviqPLLER-----GMSRQES-EIRG---GELLTHLNVperlwslapaTFSGGEQQRINIARGFIGDYPIL 174
Cdd:cd03217 70 -------------PPEERarlgiFLAFQYPpEIPGvknADFLRYVNE----------GFSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499404648 175 LLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHV-ADRLYSM 225
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVL 178
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-185 |
4.65e-13 |
|
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: 65.57 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVdkTFVLYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHR------ERWvd 78
Cdd:cd03250 1 ISVEDA--SFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiayvsqEPW-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 79 IVNADAR------HVLEIRRetvgwvsqFLRVIpRISTLNVVIQpLLERGMsrqESEI--RGgellthlnvperlwslap 150
Cdd:cd03250 77 IQNGTIRenilfgKPFDEER--------YEKVI-KACALEPDLE-ILPDGD---LTEIgeKG------------------ 125
|
170 180 190
....*....|....*....|....*....|....*
gi 499404648 151 ATFSGGEQQRINIARGFIGDYPILLLDEPTASLDA 185
Cdd:cd03250 126 INLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-225 |
5.02e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqgtrlPVFH---DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErWVDIVN 81
Cdd:PRK09700 6 ISMAGIGKSF----------GPVHalkSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN-YNKLDH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 82 ADARHVleirreTVGWVSQFLRVIPRISTL-NVVIQPLLERG------MSRQESEIRGGELLTHLNVPERLWSLApATFS 154
Cdd:PRK09700 75 KLAAQL------GIGIIYQELSVIDELTVLeNLYIGRHLTKKvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKV-ANLS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404648 155 GGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD-DEVRQhVADRLYSM 225
Cdd:PRK09700 148 ISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKlAEIRR-ICDRYTVM 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-227 |
6.31e-13 |
|
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: 65.26 E-value: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 21 GTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSL--YGNYRPDGGHIWVrhrerwvdivNADARHVLEIRREtVGWV 98
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLI----------NGRPLDKRSFRKI-IGYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 99 SQFLRVIPristlnvviqpllergmsrqeseirggelltHLNVPERLW-SLAPATFSGGEQQRINIARGFIGDYPILLLD 177
Cdd:cd03213 88 PQDDILHP-------------------------------TLTVRETLMfAAKLRGLSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499404648 178 EPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHddEVRQ---HVADRLYSMAM 227
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRLADTGRTIICSIH--QPSSeifELFDKLLLLSQ 187
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
19-216 |
7.87e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.51 E-value: 7.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 19 QQGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNADArhvlEIRRETVGWV 98
Cdd:PRK10247 16 LAGDA-KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE----DISTLKP----EIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 99 SQflrvIPRI---STLNVVIQPLLERGMSRQESEIRGGelLTHLNVPERLWSLAPATFSGGEQQRINIARGFIGDYPILL 175
Cdd:PRK10247 87 AQ----TPTLfgdTVYDNLIFPWQIRNQQPDPAIFLDD--LERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499404648 176 LDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHD-DEVRQ 216
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRyVREQNIAVLWVTHDkDEINH 203
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-220 |
7.99e-13 |
|
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: 65.85 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 13 TFVLYnqqgtRLPVfhdinlsVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGhiwvRHRER--WVDIVNADARHVLE- 89
Cdd:cd03236 14 SFKLH-----RLPV-------PREGQVLGLVGPNGIGKSTALKILAGKLKPNLG----KFDDPpdWDEILDEFRGSELQn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 90 ----IRRETVGWV--SQFLRVIPRISTLNVViqPLLERGMSRQESEirggELLTHL---NVPERLWSlapaTFSGGEQQR 160
Cdd:cd03236 78 yftkLLEGDVKVIvkPQYVDLIPKAVKGKVG--ELLKKKDERGKLD----ELVDQLelrHVLDRNID----QLSGGELQR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 161 INIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVAD 220
Cdd:cd03236 148 VAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSD 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-198 |
8.26e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.18 E-value: 8.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 2 DTQLRIENVDktFVLYNQQGTRL--PvfhdINLSVKCGECVALHGHSGTGKSTLLRSLYGN--YRpdgGHIwvrhrerwv 77
Cdd:PRK11174 345 NDPVTIEAED--LEILSPDGKTLagP----LNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSL--------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 78 dIVNADARHVLEIR--RETVGWVSQflrvipristlnvviQPLLERGMSRQ----------ESEIRggELLTHLNVPERL 145
Cdd:PRK11174 407 -KINGIELRELDPEswRKHLSWVGQ---------------NPQLPHGTLRDnvllgnpdasDEQLQ--QALENAWVSEFL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499404648 146 WSLAP----------ATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDA 198
Cdd:PRK11174 469 PLLPQgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA 531
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-225 |
9.37e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.97 E-value: 9.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 2 DTQLRIENVdktfVLYNQQGtrLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVN 81
Cdd:COG3845 255 EVVLEVENL----SVRDDRG--VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE----DITG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 82 ADARhvlEIRRETVGWVSQfLR----VIPRIS-TLNVVIQ-----PLLERG-MSRQESEIRGGELLTHLNV-PERLWSLA 149
Cdd:COG3845 325 LSPR---ERRRLGVAYIPE-DRlgrgLVPDMSvAENLILGryrrpPFSRGGfLDRKAIRAFAEELIEEFDVrTPGPDTPA 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 150 pATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD-DEVRQhVADRLYSM 225
Cdd:COG3845 401 -RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDlDEILA-LSDRIAVM 475
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-210 |
1.11e-12 |
|
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: 66.77 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWvrhrerwvdIVNADARHV-LEIRRETVGWVSQ--- 100
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIL---------IDGQDIRDVtQASLRAAIGIVPQdtv 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 101 -FlrvipristlNVVI-------QPllerGMSRQESE--IRG---GELLTHL------NVPERLWSLapatfSGGEQQRI 161
Cdd:COG5265 443 lF----------NDTIayniaygRP----DASEEEVEaaARAaqiHDFIESLpdgydtRVGERGLKL-----SGGEKQRV 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499404648 162 NIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAkSKGCAVVGIFH 210
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGRTTLVIAH 551
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-225 |
1.15e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.80 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 15 VLYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHI-----WVRHRERWV-DIVNADARHVL 88
Cdd:PRK10261 20 IAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSRQViELSEQSAAQMR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 89 EIRRETVGWVSQflrviPRISTLNVVI--------QPLLERGMSRQESEIRGGELLTHLNVPER--LWSLAPATFSGGEQ 158
Cdd:PRK10261 100 HVRGADMAMIFQ-----EPMTSLNPVFtvgeqiaeSIRLHQGASREEAMVEAKRMLDQVRIPEAqtILSRYPHQLSGGMR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404648 159 QRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVlQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
29-225 |
2.21e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.83 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHrerwVDIVNADARHVLEIRRETVGWVSQFLRVIPRI 108
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG----VDIAKISDAELREVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 109 STLNVVIQPLLERGMSRQESEIRGGELLTHLNVpERLWSLAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNR 188
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190
....*....|....*....|....*....|....*...
gi 499404648 189 LAVT-QLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK10070 201 TEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-211 |
2.46e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.65 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 3 TQLRIENVDktfVLYNQQgtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERWVDIVNA 82
Cdd:PRK11231 1 MTLRTENLT---VGYGTK----RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 83 DARHVLEIR-----------RETVG-----WVSQFLRvipristLNVVIQPLLERGMSRQEseirggelLTHLnVPERLW 146
Cdd:PRK11231 74 LARRLALLPqhhltpegitvRELVAygrspWLSLWGR-------LSAEDNARVNQAMEQTR--------INHL-ADRRLT 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 147 SLapatfSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD 211
Cdd:PRK11231 138 DL-----SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD 197
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-216 |
2.48e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVDIVNAdaRHVLEirrETVGWVSQFLRVIPRI 108
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKE--IDFKSS--KEALE---NGISMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 109 STL-NVVIQPLLERG-------MSRQESEIRGgELLTHLNVPERLwslapATFSGGEQQRINIARGFIGDYPILLLDEPT 180
Cdd:PRK10982 89 SVMdNMWLGRYPTKGmfvdqdkMYRDTKAIFD-ELDIDIDPRAKV-----ATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 499404648 181 ASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD-DEVRQ 216
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERGCGIVYISHKmEEIFQ 199
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-197 |
2.57e-12 |
|
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: 64.03 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVdkTFVLYNQQGTrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdIV 80
Cdd:cd03248 8 LKGIVKFQNV--TFAYPTRPDT--LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKP----IS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 NADARHVleirRETVGWVSQ----FLRVI--------PRISTLNVV----------IQPLLERGMSRQESEiRGGELlth 138
Cdd:cd03248 80 QYEHKYL----HSKVSLVGQepvlFARSLqdniayglQSCSFECVKeaaqkahahsFISELASGYDTEVGE-KGSQL--- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499404648 139 lnvperlwslapatfSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD 197
Cdd:cd03248 152 ---------------SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYD 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
30-225 |
3.12e-12 |
|
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: 65.21 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 30 INLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERWVDIVNADA----------------------RHV 87
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPdgrgrakryigilhqeydlyphRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 88 LEIRRETVGWVSQF-LRVIPRISTLNVViqpllerGMSRQESEirggellthlNVPERLwslaPATFSGGEQQRINIARG 166
Cdd:TIGR03269 383 LDNLTEAIGLELPDeLARMKAVITLKMV-------GFDEEKAE----------EILDKY----PDELSEGERHRVALAQV 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 167 FIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:TIGR03269 442 LIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALM 501
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-209 |
3.19e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 64.74 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRLPVfHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiVNADA 84
Cdd:COG4152 2 LELKGLTKRF------GDKTAV-DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP-----LDPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVL----EIR----RETVGWVSQFLrvipriSTLnvviqplleRGMSRQESEIRGGELLTHLNVPER----LWSLapat 152
Cdd:COG4152 70 RRRIgylpEERglypKMKVGEQLVYL------ARL---------KGLSKAEAKRRADEWLERLGLGDRankkVEEL---- 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 153 fSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVvgIF 209
Cdd:COG4152 131 -SKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTV--IF 184
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
26-184 |
4.33e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKST----LLRSLygnyrPDGGHIWVRHRErwvdIVNADARHVLEIRRE-TVGWVSQ 100
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQP----LHNLNRRQLLPVRHRiQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 101 FLRVIPRISTLNVVIQPLL--ERGMSRQESEIRGGELLTHLNVPERLWSLAPATFSGGEQQRINIARGFIGDYPILLLDE 178
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
....*.
gi 499404648 179 PTASLD 184
Cdd:PRK15134 452 PTSSLD 457
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-188 |
4.34e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.74 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRLpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrhrerwvdivnaDA 84
Cdd:PRK11432 7 VVLKNITKRF------GSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI------------DG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLE--IRRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRggellthlnVPERLWSLAPATF--------S 154
Cdd:PRK11432 68 EDVTHrsIQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQR---------VKEALELVDLAGFedryvdqiS 138
|
170 180 190
....*....|....*....|....*....|....
gi 499404648 155 GGEQQRINIARGFIGDYPILLLDEPTASLDAKNR 188
Cdd:PRK11432 139 GGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
23-223 |
4.55e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.36 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 23 RLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVN-ADARhvleIRRETVGWVSQF 101
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK----DITDwQTAK----IMREAVAIVPEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 102 LRVIPRIST-LNVVIQPLLERGMSRQESEIRGGELLTHLNvpERLWSLApATFSGGEQQRINIARGFIGDYPILLLDEPT 180
Cdd:PRK11614 89 RRVFSRMTVeENLAMGGFFAERDQFQERIKWVYELFPRLH--ERRIQRA-GTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499404648 181 ASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLY 223
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGY 208
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
29-233 |
1.13e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.20 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVALHGHSGTGKS----TLLRSLYGNYRPDGGHIWvRHRErwvdIVNADARHVLEIRRETVGWVSQ---- 100
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIGGSATF-NGRE----ILNLPEKELNKLRAEQISMIFQdpmt 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 101 ----FLRVIPRistLNVVIQplLERGMSRQESEIRGGELLTHLNVPE---RLwSLAPATFSGGEQQRINIARGFIGDYPI 173
Cdd:PRK09473 109 slnpYMRVGEQ---LMEVLM--LHKGMSKAEAFEESVRMLDAVKMPEarkRM-KMYPHEFSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404648 174 LLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADRLYSMaMTSRTQE 233
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM-YAGRTME 242
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-220 |
2.28e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.78 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLRS------LYGNYRPDGghiwvRHRERWVDIVNADARHVlEIRREtVGWVS 99
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlleLNEEARVEG-----EVRLFGRNIYSPDVDPI-EVRRE-VGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 100 QFLRVIPRISTLNVVIQPLLERGMSRQESEIrggellthlnvPERL-WSLA---------------PATFSGGEQQRINI 163
Cdd:PRK14267 92 QYPNPFPHLTIYDNVAIGVKLNGLVKSKKEL-----------DERVeWALKkaalwdevkdrlndyPSNLSGGQRQRLVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 164 ARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKsKGCAVVGIFHDDEVRQHVAD 220
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELK-KEYTIVLVTHSPAQAARVSD 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-196 |
2.49e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 62.73 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 15 VLYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrhrerwvDIVNADArHVLEIRRET 94
Cdd:PRK11176 347 VTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-------DGHDLRD-YTLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 95 VGWVSQFLRVIPriSTLNVVIQPLLERGMSRQESEiRGGELLTHLNVPERLwslaP-----------ATFSGGEQQRINI 163
Cdd:PRK11176 419 VALVSQNVHLFN--DTIANNIAYARTEQYSREQIE-EAARMAYAMDFINKM----DngldtvigengVLLSGGQRQRIAI 491
|
170 180 190
....*....|....*....|....*....|...
gi 499404648 164 ARGFIGDYPILLLDEPTASLDAKNRLAVTQLID 196
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALD 524
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-205 |
2.58e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 61.20 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvDIVNada 84
Cdd:COG1137 4 LEAENLVKSY------GKR-TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE----DITH--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 rhvLEI--R-RETVGWVSQ----FLRvipristLNVV--IQPLLE-RGMSRQESEIRGGELLTHLNVPERLWSLApATFS 154
Cdd:COG1137 70 ---LPMhkRaRLGIGYLPQeasiFRK-------LTVEdnILAVLElRKLSKKEREERLEELLEEFGITHLRKSKA-YSLS 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499404648 155 GGEQQRINIARGFIGDYPILLLDEPTASLDAknrLAVT---QLIDDAKSKGCAV 205
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDEPFAGVDP---IAVAdiqKIIRHLKERGIGV 189
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-225 |
3.65e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.42 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDktfVLYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKS----TLLRSL--------YGNYRPDGGhiwvrh 72
Cdd:PRK15134 6 LAIENLS---VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypSGDIRFHGE------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 73 rerwvDIVNADARHVLEIRRETVGWVSQFlrviPRIStLNvviqPL------------LERGMSRQESEirgGELLTHL- 139
Cdd:PRK15134 77 -----SLLHASEQTLRGVRGNKIAMIFQE----PMVS-LN----PLhtlekqlyevlsLHRGMRREAAR---GEILNCLd 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 140 -----NVPERLWSLaPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDE 213
Cdd:PRK15134 140 rvgirQAAKRLTDY-PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLS 218
|
250
....*....|..
gi 499404648 214 VRQHVADRLYSM 225
Cdd:PRK15134 219 IVRKLADRVAVM 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
40-225 |
3.76e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 61.36 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 40 VALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdIVNADARHVleirRETVGWVSQflrvipriSTLNVVIQPLL 119
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEP----ITKENIREV----RKFVGLVFQ--------NPDDQIFSPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 120 ER---------GMSRQESEIRGGELLTHLNVpERLWSLAPATFSGGEQQRINIArGFIGDYP-ILLLDEPTASLDAKNRL 189
Cdd:PRK13652 97 EQdiafgpinlGLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIA-GVIAMEPqVLVLDEPTAGLDPQGVK 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 499404648 190 AVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK13652 175 ELIDFLNDlPETYGMTVIFSTHQLDLVPEMADYIYVM 211
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-184 |
4.40e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.83 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqgTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhreRWVDivNA-- 82
Cdd:PRK15064 320 LEVENLTKGF-------DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------KWSE--NAni 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 83 -----DARHVLEIRRETVGWVSQFlrvipristlnvviqplleRGMSRQESEIRG--GELL-THLNVPERLWSLapatfS 154
Cdd:PRK15064 385 gyyaqDHAYDFENDLTLFDWMSQW-------------------RQEGDDEQAVRGtlGRLLfSQDDIKKSVKVL-----S 440
|
170 180 190
....*....|....*....|....*....|
gi 499404648 155 GGEQQRINIARGFIGDYPILLLDEPTASLD 184
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-213 |
5.01e-11 |
|
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: 62.34 E-value: 5.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 7 IENVDKTFVLYNQqgtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvdivnaDARH 86
Cdd:TIGR01257 931 VKNLVKIFEPSGR-----PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK---------DIET 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 87 VLEIRRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLApATFSGGEQQRINIARG 166
Cdd:TIGR01257 997 NLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEA-QDLSGGMQRKLSVAIA 1075
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499404648 167 FIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDE 213
Cdd:TIGR01257 1076 FVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDE 1122
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-222 |
6.18e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 6.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 34 VKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhrERWVDIvnadARHVLEIRRETVGWVSQFLRVIPRI---ST 110
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-----DPELKI----SYKPQYIKPDYDGTVEDLLRSITDDlgsSY 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 111 LNV-VIQPL-LERGMSRQeseirggelLTHLnvperlwslapatfSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNR 188
Cdd:PRK13409 433 YKSeIIKPLqLERLLDKN---------VKDL--------------SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
170 180 190
....*....|....*....|....*....|....*
gi 499404648 189 LAVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADRL 222
Cdd:PRK13409 490 LAVAKAIRRiAEEREATALVVDHDIYMIDYISDRL 524
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-193 |
6.61e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.66 E-value: 6.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 6 RIENVDKTFVLYNQQgtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiVNADAR 85
Cdd:PRK10790 340 RIDIDNVSFAYRDDN----LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRP-----LSSLSH 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 86 HVLeirRETVGWVSQFLRVIPRISTLNVVI-QPLLERGMSRQESEIRGGELLTHLnvPERLWSL---APATFSGGEQQRI 161
Cdd:PRK10790 411 SVL---RQGVAMVQQDPVVLADTFLANVTLgRDISEEQVWQALETVQLAELARSL--PDGLYTPlgeQGNNLSVGQKQLL 485
|
170 180 190
....*....|....*....|....*....|..
gi 499404648 162 NIARGFIGDYPILLLDEPTASLDAKNRLAVTQ 193
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQ 517
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-74 |
6.74e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.48 E-value: 6.74e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404648 5 LRIENVDKTFVlynqQGTRL--PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRE 74
Cdd:COG1101 2 LELKNLSKTFN----PGTVNekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD 69
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-206 |
8.03e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.43 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhreRWVDIVNADAR-----------HVLEIRRE 93
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV------LWQGEPIRRQRdeyhqdllylgHQPGIKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 94 TVGWVS-QFLRVIPRISTLNVVIQPLLERGMSRQEseirggellthlNVPERlwslapaTFSGGEQQRINIARGFIGDYP 172
Cdd:PRK13538 89 LTALENlRFYQRLHGPGDDEALWEALAQVGLAGFE------------DVPVR-------QLSAGQQRRVALARLWLTRAP 149
|
170 180 190
....*....|....*....|....*....|....*
gi 499404648 173 ILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVV 206
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALLAQhAEQGGMVIL 184
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-226 |
8.48e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.10 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVdktfVLYnqqgTRLPVFHDINLSVKCGECVALHGHSGTGKS-TLLRSLygNYRPDGghiwVRhreRWVDI 79
Cdd:PRK10418 1 MPQQIELRNI----ALQ----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAAL--GILPAG----VR---QTAGR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 80 VNADARHVL--EIRRETVGWVSQFlrviPRiSTLNVV-------IQPLLERGMSRQESEIRGGELLTHLNVPERLWSLAP 150
Cdd:PRK10418 64 VLLDGKPVApcALRGRKIATIMQN----PR-SAFNPLhtmhthaRETCLALGKPADDATLTAALEAVGLENAARVLKLYP 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 151 ATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADRLYSMA 226
Cdd:PRK10418 139 FEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESiVQKRALGMLLVTHDMGVVARLADDVAVMS 215
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-210 |
8.79e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.17 E-value: 8.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTFvlynqQGTRlpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERwvdiV 80
Cdd:PRK10762 1 MQALLQLKGIDKAF-----PGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV----T 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 NADARHVLEirrETVGWVSQFLRVIPRISTL-NVviqpLLERGMSRQESEI-------RGGELLTHLNVPERLWSLApAT 152
Cdd:PRK10762 70 FNGPKSSQE---AGIGIIHQELNLIPQLTIAeNI----FLGREFVNRFGRIdwkkmyaEADKLLARLNLRFSSDKLV-GE 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499404648 153 FSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFH 210
Cdd:PRK10762 142 LSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISH 199
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-196 |
9.40e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 15 VLYNQQgtrlPVFHDINLSVKCGECVALHGHSGTGKSTLLR--------------SLYGNYRPDGGHIWvrhrerwvDIv 80
Cdd:PRK10938 268 VSYNDR----PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSlitgdhpqgysndlTLFGRRRGSGETIW--------DI- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 nadARHVleirretvGWVSQFLRVIPRIST--LNVVIQPLLER-GMSRQESE---IRGGELLTHLNVPERLwslAPATF- 153
Cdd:PRK10938 335 ---KKHI--------GYVSSSLHLDYRVSTsvRNVILSGFFDSiGIYQAVSDrqqKLAQQWLDILGIDKRT---ADAPFh 400
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499404648 154 --SGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLID 196
Cdd:PRK10938 401 slSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVD 445
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
37-227 |
9.66e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 9.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 37 GECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdIVNADARHVLEIRREtVGWVSQ--FLRVIPRISTLNVV 114
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQR----IDTLSPGKLQALRRD-IQFIFQdpYASLDPRQTVGDSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 115 IQPLLERGMSR-QESEIRGGELLTHLNV-PERLWSLaPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVT 192
Cdd:PRK10261 425 MEPLRVHGLLPgKAAAARVAWLLERVGLlPEHAWRY-PHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQII 503
|
170 180 190
....*....|....*....|....*....|....*.
gi 499404648 193 QL-IDDAKSKGCAVVGIFHDDEVRQHVADRLYSMAM 227
Cdd:PRK10261 504 NLlLDLQRDFGIAYLFISHDMAVVERISHRVAVMYL 539
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
1.16e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.13 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTFvlynQQGTRlpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiV 80
Cdd:PRK13647 1 MDNIIEVEDLHFRY----KDGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE-----V 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 NadARHVLEIRREtVGWVSQFL--RVIPRISTLNVVIQPlLERGMSRQESEIRGGELLTHLnvpeRLWSL---APATFSG 155
Cdd:PRK13647 70 N--AENEKWVRSK-VGLVFQDPddQVFSSTVWDDVAFGP-VNMGLDKDEVERRVEEALKAV----RMWDFrdkPPYHLSY 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 156 GEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRL 222
Cdd:PRK13647 142 GQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQV 208
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-190 |
1.17e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 60.24 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 4 QLRIENVDKTFvlynqqGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvdIVNAd 83
Cdd:PRK11650 3 GLKLQAVRKSY------DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR-----VVNE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 84 arhvLEIRRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVpERLWSLAPATFSGGEQQRINI 163
Cdd:PRK11650 71 ----LEPADRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILEL-EPLLDRKPRELSGGQRQRVAM 145
|
170 180
....*....|....*....|....*..
gi 499404648 164 ARGFIGDYPILLLDEPTASLDAKNRLA 190
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAKLRVQ 172
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
15-184 |
1.24e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.79 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 15 VLYNQQGTrlpvFHDINLSVKCGECVALHGHSGTGKSTLLRSL--YGNYRPD----GGHIWVRHrerwvDIVNADARHVl 88
Cdd:PRK14239 13 VYYNKKKA----LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtitGSIVYNGH-----NIYSPRTDTV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 89 EIRREtVGWVSQFLRVIPrISTLNVVIQPLLERGMSRQ-------ESEIRGGELLTHlnVPERLWSLAPAtFSGGEQQRI 161
Cdd:PRK14239 83 DLRKE-IGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKqvldeavEKSLKGASIWDE--VKDRLHDSALG-LSGGQQQRV 157
|
170 180
....*....|....*....|...
gi 499404648 162 NIARGFIGDYPILLLDEPTASLD 184
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALD 180
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
29-221 |
1.69e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.19 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYrPDG---GHIWVRHRE-RWVDIVNADARHVLEIRREtvgwvsqfLRV 104
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVcRFKDIRDSEALGIVIIHQE--------LAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 IPRIS-TLNVVI-QPLLERG-MSRQESEIRGGELLTHLNVPErlwslAPATFSG----GEQQRINIARGFIGDYPILLLD 177
Cdd:NF040905 90 IPYLSiAENIFLgNERAKRGvIDWNETNRRARELLAKVGLDE-----SPDTLVTdigvGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499404648 178 EPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD-DEVRQhVADR 221
Cdd:NF040905 165 EPTAALNEEDSAALLDLLLELKAQGITSIIISHKlNEIRR-VADS 208
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
30-225 |
1.77e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 59.23 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 30 INLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiVNADARHvlEIRRETVGWVSQFLRVIPRIS 109
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQH-----IEGLPGH--QIARMGVVRTFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 110 TLN--VVIQPL-LERGM------------SRQESEIRGGELLTHLNvperLWSLA--PA-TFSGGEQQRINIARGFIGDY 171
Cdd:PRK11300 97 VIEnlLVAQHQqLKTGLfsgllktpafrrAESEALDRAATWLERVG----LLEHAnrQAgNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 172 PILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
25-210 |
1.88e-10 |
|
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: 58.66 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrhrerwvdivnaDARHVLEIRRETvgwvsqfLRv 104
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI------------DGVDISKIGLHD-------LR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 ipriSTLNVVIQ-PLLERGMSRQ---------ESEIRGGELLTHL-----NVPERLWSLA---PATFSGGEQQRINIARG 166
Cdd:cd03244 78 ----SRISIIPQdPVLFSGTIRSnldpfgeysDEELWQALERVGLkefveSLPGGLDTVVeegGENLSVGQRQLLCLARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499404648 167 FIGDYPILLLDEPTASLDAKNRLAVTQLIDDAkSKGCAVVGIFH 210
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREA-FKDCTVLTIAH 196
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-225 |
2.81e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 58.95 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVdktfVLYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYrpdgghiwvrhrERWVDIV 80
Cdd:PRK13642 1 MNKILEVENL----VFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLF------------EEFEGKV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 NAD-----ARHVLEIRREtVGWV-----SQFLRVipriSTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPErLWSLAP 150
Cdd:PRK13642 65 KIDgelltAENVWNLRRK-IGMVfqnpdNQFVGA----TVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLD-FKTREP 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404648 151 ATFSGGEQQRINIArGFIGDYP-ILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHD-DEVRQhvADRLYSM 225
Cdd:PRK13642 139 ARLSGGQKQRVAVA-GIIALRPeIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDlDEAAS--SDRILVM 213
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-195 |
3.08e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.96 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHI--------WVRHRERWVDIVNADARH-VLEIRRETV 95
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkldggdidDPDVAEACHYLGHRNAMKpALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 96 GWvSQFLRviprisTLNVVIQPLLER-GMSRQEsEIRGGELlthlnvperlwslapatfSGGEQQRINIARGFIGDYPIL 174
Cdd:PRK13539 96 FW-AAFLG------GEELDIAAALEAvGLAPLA-HLPFGYL------------------SAGQKRRVALARLLVSNRPIW 149
|
170 180
....*....|....*....|.
gi 499404648 175 LLDEPTASLDAKNRLAVTQLI 195
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELI 170
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
29-184 |
4.86e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 58.73 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdIVNADARHVLEIRRETVGWVSQFLRVIPRI 108
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRV----LFDAEKGICLPPEKRRIGYVFQDARLFPHY 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404648 109 StlnvvIQPLLERGMSRQESEiRGGELLTHLNVpERLWSLAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLD 184
Cdd:PRK11144 92 K-----VRGNLRYGMAKSMVA-QFDKIVALLGI-EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
29-225 |
5.07e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 58.32 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiVNADARHVLEIrRETVGWVSQ------FL 102
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP-----IDYSRKGLMKL-RESVGMVFQdpdnqlFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 103 RVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWslapatFSGGEQQRINIARGFIGDYPILLLDEPTAS 182
Cdd:PRK13636 98 ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHC------LSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499404648 183 LDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK13636 172 LDPMGVSEIMKLLVEmQKELGLTIIIATHDIDIVPLYCDNVFVM 215
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-210 |
5.07e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 58.91 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 28 HDINLSVKCGECVALHGHSGTGKSTLLRSLyGNYRPDGghiwvrhRERWVDI-VNADARHVLEIRRETvGWVSQFLRVIP 106
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKG-------VKGSGSVlLNGMPIDAKEMRAIS-AYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 107 RIST---LNVVIQPLLERGMSRQESEIRGGELLTHLN----------VPERLWSLapatfSGGEQQRINIARGFIGDYPI 173
Cdd:TIGR00955 113 TLTVrehLMFQAHLRMPRRVTKKEKRERVDEVLQALGlrkcantrigVPGRVKGL-----SGGERKRLAFASELLTDPPL 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 499404648 174 LLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFH 210
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-222 |
7.10e-10 |
|
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: 58.26 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 33 SVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhrERWVDI------VNADARhvleirretvGWVSQFLR--V 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----DEDLKIsykpqyISPDYD----------GTVEEFLRsaN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 IPRIST---LNVVIQPL-LERGMsrqESEIRggELlthlnvperlwslapatfSGGEQQRINIARGFIGDYPILLLDEPT 180
Cdd:COG1245 427 TDDFGSsyyKTEIIKPLgLEKLL---DKNVK--DL------------------SGGELQRVAIAACLSRDADLYLLDEPS 483
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499404648 181 ASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADRL 222
Cdd:COG1245 484 AHLDVEQRLAVAKAIRRfAENRGKTAMVVDHDIYLIDYISDRL 526
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
26-226 |
7.38e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.53 E-value: 7.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERWVdiVNADARHVLEIrretvgwvsqflrvi 105
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVT--LNGEPLAAIDA--------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 106 PRISTLNVVIQPLLERGMSRQESEI----------RGGELLTHL-NVPERLWSLAPA---------TFSGGEQQRINIAR 165
Cdd:PRK13547 79 PRLARLRAVLPQAAQPAFAFSAREIvllgrypharRAGALTHRDgEIAWQALALAGAtalvgrdvtTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404648 166 GFIGDYP---------ILLLDEPTASLDA--KNRLAVTqLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSMA 226
Cdd:PRK13547 159 VLAQLWPphdaaqpprYLLLDEPTAALDLahQHRLLDT-VRRLARDWNLGVLAIVHDPNLAARHADRIAMLA 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-225 |
8.00e-10 |
|
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: 58.49 E-value: 8.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERWVDIVNAda 84
Cdd:TIGR01257 1938 LRLNELTKVY-----SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV-- 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 rhvleirRETVGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLApATFSGGEQQRINIA 164
Cdd:TIGR01257 2011 -------HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLA-GTYSGGNKRKLSTA 2082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-220 |
1.02e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.10 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 2 DTQLRIENVDktfVLYnqqGTRLPVfHDINLSVKCGECVALHGHSGTGKSTLLR------SLYGNYRPDGGHIWVRHrer 75
Cdd:PRK14243 8 ETVLRTENLN---VYY---GSFLAV-KNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlnDLIPGFRVEGKVTFHGK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 76 wvdivNADARHV--LEIRREtVGWVSQ----FLRVI-------PRISTLNVVIQPLLERGMsRQESeirggellthlnvp 142
Cdd:PRK14243 78 -----NLYAPDVdpVEVRRR-IGMVFQkpnpFPKSIydniaygARINGYKGDMDELVERSL-RQAA-------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 143 erLWS-------LAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVgIFHDDEVR 215
Cdd:PRK14243 137 --LWDevkdklkQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIII-VTHNMQQA 213
|
....*
gi 499404648 216 QHVAD 220
Cdd:PRK14243 214 ARVSD 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
37-225 |
1.43e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.58 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 37 GECVALHGHSGTGKSTLLRSLYGNYRPDG--GHIWVRHRERwvdivnadARHVLeiRRetVGWVSQFLRVIPRIS---TL 111
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP--------TKQIL--KR--TGFVTQDDILYPHLTvreTL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 112 NVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLAPATF----SGGEQQRINIARGFIGDYPILLLDEPTASLDAKN 187
Cdd:PLN03211 162 VFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180 190
....*....|....*....|....*....|....*...
gi 499404648 188 RLAVTQLIDDAKSKGCAVVGIFHDDevrqhvADRLYSM 225
Cdd:PLN03211 242 AYRLVLTLGSLAQKGKTIVTSMHQP------SSRVYQM 273
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-223 |
1.56e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.55 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiVNADARHVLEIRRETVGWVSQFLRV 104
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKP-----LDYSKRGLLALRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 IPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVpERLWSLAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLD 184
Cdd:PRK13638 90 IFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDA-QHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 499404648 185 AKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRLY 223
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVY 207
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
14-211 |
1.58e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.49 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 14 FVLYnqqgtRLPVfhdinlsVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHI-----W--VRHRER-------WVDI 79
Cdd:COG1245 88 FRLY-----GLPV-------PKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepsWdeVLKRFRgtelqdyFKKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 80 VNADARHVLEIrretvgwvsQFLRVIPRISTLNVviQPLL----ERGMSRqeseirggELLTHLNVpERLWSLAPATFSG 155
Cdd:COG1245 156 ANGEIKVAHKP---------QYVDLIPKVFKGTV--RELLekvdERGKLD--------ELAEKLGL-ENILDRDISELSG 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499404648 156 GEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD 211
Cdd:COG1245 216 GELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHD 271
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-184 |
1.73e-09 |
|
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: 56.79 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvRHRERwvdivnadarhvleirretVGWVSQFLRV 104
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--KHSGR-------------------ISFSSQFSWI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 IPRISTLNVVIqpllerGMS----RQESEIRGGELLTHL-NVPERLWSL---APATFSGGEQQRINIARGFIGDYPILLL 176
Cdd:cd03291 110 MPGTIKENIIF------GVSydeyRYKSVVKACQLEEDItKFPEKDNTVlgeGGITLSGGQRARISLARAVYKDADLYLL 183
|
....*...
gi 499404648 177 DEPTASLD 184
Cdd:cd03291 184 DSPFGYLD 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
25-211 |
1.81e-09 |
|
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: 56.19 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERWVDivnaDARHVLEI-----RRETVGWVs 99
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKR----RKKFLRRIgvvfgQKTQLWWD- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 100 qflrvIPRISTLNVV--IQPLLERGMSRQESEIrgGELL--TH-LNVPERLWSLapatfsgGEQQRINIARGFIGDYPIL 174
Cdd:cd03267 110 -----LPVIDSFYLLaaIYDLPPARFKKRLDEL--SELLdlEElLDTPVRQLSL-------GQRMRAEIAAALLHEPEIL 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 499404648 175 LLDEPTASLDAKNRLAVTQLIDDA-KSKGCAVVGIFHD 211
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHY 213
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
25-184 |
2.37e-09 |
|
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: 55.50 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhrerwvDIVNADARHV-LEIRRETVGWVSQflr 103
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI---------EIDGIDISTIpLEDLRSSLTIIPQ--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 104 vipristlnvviQPLLERGMSRQ----ESEIRGGELLTHLNVPErlwslAPATFSGGEQQRINIARGFIGDYPILLLDEP 179
Cdd:cd03369 90 ------------DPTLFSGTIRSnldpFDEYSDEEIYGALRVSE-----GGLNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
....*
gi 499404648 180 TASLD 184
Cdd:cd03369 153 TASID 157
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-185 |
3.16e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.71 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 28 HDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERWVD----IVNADAR-HVLEIRRETVGWVSQFL 102
Cdd:PTZ00243 677 RDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPqqawIMNATVRgNILFFDEEDAARLADAV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 103 RVipriSTLNVVIQpLLERGMsrqESEIrgGELLTHLnvperlwslapatfSGGEQQRINIARGFIGDYPILLLDEPTAS 182
Cdd:PTZ00243 757 RV----SQLEADLA-QLGGGL---ETEI--GEKGVNL--------------SGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
...
gi 499404648 183 LDA 185
Cdd:PTZ00243 813 LDA 815
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-225 |
5.54e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.18 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 3 TQLRIENVDKTFVLyNQQGTRLP---VFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHR--ERWV 77
Cdd:PRK10575 1 MQEYTNHSDTTFAL-RNVSFRVPgrtLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 78 DivNADARHVLEIRRE---TVGWVSQFLRVIPRISTLNVViqpllerGMSRQESEIRGGELLThlnvperLWSLAP---- 150
Cdd:PRK10575 80 S--KAFARKVAYLPQQlpaAEGMTVRELVAIGRYPWHGAL-------GRFGAADREKVEEAIS-------LVGLKPlahr 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404648 151 --ATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK10575 144 lvDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRlSQERGLTVIAVLHDINMAARYCDYLVAL 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
29-225 |
6.20e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.01 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVAlhGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwvdiVNADARHVLEIR--RETVGWVSQF--LRV 104
Cdd:PRK13645 31 SLTFKKNKVTCVI--GTTGSGKSTMIQLTNGLIISETGQTIVGDYA-----IPANLKKIKEVKrlRKEIGLVFQFpeYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 IPRISTLNVVIQPLlERGMSRQESEIRGGELLTHLNVPERLWSLAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLD 184
Cdd:PRK13645 104 FQETIEKDIAFGPV-NLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499404648 185 AKNRLAVTQLIDDA-KSKGCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK13645 183 PKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-212 |
6.94e-09 |
|
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: 54.04 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvdivnADARHVLEIRRE-----------T 94
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG--------PLDFQRDSIARGllylghapgikT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 95 VGWVSQFLRVIPRISTLNVVIQPLLERGMSRQESeirggellthlnvperlwsLAPATFSGGEQQRINIARGFIGDYPIL 174
Cdd:cd03231 87 TLSVLENLRFWHADHSDEQVEEALARVGLNGFED-------------------RPVAQLSAGQQRRVALARLLLSGRPLW 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 499404648 175 LLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDD 212
Cdd:cd03231 148 ILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-184 |
7.86e-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: 55.69 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvRHRERwvdivnadarhvleirretVGWVSQFLRV 104
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--KHSGR-------------------ISFSPQTSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 IPRISTLNVVIqpllerGMS----RQESEIRGGELLTHLNV-PER---LWSLAPATFSGGEQQRINIARGFIGDYPILLL 176
Cdd:TIGR01271 499 MPGTIKDNIIF------GLSydeyRYTSVIKACQLEEDIALfPEKdktVLGEGGITLSGGQRARISLARAVYKDADLYLL 572
|
....*...
gi 499404648 177 DEPTASLD 184
Cdd:TIGR01271 573 DSPFTHLD 580
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-225 |
1.14e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.03 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTFV----LYNQQgtRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWV------ 70
Cdd:PRK15112 1 VETLLEVRNLSKTFRyrtgWFRRQ--TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddhplh 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 71 ----RHRERWVDIVNADARHVLEIRREtvgwVSQFLRVIPRISTlnvviqpllerGMSRQESEIRGGELLTHLNVPERLW 146
Cdd:PRK15112 79 fgdySYRSQRIRMIFQDPSTSLNPRQR----ISQILDFPLRLNT-----------DLEPEQREKQIIETLRQVGLLPDHA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 147 SLAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK-GCAVVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK15112 144 SYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVM 223
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
30-225 |
1.32e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.59 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 30 INLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVDIVNADArhvleirretvgwvsqFLRVIPRIS 109
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP--VTAEQPED----------------YRKLFSAVF 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 110 TLNVVIQPLLERGMSRQESEIrGGELLTHLNVPERL----WSLAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDA 185
Cdd:PRK10522 404 TDFHLFDQLLGPEGKPANPAL-VEKWLERLKMAHKLeledGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499404648 186 K-NRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHvADRLYSM 225
Cdd:PRK10522 483 HfRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEM 522
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-199 |
1.44e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERWVDIVnadarhvLEIRRETVGWVSQ----F 101
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDIN-------LKWWRSKIGVVSQdpllF 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 102 LRVIPR--------ISTLNVVIQPLLERGMSRQES----------------------------EIR-------------- 131
Cdd:PTZ00265 473 SNSIKNnikyslysLKDLEALSNYYNEDGNDSQENknkrnscrakcagdlndmsnttdsneliEMRknyqtikdsevvdv 552
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499404648 132 GGELLTHLNV---PERLWSLA---PATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAK 199
Cdd:PTZ00265 553 SKKVLIHDFVsalPDKYETLVgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLK 626
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
14-211 |
3.01e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 14 FVLYnqqgtRLPVfhdinlsVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGhiwvRHRER--WVDIVNADARHVL--- 88
Cdd:PRK13409 88 FKLY-----GLPI-------PKEGKVTGILGPNGIGKTTAVKILSGELIPNLG----DYEEEpsWDEVLKRFRGTELqny 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 89 -------EIRretvgwVS---QFLRVIPRISTLNV--VIQPLLERGMSRqeseirggELLTHLNVpERLWSLAPATFSGG 156
Cdd:PRK13409 152 fkklyngEIK------VVhkpQYVDLIPKVFKGKVreLLKKVDERGKLD--------EVVERLGL-ENILDRDISELSGG 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 157 EQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAkSKGCAVVGIFHD 211
Cdd:PRK13409 217 ELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIREL-AEGKYVLVVEHD 270
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
25-210 |
3.26e-08 |
|
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: 51.39 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLygnyrpdgGHIWVRHRERWVdivnadaRHvleiRRETVGWVSQflrv 104
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL--------AGLWPWGSGRIG-------MP----EGEDLLFLPQ---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 ipristlnvviQPLLERGMSRQEseirggellthLNVPerlWSlapATFSGGEQQRINIARGFIGDYPILLLDEPTASLD 184
Cdd:cd03223 72 -----------RPYLPLGTLREQ-----------LIYP---WD---DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180
....*....|....*....|....*.
gi 499404648 185 AKNRLAVTQLIddaKSKGCAVVGIFH 210
Cdd:cd03223 124 EESEDRLYQLL---KELGITVISVGH 146
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-233 |
4.25e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.88 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNY--RPDGGHIWVRHRERWVDIVNADArhvleirretvgwvsqfl 102
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREASLIDA------------------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 103 rvIPRISTLNVVIQPLLERGMSrqeseirggellthlNVPerLWSLAPATFSGGEQQRINIARGFIGDYPILLLDEPTAS 182
Cdd:COG2401 106 --IGRKGDFKDAVELLNAVGLS---------------DAV--LWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 183 LD---AKnRLAVTqLIDDAKSKGCAVVGIFHDDEVRQHVA-DRLYSMAMTSRTQE 233
Cdd:COG2401 167 LDrqtAK-RVARN-LQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPEE 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-221 |
5.11e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.41 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLRSL------YGNYRPDGgHIWVRHRERWvdivnaDARHVLEIRREtVGWVS 99
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkVSGYRYSG-DVLLGGRSIF------NYRDVLEFRRR-VGMLF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 100 QFLRVIPRISTLNVVI----QPLLERGMSRQESEIRGGELLTHLNVPERLwSLAPATFSGGEQQRINIARGFIGDYPILL 175
Cdd:PRK14271 108 QRPNPFPMSIMDNVLAgvraHKLVPRKEFRGVAQARLTEVGLWDAVKDRL-SDSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499404648 176 LDEPTASLDAKNRLAVTQLIDDAKSKgCAVVGIFHDDEVRQHVADR 221
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDR 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
29-211 |
6.05e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 52.34 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrHRERWVDIVNADarhvleirrETVGWVSQFLRVIPRI 108
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRMNDVPPAE---------RGVGMVFQSYALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 109 STLNVVIQPLLERGMSRQESEIR---GGELLTHLNVPERLwslaPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDA 185
Cdd:PRK11000 91 SVAENMSFGLKLAGAKKEEINQRvnqVAEVLQLAHLLDRK----PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
170 180 190
....*....|....*....|....*....|
gi 499404648 186 ----KNRLAVTQLiddAKSKGCAVVGIFHD 211
Cdd:PRK11000 167 alrvQMRIEISRL---HKRLGRTMIYVTHD 193
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-208 |
6.69e-08 |
|
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: 52.52 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 2 DTQLRIENVdktfVLYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPD-GGHIWVRHRErwVDIV 80
Cdd:TIGR02633 255 DVILEARNL----TCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKP--VDIR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 81 N-ADA-RH----VLEIRRETvGWVSQfLRVIPRIsTLNVvIQPLLERGMSRQESEIRG-GELLTHLNVPERLWSLAPATF 153
Cdd:TIGR02633 329 NpAQAiRAgiamVPEDRKRH-GIVPI-LGVGKNI-TLSV-LKSFCFKMRIDAAAELQIiGSAIQRLKVKTASPFLPIGRL 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 154 SGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGI 208
Cdd:TIGR02633 405 SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVV 459
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-184 |
8.44e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.00 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrhrerwvdivnaDARHVLEIRRET-VGWVSQFLR 103
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI------------DGKTATRGDRSRfMAYLGHLPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 104 VIPRISTL-NVVIQPLLERGMSRQESeirgGELLTHLNVPERLWSLApATFSGGEQQRINIARGFIGDYPILLLDEPTAS 182
Cdd:PRK13543 93 LKADLSTLeNLHFLCGLHGRRAKQMP----GSALAIVGLAGYEDTLV-RQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
..
gi 499404648 183 LD 184
Cdd:PRK13543 168 LD 169
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-225 |
8.79e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 2 DTQLRIENVdktfvlynqQGTRLPvfHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRErwVDIVN 81
Cdd:PRK11288 255 EVRLRLDGL---------KGPGLR--EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKP--IDIRS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 82 -ADA-RH--VL--EIRRE----TVGWVSQFLRVIPR--ISTLNVVIQPLLERGMSRQesEIRggelltHLNVPERLWSLA 149
Cdd:PRK11288 322 pRDAiRAgiMLcpEDRKAegiiPVHSVADNINISARrhHLRAGCLINNRWEAENADR--FIR------SLNIKTPSREQL 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499404648 150 PATFSGGEQQRINIARGFIGDYPILLLDEPTASLD--AKNRlaVTQLIDDAKSKGCAVVGIFHD-DEVrQHVADRLYSM 225
Cdd:PRK11288 394 IMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDvgAKHE--IYNVIYELAAQGVAVLFVSSDlPEV-LGVADRIVVM 469
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-208 |
1.19e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 2 DTQLRIENVdktfVLYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRpdG---GHIWVRHRErwVD 78
Cdd:PRK13549 257 EVILEVRNL----TAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GrweGEIFIDGKP--VK 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 79 IVN-ADA-RH----VLEIRRETvGWVSQfLRVIPRIsTLnVVIQPLLERGMSRQESEIRG-GELLTHLNV----PErlws 147
Cdd:PRK13549 329 IRNpQQAiAQgiamVPEDRKRD-GIVPV-MGVGKNI-TL-AALDRFTGGSRIDDAAELKTiLESIQRLKVktasPE---- 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404648 148 LAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGI 208
Cdd:PRK13549 401 LAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
30-211 |
1.28e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 50.99 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 30 INLSVKCGECVALHGHSGTGKSTLLRSLYGnYRPDGGHIWVRHRerwvDIVNADARHVLEIRretvGWVSQ------FLR 103
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGR----PLSDWSAAELARHR----AYLSQqqsppfAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 104 V-------IPR-------ISTLNVVIQPL-LERGMSRQeseirggelLTHLnvperlwslapatfSGGEQQRINIARGFI 168
Cdd:COG4138 86 VfqylalhQPAgasseavEQLLAQLAEALgLEDKLSRP---------LTQL--------------SGGEWQRVRLAAVLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499404648 169 GDYP-------ILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD 211
Cdd:COG4138 143 QVWPtinpegqLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHD 192
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-223 |
1.60e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRLpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRERwvdiVNADA 84
Cdd:PRK10636 313 LKMEKVSAGY------GDRI-ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIK----LGYFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 85 RHVLEIRRETVGWVSQFLRVIPRIstlnvviqpllergMSRQESEIRGGELLTHLNVPErlwslAPATFSGGEQQRINIA 164
Cdd:PRK10636 382 QHQLEFLRADESPLQHLARLAPQE--------------LEQKLRDYLGGFGFQGDKVTE-----ETRRFSGGEKARLVLA 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 165 RGFIGDYPILLLDEPTASLDAKNRLAVTQ-LIDdakSKGCAVVgIFHDDEVRQHVADRLY 223
Cdd:PRK10636 443 LIVWQRPNLLLLDEPTNHLDLDMRQALTEaLID---FEGALVV-VSHDRHLLRSTTDDLY 498
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
29-211 |
1.85e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.52 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 29 DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvdIVNAdarHVLEIRRETVGWV-----SQFLR 103
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ-----AITD---DNFEKLRKHIGIVfqnpdNQFVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 104 vipriSTLNVVIQPLLERGM-SRQESEIRGGELLTHLNVPERLWSlAPATFSGGEQQRINIARGFIGDYPILLLDEPTAS 182
Cdd:PRK13648 99 -----SIVKYDVAFGLENHAvPYDEMHRRVSEALKQVDMLERADY-EPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190
....*....|....*....|....*....|
gi 499404648 183 LDAKNRLAVTQLIDDAKS-KGCAVVGIFHD 211
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSeHNITIISITHD 202
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-210 |
2.78e-07 |
|
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: 49.16 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 21 GTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGnyRPDGGHIwvrhrerwVDIVNADARHVLEIRRETVGWVSQ 100
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVI--------TGEILINGRPLDKNFQRSTGYVEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 101 flrvipristlnvviQPLLERGMSRQESeIRGGELLTHLNVPERlwslapatfsggeqQRINIARGFIGDYPILLLDEPT 180
Cdd:cd03232 87 ---------------QDVHSPNLTVREA-LRFSALLRGLSVEQR--------------KRLTIGVELAAKPSILFLDEPT 136
|
170 180 190
....*....|....*....|....*....|
gi 499404648 181 ASLDAKNRLAVTQLIDDAKSKGCAVVGIFH 210
Cdd:cd03232 137 SGLDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
123-200 |
5.36e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.73 E-value: 5.36e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404648 123 MSRQESEIRGGELLTHLNVPERLwSLAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRlavTQLIDDAKS 200
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAA-GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR---NEVWDEVRS 189
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-218 |
7.65e-07 |
|
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: 49.16 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 5 LRIENVDKTFvlynqqGTRLpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwVDIVNAD- 83
Cdd:TIGR03719 323 IEAENLTKAF------GDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET---VKLAYVDq 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 84 ARHVLEIRReTVgW--VSQFLRVIpRISTLNVVIQPLLER-GMSRQESEIRGGELlthlnvperlwslapatfSGGEQQR 160
Cdd:TIGR03719 393 SRDALDPNK-TV-WeeISGGLDII-KLGKREIPSRAYVGRfNFKGSDQQKKVGQL------------------SGGERNR 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404648 161 INIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAksKGCAVVgIFHD----DEVRQHV 218
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVV-ISHDrwflDRIATHI 510
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
152-201 |
7.87e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 7.87e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 499404648 152 TFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSK 201
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK 1407
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
154-222 |
1.11e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.57 E-value: 1.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 154 SGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIF-HDDEVRQHVADRL 222
Cdd:cd03222 73 SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVeHDLAVLDYLSDRI 142
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
24-185 |
1.50e-06 |
|
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: 47.26 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 24 LPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYG----NYRPDG--------GHIWVRHRERWVDIVNADARHvleir 91
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSVEGdihyngipYKEFAEKYPGEIIYVSEEDVH----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 92 retvgwvsqflrviprISTLNVviQPLLERGMSRQESE-IRGgellthlnvperlwslapatFSGGEQQRINIARGFIGD 170
Cdd:cd03233 95 ----------------FPTLTV--RETLDFALRCKGNEfVRG--------------------ISGGERKRVSIAEALVSR 136
|
170
....*....|....*
gi 499404648 171 YPILLLDEPTASLDA 185
Cdd:cd03233 137 ASVLCWDNSTRGLDS 151
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
30-225 |
1.73e-06 |
|
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: 48.26 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 30 INLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVrhrerwvdivnaDARHVLEIRREtvgWVSQFLRVI---- 105
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL------------DGQPVTADNRE---AYRQLFSAVfsdf 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 106 --------PRISTLNVVIQPLLER-GMSRQESeIRGGELLT-HLnvperlwslapatfSGGEQQRINIARGFIGDYPILL 175
Cdd:COG4615 416 hlfdrllgLDGEADPARARELLERlELDHKVS-VEDGRFSTtDL--------------SQGQRKRLALLVALLEDRPILV 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499404648 176 LDEPTASLDAKNRlAV--TQLIDDAKSKGCAVVGIFHDDevRQ-HVADRLYSM 225
Cdd:COG4615 481 FDEWAADQDPEFR-RVfyTELLPELKARGKTVIAISHDD--RYfDLADRVLKM 530
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
25-210 |
2.41e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.33 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGN--YRPDGGHIWVRHRerwvDIVNADARhvlEIRRETVGWVSQFL 102
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGE----SILDLEPE---ERAHLGIFLAFQYP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 103 RVIPRISTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLAPA--------TFSGGEQQRINIARGFIGDYPIL 174
Cdd:CHL00131 94 IEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSflsrnvneGFSGGEKKRNEILQMALLDSELA 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 499404648 175 LLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFH 210
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
9-225 |
2.57e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.43 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 9 NVDKTFVLYNQQGTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhrerwVDIVNADARHVL 88
Cdd:PRK11022 5 NVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVM--------AEKLEFNGQDLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 89 EI----RRETVGWVSQFLRVIPRIS-----TLNVVIQPLLE--RGMSRQESEIRGGELLTHLNVPE---RLwSLAPATFS 154
Cdd:PRK11022 77 RIsekeRRNLVGAEVAMIFQDPMTSlnpcyTVGFQIMEAIKvhQGGNKKTRRQRAIDLLNQVGIPDpasRL-DVYPHQLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404648 155 GGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGC-AVVGIFHDDEVRQHVADRLYSM 225
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLALVAEAAHKIIVM 227
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-212 |
4.02e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.10 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVRHRerwvdivnadarhvlEIRRETVGWVSQFLRV 104
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ---------------SIKKDLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 IPRIST---LNVVIQPLLERGMSRQESEIRggELLTHLNVpERLWSLAPATFSGGEQQRINIARGFIGDYPILLLDEPTA 181
Cdd:PRK13540 80 GHRSGInpyLTLRENCLYDIHFSPGAVGIT--ELCRLFSL-EHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190
....*....|....*....|....*....|.
gi 499404648 182 SLDAKNRLAVTQLIDDAKSKGCAVVGIFHDD 212
Cdd:PRK13540 157 ALDELSLLTIITKIQEHRAKGGAVLLTSHQD 187
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-185 |
4.10e-06 |
|
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: 47.25 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrHRERWVDIVNADARHVLEIRRETVGWVSQFLRV 104
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV---HMKGSVAYVPQQAWIQNDSLRENILFGKALNEK 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 105 IPRISTLNVVIQPLLERGMSRQESEIrgGELLTHLnvperlwslapatfSGGEQQRINIARGFIGDYPILLLDEPTASLD 184
Cdd:TIGR00957 729 YYQQVLEACALLPDLEILPSGDRTEI--GEKGVNL--------------SGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
.
gi 499404648 185 A 185
Cdd:TIGR00957 793 A 793
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
39-223 |
5.17e-06 |
|
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: 45.68 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 39 CVALHGHSGTGKSTLLR----SLYGNYRP--DGGHIW---VRHRERWVDI---VNADARHVLEIRREtvgwVSQFLRVIp 106
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEalkyALTGELPPnsKGGAHDpklIREGEVRAQVklaFENANGKKYTITRS----LAILENVI- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 107 ristlnvviqpllergMSRQEseirggellthlnvpERLWSLA--PATFSGGEQQ------RINIARGFIGDYPILLLDE 178
Cdd:cd03240 99 ----------------FCHQG---------------ESNWPLLdmRGRCSGGEKVlasliiRLALAETFGSNCGILALDE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499404648 179 PTASLDAKNR-LAVTQLIDDAKSKGC-AVVGIFHDDEVRQHvADRLY 223
Cdd:cd03240 148 PTTNLDEENIeESLAEIIEERKSQKNfQLIVITHDEELVDA-ADHIY 193
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
10-211 |
6.82e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.03 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 10 VDKTFVLYNQQGTRLpvfHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhrerwvDIVNADARHVLe 89
Cdd:PRK15056 9 VNDVTVTWRNGHTAL---RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI---------SILGQPTRQAL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 90 iRRETVGWVSQFLRVIpriSTLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLAPATF--------SGGEQQRI 161
Cdd:PRK15056 76 -QKNLVAYVPQSEEVD---WSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFrhrqigelSGGQKKRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499404648 162 NIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD 211
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
19-211 |
7.26e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 45.69 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 19 QQGTRL-PVfhdiNLSVKCGECVALHGHSGTGKSTLLRSLYGnYRPDGGHIWVRHRerwvDIVNADARHvLEIRRetvGW 97
Cdd:PRK03695 7 AVSTRLgPL----SAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQ----PLEAWSAAE-LARHR---AY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 98 VSQFLRVIPRIStlnvVIQPL-LERGMSRQESEIRG--GELLTHLNVPERLWSLApATFSGGEQQRINIARGFIGDYP-- 172
Cdd:PRK03695 74 LSQQQTPPFAMP----VFQYLtLHQPDKTRTEAVASalNEVAEALGLDDKLGRSV-NQLSGGEWQRVRLAAVVLQVWPdi 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499404648 173 -----ILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHD 211
Cdd:PRK03695 149 npagqLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHD 192
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-185 |
1.07e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 22 TRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPdgghiwvrHRERWVDIvnadarhvleirRETVGWVSQF 101
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH--------AETSSVVI------------RGSVAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 102 LRVIPRISTLNVVIQPLLE-----RGMS----RQESEIRGGELLTHLNvpERlwslaPATFSGGEQQRINIARGFIGDYP 172
Cdd:PLN03232 688 SWIFNATVRENILFGSDFEserywRAIDvtalQHDLDLLPGRDLTEIG--ER-----GVNISGGQKQRVSMARAVYSNSD 760
|
170
....*....|...
gi 499404648 173 ILLLDEPTASLDA 185
Cdd:PLN03232 761 IYIFDDPLSALDA 773
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
154-206 |
1.41e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.38 E-value: 1.41e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 499404648 154 SGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVV 206
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSII 449
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
25-211 |
3.47e-05 |
|
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: 44.16 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIWVR--------HRERWVDiVNADAR-HVLEIRRETV 95
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpgikvgylPQEPQLD-PTKTVReNVEEGVAEIK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 96 GWVSQFLRVIPRISTLNVVIQPLLERgMSRQESEIRGGELLTH----------LNVPErlWSLAPATFSGGEQQRINIAR 165
Cdd:TIGR03719 98 DALDRFNEISAKYAEPDADFDKLAAE-QAELQEIIDAADAWDLdsqleiamdaLRCPP--WDADVTKLSGGERRRVALCR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499404648 166 GFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSkgcAVVGIFHD 211
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTHD 217
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-186 |
4.18e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 43.93 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 21 GTRLPVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHIwvrhreRWVDIVNADARhvLEIRRETVGWVSQ 100
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI------RFHDIPLTKLQ--LDSWRSRLAVVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 101 flrvIPRISTLNVVIQPLLERGMSRQEsEIRGGELLThlNVPERLWSLAPA----------TFSGGEQQRINIARGFIGD 170
Cdd:PRK10789 397 ----TPFLFSDTVANNIALGRPDATQQ-EIEHVARLA--SVHDDILRLPQGydtevgergvMLSGGQKQRISIARALLLN 469
|
170
....*....|....*.
gi 499404648 171 YPILLLDEPTASLDAK 186
Cdd:PRK10789 470 AEILILDDALSAVDGR 485
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-185 |
5.90e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.96 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRP-DGGHIWVRHRERWVD----IVNADARhvleirrETVGWVS 99
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGTVAYVPqvswIFNATVR-------DNILFGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 100 QF-----LRVIpRISTLnvviqpllergmsRQESEIRGGELLTHLNvpERlwslaPATFSGGEQQRINIARGFIGDYPIL 174
Cdd:PLN03130 704 PFdperyERAI-DVTAL-------------QHDLDLLPGGDLTEIG--ER-----GVNISGGQKQRVSMARAVYSNSDVY 762
|
170
....*....|.
gi 499404648 175 LLDEPTASLDA 185
Cdd:PLN03130 763 IFDDPLSALDA 773
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
151-225 |
6.13e-05 |
|
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: 42.31 E-value: 6.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404648 151 ATFSGGEQQRINIARgFIGDYP---ILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHvADRLYSM 225
Cdd:cd03238 86 STLSGGELQRVKLAS-ELFSEPpgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDF 161
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-222 |
1.13e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 19 QQGTRLpVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGHI---------WVRHRERWVDIVNADarHVLE 89
Cdd:PRK10636 10 RRGVRV-LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlaWVNQETPALPQPALE--YVID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 90 IRRETVGWVSQFLRVIPR-----ISTLNV---VIQPLLERgmSRQESEIRG-GELLTHLNVPERlwslapaTFSGGEQQR 160
Cdd:PRK10636 87 GDREYRQLEAQLHDANERndghaIATIHGkldAIDAWTIR--SRAASLLHGlGFSNEQLERPVS-------DFSGGWRMR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404648 161 INIARGFIGDYPILLLDEPTASLDAKnrlAVTQLIDDAKSKGCAVVGIFHDDEVRQHVADRL 222
Cdd:PRK10636 158 LNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQGTLILISHDRDFLDPIVDKI 216
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
40-199 |
1.33e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.53 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 40 VALHGHSGTGKSTLLRS----LYGNYRPDGG----HIWVRHRERWVDIVNADARHVLEIRR----------ETVGWVSQF 101
Cdd:COG0419 26 NLIVGPNGAGKSTILEAiryaLYGKARSRSKlrsdLINVGSEEASVELEFEHGGKRYRIERrqgefaefleAKPSERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 102 LRVIPRISTLNVVIQPL--LERGMSRQESEIRGGELLTHLNVpERLWSLAPA-TFSGGEQQRINIArgfigDYPILLLDe 178
Cdd:COG0419 106 LKRLLGLEIYEELKERLkeLEEALESALEELAELQKLKQEIL-AQLSGLDPIeTLSGGERLRLALA-----DLLSLILD- 178
|
170 180
....*....|....*....|.
gi 499404648 179 pTASLDAKNRLAVTQLIDDAK 199
Cdd:COG0419 179 -FGSLDEERLERLLDALEELA 198
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
154-230 |
1.40e-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: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 154 SGGEQQRINIARGF----IGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQhVADRLYSMAMTS 229
Cdd:cd03227 79 SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAE-LADKLIHIKKVI 157
|
.
gi 499404648 230 R 230
Cdd:cd03227 158 T 158
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
128-184 |
1.43e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 1.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 128 SEIRGGELLTHLNVPERLWSLAPATFSGGEQQRINIARGFIGDYPILLLDEPTASLD 184
Cdd:PLN03073 320 AEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-68 |
1.46e-04 |
|
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: 40.82 E-value: 1.46e-04
10 20 30
....*....|....*....|....*....|..
gi 499404648 37 GECVALHGHSGTGKSTLLRSLYGNYRPDGGHI 68
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV 33
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-235 |
2.06e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 41.56 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 26 VFHDINLSVKCGECVALHGHSGTGKSTLLRSLyGNYRPDGGHIWVRHRERWVDIVNADARHVLEIRRETVGWVSQFLRVI 105
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYERRVNLNRLRRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 106 PRISTLNVVI-------QPLLERGmSRQESEIRGGELLTHlnVPERLWSLApATFSGGEQQRINIARGFIGDYPILLLDE 178
Cdd:PRK14258 101 PMSVYDNVAYgvkivgwRPKLEID-DIVESALKDADLWDE--IKHKIHKSA-LDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 179 PTASLDAKNRLAVTQLIDDAK-----------------SKGCAVVGIFHDDEVR--QHV----ADRLYSMAMTSRTQENV 235
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLRlrseltmvivshnlhqvSRLSDFTAFFKGNENRigQLVefglTKKIFNSPHDSRTREYV 256
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
152-208 |
2.34e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 2.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 499404648 152 TFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGI 208
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII 447
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
147-213 |
4.57e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 147 SLAPATFSGGEQQRINI----------ARGFIGDYPI--LLLDEPTASLDAKNrlaVTQ---LIDDAKSKGCA-VVGIFH 210
Cdd:PRK02224 776 PLEPEQLSGGERALFNLslrcaiyrllAEGIEGDAPLppLILDEPTVFLDSGH---VSQlvdLVESMRRLGVEqIVVVSH 852
|
...
gi 499404648 211 DDE 213
Cdd:PRK02224 853 DDE 855
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-211 |
6.58e-04 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 39.68 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 6 RIENVDKTfvlYNQQgtrlPVFHDINLSVKCGECVALHGHSGTGKSTLL----RSLygnyRPDGGHIWVRHRerwvDIVN 81
Cdd:COG4604 3 EIKNVSKR---YGGK----VVLDDVSLTIPKGGITALIGPNGAGKSTLLsmisRLL----PPDSGEVLVDGL----DVAT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 82 AD----ARHVLEIRRETVgwvsqflrVIPRIStlnvvIQPLLE-------RGMSRQESEIRGGELLTHLNvperLWSLAP 150
Cdd:COG4604 68 TPsrelAKRLAILRQENH--------INSRLT-----VRELVAfgrfpysKGRLTAEDREIIDEAIAYLD----LEDLAD 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404648 151 A---TFSGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AKSKGCAVVGIFHD 211
Cdd:COG4604 131 RyldELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRlADELGKTVVIVLHD 195
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
36-67 |
1.27e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 38.25 E-value: 1.27e-03
10 20 30
....*....|....*....|....*....|..
gi 499404648 36 CGECVALHGHSGTGKSTLLRSLYGNYRPDGGH 67
Cdd:pfam13191 23 RPPSVLLTGEAGTGKTTLLRELLRALERDGGY 54
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
25-184 |
1.38e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.00 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 25 PVFHDINLSVKCGECVALHGHSGTGKSTLLRSLYG--NYRPDGGHIWVRHRerwvDIVNADARhvlEIRRETVGWVSQFL 102
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGK----DLLELSPE---DRAGEGIFMAFQYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 103 RVIPRIS-------TLNVVIQPLLERGMSRQESEIRGGELLTHLNVPERLWSLA-PATFSGGEQQRINIARGFIGDYPIL 174
Cdd:PRK09580 88 VEIPGVSnqfflqtALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSvNVGFSGGEKKRNDILQMAVLEPELC 167
|
170
....*....|
gi 499404648 175 LLDEPTASLD 184
Cdd:PRK09580 168 ILDESDSGLD 177
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
152-225 |
1.63e-03 |
|
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: 38.39 E-value: 1.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404648 152 TFSGGEQQRINIAR----GFIGdyPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQHvADRLYSM 225
Cdd:cd03270 137 TLSGGEAQRIRLATqigsGLTG--VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVIDI 211
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-68 |
1.92e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.10 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTFVLYNQQGTRLP---------VFH----DINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGH 67
Cdd:PRK13545 1 MNYKVKFEHVTKKYKMYNKPFDKLKdlffrskdgEYHyalnNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT 80
|
.
gi 499404648 68 I 68
Cdd:PRK13545 81 V 81
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-222 |
2.28e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 142 PERlwslAPATFSGGEQQRINIARGFIGDYP--ILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQhVA 219
Cdd:PRK00635 470 PER----ALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMIS-LA 544
|
...
gi 499404648 220 DRL 222
Cdd:PRK00635 545 DRI 547
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
154-211 |
2.70e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.56 E-value: 2.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 499404648 154 SGGEQQRINIARGFIGDYPILLLDEPTASLDAKNRLAVTQLIDD-AkskGCAVVgIFHD 211
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEfP---GCAVV-ISHD 501
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-82 |
3.70e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 37.49 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 1 MDTQLRIENVDKTFVLYNQQGTRLP-------------VFHDINLSVKCGECVALHGHSGTGKSTLLRSLYGNYRPDGGH 67
Cdd:PRK13546 1 MNVSVNIKNVTKEYRIYRTNKERMKdalipkhknktffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
90
....*....|....*
gi 499404648 68 IwVRHRERWVDIVNA 82
Cdd:PRK13546 81 V-DRNGEVSVIAISA 94
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
150-221 |
3.85e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.12 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404648 150 PATF-SGGEqqRINIARGF--------IGDYPILLLDEPTASLDAKNRLAVTQLIDDAKSKGCAVVGIFHDDEVRQhVAD 220
Cdd:PRK03918 785 PLTFlSGGE--RIALGLAFrlalslylAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHDEELKD-AAD 861
|
.
gi 499404648 221 R 221
Cdd:PRK03918 862 Y 862
|
|
| |
