|
Name |
Accession |
Description |
Interval |
E-value |
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-224 |
1.89e-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: 419.92 E-value: 1.89e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDEWVDLVTAP 80
Cdd:COG4778 4 LLEVENLSKTFTLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKTTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLAPSTFSGGEQQRVNI 160
Cdd:COG4778 84 PREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131922 161 ARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRLHPMGA 224
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
1-219 |
2.90e-148 |
|
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: 411.78 E-value: 2.90e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDEWVDLVTAP 80
Cdd:TIGR02324 1 LLEVEDLSKTFTLHQQGGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEGAWVDLAQAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKTTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLAPSTFSGGEQQRVNI 160
Cdd:TIGR02324 81 PREVLEVRRKTIGYVSQFLRVIPRVSALEVVAEPLLERGVPREAARARARELLARLNIPERLWHLPPATFSGGEQQRVNI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131922 161 ARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:TIGR02324 161 ARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKARGAALIGIFHDEEVRELVADRV 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-218 |
4.16e-59 |
|
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: 185.39 E-value: 4.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgdEWVDLVTAPA 81
Cdd:cd03255 1 IELKNLSKTY---GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRV----DGTDISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVVEIRKTTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLaPSTFSGGEQQRVNIA 161
Cdd:cd03255 74 KELAAFRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHY-PSELSGGQQQRVAIA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 162 RGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVrNDVADR 218
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRElNKEAGTTIVVVTHDPEL-AEYADR 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-218 |
4.51e-58 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 182.94 E-value: 4.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGdewVDLVTAP 80
Cdd:COG1136 4 LLELRNLTKSY---GTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLI-DG---QDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKTTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLaPSTFSGGEQQRVNI 160
Cdd:COG1136 77 ERELARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHR-PSQLSGGQQQRVAI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131922 161 ARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRnDVADR 218
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVTHDPELA-ARADR 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-178 |
3.21e-47 |
|
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: 152.80 E-value: 3.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 24 LNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDEWVDLVTAPARKvveirkttVGWVSQFLRVIP 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE--------IGYVFQDPQLFP 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 104 RISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPE---RLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTA 178
Cdd:pfam00005 73 RLTVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-203 |
1.29e-45 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 150.97 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqQNGVrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhGDEwvDLVTAP 80
Cdd:COG2884 1 MIRFENVSKRY----PGGR--EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLV--NGQ--DLSRLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKTtVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLaPSTFSGGEQQRVNI 160
Cdd:COG2884 71 RREIPYLRRR-IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKAL-PHELSGGEQQRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131922 161 ARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIV 203
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVL 191
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-210 |
5.59e-44 |
|
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: 147.20 E-value: 5.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIK-----HGDEwvD 75
Cdd:COG4181 8 IIELRGLTKTV---GTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAgqdlfALDE--D 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 76 lvtAPARkvveIRKTTVGWVSQFLRVIPRISALEVVMQPLLDTGVpREAcAAKAARLLTRLNVPERLWHLaPSTFSGGEQ 155
Cdd:COG4181 83 ---ARAR----LRARHVGFVFQSFQLLPTLTALENVMLPLELAGR-RDA-RARARALLERVGLGHRLDHY-PAQLSGGEQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131922 156 QRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEA 210
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFElNRERGTTLVLVTHDPA 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-222 |
1.05e-41 |
|
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: 141.10 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHqqnGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlVTAP 80
Cdd:cd03257 1 LLEVKNLSVSFPTG---GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKD-----LLKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKTTVGWVSQ--FLRVIPRISALEVVMQPLLDTGVPREACAAKAAR--LLTRLNVPERLWHLAPSTFSGGEQQ 156
Cdd:cd03257 73 SRRLRKIRRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVllLLVGVGLPEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 157 RVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKT-RGAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-218 |
1.76e-39 |
|
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: 134.96 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFILHQqngvrlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYL--PDEGQIQIkHGDEwvdlVTA 79
Cdd:cd03262 1 IEIKNLHKSFGDFH-------VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI--NLLeePDSGTIII-DGLK----LTD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 80 PARKVVEIRKTtVGWVSQFLRVIPRISALEVVMQPLLDT-GVPREACAAKAARLLTRLNVPERLwHLAPSTFSGGEQQRV 158
Cdd:cd03262 67 DKKNINELRQK-VGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKA-DAYPAQLSGGQQQRV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 159 NIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADR 218
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADR 204
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-222 |
2.57e-39 |
|
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: 135.70 E-value: 2.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGDEwvdlVTAP 80
Cdd:COG1124 1 MLEVRNLSVSY---GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTF-DGRP----VTRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVveiRKTTVGWVSQ--FLRVIPRISALEVVMQPLLDTGVPREAcaAKAARLLTRLNVPERLWHLAPSTFSGGEQQRV 158
Cdd:COG1124 73 RRKA---FRRRVQMVFQdpYASLHPRHTVDRILAEPLRIHGLPDRE--ERIAELLEQVGLPPSFLDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131922 159 NIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAK-TRGAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-218 |
9.63e-39 |
|
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: 140.04 E-value: 9.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHQQNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHgdewVDLVTAP 80
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVR--AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDG----KDLTKLS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKTtVGWVSQ--FLRVIPRISALEVVMQPL-LDTGVPREACAAKAARLLTRLNVPERLWHLAPSTFSGGEQQR 157
Cdd:COG1123 334 RRSLRELRRR-VQMVFQdpYSSLNPRMTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQR 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131922 158 VNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADR 218
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlQRELGLTYLFISHDLAVVRYIADR 474
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-203 |
1.24e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 134.03 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqQNGVrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYL--PDEGQIQIkHGdewVDLVT 78
Cdd:COG3638 2 MLELRNLSKRY----PGGT--PALDDVSLEIERGEFVALIGPSGAGKSTLLRCL--NGLvePTSGEILV-DG---QDVTA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 79 APARKVVEIRKTtVGWVSQFLRVIPRISALEVVMQPLL-DTGVPR-------EACAAKAARLLTRLNVPERLWHLApSTF 150
Cdd:COG3638 70 LRGRALRRLRRR-IGMIFQQFNLVPRLSVLTNVLAGRLgRTSTWRsllglfpPEDRERALEALERVGLADKAYQRA-DQL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131922 151 SGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIV 203
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRiAREDGITVV 201
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-219 |
5.95e-38 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 132.14 E-value: 5.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHQqngvrlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYLPdegqiQIKHGDEWVD--LVT 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQ-------VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI--NKLE-----EITSGDLIVDglKVN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 79 APARKVVEIRKTTvGWVSQFLRVIPRISALEVVM-QPLLDTGVPREACAAKAARLLTRLNVPERLWHLaPSTFSGGEQQR 157
Cdd:PRK09493 67 DPKVDERLIRQEA-GMVFQQFYLFPHLTALENVMfGPLRVRGASKEEAEKQARELLAKVGLAERAHHY-PSELSGGQQQR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131922 158 VNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRL 206
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
22-224 |
6.49e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.09 E-value: 6.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhgDEWVDLVTAPA--RKVVEIRKTTVGW---VS 96
Cdd:COG4619 14 PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLD--GKPLSAMPPPEwrRQVAYVPQEPALWggtVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 97 QFLRVIPRISALEVVMQplldtgvpreacaaKAARLLTRLNVPERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEP 176
Cdd:COG4619 92 DNLPFPFQLRERKFDRE--------------RALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131922 177 TASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRLHPMGA 224
Cdd:COG4619 158 TSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-218 |
6.55e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 131.65 E-value: 6.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqnGvRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYL--PDEGQIQIkHGDEwvdlVT 78
Cdd:COG1126 1 MIEIENLHKSF------G-DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI--NLLeePDSGTITV-DGED----LT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 79 APARKVVEIRKTtVGWVSQ----FlrviPRISALEVVMQPLLDT-GVPREACAAKAARLLTRLNVPERLWHLaPSTFSGG 153
Cdd:COG1126 67 DSKKDINKLRRK-VGMVFQqfnlF----PHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAY-PAQLSGG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131922 154 EQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADR 218
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADR 205
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-219 |
1.54e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 128.26 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqnGvRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGdewVDLVTAPA 81
Cdd:COG1131 1 IEVRGLTKRY------G-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRV-LG---EDVARDPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 rkvvEIRKTtVGWVSQFLRVIPRISALEVV--MQPLLdtGVPREACAAKAARLLTRLNVPERLwHLAPSTFSGGEQQRVN 159
Cdd:COG1131 70 ----EVRRR-IGYVPQEPALYPDLTVRENLrfFARLY--GLPRKEARERIDELLELFGLTDAA-DRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131922 160 IARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIvgIF--H--DEAVRndVADRL 219
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTV--LLstHylEEAER--LCDRV 201
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-225 |
2.27e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 128.28 E-value: 2.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyANYL-PDEGQIQIkHGDEwvdlVTA 79
Cdd:COG1116 7 ALELRGVSKRF---PTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLI-AGLEkPTSGEVLV-DGKP----VTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 80 PARKVveirkttvGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLaPSTFSGGEQQRVN 159
Cdd:COG1116 78 PGPDR--------GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAY-PHQLSGGMRQRVA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131922 160 IARGFIVDYPILLLDEPTASLDAKNSAAV-VELIREAKTRGAAIVGIFHD--EAVRndVADRLHPMGAS 225
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLqDELLRLWQETGKTVLFVTHDvdEAVF--LADRVVVLSAR 215
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-219 |
8.97e-36 |
|
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: 125.44 E-value: 8.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqQNGVrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgdEWVDLVTAP 80
Cdd:TIGR02673 1 MIEFHNVSKAY----PGGV--AALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRI----AGEDVNRLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKTtVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLaPSTFSGGEQQRVNI 160
Cdd:TIGR02673 71 GRQLPLLRRR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAF-PEQLSGGEQQRVAI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131922 161 ARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:TIGR02673 149 ARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRV 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
22-219 |
1.09e-35 |
|
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: 126.31 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHgdewVDLVTAPARkvvEIRKTtVGWVSQFLRV 101
Cdd:COG1120 15 PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG----RDLASLSRR---ELARR-IAYVPQEPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPRISALEVVM------QPLLdtGVPREACAAKAARLLTRLNvperLWHLAP---STFSGGEQQRVNIARGFIVDYPILL 172
Cdd:COG1120 87 PFGLTVRELVAlgryphLGLF--GRPSAEDREAVEEALERTG----LEHLADrpvDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131922 173 LDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHD--EAVRndVADRL 219
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRlARERGRTVVMVLHDlnLAAR--YADRL 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-218 |
1.46e-35 |
|
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: 125.39 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYL--PDEGQIQIkHGdewVDLVT 78
Cdd:cd03258 1 MIELKNVSKVF---GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI--NGLerPTSGSVLV-DG---TDLTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 79 APARKVVEIRKTtVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLwHLAPSTFSGGEQQRV 158
Cdd:cd03258 72 LSGKELRKARRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKA-DAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131922 159 NIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREA-KTRGAAIVGIFHDEAVRNDVADR 218
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDR 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-222 |
5.56e-35 |
|
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: 129.64 E-value: 5.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyANYLPDEGQIQIKHGDEWVDLVTAP 80
Cdd:COG1123 4 LLEVRDLSVRY-----PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAL-MGLLPHGGRISGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARkvveIRKTTVGWVSQ-FLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVpERLWHLAPSTFSGGEQQRVN 159
Cdd:COG1123 78 EA----LRGRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131922 160 IARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLGVVAEIADRVVVM 216
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-218 |
8.70e-35 |
|
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: 122.90 E-value: 8.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqQNGVrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHgdewVDLVTAPA 81
Cdd:cd03292 1 IEFINVTKTY----PNGT--AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNG----QDVSDLRG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVVEIRKTtVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLwHLAPSTFSGGEQQRVNIA 161
Cdd:cd03292 71 RAIPYLRRK-IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKH-RALPAELSGGEQQRVAIA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 162 RGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADR 218
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHR 205
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-219 |
8.92e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 123.97 E-value: 8.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFILHQqngvrlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhGDEWVDLVTAP- 80
Cdd:COG4161 3 IQLKNINCFYGSHQ-------ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNI--AGHQFDFSQKPs 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKTtVGWVSQFLRVIPRISalevVMQPLLDT-----GVPREACAAKAARLLTRLNVPERLwHLAPSTFSGGEQ 155
Cdd:COG4161 74 EKAIRLLRQK-VGMVFQQYNLWPHLT----VMENLIEApckvlGLSKEQAREKAMKLLARLRLTDKA-DRFPLHLSGGQQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131922 156 QRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQV 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-218 |
3.14e-34 |
|
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: 121.42 E-value: 3.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 4 VQNVSktfilHQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlvtAPARK 83
Cdd:cd03225 2 LKNLS-----FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKD-------LTKLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 84 VVEIRKTtVGWV-----SQFLRVipriSALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLaPSTFSGGEQQRV 158
Cdd:cd03225 70 LKELRRK-VGLVfqnpdDQFFGP----TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRS-PFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 159 NIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADR 218
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADR 203
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-219 |
4.37e-34 |
|
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: 121.91 E-value: 4.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqQNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYL--PDEGQIQIkhgdEWVDLVTA 79
Cdd:cd03256 1 IEVENLSKTY----PNGKK--ALKDVSLSINPGEFVALIGPSGAGKSTLLRCL--NGLvePTSGSVLI----DGTDINKL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 80 PARKVVEIRKTtVGWVSQFLRVIPRISALEVVMQPLLDT--------GVPREACAAKAARLLTRLNVPERLWHLApSTFS 151
Cdd:cd03256 69 KGKALRQLRRQ-IGMIFQQFNLIERLSVLENVLSGRLGRrstwrslfGLFPKEEKQRALAALERVGLLDKAYQRA-DQLS 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131922 152 GGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRiNREEGITVIVSLHQVDLAREYADRI 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-203 |
2.05e-33 |
|
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: 119.12 E-value: 2.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqNGVrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDEWVDLVTAP 80
Cdd:COG4133 2 MLEAENLSCRR-----GER--LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARkvveirkttVGWVSQFLRVIPRISALE--VVMQPLLDTGVPREACAAkaarLLTRLNVpERLWHLAPSTFSGGEQQRV 158
Cdd:COG4133 75 RR---------LAYLGHADGLKPELTVREnlRFWAALYGLRADREAIDE----ALEAVGL-AGLADLPVRQLSAGQKRRV 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131922 159 NIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIV 203
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVL 185
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-219 |
4.17e-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: 117.50 E-value: 4.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqnGVRlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlvtaPA 81
Cdd:cd03230 1 IEVRNLSKRY------GKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD--------IK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVVEIRKtTVGWVSQFLRVIPRISALEVVMqplldtgvpreacaakaarlltrlnvperlwhlapstFSGGEQQRVNIA 161
Cdd:cd03230 66 KEPEEVKR-RIGYLPEEPSLYENLTVRENLK-------------------------------------LSGGMKQRLALA 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 162 RGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRV 165
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-224 |
5.45e-33 |
|
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: 118.34 E-value: 5.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRsLYANYL-PDEGQIQIkHGDEwvdlVTAP 80
Cdd:cd03293 1 LEVRNVSKTY---GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLR-IIAGLErPTSGEVLV-DGEP----VTGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVveirkttvGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLwHLAPSTFSGGEQQRVNI 160
Cdd:cd03293 72 GPDR--------GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFE-NAYPHQLSGGMRQRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 161 ARGFIVDYPILLLDEPTASLDAKNSAAVVELIREA-KTRGAAIVGIFHD--EAVRndVADRLHPMGA 224
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDidEAVF--LADRVVVLSA 207
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-219 |
1.03e-32 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 118.58 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFILHQqngvrlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhGDEWVDLVTAPA 81
Cdd:PRK11124 3 IQLNGINCFYGAHQ-------ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNI--AGNHFDFSKTPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVVEIRKTTVGWVSQFLRVIPRISalevVMQPLLDT-----GVPREACAAKAARLLTRLnvpeRLWHLA---PSTFSGG 153
Cdd:PRK11124 74 DKAIRELRRNVGMVFQQYNLWPHLT----VQQNLIEApcrvlGLSKDQALARAEKLLERL----RLKPYAdrfPLHLSGG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131922 154 EQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRV 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-203 |
1.40e-32 |
|
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: 118.04 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqNGVrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlvtaP 80
Cdd:COG4555 1 MIEVENLSKKY-----GKV--PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED--------V 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKTtVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPE---RLWHlapsTFSGGEQQR 157
Cdd:COG4555 66 RKEPREARRQ-IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEfldRRVG----ELSTGMKKK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131922 158 VNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIV 203
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVL 186
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-219 |
1.17e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.57 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVskTFILHQQngvrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyanyL----PDEGQIQIkhgdewvdl 76
Cdd:COG1121 6 AIELENL--TVSYGGR-----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAI----LgllpPTSGTVRL--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 77 vtapARKVVEIRKTTVGWVSQFLRVIPR--ISALEVVMQPLLDT----GVPREACAAKAARLLTRLNvperLWHLAP--- 147
Cdd:COG1121 66 ----FGKPPRRARRRIGYVPQRAEVDWDfpITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVG----LEDLADrpi 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131922 148 STFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHD-EAVRnDVADRL 219
Cdd:COG1121 138 GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDlGAVR-EYFDRV 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-218 |
1.35e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 115.62 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilHQQNgvrlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYL--PDEGQIQIkhGDEWVDLVT 78
Cdd:PRK11264 3 AIEVKNLVKKF--HGQT-----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI--NLLeqPEAGTIRV--GDITIDTAR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 79 APARKVVEIR--KTTVGWVSQFLRVIPRISALEVVMQ-PLLDTGVPREACAAKAARLLTRLNV-------PERLwhlaps 148
Cdd:PRK11264 72 SLSQQKGLIRqlRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLagketsyPRRL------ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 149 tfSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADR 218
Cdd:PRK11264 146 --SGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADR 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-218 |
1.87e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 117.49 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhQQNGVRLPVLNRASLTVNAGE--CVVlhGHSGSGKSTLLRSLyaNYL--PDEGQIQIkHGdewVDL 76
Cdd:COG1135 1 MIELENLSKTF---PTKGGPVTALDDVSLTIEKGEifGII--GYSGAGKSTLIRCI--NLLerPTSGSVLV-DG---VDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 77 VTAPARKVVEIRKtTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLaPSTFSGGEQQ 156
Cdd:COG1135 70 TALSERELRAARR-KIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAY-PSQLSGGQKQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131922 157 RVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHD-EAVRnDVADR 218
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEmDVVR-RICDR 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-219 |
5.21e-31 |
|
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: 113.58 E-value: 5.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqQNGVrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhgdewvDLVTAPa 81
Cdd:COG1122 1 IELENLSFSY----PGGT--PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD------GKDITK- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVVEIRKtTVGWV-----SQFLRVipriSALEVVMQPLLDTGVPREACAAKAARLLTRLNvperLWHLA---PSTFSGG 153
Cdd:COG1122 68 KNLRELRR-KVGLVfqnpdDQLFAP----TVEEDVAFGPENLGLPREEIRERVEEALELVG----LEHLAdrpPHELSGG 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 154 EQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHD-EAVRnDVADRL 219
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDlDLVA-ELADRV 204
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-218 |
6.17e-31 |
|
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: 112.71 E-value: 6.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 4 VQNVSKTFILHQqngvrlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEWVDLVTAPARK 83
Cdd:TIGR03608 1 LKNISKKFGDKV-------ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLN-GQETPPLNSKKASK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 84 vveIRKTTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLwHLAPSTFSGGEQQRVNIARG 163
Cdd:TIGR03608 73 ---FRREKLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKL-KQKIYELSGGEQQRVALARA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131922 164 FIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNdVADR 218
Cdd:TIGR03608 149 ILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK-QADR 202
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-219 |
9.47e-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: 113.55 E-value: 9.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqQNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYL--PDEGQIQIKHGDewvdLVT 78
Cdd:TIGR02315 1 MLEVENLSKVY----PNGKQ--ALKNINLNINPGEFVAIIGPSGAGKSTLLRCI--NRLvePSSGSILLEGTD----ITK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 79 APARKVVEIRKTTvGWVSQFLRVIPRISALEVVMQPLLDT--------GVPREACAAKAARLLTRLNVPErLWHLAPSTF 150
Cdd:TIGR02315 69 LRGKKLRKLRRRI-GMIFQHYNLIERLTVLENVLHGRLGYkptwrsllGRFSEEDKERALSALERVGLAD-KAYQRADQL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 151 SGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRiNKEDGITVIINLHQVDLAKKYADRI 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-219 |
1.52e-30 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 115.20 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqNGVrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGDEWVDLvtaP 80
Cdd:COG3842 5 ALELENVSKRY-----GDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL-DGRDVTGL---P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKvveiRKttVGWVSQ----FlrviPRISALEVVMQPLLDTGVPREACAAKAARLLTRLnvpeRLWHLA---PSTFSGG 153
Cdd:COG3842 74 PEK----RN--VGMVFQdyalF----PHLTVAENVAFGLRMRGVPKAEIRARVAELLELV----GLEGLAdryPHQLSGG 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131922 154 EQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREA-KTRGAAIVGIFHD--EAVRndVADRL 219
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDqeEALA--LADRI 206
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-219 |
2.63e-30 |
|
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: 111.46 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 4 VQNVSKTFilhqqNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhGDEwvDLVTAPARK 83
Cdd:cd03259 3 LKGLSKTY-----GSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI--DGR--DVTGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 84 vveirkTTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLwHLAPSTFSGGEQQRVNIARG 163
Cdd:cd03259 72 ------RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLL-NRYPHELSGGQQQRVALARA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131922 164 FIVDYPILLLDEPTASLDAKNSAAVVELIREA-KTRGAAIVGIFHD--EAVRndVADRL 219
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDqeEALA--LADRI 201
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-219 |
3.78e-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: 111.44 E-value: 3.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqnGVRlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGDEWVDLVTAPA 81
Cdd:cd03261 1 IELRGLTKSF------GGR-TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI-DGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RkvvEIRKTtVGWVSQFlrvipriSAL-------EVVMQPLLD-TGVPREACAAKAARLLTRLNVPERLwHLAPSTFSGG 153
Cdd:cd03261 73 Y---RLRRR-MGMLFQS-------GALfdsltvfENVAFPLREhTRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 154 EQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:cd03261 141 MKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAIADRI 207
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
22-208 |
5.80e-30 |
|
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: 109.45 E-value: 5.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGDewvDLVTAPARKVVEIrkttVGWVSQflrv 101
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL-DGK---DLASLSPKELARK----IAYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 iprisALEVVmqplldtGVpreacAAKAARLLTRLnvperlwhlapstfSGGEQQRVNIARGFIVDYPILLLDEPTASLD 181
Cdd:cd03214 81 -----ALELL-------GL-----AHLADRPFNEL--------------SGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180
....*....|....*....|....*...
gi 16131922 182 AKNSAAVVELIRE-AKTRGAAIVGIFHD 208
Cdd:cd03214 130 IAHQIELLELLRRlARERGKTVVMVLHD 157
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
13-222 |
6.82e-30 |
|
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: 111.58 E-value: 6.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 13 LHQQNGVRLPVlNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgdEWVDLVTAPARKVVEIRKTTV 92
Cdd:cd03294 30 ILKKTGQTVGV-NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI----DGQDIAAMSRKELRELRRKKI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 93 GWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLaPSTFSGGEQQRVNIARGFIVDYPILL 172
Cdd:cd03294 105 SMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKY-PDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131922 173 LDEPTASLDA-KNSAAVVELIREAKTRGAAIVGIFHD--EAVRndVADRLHPM 222
Cdd:cd03294 184 MDEAFSALDPlIRREMQDELLRLQAELQKTIVFITHDldEALR--LGDRIAIM 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
22-203 |
8.26e-30 |
|
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: 110.94 E-value: 8.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQ-IQI---KHGDEwvdlvtaparKVVEIRKTtVGWVSQ 97
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLfgeRRGGE----------DVWELRKR-IGLVSP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 98 FL--RVIPRISALEVVMQPLLDT-GVPREACAA---KAARLLTRLnvpeRLWHLAPSTF---SGGEQQRVNIARGFIVDY 168
Cdd:COG1119 86 ALqlRFPRDETVLDVVLSGFFDSiGLYREPTDEqreRARELLELL----GLAHLADRPFgtlSQGEQRRVLIARALVKDP 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 16131922 169 PILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIV 203
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLV 197
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-220 |
1.34e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 110.29 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 6 NVSKTFilhQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhgDEWVDLVTAPARkvV 85
Cdd:PRK11629 10 NLCKRY---QEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN--GQPMSKLSSAAK--A 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 86 EIRKTTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHlAPSTFSGGEQQRVNIARGFI 165
Cdd:PRK11629 83 ELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANH-RPSELSGGERQRVAIARALV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131922 166 VDYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHDEavrnDVADRLH 220
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDL----QLAKRMS 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-218 |
1.37e-29 |
|
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: 110.07 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqnGvRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGdewVDLVTAP 80
Cdd:COG1127 5 MIEVRNLTKSF------G-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV-DG---QDITGLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKTtVGWVSQFlrvipriSAL-------EVVMQPLLD-TGVPREACAAKAARLLTRLNVPErLWHLAPSTFSG 152
Cdd:COG1127 74 EKELYELRRR-IGMLFQG-------GALfdsltvfENVAFPLREhTDLSEAEIRELVLEKLELVGLPG-AADKMPSELSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 153 GEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADR 218
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRElRDELGLTSVVVTHDLDSAFAIADR 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-218 |
2.81e-29 |
|
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: 111.30 E-value: 2.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilHQQNGVrLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRS---LYANYLPDEGQIQIKhGdewVDLV 77
Cdd:COG0444 1 LLEVRNLKVYF--PTRRGV-VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAilgLLPPPGITSGEILFD-G---EDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 78 TAPARKVVEIRKTTVGWVSQflr--viPRISALEVVMQPLLD-TGVPREACAAKAARLLTR--LNVPERLWHLAPSTFSG 152
Cdd:COG0444 74 KLSEKELRKIRGREIQMIFQdpmtslnPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERvgLPDPERRLDRYPHELSG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 153 GEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADR 218
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDlQRELGLAILFITHDLGVVAEIADR 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-219 |
6.15e-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: 6.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFILHQqngvrlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGDEWVDLvtapa 81
Cdd:cd03229 1 LELKNVSKRYGQKT-------VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI-DGEDLTDL----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVVEIRKTTVGWVSQFLRVIPRISALEVVMQPLldtgvpreacaakaarlltrlnvperlwhlapstfSGGEQQRVNIA 161
Cdd:cd03229 68 EDELPPLRRRIGMVFQDFALFPHLTVLENIALGL-----------------------------------SGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131922 162 RGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHD--EAVRndVADRL 219
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDldEAAR--LADRV 171
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-219 |
8.14e-28 |
|
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: 103.09 E-value: 8.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 4 VQNVSKTFILHqqngvrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlvtaPARK 83
Cdd:cd00267 2 IENLSFRYGGR-------TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD--------IAKL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 84 VVEIRKTTVGWVSQFlrviprisalevvmqplldtgvpreacaakaarlltrlnvperlwhlapstfSGGEQQRVNIARG 163
Cdd:cd00267 67 PLEELRRRIGYVPQL----------------------------------------------------SGGQRQRVALARA 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131922 164 FIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRV 150
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-224 |
2.23e-27 |
|
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: 104.69 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqNGVRlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYL--PDEGQIQIKHGD--EWvdlv 77
Cdd:cd03295 1 IEFENVTKRY-----GGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI--NRLiePTSGEIFIDGEDirEQ---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 78 taparKVVEIRKTtVGWVSQFLRVIPRISALE-VVMQPLLDtGVPREACAAKAARLLTRLNV-PERLWHLAPSTFSGGEQ 155
Cdd:cd03295 69 -----DPVELRRK-IGYVIQQIGLFPHMTVEEnIALVPKLL-KWPKEKIRERADELLALVGLdPAEFADRYPHELSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131922 156 QRVNIARGFIVDYPILLLDEPTASLDAKNSAAVV-ELIREAKTRGAAIVGIFHD--EAVRndVADRLHPMGA 224
Cdd:cd03295 142 QRVGVARALAADPPLLLMDEPFGALDPITRDQLQeEFKRLQQELGKTIVFVTHDidEAFR--LADRIAIMKN 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-208 |
2.83e-27 |
|
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: 103.38 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhgdewvdlvtapARKVVEIRKTtVGWVSQFlRV 101
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF------------GKPLEKERKR-IGYVPQR-RS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPR---ISALEVVMQPLLDTGV----PREACAAKAARLLTRLNVPErLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLD 174
Cdd:cd03235 79 IDRdfpISVRDVVLMGLYGHKGlfrrLSKADKAKVDEALERVGLSE-LADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190
....*....|....*....|....*....|....
gi 16131922 175 EPTASLDAKNSAAVVELIREAKTRGAAIVGIFHD 208
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTHD 191
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-220 |
2.90e-27 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 104.50 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqnGvRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYL--PDEGQIQIkHGDE--WV-- 74
Cdd:COG4598 8 ALEVRDLHKSF------G-DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCI--NLLetPDSGEIRV-GGEEirLKpd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 75 ---DLVTAPARKVVEIRkTTVGWVSQFLRVIPRISALEVVMQ-PLLDTGVPREACAAKAARLLTRLNVPERLwHLAPSTF 150
Cdd:COG4598 78 rdgELVPADRRQLQRIR-TRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKR-DAYPAHL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131922 151 SGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADR---LH 220
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHvvfLH 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
23-218 |
4.89e-27 |
|
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: 103.03 E-value: 4.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSL-----YANYLPDEGQIQIKHGDewvdlVTAPARKVVEIRKTtVGWVSQ 97
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKD-----IYDLDVDVLELRRR-VGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 98 FLRVIPrISALEVVMQPLLDTGV-PREACAAKAARLLTRLNVPERLW-HLAPSTFSGGEQQRVNIARGFIVDYPILLLDE 175
Cdd:cd03260 89 KPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKdRLHALGLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131922 176 PTASLDAKNSAAVVELIREAKTRgAAIVGIFHD--EAVRndVADR 218
Cdd:cd03260 168 PTSALDPISTAKIEELIAELKKE-YTIVIVTHNmqQAAR--VADR 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-218 |
5.00e-27 |
|
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: 101.69 E-value: 5.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGDEWVDLVTAPA 81
Cdd:cd03228 1 IEFKNVSFSY-----PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI-DGVDLRDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKvveirktTVGWVSQflrviprisalevvmQPLLDTGVPREacaakaarlltrlNVperlwhlapstFSGGEQQRVNIA 161
Cdd:cd03228 75 RK-------NIAYVPQ---------------DPFLFSGTIRE-------------NI-----------LSGGQRQRIAIA 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 162 RGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVgIFHD-EAVRNdvADR 218
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIV-IAHRlSTIRD--ADR 163
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-222 |
6.96e-27 |
|
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: 102.90 E-value: 6.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 4 VQNVSKTFilhqqNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlVTApaRK 83
Cdd:cd03219 3 VRGLTKRF-----GGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGED-----ITG--LP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 84 VVEIRKTTVGWVSQFLRVIPRISALEVVM--------QPLLDTGVPRE--ACAAKAARLLTRLNVpERLWHLAPSTFSGG 153
Cdd:cd03219 69 PHEIARLGIGRTFQIPRLFPELTVLENVMvaaqartgSGLLLARARREerEARERAEELLERVGL-ADLADRPAGELSYG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 154 EQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHD-EAVRnDVADRLHPM 222
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDmDVVM-SLADRVTVL 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-218 |
1.01e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.64 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 4 VQNVSKTFilhqqNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGdewvdlvtaparK 83
Cdd:COG1129 7 MRGISKSF-----GGVK--ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD-G------------E 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 84 VVEIRKTT------VGWVSQFLRVIPRISALEVVM---QP----LLDtgvpREACAAKAARLLTRLNVPERLWHLApSTF 150
Cdd:COG1129 67 PVRFRSPRdaqaagIAIIHQELNLVPNLSVAENIFlgrEPrrggLID----WRAMRRRARELLARLGLDIDPDTPV-GDL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 151 SGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFH--DEAVRndVADR 218
Cdd:COG1129 142 SVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHrlDEVFE--IADR 209
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-222 |
1.48e-26 |
|
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: 102.96 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHQQNGV--RLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEWVDLVT 78
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFGAkqRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFR-GQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 79 APARKVveirKTTVGWVSQ--FLRVIPRISALEVVMQPLLD-TGVPREACAAKAARLLTRLNVPERLWHLAPSTFSGGEQ 155
Cdd:TIGR02769 81 KQRRAF----RRDVQLVFQdsPSAVNPRMTVRQIIGEPLRHlTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 156 QRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVM 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
23-219 |
5.34e-26 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 105.19 E-value: 5.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHgdewVDLVTAPARKVVEIRKTTVGWVSQFLRVI 102
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAG----QDVATLDADALAQLRREHFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 103 PRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLwHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDA 182
Cdd:PRK10535 99 SHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRV-EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 16131922 183 KNSAAVVELIREAKTRGAAIVGIFHDEAVRNDvADRL 219
Cdd:PRK10535 178 HSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERV 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
6.63e-25 |
|
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: 97.44 E-value: 6.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgdEWVDLVTAP 80
Cdd:cd03266 1 MITADALTKRF---RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV----DGFDVVKEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ArkvvEIRKTtVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLApSTFSGGEQQRVNI 160
Cdd:cd03266 74 A----EARRR-LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRV-GGFSTGMRQKVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 161 ARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFH--DEAVRndVADR 218
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHimQEVER--LCDR 205
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-218 |
9.68e-25 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 99.01 E-value: 9.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqQNGVrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYL--PDEGQIQIKhGDEwvdlVT 78
Cdd:COG1125 1 MIEFENVTKRY----PDGT--VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMI--NRLiePTSGRILID-GED----IR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 79 ApaRKVVEIRKTtVGWVSQ----F--LRVIPRISaleVVmqPLLdTGVPREACAAKAARLLTRLNV-PERLWHLAPSTFS 151
Cdd:COG1125 68 D--LDPVELRRR-IGYVIQqiglFphMTVAENIA---TV--PRL-LGWDKERIRARVDELLELVGLdPEEYRDRYPHELS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131922 152 GGEQQRVNIARGFIVDYPILLLDEPTASLDaknsaAVV------ELIREAKTRGAAIVGIFHD--EAVRndVADR 218
Cdd:COG1125 139 GGQQQRVGVARALAADPPILLMDEPFGALD-----PITreqlqdELLRLQRELGKTIVFVTHDidEALK--LGDR 206
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-219 |
1.44e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 99.07 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqnGvRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhGDEwvDLVTA-P 80
Cdd:COG1118 3 IEVRNISKRF------G-SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL--NGR--DLFTNlP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKvveiRKttVGWVSQ----------------FLRVIPRisalevvmqplldtgvPREACAAKAARLLTRLnvpeRLWH 144
Cdd:COG1118 72 PRE----RR--VGFVFQhyalfphmtvaeniafGLRVRPP----------------SKAEIRARVEELLELV----QLEG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 145 LA---PSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE--AKTRGAAivgIF--HD--EAVRndV 215
Cdd:COG1118 126 LAdryPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRlhDELGGTT---VFvtHDqeEALE--L 200
|
....
gi 16131922 216 ADRL 219
Cdd:COG1118 201 ADRV 204
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-218 |
1.45e-24 |
|
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: 101.00 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhGDewVDLVTAPA 81
Cdd:COG4987 334 LELEDVSFRY-----PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL--GG--VDLRDLDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RkvvEIRKTtVGWVSQ----F-------LRVI-PRISALEVvmqplldtgvpREAC-AAKAARLLTRLnvPERL--W-HL 145
Cdd:COG4987 405 D---DLRRR-IAVVPQrphlFdttlrenLRLArPDATDEEL-----------WAALeRVGLGDWLAAL--PDGLdtWlGE 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131922 146 APSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAkTRGAAIVGIFHDEAVRnDVADR 218
Cdd:COG4987 468 GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGL-ERMDR 538
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
22-218 |
1.78e-24 |
|
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: 100.60 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGDEWVDLVTAPARKvveirktTVGWVSQflR- 100
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI-NGVDLSDLDPASWRR-------QIAWVPQ--Np 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 101 VIPRISALEVVMqpLLDTGVPREAC--AAKAARLLTRLNVPERLWHLAP----STFSGGEQQRVNIARGFIVDYPILLLD 174
Cdd:COG4988 421 YLFAGTIRENLR--LGRPDASDEELeaALEAAGLDEFVAALPDGLDTPLgeggRGLSGGQAQRLALARALLRDAPLLLLD 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131922 175 EPTASLDAKNSAAVVELIREAKtRGAAIVGIFHDEAVRNDvADR 218
Cdd:COG4988 499 EPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADR 540
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-211 |
2.19e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 97.24 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLrSLYANYL-PDEGQIQIKHgdewvDLVTA 79
Cdd:COG4525 3 MLTVRHVSVRY---PGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLL-NLIAGFLaPSSGEITLDG-----VPVTG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 80 PA--RKVVeirkttvgwvSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPE----RLWHLapstfSGG 153
Cdd:COG4525 74 PGadRGVV----------FQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADfarrRIWQL-----SGG 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131922 154 EQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHD--EAV 211
Cdd:COG4525 139 MRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSveEAL 199
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-219 |
3.82e-24 |
|
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: 95.40 E-value: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFILHqqngvrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhGDEWVDLVTAPA 81
Cdd:cd03301 1 VELENVTKRFGNV-------TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYI--GGRDVTDLPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVveirkttvGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAK---AARLLTRLNVPERLwhlaPSTFSGGEQQRV 158
Cdd:cd03301 72 RDI--------AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERvreVAELLQIEHLLDRK----PKQLSGGQRQRV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131922 159 NIARGFIVDYPILLLDEPTASLDAKNSAAV-VELIREAKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDAKLRVQMrAELKRLQQRLGTTTIYVTHDQVEAMTMADRI 201
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-222 |
3.95e-24 |
|
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: 95.77 E-value: 3.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqNGVrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHgdewVDLVTAPA 81
Cdd:cd03300 1 IELENVSKFY-----GGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG----KDITNLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKvveiRKttVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLtRLNVPERLWHLAPSTFSGGEQQRVNIA 161
Cdd:cd03300 70 HK----RP--VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEAL-DLVQLEGYANRKPSQLSGGQQQRVAIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131922 162 RGFIVDYPILLLDEPTASLDAK-NSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDLKlRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVM 204
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-219 |
4.26e-24 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 96.35 E-value: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSktFILHQQNgvrLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhgdewvDLVTAPA 81
Cdd:TIGR04520 1 IEVENVS--FSYPESE---KPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD------GLDTLDE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVVEIRKtTVGWV-----SQFlrviprISA---------LEvvmqpllDTGVPREACAAKAARLLTRLNVPERLWHlAP 147
Cdd:TIGR04520 70 ENLWEIRK-KVGMVfqnpdNQF------VGAtveddvafgLE-------NLGVPREEMRKRVDEALKLVGMEDFRDR-EP 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131922 148 STFSGGEQQRVNIArGFIVDYP-ILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHD--EAVRndvADRL 219
Cdd:TIGR04520 135 HLLSGGQKQRVAIA-GVLAMRPdIIILDEATSMLDPKGRKEVLETIRKlNKEEGITVISITHDmeEAVL---ADRV 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-208 |
6.10e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 95.81 E-value: 6.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 13 LHQQNGvRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYL--PDEGQIQIKhgDEWVDLV-------TAPARK 83
Cdd:PRK10619 11 LHKRYG-EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI--NFLekPSEGSIVVN--GQTINLVrdkdgqlKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 84 VVEIRKTTVGWVSQFLRVIPRISALEVVMQ-PLLDTGVPREACAAKAARLLTRLNVPERLWHLAPSTFSGGEQQRVNIAR 162
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEaPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131922 163 GFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHD 208
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-219 |
8.48e-24 |
|
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: 95.49 E-value: 8.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHgdewVDLVTAP 80
Cdd:COG0411 4 LLEVRGLTKRF-----GGLV--AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG----RDITGLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVE--IRKTTvgwvsQFLRVIPRISALEVVM------------QPLLDTGVPR---EACAAKAARLLTRLNVpERLW 143
Cdd:COG0411 73 PHRIARlgIARTF-----QNPRLFPELTVLENVLvaaharlgrgllAALLRLPRARreeREARERAEELLERVGL-ADRA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 144 HLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHD-EAVRnDVADRL 219
Cdd:COG0411 147 DEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRlRDERGITILLIEHDmDLVM-GLADRI 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-219 |
9.59e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 94.46 E-value: 9.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 20 RLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYAnyLPDEGQiqikhGDewVDLVTAPARKVVE-----IRKTTVGW 94
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAG--LDDGSS-----GE--VSLVGQPLHQMDEearakLRAKHVGF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 95 VSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLaPSTFSGGEQQRVNIARGFIVDYPILLLD 174
Cdd:PRK10584 93 VFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHL-PAQLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131922 175 EPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHDE--AVRNDVADRL 219
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLqlAARCDRRLRL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-182 |
1.43e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 4 VQNVSKTFilhqqnGVRlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGdewvdlvtapark 83
Cdd:COG0488 1 LENLSKSF------GGR-PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 84 vveirkTTVGWVSQFLRVIPRISALEVVMQ---PLLDTGVPREACA-----------------------------AKAAR 131
Cdd:COG0488 61 ------LRIGYLPQEPPLDDDLTVLDTVLDgdaELRALEAELEELEaklaepdedlerlaelqeefealggweaeARAEE 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131922 132 LLTRLNVPERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDA 182
Cdd:COG0488 135 ILSGLGFPEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-212 |
2.94e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 94.31 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHQqngvrlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDegQIQIKHGDEWVDLVTAP 80
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ-------ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGD--KSAGSHIELLGRTVQRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKTT--VGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAA--------KAARLLTRLNVPErLWHLAPSTF 150
Cdd:PRK09984 75 GRLARDIRKSRanTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSwftreqkqRALQALTRVGMVH-FAHQRVSTL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131922 151 SGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREA-KTRGAAIVGIFH--DEAVR 212
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHqvDYALR 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-218 |
7.77e-23 |
|
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: 90.57 E-value: 7.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 4 VQNVSKTFilhqqNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGdewvdlvtaparK 83
Cdd:cd03216 3 LRGITKRF-----GGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-DG------------K 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 84 VVEIRKttvgwvsqflrviprisalevvmqplldtgvPREACAAKAArLLTRLnvperlwhlapstfSGGEQQRVNIARG 163
Cdd:cd03216 63 EVSFAS-------------------------------PRDARRAGIA-MVYQL--------------SVGERQMVEIARA 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 164 FIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFH--DEAVRndVADR 218
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHrlDEVFE--IADR 151
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-219 |
1.04e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.16 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHgdewvdlVTAPARKVVEIRKtTVGWV-----S 96
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-------MVLSEETVWDVRR-QVGMVfqnpdN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 97 QFLRVIPRisalEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLwHLAPSTFSGGEQQRVNIArGFIVDYP-ILLLDE 175
Cdd:PRK13635 93 QFVGATVQ----DDVAFGLENIGVPREEMVERVDQALRQVGMEDFL-NREPHRLSGGQKQRVAIA-GVLALQPdIIILDE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131922 176 PTASLDAKNSAAVVELIREAKTRGAAIV-GIFHD--EAVRndvADRL 219
Cdd:PRK13635 167 ATSMLDPRGRREVLETVRQLKEQKGITVlSITHDldEAAQ---ADRV 210
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-222 |
1.05e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 92.84 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFIlHQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhgdewvDLVTAP 80
Cdd:PRK13633 4 MIKCKNVSYKYE-SNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVD------GLDTSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKTTvGWVSQFL--RVIPRISALEVVMQPlLDTGVPREACAAKAARLLTRLNVPERLWHlAPSTFSGGEQQRV 158
Cdd:PRK13633 77 EENLWDIRNKA-GMVFQNPdnQIVATIVEEDVAFGP-ENLGIPPEEIRERVDESLKKVGMYEYRRH-APHLLSGGQKQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 159 NIArGFIVDYP-ILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFH--DEAVRndvADRLHPM 222
Cdd:PRK13633 154 AIA-GILAMRPeCIIFDEPTAMLDPSGRREVVNTIKElNKKYGITIILITHymEEAVE---ADRIIVM 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-208 |
1.31e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.14 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSktfilhqqngVRL---PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyANYL-PDEGQIQIKHgdewVDL 76
Cdd:PRK13548 2 MLEARNLS----------VRLggrTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL-SGELsPDSGEVRLNG----RPL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 77 VTAPARKVVEIRKttvgwvsqflrVIPRISAL-------EVV-M--QPLLDTGVPREACAAKAARLLtrlnvpeRLWHLA 146
Cdd:PRK13548 67 ADWSPAELARRRA-----------VLPQHSSLsfpftveEVVaMgrAPHGLSRAEDDALVAAALAQV-------DLAHLA 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131922 147 PS---TFSGGEQQRVNIARgfiV---------DYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHD 208
Cdd:PRK13548 129 GRdypQLSGGEQQRVQLAR---VlaqlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQlAHERGLAVIVVLHD 200
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-208 |
2.45e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 91.33 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSktFILHQQngvrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGdewVDLVTAP 80
Cdd:COG4559 1 MLEAENLS--VRLGGR-----TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRL-NG---RPLAAWS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKttvgwvsqflrVIPRISAL-------EVVMQPLLDTGVPREACAAKAARLLTRLNvperLWHLAP---STF 150
Cdd:COG4559 70 PWELARRRA-----------VLPQHSSLafpftveEVVALGRAPHGSSAAQDRQIVREALALVG----LAHLAGrsyQTL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131922 151 SGGEQQRVNIAR------GFIVDYP-ILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHD 208
Cdd:COG4559 135 SGGEQQRVQLARvlaqlwEPVDGGPrWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHD 199
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-219 |
5.63e-22 |
|
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: 93.51 E-value: 5.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 20 RLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGDEWVDLVTAPARKvveirktTVGWVSQfL 99
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV-NGVPLADADADSWRD-------QIAWVPQ-H 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 100 RVIPRISALEVVMqpLLDTGVPREAC--AAKAARLLTRLNVPERLWHL----APSTFSGGEQQRVNIARGFIVDYPILLL 173
Cdd:TIGR02857 405 PFLFAGTIAENIR--LARPDASDAEIreALERAGLDEFVAALPQGLDTpigeGGAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131922 174 DEPTASLDAKNSAAVVELIREAkTRGAAIVGIFHDEAVRNDvADRL 219
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAAL-ADRI 526
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
23-219 |
6.23e-22 |
|
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: 89.24 E-value: 6.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyanylpdEGQIQIKHGDEWVDLVTAPARKvveiRKTTVGWVSQFLRvi 102
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKIL-------AGLIKESSGSILLNGKPIKAKE----RRKSIGYVMQDVD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 103 pRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPE-RLWHlaPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLD 181
Cdd:cd03226 82 -YQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYAlKERH--PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 16131922 182 AKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:cd03226 159 YKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRV 196
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-222 |
6.66e-22 |
|
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: 89.49 E-value: 6.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 4 VQNVSKTFilhqqNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDEwvdlvtapARK 83
Cdd:cd03263 3 IRNLTKTY-----KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--------RTD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 84 VVEIRKtTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVpERLWHLAPSTFSGGEQQRVNIARG 163
Cdd:cd03263 70 RKAARQ-SLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131922 164 FIVDYPILLLDEPTASLDAKNSAAVVELIREAKtRGAAIVGIFH--DEAvrNDVADRLHPM 222
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHsmDEA--EALCDRIAIM 205
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-183 |
7.56e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 91.67 E-value: 7.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqNGVrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhGDEwvDLVTAP 80
Cdd:COG3839 3 SLELENVSKSY-----GGV--EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI--GGR--DVTDLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKvveiRKttVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLwHLAPSTFSGGEQQRVNI 160
Cdd:COG3839 72 PKD----RN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLL-DRKPKQLSGGQRQRVAL 144
|
170 180
....*....|....*....|...
gi 16131922 161 ARGFIVDYPILLLDEPTASLDAK 183
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAK 167
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-219 |
7.68e-22 |
|
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: 89.71 E-value: 7.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqngVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlVTApa 81
Cdd:cd03296 3 IEVRNVSKRF-------GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED-----ATD-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 rkvVEIRKTTVGWVSQFLRVIPRISALEVV-----MQPLLDTgvPREACAAKAARLLTRLNVPERLWHLAPSTFSGGEQQ 156
Cdd:cd03296 69 ---VPVQERNVGFVFQHYALFRHMTVFDNVafglrVKPRSER--PPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131922 157 RVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHDEAVRNDVADRL 219
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRV 207
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
28-222 |
1.01e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 89.99 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGD-EWVDLVTAPARKVVEIRKTTVGWVSQF----LRvi 102
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgQLRDLYALSEAERRRLLRTEWGFVHQHprdgLR-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 103 PRISALEVVMQPLLDTGVpRE--ACAAKAARLLTRLNVPERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASL 180
Cdd:PRK11701 104 MQVSAGGNIGERLMAVGA-RHygDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131922 181 DAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:PRK11701 183 DVSVQARLLDLLRGlVRELGLAVVIVTHDLAVARLLAHRLLVM 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-207 |
1.07e-21 |
|
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: 88.14 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFiLHQQNgvrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQikhgdewvdLVTAPA 81
Cdd:cd03247 1 LSINNVSFSY-PEQEQ----QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT---------LDGVPV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVVEIRKTTVGWVSQflrviprisalevvmQP-LLDTGVpreacaakaarlltRLNVPERlwhlapstFSGGEQQRVNI 160
Cdd:cd03247 67 SDLEKALSSLISVLNQ---------------RPyLFDTTL--------------RNNLGRR--------FSGGERQRLAL 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131922 161 ARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAkTRGAAIVGIFH 207
Cdd:cd03247 110 ARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEV-LKDKTLIWITH 155
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-219 |
1.80e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 88.66 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSktfilHQQNGVRLpvlnRASLTVNAGECVVLHGHSGSGKSTLLrSLYANYL-PDEGQIQIkHGdewVDLV-T 78
Cdd:COG3840 1 MLRLDDLT-----YRYGDFPL----RFDLTIAAGERVAILGPSGAGKSTLL-NLIAGFLpPDSGRILW-NG---QDLTaL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 79 APARKVVEIrkttvgwVSQ----FlrviPRISALEVV---MQPLLD-TGVPREACAAKAAR-----LLTRLnvperlwhl 145
Cdd:COG3840 67 PPAERPVSM-------LFQennlF----PHLTVAQNIglgLRPGLKlTAEQRAQVEQALERvglagLLDRL--------- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 146 aPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFH--DEAVRndVADRL 219
Cdd:COG3840 127 -PGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDElCRERGLTVLMVTHdpEDAAR--IADRV 200
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-208 |
2.02e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.15 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilHQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGD---------- 71
Cdd:PRK13651 3 IKVKNIVKIF--NKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 72 EWV--DLVTAPAR-----KVVEIRKTtVGWVSQFLRVIPRISALE--VVMQPLlDTGVPREACAAKAARLLTRLNVPERL 142
Cdd:PRK13651 81 EKVleKLVIQKTRfkkikKIKEIRRR-VGVVFQFAEYQLFEQTIEkdIIFGPV-SMGVSKEEAKKRAAKYIELVGLDESY 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131922 143 WHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHD 208
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
28-208 |
2.06e-21 |
|
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: 88.55 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgdEWVDLVTAPARKvveirkTTVGWVSQFLRVIPRISA 107
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL----NGKDITNLPPEK------RDISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 108 LEVVMQPLLDTGVPREACAAKAARLLTRLNVpERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAA 187
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180
....*....|....*....|..
gi 16131922 188 VVELIREA-KTRGAAIVGIFHD 208
Cdd:cd03299 168 LREELKKIrKEFGVTVLHVTHD 189
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-223 |
2.07e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 90.53 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqngVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewVDLVTAPA 81
Cdd:PRK10851 3 IEIANIKKSF-------GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTD--VSRLHARD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKV-------VEIRKTTVGWVSQF-LRVIPRISalevvmQPlldtgvPREACAAKAARLLTRLnvpeRLWHLA---PSTF 150
Cdd:PRK10851 74 RKVgfvfqhyALFRHMTVFDNIAFgLTVLPRRE------RP------NAAAIKAKVTQLLEMV----QLAHLAdryPAQL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 151 SGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIR----EAKTRGaaiVGIFHDEAVRNDVADRLHPMG 223
Cdd:PRK10851 138 SGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRqlheELKFTS---VFVTHDQEEAMEVADRVVVMS 211
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-218 |
3.03e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 89.79 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 4 VQNVSKTFilhqqnGVRLPVLNRA----------SLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGdew 73
Cdd:COG4608 10 VRDLKKHF------PVRGGLFGRTvgvvkavdgvSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD-G--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 74 VDLVTAPARKVVEIRKTtvgwvsqfLRVI---------PRISALEVVMQPLLDTGV-PREACAAKAARLLTR--LNvPEr 141
Cdd:COG4608 80 QDITGLSGRELRPLRRR--------MQMVfqdpyaslnPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELvgLR-PE- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 142 lwHLA--PSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHDEAVRNDVADR 218
Cdd:COG4608 150 --HADryPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDR 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-218 |
5.39e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 89.47 E-value: 5.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYL--PDEGQIQIkhgdEWVDLVT 78
Cdd:PRK11153 1 MIELKNISKVF---PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCI--NLLerPTSGRVLV----DGQDLTA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 79 APARKVVEIRKtTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNvperLWHLA---PSTFSGGEQ 155
Cdd:PRK11153 72 LSEKELRKARR-QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVG----LSDKAdryPAQLSGGQK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131922 156 QRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHDEAVRNDVADR 218
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDR 210
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
22-220 |
9.92e-21 |
|
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: 86.90 E-value: 9.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlvtaparkvveIRKTTVgwvsQFLRv 101
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD---------------IREVTL----DSLR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 ipriSALEVVMQ--PLLDTGVPREAC-------------AAKAARLLTRLN---------VPERLWHLapstfSGGEQQR 157
Cdd:cd03253 75 ----RAIGVVPQdtVLFNDTIGYNIRygrpdatdeevieAAKAAQIHDKIMrfpdgydtiVGERGLKL-----SGGEKQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131922 158 VNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVgifhdeavrndVADRLH 220
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIV-----------IAHRLS 197
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-198 |
1.04e-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: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqQNGVrlpVLNRASLTVNAGECVVLhGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlvtaPA 81
Cdd:cd03264 1 LQLENLTKRY----GKKR---ALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQD--------VL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVVEIRKTtVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLwHLAPSTFSGGEQQRVNIA 161
Cdd:cd03264 65 KQPQKLRRR-IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIA 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 16131922 162 RGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTR 198
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSElGEDR 180
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-218 |
1.14e-20 |
|
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: 89.89 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgDEwVDLVTAPA 81
Cdd:COG2274 474 IELENVSFRY-----PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI---DG-IDLRQIDP 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RkvvEIRKTtVGWVSQ----FLRVI--------PRISALEVVmqplldtgvprEAC-AAKAARLLTRLnvPERLWH-LAP 147
Cdd:COG2274 545 A---SLRRQ-IGVVLQdvflFSGTIrenitlgdPDATDEEII-----------EAArLAGLHDFIEAL--PMGYDTvVGE 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131922 148 --STFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKtRGAAIVGIFHD-EAVRNdvADR 218
Cdd:COG2274 608 ggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRlSTIRL--ADR 678
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
23-218 |
1.61e-20 |
|
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: 86.58 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYLPD-------EGQIqIKHGDEwvdlVTAPARKVVEIRKTtVGWV 95
Cdd:TIGR00972 16 ALKNINLDIPKNQVTALIGPSGCGKSTLLRSL--NRMNDlvpgvriEGKV-LFDGQD----IYDKKIDVVELRRR-VGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 96 SQ----FLRVI-------PRISAL-------EVVMQPLLDTGVPREacaakaarlltrlnVPERLwHLAPSTFSGGEQQR 157
Cdd:TIGR00972 88 FQkpnpFPMSIydniaygPRLHGIkdkkeldEIVEESLKKAALWDE--------------VKDRL-HDSALGLSGGQQQR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131922 158 VNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRgAAIVGIFHD--EAVRndVADR 218
Cdd:TIGR00972 153 LCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNmqQAAR--ISDR 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
24-219 |
1.67e-20 |
|
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: 89.36 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 24 LNRASLTVNAGECVVLHGHSGSGKSTLLRSLyANYLPDEGQIQIkHGDEWVDLVTA---PARKVVEIrkttvgwVSQ--F 98
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLAL-LRLIPSEGEIRF-DGQDLDGLSRRalrPLRRRMQV-------VFQdpF 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 99 LRVIPRISALEVVMQPL--LDTGVPREACAAKAARLLTRLNVPERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEP 176
Cdd:COG4172 373 GSLSPRMTVGQIIAEGLrvHGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131922 177 TASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:COG4172 453 TSALDVSVQAQILDLLRDlQREHGLAYLFISHDLAVVRALAHRV 496
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-217 |
1.77e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.10 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhQQNGvrlPVLNRA----SLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhgdewvDL 76
Cdd:PRK13643 1 MIKFEKVNYTY---QPNS---PFASRAlfdiDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG------DI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 77 VTAPARKVVEIR--KTTVGWVSQF--LRVIPRISALEVVMQPLlDTGVPREACAAKAARLLTRLNVPERLWHLAPSTFSG 152
Cdd:PRK13643 69 VVSSTSKQKEIKpvRKKVGVVFQFpeSQLFEETVLKDVAFGPQ-NFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131922 153 GEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHdeaVRNDVAD 217
Cdd:PRK13643 148 GQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH---LMDDVAD 209
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-218 |
1.96e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.98 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlvtaparkvveirktTVGWVSQFLRV 101
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-------------------RVAYVPQRSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPR--ISALEVVM----QPLLDTGVPREACAAKAARLLTRLNVpERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDE 175
Cdd:NF040873 67 PDSlpLTVRDLVAmgrwARRGLWRRLTRDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131922 176 PTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDvADR 218
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADP 187
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
22-207 |
2.50e-20 |
|
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: 84.19 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHgdewvdlvtAPARKV-VEIRKTTVGWVSQflr 100
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG---------ADISQWdPNELGDHVGYLPQ--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 101 viprisalEVvmqpLLDTGVPREacaakaarlltrlNVperlwhlapstFSGGEQQRVNIARGFIVDYPILLLDEPTASL 180
Cdd:cd03246 84 --------DD----ELFSGSIAE-------------NI-----------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180
....*....|....*....|....*..
gi 16131922 181 DAKNSAAVVELIREAKTRGAAIVGIFH 207
Cdd:cd03246 128 DVEGERALNQAIAALKAAGATRIVIAH 154
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
25-222 |
3.68e-20 |
|
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: 85.65 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 25 NRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQ-IKHGDEWVDLVTAPARKVVEIRKTTVGWVSQF----L 99
Cdd:TIGR02323 20 RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATyIMRSGAELELYQLSEAERRRLMRTEWGFVHQNprdgL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 100 RVipRISALEVVMQPLLDTGVPREA-CAAKAARLLTRLNVPERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTA 178
Cdd:TIGR02323 100 RM--RVSAGANIGERLMAIGARHYGnIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTG 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131922 179 SLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:TIGR02323 178 GLDVSVQARLLDLLRGlVRDLGLAVIIVTHDLGVARLLAQRLLVM 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-217 |
8.65e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.18 E-value: 8.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqQNGVrlPVLNRA----SLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgDEWVDLV 77
Cdd:PRK13649 3 INLQNVSYTY----QAGT--PFEGRAlfdvNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRV---DDTLITS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 78 TAPARKVVEIRKTtVGWVSQFlrviPRiSAL--EVVMQPLL----DTGVPREACAAKAARLLTRLNVPERLWHLAPSTFS 151
Cdd:PRK13649 74 TSKNKDIKQIRKK-VGLVFQF----PE-SQLfeETVLKDVAfgpqNFGVSQEEAEALAREKLALVGISESLFEKNPFELS 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131922 152 GGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHdeaVRNDVAD 217
Cdd:PRK13649 148 GGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH---LMDDVAN 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-203 |
1.30e-19 |
|
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: 83.64 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 20 RLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHgdewVDLVTAPARKVVEIrktTVGWVSQFL 99
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG----RDITGLPPHERARA---GIGYVPEGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 100 RVIPRISalevVMQPLLDTGVPREACAAKAAR-----LLTRLnvPERLWHLApSTFSGGEQQRVNIARGFIVDYPILLLD 174
Cdd:cd03224 85 RIFPELT----VEENLLLGAYARRRAKRKARLervyeLFPRL--KERRKQLA-GTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180
....*....|....*....|....*....
gi 16131922 175 EPTASLDAKNSAAVVELIREAKTRGAAIV 203
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGVTIL 186
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
1.31e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 84.66 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgdewvDLVTAP 80
Cdd:PRK13632 7 MIKVENVSFSY-----PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI-------DGITIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKtTVGWV-----SQFLrvipRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHlAPSTFSGGEQ 155
Cdd:PRK13632 75 KENLKEIRK-KIGIIfqnpdNQFI----GATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDK-EPQNLSGGQK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 156 QRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHD--EAVRndvADRL 219
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlRKTRKKTLISITHDmdEAIL---ADKV 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-219 |
3.83e-19 |
|
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: 82.25 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFILHQQNGVRLPvlnraSLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgdEWVDLVTAPa 81
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNV-----SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL----DGTDIRQLD- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 rkVVEIRKTtVGWVSQ----F---LRVIPRISALEVVMQPLLDtgVPREACAAKAARLLTR---LNVPERLWHLapstfS 151
Cdd:cd03245 73 --PADLRRN-IGYVPQdvtlFygtLRDNITLGAPLADDERILR--AAELAGVTDFVNKHPNgldLQIGERGRGL-----S 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 152 GGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAkTRGAAIVGIFHDEAVRnDVADRL 219
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPSLL-DLVDRI 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-208 |
5.06e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 82.81 E-value: 5.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHQQNGVR--LPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGDEWVDLVT 78
Cdd:PRK10419 3 LLNVSGLSHHYAHGGLSGKHqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW-RGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 79 APARKVveirKTTVGWVSQ--FLRVIPRISALEVVMQPLLD-TGVPREACAAKAARLLTRLNVPERLWHLAPSTFSGGEQ 155
Cdd:PRK10419 82 AQRKAF----RRDIQMVFQdsISAVNPRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131922 156 QRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHD 208
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHD 211
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-222 |
8.87e-19 |
|
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: 83.16 E-value: 8.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFILHQqngvrlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGDEWVDLvtAPA 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFT-------ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQ-GGRDITRL--PPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKvveirktTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVP--ERLWhlaPSTFSGGEQQRVN 159
Cdd:TIGR03265 75 KR-------DYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPgsERKY---PGQLSGGQQQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131922 160 IARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHD--EAVrnDVADRLHPM 222
Cdd:TIGR03265 145 LARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDqeEAL--SMADRIVVM 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-222 |
8.99e-19 |
|
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: 84.35 E-value: 8.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKS----TLLRSLYANYLPDEGQIQIKHgdewVDL 76
Cdd:COG4172 6 LLSVEDLSVAF---GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDG----QDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 77 VTAPARKVVEIRKTTVGWVSQ--------FLRVIPRISalEVVMqplLDTGVPREACAAKAARLLTRLNVPE---RLwHL 145
Cdd:COG4172 79 LGLSERELRRIRGNRIAMIFQepmtslnpLHTIGKQIA--EVLR---LHRGLSGAAARARALELLERVGIPDperRL-DA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 146 APSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:COG4172 153 YPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVM 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-218 |
9.32e-19 |
|
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: 84.08 E-value: 9.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYA--NYLPDEGQIqIKHGD-----EWV 74
Cdd:TIGR03269 1 IEVKNLTKKF-----DGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRI-IYHVAlcekcGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 75 DLVTAPARKVVEIRKTTVGWVSQFL--------RVIPRIS--------------ALEVVMQPLLDTGVPREACAAKAARL 132
Cdd:TIGR03269 73 ERPSKVGEPCPVCGGTLEPEEVDFWnlsdklrrRIRKRIAimlqrtfalygddtVLDNVLEALEEIGYEGKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 133 LTRLNVPERLWHLApSTFSGGEQQRVNIARGfIVDYPILLL-DEPTASLDAKNSAAVVELIREA-KTRGAAIVGIFHDEA 210
Cdd:TIGR03269 153 IEMVQLSHRITHIA-RDLSGGEKQRVVLARQ-LAKEPFLFLaDEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPE 230
|
....*...
gi 16131922 211 VRNDVADR 218
Cdd:TIGR03269 231 VIEDLSDK 238
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-218 |
9.80e-19 |
|
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: 79.03 E-value: 9.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqnGVRlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGdewvdlvtapa 81
Cdd:cd03221 1 IELENLSKTY------GGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 rkvveirkTTVGWVSQFlrviprisalevvmqplldtgvpreacaakaarlltrlnvperlwhlapstfSGGEQQRVNIA 161
Cdd:cd03221 63 --------VKIGYFEQL----------------------------------------------------SGGEKMRLALA 82
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 162 RGFIVDYPILLLDEPTASLDAKNSAAVVELIREakTRGAAIVgIFHDEAVRNDVADR 218
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEALKE--YPGTVIL-VSHDRYFLDQVATK 136
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-202 |
1.30e-18 |
|
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: 80.34 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilHQQNgvrlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEWVDLVTAPA 81
Cdd:cd03268 1 LKTNDLTKTY--GKKR-----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFD-GKSYQKNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RkvveirkttVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACaakaARLLTRLNVPERLwHLAPSTFSGGEQQRVNIA 161
Cdd:cd03268 73 R---------IGALIEAPGFYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16131922 162 RGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAI 202
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITV 179
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-217 |
1.36e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 82.18 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 24 LNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhGDEWVDLVTApARKVVEIRKTtVGWVSQFLRV-I 102
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITI--AGYHITPETG-NKNLKKLRKK-VSLVFQFPEAqL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 103 PRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLAPSTFSGGEQQRVNIArGFIVDYP-ILLLDEPTASLD 181
Cdd:PRK13641 99 FENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIA-GVMAYEPeILCLDEPAAGLD 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 16131922 182 AKNSAAVVELIREAKTRGAAIVGIFHDeavRNDVAD 217
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHN---MDDVAE 210
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
2.67e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.82 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHQQNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIK------HGDEWV 74
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENELV--ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 75 DLVTAPARKVV---EIRKTtVGWVSQF--LRVIPRISALEVVMQPLlDTGVPREACAAKAARLLTRLNVPERLWHLAPST 149
Cdd:PRK13631 99 LITNPYSKKIKnfkELRRR-VSMVFQFpeYQLFKDTIEKDIMFGPV-ALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFG 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 150 FSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVAD 217
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVAD 244
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-212 |
2.80e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.22 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNA----GECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhGDEwvdLVTAPAR--KVVEIRKtTVGWV 95
Cdd:PRK13634 17 PFERRALYDVNVsipsGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI--GER---VITAGKKnkKLKPLRK-KVGIV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 96 SQFlrviPRISALEVVMQ------PlLDTGVPREACAAKAARLLTRLNVPERLWHLAPSTFSGGEQQRVNIARGFIVDYP 169
Cdd:PRK13634 91 FQF----PEHQLFEETVEkdicfgP-MNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131922 170 ILLLDEPTASLDAKNSAAVVELI-REAKTRGAAIVGIFH--DEAVR 212
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFyKLHKEKGLTTVLVTHsmEDAAR 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-207 |
2.90e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.67 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 5 QNVSKTFilhqqNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSL-----YANYlpdEGQIQIKhGDEWVdlvta 79
Cdd:PRK13549 9 KNITKTF-----GGVK--ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvypHGTY---EGEIIFE-GEELQ----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 80 pARKVVEIRKTTVGWVSQFLRVIPRISAL-------EVVMQPLLDTgvprEACAAKAARLLTRL----NVPERLWHLaps 148
Cdd:PRK13549 73 -ASNIRDTERAGIAIIHQELALVKELSVLeniflgnEITPGGIMDY----DAMYLRAQKLLAQLkldiNPATPVGNL--- 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131922 149 tfSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFH 207
Cdd:PRK13549 145 --GLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-213 |
3.76e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSL-----YAnylpdEGQIQIKHGDEwvdlvtaparkvveirkttVGWVS 96
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpYG-----SGRIARPAGAR-------------------VLFLP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 97 QflRV-IPRISALEVVMQPLLDTGVPREACAA--KAARL---LTRLNVpERLWHlapSTFSGGEQQRVNIARGFIVDYPI 170
Cdd:COG4178 433 Q--RPyLPLGTLREALLYPATAEAFSDAELREalEAVGLghlAERLDE-EADWD---QVLSLGEQQRLAFARLLLHKPDW 506
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131922 171 LLLDEPTASLDAKNSAAVVELIREAkTRGAAIVGIFHDEAVRN 213
Cdd:COG4178 507 LFLDEATSALDEENEAALYQLLREE-LPGTTVISVGHRSTLAA 548
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-194 |
5.03e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 82.13 E-value: 5.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgDEwVDLVTAPARkvvEIRKTtVGWVSQ--FL 99
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI---DG-VDIRDLTLE---SLRRQ-IGVVPQdtFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 100 ------------RviPRISALEVvmqplldtgvpREAC-AAKAARLLTRLnvPERLWHL---APSTFSGGEQQRVNIARG 163
Cdd:COG1132 426 fsgtirenirygR--PDATDEEV-----------EEAAkAAQAHEFIEAL--PDGYDTVvgeRGVNLSGGQRQRIAIARA 490
|
170 180 190
....*....|....*....|....*....|.
gi 16131922 164 FIVDYPILLLDEPTASLDAKNSAAVVELIRE 194
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALER 521
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-219 |
7.31e-18 |
|
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: 78.48 E-value: 7.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFILHQqngvrlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhgdewvdlvtapA 81
Cdd:cd03269 1 LEVENVTKRFGRVT-------ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD------------G 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVVEIRKTTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERlWHLAPSTFSGGEQQRVNIA 161
Cdd:cd03269 62 KPLDIAARNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEY-ANKRVEELSKGNQQKVQFI 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 162 RGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRV 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-207 |
8.20e-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: 8.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYlPD---EGQIqIKHGDEWVdlv 77
Cdd:TIGR02633 1 LLEMKGIVKTF-----GGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEI-YWSGSPLK--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 78 tapARKVVEIRKTTVGWVSQFLRVIPRISALE-VVMQPLLDTGVPREACAA---KAARLLTRLNVPERLWHLAPSTFSGG 153
Cdd:TIGR02633 69 ---ASNIRDTERAGIVIIHQELTLVPELSVAEnIFLGNEITLPGGRMAYNAmylRAKNLLRELQLDADNVTRPVGDYGGG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131922 154 EQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFH 207
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISH 199
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
5-222 |
8.46e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.85 E-value: 8.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 5 QNVSKTFILhQQNGVRLPVLNrASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgdEWVDLVTAPARKV 84
Cdd:PRK10070 27 QGLSKEQIL-EKTGLSLGVKD-ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI----DGVDIAKISDAEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 85 VEIRKTTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVpERLWHLAPSTFSGGEQQRVNIARGF 164
Cdd:PRK10070 101 REVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131922 165 IVDYPILLLDEPTASLDAK-NSAAVVELIREAKTRGAAIVGIFH--DEAVRndVADRLHPM 222
Cdd:PRK10070 180 AINPDILLMDEAFSALDPLiRTEMQDELVKLQAKHQRTIVFISHdlDEAMR--IGDRIAIM 238
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-219 |
1.10e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.26 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqnGVRlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQikhgdewVDLVTAPA 81
Cdd:PRK13536 42 IDLAGVSKSY------GDK-AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKIT-------VLGVPVPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RkvVEIRKTTVGWVSQFLRVIP---------------RISA--LEVVMQPLLDTgvpreacaakaARLLTRLNVPerlwh 144
Cdd:PRK13536 108 R--ARLARARIGVVPQFDNLDLeftvrenllvfgryfGMSTreIEAVIPSLLEF-----------ARLESKADAR----- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 145 laPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFH--DEAVRndVADRL 219
Cdd:PRK13536 170 --VSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHfmEEAER--LCDRL 242
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-208 |
1.15e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.66 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqngVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDEWVDLVTAP 80
Cdd:PRK09536 3 MIDVSDLSVEF-------GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEI-RKTTVGW---VSQFLRV--IPRISALEvVMQPLLDTGVPREACAAKAARLLTRlnvperlwhlAPSTFSGGE 154
Cdd:PRK09536 76 SRRVASVpQDTSLSFefdVRQVVEMgrTPHRSRFD-TWTETDRAAVERAMERTGVAQFADR----------PVTSLSGGE 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131922 155 QQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHD 208
Cdd:PRK09536 145 RQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHD 198
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
23-198 |
1.61e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 78.54 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYLPD-------EGQIQIkHGDEwvdlVTAPARKVVEIRKTtVGWV 95
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCL--NRMNDlipgarvEGEILL-DGED----IYDPDVDVVELRRR-VGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 96 SQ----FLRVI-------PRI------SAL-EVVMQPLLDTGVPREacaakaarlltrlnVPERLWHLApSTFSGGEQQR 157
Cdd:COG1117 98 FQkpnpFPKSIydnvaygLRLhgikskSELdEIVEESLRKAALWDE--------------VKDRLKKSA-LGLSGGQQQR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16131922 158 VNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR 198
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD 203
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
28-203 |
1.70e-17 |
|
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: 77.80 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlVTAPARKVveirKTTVGWVSQFLRVIPRISA 107
Cdd:cd03265 20 SFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHD-----VVREPREV----RRRIGIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 108 LE-VVMQPLLdTGVPREACAAKAARLLTRLNVPERLWHLApSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSA 186
Cdd:cd03265 91 WEnLYIHARL-YGVPGAERRERIDELLDFVGLLEAADRLV-KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170
....*....|....*..
gi 16131922 187 AVVELIREAKTRGAAIV 203
Cdd:cd03265 169 HVWEYIEKLKEEFGMTI 185
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
22-209 |
2.63e-17 |
|
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: 80.10 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQikhgdewVDLVTAPARKVVEIRKTtVGWVSQ---- 97
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT-------LDGVPVSSLDQDEVRRR-VSVCAQdahl 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 98 F---LRVIPRISALEVVMQPLLDtgvpreacAAKAARLLtrlNVPERLWHLAPS-------TFSGGEQQRVNIARGFIVD 167
Cdd:TIGR02868 421 FdttVRENLRLARPDATDEELWA--------ALERVGLA---DWLRALPDGLDTvlgeggaRLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16131922 168 YPILLLDEPTASLDAKNSAAVVELIREAkTRGAAIVGIFHDE 209
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLEDLLAA-LSGRTVVLITHHL 530
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-194 |
3.98e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.48 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSktFILHQQNgvrLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGD--EWVDLVTA 79
Cdd:PRK11160 339 LTLNNVS--FTYPDQP---QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiaDYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 80 PARKVVEIRkttVGWVSQFLR-----VIPRIS--ALEVVMQP-----LLDTGVPREACAAKAARLLtrlnvperlwhlap 147
Cdd:PRK11160 414 QAISVVSQR---VHLFSATLRdnlllAAPNASdeALIEVLQQvglekLLEDDKGLNAWLGEGGRQL-------------- 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131922 148 stfSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE 194
Cdd:PRK11160 477 ---SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE 520
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-207 |
4.90e-17 |
|
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: 76.81 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHgdewVDLVTAPARkvvEIRKTtVGWVSQ---- 97
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG----VDIRDLNLR---WLRSQ-IGLVSQepvl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 98 FLRVI--------PRISALEVVmqplldtgvprEAC-AAKAARLLTRLnvPERLWHLA---PSTFSGGEQQRVNIARGFI 165
Cdd:cd03249 89 FDGTIaenirygkPDATDEEVE-----------EAAkKANIHDFIMSL--PDGYDTLVgerGSQLSGGQKQRIAIARALL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16131922 166 VDYPILLLDEPTASLDAKNSAAVVELIREAKtRGAAIVGIFH 207
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAH 196
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-203 |
5.76e-17 |
|
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: 76.56 E-value: 5.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 20 RLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyANYLP-DEGQIQIKHgdewVDLVTAPARKVVEIRkttVGWVSQF 98
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAI-SGLLPpRSGSIRFDG----EDITGLPPHRIARLG---IGYVPEG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 99 LRVIPRISA---LEVVMQPLLDTGVPREAcAAKAARLLTRLNvpERLWHLApSTFSGGEQQRVNIARGFIVDYPILLLDE 175
Cdd:COG0410 87 RRIFPSLTVeenLLLGAYARRDRAEVRAD-LERVYELFPRLK--ERRRQRA-GTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180
....*....|....*....|....*...
gi 16131922 176 PTASLDAKNSAAVVELIREAKTRGAAIV 203
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRLNREGVTIL 190
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-222 |
5.98e-17 |
|
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: 79.08 E-value: 5.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHQQNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDEWVDLvTAP 80
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVVK--AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDM-TKP 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKTTVGWVSQFLRVIPRISALEVVMQPL-LDtgVPREACAAKAARLLTRLNVPER----LWHLAPSTFSGGEQ 155
Cdd:TIGR03269 356 GPDGRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIgLE--LPDELARMKAVITLKMVGFDEEkaeeILDKYPDELSEGER 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 156 QRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALM 501
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-222 |
6.20e-17 |
|
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: 77.92 E-value: 6.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 39 LHGHSGSGKSTLLRSLYANYLPDEGQIqiKHGDEWVDLVTAPARkvveirktTVGWVSQFLRVIPRISALEVVMQPLLDT 118
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSI--MLDGEDVTNVPPHLR--------HINMVFQSYALFPHMTVEENVAFGLKMR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 119 GVPREACAAKAARLLTRLNVPERLwHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAK-NSAAVVELIREAKT 197
Cdd:TIGR01187 71 KVPRAEIKPRVLEALRLVQLEEFA-DRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlRDQMQLELKTIQEQ 149
|
170 180
....*....|....*....|....*
gi 16131922 198 RGAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIM 174
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-181 |
7.90e-17 |
|
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: 75.99 E-value: 7.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGdewVDLVTA-PARKVVEIrkttvgwVSQFLRVIPRIS 106
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLI-NG---VDVTAApPADRPVSM-------LFQENNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 107 ALEVV---MQPLLD-TGVPREACAAKAAR-----LLTRLnvperlwhlaPSTFSGGEQQRVNIARGFIVDYPILLLDEPT 177
Cdd:cd03298 87 VEQNVglgLSPGLKlTAEDRQAIEVALARvglagLEKRL----------PGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
....
gi 16131922 178 ASLD 181
Cdd:cd03298 157 AALD 160
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-207 |
8.98e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.55 E-value: 8.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqNGVrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGDEWVDLVTAP 80
Cdd:PRK15439 11 LLCARSISKQY-----SGV--EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEI-GGNPCARLTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVveirktTVGWVSQFLRVIPRISALEVVMqplldTGVPREACA-AKAARLLTRLNVPERLwHLAPSTFSGGEQQRVN 159
Cdd:PRK15439 83 AHQL------GIYLVPQEPLLFPNLSVKENIL-----FGLPKRQASmQKMKQLLAALGCQLDL-DSSAGSLEVADRQIVE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131922 160 IARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFH 207
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISH 198
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-211 |
9.22e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 76.66 E-value: 9.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLrSLYANYL-PDEGQIQIkhgdewvdlvtapARKVVEIRKTTVGWVSQFLR 100
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLL-NLIAGFVpYQHGSITL-------------DGKPVEGPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 101 VIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPE----RLWHLapstfSGGEQQRVNIARGFIVDYPILLLDEP 176
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGaekrYIWQL-----SGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 16131922 177 TASLDAKNSAAVVE-LIREAKTRGAAIVGIFHD--EAV 211
Cdd:PRK11248 156 FGALDAFTREQMQTlLLKLWQETGKQVLLITHDieEAV 193
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-207 |
1.10e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.03 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 6 NVSKTFilhqqNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEwvdLVTAPARKVV 85
Cdd:PRK11288 9 GIGKTF-----PGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID-GQE---MRFASTTAAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 86 EirkTTVGWVSQFLRVIPRISALEVVMQPLLDTG---VPREACAAKAARLLTRLNVperlwHLAPST----FSGGEQQRV 158
Cdd:PRK11288 78 A---AGVAIIYQELHLVPEMTVAENLYLGQLPHKggiVNRRLLNYEAREQLEHLGV-----DIDPDTplkyLSIGQRQMV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131922 159 NIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFH 207
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-183 |
1.39e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 77.29 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFILHQqngvrlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewVDLVTAPA 81
Cdd:PRK09452 15 VELRGISKSFDGKE-------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD--ITHVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVveirkTTVgwvSQFLRVIPRISALEVV-----MQplldtGVPREACAAK---AARLLtrlnvpeRLWHLA---PSTF 150
Cdd:PRK09452 86 RHV-----NTV---FQSYALFPHMTVFENVafglrMQ-----KTPAAEITPRvmeALRMV-------QLEEFAqrkPHQL 145
|
170 180 190
....*....|....*....|....*....|....
gi 16131922 151 SGGEQQRVNIARGfIVDYP-ILLLDEPTASLDAK 183
Cdd:PRK09452 146 SGGQQQRVAIARA-VVNKPkVLLLDESLSALDYK 178
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
24-222 |
1.42e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.93 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 24 LNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlVTAPARKVVEIRKTTVGWVSQ--FLRV 101
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQD-----LLKADPEAQKLLRQKIQIVFQnpYGSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPRISALEVVMQPLL-DTGVPREACAAKAARLLTRLNV-PERlWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTAS 179
Cdd:PRK11308 106 NPRKKVGQILEEPLLiNTSLSAAERREKALAMMAKVGLrPEH-YDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131922 180 LDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:PRK11308 185 LDVSVQAQVLNLMMDlQQELGLSYVFISHDLSVVEHIADEVMVM 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-218 |
2.28e-16 |
|
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: 74.89 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 4 VQNVSKTFilhqqnGVRlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHgdewVDLVTAP--- 80
Cdd:cd03218 3 AENLSKRY------GKR-KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG----QDITKLPmhk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 -ARKvveirktTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVpERLWHLAPSTFSGGEQQRVN 159
Cdd:cd03218 72 rARL-------GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVE 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131922 160 IARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGaaiVGIF-HDEAVRN--DVADR 218
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRG---IGVLiTDHNVREtlSITDR 202
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-208 |
2.44e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.91 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHQQngvrlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIqikhgdeWV---DLV 77
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQ------ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKI-------WFsghDIT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 78 TAPARKVVEIRKTtVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLaPSTFSGGEQQR 157
Cdd:PRK10908 68 RLKNREVPFLRRQ-IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNF-PIQLSGGEQQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131922 158 VNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHD 208
Cdd:PRK10908 146 VGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHD 196
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-195 |
2.59e-16 |
|
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: 77.17 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlvtaparkvveIRKttvgwVSQ-FLR 100
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD---------------IRD-----VTQaSLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 101 vipriSALEVVMQpllDT----------------GVPREAC--AAKAARL---LTRL------NVPERLWHLapstfSGG 153
Cdd:COG5265 432 -----AAIGIVPQ---DTvlfndtiayniaygrpDASEEEVeaAARAAQIhdfIESLpdgydtRVGERGLKL-----SGG 498
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16131922 154 EQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREA 195
Cdd:COG5265 499 EKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV 540
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-218 |
3.28e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.60 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGdewvdlvtap 80
Cdd:COG3845 5 ALELRGITKRF-----GGVV--ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID-G---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 arKVVEIRKTT------VGWVSQFLRVIPRISALEVV---MQPLLDTGVPREACAAKAARLLTR--LNV-PERL-WHLap 147
Cdd:COG3845 67 --KPVRIRSPRdaialgIGMVHQHFMLVPNLTVAENIvlgLEPTKGGRLDRKAARARIRELSERygLDVdPDAKvEDL-- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131922 148 stfSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFH--DEaVRnDVADR 218
Cdd:COG3845 143 ---SVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHklRE-VM-AIADR 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-203 |
3.41e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.93 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 21 LPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGdewvdlvtaPARKVVEIRKTTVGWVSQFLR 100
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT---------PLAEQRDEPHENILYLGHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 101 VIPRISALEVV--MQPLLDtGVPREACAAKAARLLTRLNvperlwHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTA 178
Cdd:TIGR01189 84 LKPELSALENLhfWAAIHG-GAQRTIEDALAAVGLTGFE------DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*
gi 16131922 179 SLDAKNSAAVVELIREAKTRGAAIV 203
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVL 181
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-218 |
4.41e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.36 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEWVDLVTAP 80
Cdd:PRK09700 5 YISMAGIGKSF-----GPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-NINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVveirktTVGWVSQFLRVIPRISALE-----------VVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLAPSt 149
Cdd:PRK09700 77 AAQL------GIGIIYQELSVIDELTVLEnlyigrhltkkVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSIS- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131922 150 fsggEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADR 218
Cdd:PRK09700 150 ----HKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDR 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
23-208 |
5.00e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 74.73 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEwvdlVTAPARKVVEIRKtTVGWVSQ----- 97
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIK-GEP----IKYDKKSLLEVRK-TVGIVFQnpddq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 98 -FlrvIPRISAlEVVMQPlLDTGVPREACAAKAARLLTRLNVpERLWHLAPSTFSGGEQQRVNIArGFIVDYP-ILLLDE 175
Cdd:PRK13639 91 lF---APTVEE-DVAFGP-LNLGLSKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIA-GILAMKPeIIVLDE 163
|
170 180 190
....*....|....*....|....*....|...
gi 16131922 176 PTASLDAKNSAAVVELIREAKTRGAAIVGIFHD 208
Cdd:PRK13639 164 PTSGLDPMGASQIMKLLYDLNKEGITIIISTHD 196
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-207 |
6.18e-16 |
|
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: 72.97 E-value: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 18 GVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSL--YANYLPDEGQIqikhgdewvdLVTAPARKVVEIRKTtVGWV 95
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEV----------LINGRPLDKRSFRKI-IGYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 96 SQFLRVIPRISALEVVMQplldtgvpreacaakAARLltrlnvperlwhlapSTFSGGEQQRVNIARGFIVDYPILLLDE 175
Cdd:cd03213 88 PQDDILHPTLTVRETLMF---------------AAKL---------------RGLSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190
....*....|....*....|....*....|..
gi 16131922 176 PTASLDAKNSAAVVELIREAKTRGAAIVGIFH 207
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-181 |
8.17e-16 |
|
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: 75.15 E-value: 8.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 27 ASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGDEWVDlvtAPARKVVEIRKTTVGWVSQFLRVIPRIS 106
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVL-NGRTLFD---SRKGIFLPPEKRRIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131922 107 ALEVVMQPLLDTGVP-REACAAKAARLLTRLNVPERLwhlaPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLD 181
Cdd:TIGR02142 92 VRGNLRYGMKRARPSeRRISFERVIELLGIGHLLGRL----PGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
22-207 |
8.18e-16 |
|
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: 73.42 E-value: 8.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEWVDLVTAPARKvveirktTVGWVSQ---- 97
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILID-GHDVRDYTLASLRR-------QIGLVSQdvfl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 98 FLRVI--------PRISALEVVmqplldtgvpREACAAKAARLLTRL------NVPERlwhlaPSTFSGGEQQRVNIARG 163
Cdd:cd03251 88 FNDTVaeniaygrPGATREEVE----------EAARAANAHEFIMELpegydtVIGER-----GVKLSGGQRQRIAIARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131922 164 FIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVgIFH 207
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFV-IAH 195
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-188 |
1.29e-15 |
|
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: 75.14 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEWVDLVTAPA 81
Cdd:TIGR02203 331 VEFRNVTFRY-----PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLD-GHDLADYTLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKvveirktTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLN-VPERLwHLA----PSTFSGGEQQ 156
Cdd:TIGR02203 405 RR-------QVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDkLPLGL-DTPigenGVLLSGGQRQ 476
|
170 180 190
....*....|....*....|....*....|..
gi 16131922 157 RVNIARGFIVDYPILLLDEPTASLDAKNSAAV 188
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLV 508
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-216 |
1.65e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 73.66 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSktFILHQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhgdewvDLVTAPA 81
Cdd:PRK13646 3 IRFDNVS--YTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD------DITITHK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVVEIR--KTTVGWVSQFlrviPRiSAL-------EVVMQPLlDTGVPREACAAKAARLLTRLNVPERLWHLAPSTFSG 152
Cdd:PRK13646 75 TKDKYIRpvRKRIGMVFQF----PE-SQLfedtverEIIFGPK-NFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131922 153 GEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKT-RGAAIVGIFHDeavRNDVA 216
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdENKTIILVSHD---MNEVA 210
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-208 |
1.73e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.95 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNAGECVVLHGHSGSGKSTLLRSLyANYLPDEGQIQIkhgDEwVDLVTAPARKVVEIRkttvGWVSQflRVIPriSA 107
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARM-AGLLPGQGEILL---NG-RPLSDWSAAELARHR----AYLSQ--QQSP--PF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 108 LEVVMQpLLDTGVPREACAAKAARLLTRLNvpERLWhLAP------STFSGGEQQRVNIARGFIVDYP-------ILLLD 174
Cdd:COG4138 83 AMPVFQ-YLALHQPAGASSEAVEQLLAQLA--EALG-LEDklsrplTQLSGGEWQRVRLAAVLLQVWPtinpegqLLLLD 158
|
170 180 190
....*....|....*....|....*....|....
gi 16131922 175 EPTASLDAKNSAAVVELIREAKTRGAAIVGIFHD 208
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELCQQGITVVMSSHD 192
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
22-197 |
2.02e-15 |
|
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: 72.26 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgDEwvdlvtaparkvVEIRKTTVGWvsqfLRv 101
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILI---DG------------IDIRDISRKS----LR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 ipriSALEVVMQ-PLL-----------------DTGVPREACAAKAARLLTRL------NVPERlwhlaPSTFSGGEQQR 157
Cdd:cd03254 77 ----SMIGVVLQdTFLfsgtimenirlgrpnatDEEVIEAAKEAGAHDFIMKLpngydtVLGEN-----GGNLSQGERQL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131922 158 VNIARGFIVDYPILLLDEPTASLDAKNSAAV---VELIREAKT 197
Cdd:cd03254 148 LAIARAMLRDPKILILDEATSNIDTETEKLIqeaLEKLMKGRT 190
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-207 |
2.35e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 4 VQNVSKTFilhqqNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEwvdlVTAPARK 83
Cdd:PRK10762 7 LKGIDKAF-----PGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYL-GKE----VTFNGPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 84 vvEIRKTTVGWVSQFLRVIPRISALEVVMqplldtgVPREACA-----------AKAARLLTRLNVPERLwHLAPSTFSG 152
Cdd:PRK10762 75 --SSQEAGIGIIHQELNLIPQLTIAENIF-------LGREFVNrfgridwkkmyAEADKLLARLNLRFSS-DKLVGELSI 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131922 153 GEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFH 207
Cdd:PRK10762 145 GEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISH 199
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-214 |
3.99e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 72.53 E-value: 3.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEG-QIQIKhgdewVDLVTAPARKVVEIRKTtVGWV----- 95
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNpNSKIT-----VDGITLTAKTVWDIREK-VGIVfqnpd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 96 SQFLRVipriSALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLwHLAPSTFSGGEQQRVNIARGFIVDYPILLLDE 175
Cdd:PRK13640 95 NQFVGA----TVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYI-DSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16131922 176 PTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHD--EAVRND 214
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKlKKKNNLTVISITHDidEANMAD 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-207 |
4.01e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 71.87 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYLPD---EGQIQikhGDEWVDLVTAPARKVVEIRKTtVGWVSQFL 99
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVF--NRLIElypEARVS---GEVYLDGQDIFKMDVIELRRR-VQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 100 RVIPRISALE-VVMQPLLDTGV-------PREACAAKAARLL----TRLNVPerlwhlaPSTFSGGEQQRVNIARGFIVD 167
Cdd:PRK14247 92 NPIPNLSIFEnVALGLKLNRLVkskkelqERVRWALEKAQLWdevkDRLDAP-------AGKLSGGQQQRLCIARALAFQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16131922 168 YPILLLDEPTASLDAKNSAAVVELIREAKtRGAAIVGIFH 207
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELK-KDMTIVLVTH 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-206 |
4.59e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.45 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHQqngvrlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEwvdlVTAP 80
Cdd:COG4152 1 MLELKGLTKRFGDKT-------AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD-GEP----LDPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVV----EIR----KTTVGWVSQFLrvipriSALevvmqplldTGVPREACAAKAARLLTRLNVPERlWHLAPSTFSG 152
Cdd:COG4152 69 DRRRIgylpEERglypKMKVGEQLVYL------ARL---------KGLSKAEAKRRADEWLERLGLGDR-ANKKVEELSK 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131922 153 GEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIvgIF 206
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTV--IF 184
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-222 |
4.70e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.95 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqNGVrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgdEWVDLVTAP 80
Cdd:PRK11607 19 LLEIRNLTKSF-----DGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML----DGVDLSHVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ArkvveiRKTTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPErLWHLAPSTFSGGEQQRVNI 160
Cdd:PRK11607 88 P------YQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQE-FAKRKPHQLSGGQRQRVAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131922 161 ARGFIVDYPILLLDEPTASLDAK----NSAAVVELIREAktrGAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIM 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-222 |
6.03e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 6.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKST-------LLRSLYANYLpdEGQIQIkHGDew 73
Cdd:PRK15134 5 LLAIENLSVAF---RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVtalsilrLLPSPPVVYP--SGDIRF-HGE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 74 vDLVTAPARKVVEIRKTTVGWVSQFlrviPRISalevvMQPL------------LDTGVPREACAAKAARLLTRL---NV 138
Cdd:PRK15134 77 -SLLHASEQTLRGVRGNKIAMIFQE----PMVS-----LNPLhtlekqlyevlsLHRGMRREAARGEILNCLDRVgirQA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 139 PERLwHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHDEAVRNDVAD 217
Cdd:PRK15134 147 AKRL-TDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLAD 225
|
....*
gi 16131922 218 RLHPM 222
Cdd:PRK15134 226 RVAVM 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-181 |
7.34e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.77 E-value: 7.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 26 RASLTVNAGECVVLHGHSGSGKSTLLrSLYANYL-PDEGQIQIKHGDEwvdLVTAPARKVVEIRKTTVGWVSQfLRVIPR 104
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLL-NLIAGFLtPASGSLTLNGQDH---TTTPPSRRPVSMLFQENNLFSH-LTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 105 ISaleVVMQPLLD-TGVPREACAAKAAR-----LLTRLnvperlwhlaPSTFSGGEQQRVNIARGFIVDYPILLLDEPTA 178
Cdd:PRK10771 92 IG---LGLNPGLKlNAAQREKLHAIARQmgiedLLARL----------PGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
...
gi 16131922 179 SLD 181
Cdd:PRK10771 159 ALD 161
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-222 |
7.94e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.05 E-value: 7.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 16 QNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQikhgdeWV--DLVTAPARKVVEIRKTtvg 93
Cdd:PRK15079 29 QPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVA------WLgkDLLGMKDDEWRAVRSD--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 94 wvsqfLRVI---------PRISALEVVMQPL--LDTGVPREACAAKAARLLTRLNVPERLWHLAPSTFSGGEQQRVNIAR 162
Cdd:PRK15079 100 -----IQMIfqdplaslnPRMTIGEIIAEPLrtYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIAR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131922 163 GFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:PRK15079 175 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQlQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-219 |
8.30e-15 |
|
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: 72.47 E-value: 8.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 18 GVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQ-----IKHGDEwvdlvtaparkvvEIRKTTV 92
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgadLSQWDR-------------EELGRHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 93 GWVSQflRV----------IPR---ISALEVVMqplldtgvpreacAAKAARL------L-----TRLNVperlwhlAPS 148
Cdd:COG4618 409 GYLPQ--DVelfdgtiaenIARfgdADPEKVVA-------------AAKLAGVhemilrLpdgydTRIGE-------GGA 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131922 149 TFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVrNDVADRL 219
Cdd:COG4618 467 RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSL-LAAVDKL 536
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-222 |
9.15e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.58 E-value: 9.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilHQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhGDEWVDLVTAPA 81
Cdd:PRK13645 7 IILDNVSYTY--AKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV--GDYAIPANLKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVVEIRKTtVGWVSQF--LRVIPRISALEVVMQPLlDTGVPREACAAKAARLLTRLNVPERLWHLAPSTFSGGEQQRVN 159
Cdd:PRK13645 83 KEVKRLRKE-IGLVFQFpeYQLFQETIEKDIAFGPV-NLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131922 160 IARGFIVDYPILLLDEPTASLDAKNSAAVVEL-IREAKTRGAAIVGIFH--DEAVRndVADRLHPM 222
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLfERLNKEYKKRIIMVTHnmDQVLR--IADEVIVM 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-222 |
1.25e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 19 VRLPVLNRASLTVNA----------GECVVLHGHSGSGKSTLLRSLYAnyLPDEGQIQIKHGDEWVDlvTAPARKVVEIR 88
Cdd:PRK10261 325 LRSGLLNRVTREVHAvekvsfdlwpGETLSLVGESGSGKSTTGRALLR--LVESQGGEIIFNGQRID--TLSPGKLQALR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 89 KTtVGWVSQ--FLRVIPRISALEVVMQPLLDTGV-PREACAAKAARLLTRLNV-PERLWHLaPSTFSGGEQQRVNIARGF 164
Cdd:PRK10261 401 RD-IQFIFQdpYASLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLlPEHAWRY-PHEFSGGQRQRICIARAL 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131922 165 IVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSIRGQIINLLLDlQRDFGIAYLFISHDMAVVERISHRVAVM 537
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-194 |
1.34e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 70.85 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVskTFILHQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlVTAPA 81
Cdd:PRK13637 3 IKIENL--THIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVD-----ITDKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVVEIRKtTVGWVSQ------FLRVIPRISALEVVMQPLLDTGVPREacaAKAARLLTRLNVpERLWHLAPSTFSGGEQ 155
Cdd:PRK13637 76 VKLSDIRK-KVGLVFQypeyqlFEETIEKDIAFGPINLGLSEEEIENR---VKRAMNIVGLDY-EDYKDKSPFELSGGQK 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16131922 156 QRVNIArGFIVDYP-ILLLDEPTASLDAKNSAAVVELIRE 194
Cdd:PRK13637 151 RRVAIA-GVVAMEPkILILDEPTAGLDPKGRDEILNKIKE 189
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-208 |
1.94e-14 |
|
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: 68.99 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 16 QNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEwvdlvTAPARKVVEIRKTTVGWV 95
Cdd:TIGR01166 2 PGGPE--VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLID-GEP-----LDYSRKGLLERRQRVGLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 96 SQ------FlrvIPRISAlEVVMQPLlDTGVPREACAAKAARLLTRLNVpERLWHLAPSTFSGGEQQRVNIARGFIVDYP 169
Cdd:TIGR01166 74 FQdpddqlF---AADVDQ-DVAFGPL-NLGLSEAEVERRVREALTAVGA-SGLRERPTHCLSGGEKKRVAIAGAVAMRPD 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 16131922 170 ILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHD 208
Cdd:TIGR01166 148 VLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-207 |
3.44e-14 |
|
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: 68.84 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyANYLPDEGqiqIKHGDEWVDlvtAPARKVVEIRKtTVGWVSQFLRVI 102
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAI-SGRVEGGG---TTSGQILFN---GQPRKPDQFQK-CVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 103 PRISALEVV--MQPLLdtgVPReaCAAKAARllTRLNVPERLWHLAPST--------FSGGEQQRVNIARGFIVDYPILL 172
Cdd:cd03234 94 PGLTVRETLtyTAILR---LPR--KSSDAIR--KKRVEDVLLRDLALTRiggnlvkgISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190
....*....|....*....|....*....|....*
gi 16131922 173 LDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFH 207
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-219 |
3.51e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.83 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqnGVRLpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQikhgdewvdLVTAPA 81
Cdd:PRK13537 8 IDFRNVEKRY------GDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIS---------LCGEPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVVEIRKTTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLL--TRLnvpERLWHLAPSTFSGGEQQRVN 159
Cdd:PRK13537 72 PSRARHARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLefAKL---ENKADAKVGELSGGMKRRLT 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131922 160 IARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFH--DEAVRndVADRL 219
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHfmEEAER--LCDRL 208
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-222 |
3.86e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.65 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 3 NVQNVSKTFILHQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQI------KHGDEWVDL 76
Cdd:PRK10261 11 DVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCdkmllrRRSRQVIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 77 VTAPARKVVEIRKTTVGWVSQ--FLRVIPRISALEVVMQPL-LDTGVPREACAAKAARLLTRLNVPERLWHLA--PSTFS 151
Cdd:PRK10261 91 SEQSAAQMRHVRGADMAMIFQepMTSLNPVFTVGEQIAESIrLHQGASREEAMVEAKRMLDQVRIPEAQTILSryPHQLS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131922 152 GGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVlQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
24-214 |
4.04e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.39 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 24 LNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHgdewvDLVTAPARKvvEIRKTtVGWV-----SQF 98
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN-----QAITDDNFE--KLRKH-IGIVfqnpdNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 99 lrvIPRISALEVVMQpLLDTGVPREACAAKAARLLTRLNVPERLWHlAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTA 178
Cdd:PRK13648 97 ---VGSIVKYDVAFG-LENHAVPYDEMHRRVSEALKQVDMLERADY-EPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 16131922 179 SLDAKNSAAVVELIREAK-TRGAAIVGIFHD--EAVRND 214
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKsEHNITIISITHDlsEAMEAD 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
22-208 |
4.11e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.27 E-value: 4.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDEWVDLVTAPARKV------------VEIRK 89
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLallpqhhltpegITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 90 TtVG-----WVSQFLRVIPRISALevVMQPLLDTGVpreacAAKAARLLTRLnvperlwhlapstfSGGEQQRVNIARGF 164
Cdd:PRK11231 96 L-VAygrspWLSLWGRLSAEDNAR--VNQAMEQTRI-----NHLADRRLTDL--------------SGGQRQRAFLAMVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131922 165 IVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHD 208
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD 197
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-68 |
4.86e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.95 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHQQNGVRL---------------PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQI 65
Cdd:COG1134 4 MIEVENVSKSYRLYHEPSRSLkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
...
gi 16131922 66 QIK 68
Cdd:COG1134 84 EVN 86
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-222 |
5.76e-14 |
|
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: 67.46 E-value: 5.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEwvdlvtaparkvVEIRKttvgwvsqflrviprisa 107
Cdd:cd03215 20 SFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD-GKP------------VTRRS------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 108 levvmqplldtgvPREACAAKAAR---------LLTRLNVPERLwhLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTA 178
Cdd:cd03215 69 -------------PRDAIRAGIAYvpedrkregLVLDLSVAENI--ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131922 179 SLDAKNSAAVVELIREAKTRGAAIVGIF--HDEAVRndVADRLHPM 222
Cdd:cd03215 134 GVDVGAKAEIYRLIRELADAGKAVLLISseLDELLG--LCDRILVM 177
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-207 |
6.22e-14 |
|
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: 67.90 E-value: 6.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGdewvdlvtaPARKVVEIRKTTVGWVSQFLRVI 102
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG---------PLDFQRDSIARGLLYLGHAPGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 103 PRISALEVV--MQPLLDTGVPREAcaakaarlLTRLNVpERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASL 180
Cdd:cd03231 86 TTLSVLENLrfWHADHSDEQVEEA--------LARVGL-NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*..
gi 16131922 181 DAKNSAAVVELIREAKTRGAAIVGIFH 207
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
22-195 |
6.30e-14 |
|
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: 68.29 E-value: 6.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgDEwVDLVTAPARKvveIRkttvgwvsQFLRV 101
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI---DG-VDISKIGLHD---LR--------SRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPRISAL-----------------EVVMQPLLDTGVpREACAAKAARLLTRLnvperlwHLAPSTFSGGEQQRVNIARGF 164
Cdd:cd03244 83 IPQDPVLfsgtirsnldpfgeysdEELWQALERVGL-KEFVESLPGGLDTVV-------EEGGENLSVGQRQLLCLARAL 154
|
170 180 190
....*....|....*....|....*....|.
gi 16131922 165 IVDYPILLLDEPTASLDAKNSAAVVELIREA 195
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIREA 185
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-195 |
6.37e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.26 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNAGECVVLHGHSGSGKSTLLRSLYAnYLPDEGQIQIkHGDEWVDLVTAPARKvveirktTVGWVSQflrviprisa 107
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKI-NGIELRELDPESWRK-------HLSWVGQ---------- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 108 levvmQPLLDTGVPRE--------ACAAKAARLLTRLNVPERLWHLAP----------STFSGGEQQRVNIARGFIVDYP 169
Cdd:PRK11174 431 -----NPQLPHGTLRDnvllgnpdASDEQLQQALENAWVSEFLPLLPQgldtpigdqaAGLSVGQAQRLALARALLQPCQ 505
|
170 180
....*....|....*....|....*.
gi 16131922 170 ILLLDEPTASLDAKNSAAVVELIREA 195
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAA 531
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
24-196 |
7.81e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 68.26 E-value: 7.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 24 LNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYLPD-------EGQIQIKHGDewvdlVTAPARKVVEIRKTtVGWVS 96
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSI--NRMNDlnpevtiTGSIVYNGHN-----IYSPRTDTVDLRKE-IGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 97 QFLRVIPrISALEVVMQPL----------LDTGVPReacAAKAARLLTRlnVPERLwHLAPSTFSGGEQQRVNIARGFIV 166
Cdd:PRK14239 93 QQPNPFP-MSIYENVVYGLrlkgikdkqvLDEAVEK---SLKGASIWDE--VKDRL-HDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190
....*....|....*....|....*....|
gi 16131922 167 DYPILLLDEPTASLDAKNSAAVVELIREAK 196
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLK 195
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-222 |
8.92e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.48 E-value: 8.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqQNGVrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlvTAP 80
Cdd:PRK13644 1 MIRLENVSYSY----PDGT--PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID------TGD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKTtVGWVSQF--LRVIPRISALEVVMQPLlDTGVPREACAAKAARLLTRLNVpERLWHLAPSTFSGGEQQRV 158
Cdd:PRK13644 69 FSKLQGIRKL-VGIVFQNpeTQFVGRTVEEDLAFGPE-NLCLPPIEIRKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131922 159 NIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHD-EAVRndVADRLHPM 222
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNlEELH--DADRIIVM 208
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-224 |
8.99e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.98 E-value: 8.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilHQQNGVRLPVlNRASLTVNAGECVVLHGHSGSGKS----TLLRSLYANylpdeGQIQ---IKHGDEW 73
Cdd:PRK09473 12 LLDVKDLRVTF--STPDGDVTAV-NDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAAN-----GRIGgsaTFNGREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 74 VDLvtaPARKVVEIRKTTVGWVSQ--------FLRVIPRIsaLEVVMqplLDTGVPREACAAKAARLLTRLNVPE---RL 142
Cdd:PRK09473 84 LNL---PEKELNKLRAEQISMIFQdpmtslnpYMRVGEQL--MEVLM---LHKGMSKAEAFEESVRMLDAVKMPEarkRM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 143 wHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHDEAVRNDVADRLHP 221
Cdd:PRK09473 156 -KMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLV 234
|
...
gi 16131922 222 MGA 224
Cdd:PRK09473 235 MYA 237
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-183 |
9.07e-14 |
|
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: 68.97 E-value: 9.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 27 ASLTVNAGECVVLHGHSGSGKSTLLRSLyANYL-PDEGQIQIkhGDE-WVDlvtaPARKV---VEIRKttVGWVSQFLRV 101
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAI-AGLErPDSGRIRL--GGEvLQD----SARGIflpPHRRR--IGYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPRISalevVMQPLLD--TGVPREACAAKAARLLTRLNVpERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTAS 179
Cdd:COG4148 89 FPHLS----VRGNLLYgrKRAPRAERRISFDEVVELLGI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
....
gi 16131922 180 LDAK 183
Cdd:COG4148 164 LDLA 167
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-219 |
1.03e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.32 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqnGVRlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGqiQIKHGDewvdlvtap 80
Cdd:COG0488 315 VLELEGLSKSY------GDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG--TVKLGE--------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 arkvveirKTTVGWVSQFLRVI-PRISALEvVMQPLLDTGVPREACAakaarLLTRLN-VPERLWHLApSTFSGGEQQRV 158
Cdd:COG0488 377 --------TVKIGYFDQHQEELdPDKTVLD-ELRDGAPGGTEQEVRG-----YLGRFLfSGDDAFKPV-GVLSGGEKARL 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131922 159 NIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKtrGAAIVgIFHDEAVRNDVADRL 219
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP--GTVLL-VSHDRYFLDRVATRI 499
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-212 |
1.08e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.35 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKST----LLRslyanYLPDEGQIqikhgdeWVD---LVTAPARKVVEIR-KTTVGW 94
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLR-----LINSQGEI-------WFDgqpLHNLNRRQLLPVRhRIQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 95 VSQFLRVIPRISALEV------VMQPLLdTGVPREAcaaKAARLLTRLNVPERLWHLAPSTFSGGEQQRVNIARGFIVDY 168
Cdd:PRK15134 369 QDPNSSLNPRLNVLQIieeglrVHQPTL-SAAQREQ---QVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131922 169 PILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHD-EAVR 212
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSlQQKHQLAYLFISHDlHVVR 490
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-208 |
1.16e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.43 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIqIKHGDewvDLVTAPArkvvEIRKTTVGWVSQflrv 101
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL-LFEGE---DISTLKP----EIYRQQVSYCAQ---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPRISALEVVMQPLLDTGVPREACAAKA-ARLLTRLNVPERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASL 180
Cdd:PRK10247 89 TPTLFGDTVYDNLIFPWQIRNQQPDPAIfLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180
....*....|....*....|....*....
gi 16131922 181 DAKNSAAVVELI-REAKTRGAAIVGIFHD 208
Cdd:PRK10247 169 DESNKHNVNEIIhRYVREQNIAVLWVTHD 197
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-203 |
1.28e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.21 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlvtaparkvveIRKTTVGWVSQFL-- 99
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---------------IDDPDVAEACHYLgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 100 --RVIPRISALEVVM--QPLLDTGVPREACAAKAARLltrlnvpERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDE 175
Cdd:PRK13539 81 rnAMKPALTVAENLEfwAAFLGGEELDIAAALEAVGL-------APLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180
....*....|....*....|....*...
gi 16131922 176 PTASLDAKNSAAVVELIREAKTRGAAIV 203
Cdd:PRK13539 154 PTAALDAAAVALFAELIRAHLAQGGIVI 181
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-202 |
1.44e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 67.36 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqnGVRlPVLNRASLTVNAGECVVLHGHSGSGKST-------LLRslyanylPDEGQIQIkhGDEw 73
Cdd:COG1137 3 TLEAENLVKSY------GKR-TVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymivgLVK-------PDSGRIFL--DGE- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 74 vDLVTAP----ARKVV-----E---IRKTTVgwvSQFLRVIprisaLEVvmqplldTGVPREACAAKAARLLTRLNvper 141
Cdd:COG1137 66 -DITHLPmhkrARLGIgylpqEasiFRKLTV---EDNILAV-----LEL-------RKLSKKEREERLEELLEEFG---- 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 142 LWHLAPS---TFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKnsaAVVE---LIREAKTRGAAI 202
Cdd:COG1137 126 ITHLRKSkaySLSGGERRRVEIARALATNPKFILLDEPFAGVDPI---AVADiqkIIRHLKERGIGV 189
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-194 |
1.58e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.80 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHQQNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlVTap 80
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKR--ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD-----VT-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 aRKVVEIRKTTVGWVSQflrviprisalevvmQPLLDT------------------------GVP---REACAAKAARL- 132
Cdd:COG1101 72 -KLPEYKRAKYIGRVFQ---------------DPMMGTapsmtieenlalayrrgkrrglrrGLTkkrRELFRELLATLg 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131922 133 --L-TRLNVPERLwhlapstFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE 194
Cdd:COG1101 136 lgLeNRLDTKVGL-------LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEK 193
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-198 |
1.87e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.21 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 5 QNVSKTFILHQqngvrlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlVTAPArkv 84
Cdd:PRK11432 10 KNITKRFGSNT-------VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED-----VTHRS--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 85 veIRKTTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKaarlltrlnVPERLWHLAPSTF--------SGGEQQ 156
Cdd:PRK11432 75 --IQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQR---------VKEALELVDLAGFedryvdqiSGGQQQ 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16131922 157 RVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR 198
Cdd:PRK11432 144 RVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQ 185
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-218 |
1.95e-13 |
|
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: 66.91 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 4 VQNVSKTFilhqqnGVRlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHgdewVDLVTAP--- 80
Cdd:TIGR04406 4 AENLIKSY------KKR-KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDG----QDITHLPmhe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 -ARkvveirkTTVGWVSQFLRVIPRISALEVVMQPL-LDTGVPREACAAKAARLLTRLNVpERLWHLAPSTFSGGEQQRV 158
Cdd:TIGR04406 73 rAR-------LGIGYLPQEASIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQI-SHLRDNKAMSLSGGERRRV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131922 159 NIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIvgIFHDEAVRN--DVADR 218
Cdd:TIGR04406 145 EIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGV--LITDHNVREtlDICDR 204
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-208 |
2.57e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNAGECVVLHGHSGSGKSTLLRSLyANYLPDEGQIQIKHgdewVDLVTAPARKVVEIRkttvGWVSQFLRVIPRISa 107
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARM-AGLLPGSGSIQFAG----QPLEAWSAAELARHR----AYLSQQQTPPFAMP- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 108 levVMQPL---LDTGVPREACAAKAARLLTRLNVPERLwHLAPSTFSGGEQQRVNIARGFIVDYP-------ILLLDEPT 177
Cdd:PRK03695 86 ---VFQYLtlhQPDKTRTEAVASALNEVAEALGLDDKL-GRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPM 161
|
170 180 190
....*....|....*....|....*....|.
gi 16131922 178 ASLDAKNSAAVVELIREAKTRGAAIVGIFHD 208
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQGIAVVMSSHD 192
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-219 |
2.86e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.05 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHgdewvDLVTA-----PAR----KVVEIRKTTV 92
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-----DLIVArlqqdPPRnvegTVYDFVAEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 93 GWVSQFLRVIPRISALevVMQPlldtgvPREACAAKAARLLTRLNVpERLWHL----------------AP-STFSGGEQ 155
Cdd:PRK11147 92 EEQAEYLKRYHDISHL--VETD------PSEKNLNELAKLQEQLDH-HNLWQLenrinevlaqlgldpdAAlSSLSGGWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 156 QRVNIARGFIVDYPILLLDEPTASLDaknsaavVELIR--EA--KTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLD-------IETIEwlEGflKTFQGSIIFISHDRSFIRNMATRI 223
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-219 |
2.86e-13 |
|
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: 66.66 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 30 TVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgdewvDLVTApARKVVEIRKTTVGWVSQFLRVIPRISALE 109
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-------ELDTV-SYKPQYIKADYEGTVRDLLSSITKDFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 110 V-----VMQPLldtgvpreacaaKAARLLTRlNVPErlwhlapstFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKN 184
Cdd:cd03237 93 PyfkteIAKPL------------QIEQILDR-EVPE---------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 16131922 185 SAAVVELIR---EAKTRGAAIVGifHDEAVRNDVADRL 219
Cdd:cd03237 151 RLMASKVIRrfaENNEKTAFVVE--HDIIMIDYLADRL 186
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-217 |
3.08e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.79 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYLPD-------EGQIQIKHGDewvdlVTAPARKVVEIRKTtVGWV 95
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTF--NRLLElneearvEGEVRLFGRN-----IYSPDVDPIEVRRE-VGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 96 SQFLRVIPRISALEVVMQPLLDTGV--------PREACAAKAARLLTRlnVPERLwHLAPSTFSGGEQQRVNIARGFIVD 167
Cdd:PRK14267 91 FQYPNPFPHLTIYDNVAIGVKLNGLvkskkeldERVEWALKKAALWDE--VKDRL-NDYPSNLSGGQRQRLVIARALAMK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131922 168 YPILLLDEPTASLDAKNSAAVVELIREAKTRgAAIVGIFHDEAVRNDVAD 217
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSD 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-222 |
3.66e-13 |
|
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: 66.36 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgdEWVDLVTAPArkvvEIRKTTVGWVSQ----F 98
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV----DGHDLALADP----AWLRRQVGVVLQenvlF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 99 LRVIPRISALEvvmqpllDTGVPREACAAkAARLLTR----LNVPERLWHLA---PSTFSGGEQQRVNIARGFIVDYPIL 171
Cdd:cd03252 89 NRSIRDNIALA-------DPGMSMERVIE-AAKLAGAhdfiSELPEGYDTIVgeqGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131922 172 LLDEPTASLDAKNSAAVVELIREAkTRGAAIVGIFHD-EAVRNdvADRLHPM 222
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRlSTVKN--ADRIIVM 209
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-222 |
5.06e-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: 65.24 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSL--YANYLPDEGQIQIKhGDEWVDL-VTAPARKVVeirktTVGWVSQfl 99
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFK-GEDITDLpPEERARLGI-----FLAFQYP-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 100 rviPRISalevvmqplldtGVpreacaaKAARLLTRLNVperlwhlapsTFSGGEQQRVNIARGFIVDYPILLLDEPTAS 179
Cdd:cd03217 87 ---PEIP------------GV-------KNADFLRYVNE----------GFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131922 180 LDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDV-ADRLHPM 222
Cdd:cd03217 135 LDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVL 178
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-219 |
5.11e-13 |
|
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: 65.95 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 24 LNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEwvdlVTAPA--RKVVEIRKTTVGW------- 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILE-GKQ----ITEPGpdRMVVFQNYSLLPWltvreni 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 95 ---VSQFLRVIPRISALEVVMQPLLDTGVPREAcaakaarlltrlnvperlwHLAPSTFSGGEQQRVNIARGFIVDYPIL 171
Cdd:TIGR01184 76 alaVDRVLPDLSKSERRAIVEEHIALVGLTEAA-------------------DKRPGQLSGGMKQRVAIARALSIRPKVL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131922 172 LLDEPTASLDAKNSAAVVE-LIREAKTRGAAIVGIFH--DEAVRndVADRL 219
Cdd:TIGR01184 137 LLDEPFGALDALTRGNLQEeLMQIWEEHRVTVLMVTHdvDEALL--LSDRV 185
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-217 |
7.16e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.84 E-value: 7.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 41 GHSGSGKSTLLRSL------YANYLPDEGQIqIKHGDEWVDLvtaparKVVEIRKTtVGWVSQFLRVIPRISALEVVMQP 114
Cdd:PRK14246 43 GPSGSGKSTLLKVLnrlieiYDSKIKVDGKV-LYFGKDIFQI------DAIKLRKE-VGMVFQQPNPFPHLSIYDNIAYP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 115 LLDTGVPR--------EACAAKAA---RLLTRLNVPerlwhlaPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAK 183
Cdd:PRK14246 115 LKSHGIKEkreikkivEECLRKVGlwkEVYDRLNSP-------ASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIV 187
|
170 180 190
....*....|....*....|....*....|....
gi 16131922 184 NSAAVVELIREAKTRgAAIVGIFHDEAVRNDVAD 217
Cdd:PRK14246 188 NSQAIEKLITELKNE-IAIVIVSHNPQQVARVAD 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-207 |
1.08e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.61 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 20 RLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyANYLPDEGQIQikhGDEWVDLVTAPARKVVEIrkttVGWVSQFL 99
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKGVKGS---GSVLLNGMPIDAKEMRAI----SAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 100 RVIPRISALEVVM---------------------QPLLDTGVpreacaAKAARllTRLNVPERLWHLapstfSGGEQQRV 158
Cdd:TIGR00955 109 LFIPTLTVREHLMfqahlrmprrvtkkekrervdEVLQALGL------RKCAN--TRIGVPGRVKGL-----SGGERKRL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131922 159 NIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFH 207
Cdd:TIGR00955 176 AFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
23-218 |
1.55e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.53 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhgDEWVDLVTAPARKvveirKTTVGWVSQFLRVI 102
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID--DEDISLLPLHARA-----RRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 103 PRISALEVVMQPL-LDTGVPREACAAKAARLLTRLNVPerlwHLAPS---TFSGGEQQRVNIARGFIVDYPILLLDEPTA 178
Cdd:PRK10895 91 RRLSVYDNLMAVLqIRDDLSAEQREDRANELMEEFHIE----HLRDSmgqSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16131922 179 SLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADR 218
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCER 206
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
28-197 |
1.63e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 66.14 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlvtaparkvveIRKTTVgwvsQFLRvipriSA 107
Cdd:PRK13657 355 SFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTD---------------IRTVTR----ASLR-----RN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 108 LEVVMQ-PLL-----------------DTGVPREACAAKAARLLTR------LNVPERlwhlaPSTFSGGEQQRVNIARG 163
Cdd:PRK13657 411 IAVVFQdAGLfnrsiednirvgrpdatDEEMRAAAERAQAHDFIERkpdgydTVVGER-----GRQLSGGERQRLAIARA 485
|
170 180 190
....*....|....*....|....*....|....*..
gi 16131922 164 FIVDYPILLLDEPTASLDAKNSAAV---VELIREAKT 197
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVkaaLDELMKGRT 522
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
23-177 |
1.78e-12 |
|
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: 64.08 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgdEWVDLVTAPARKVVeirKTTVGWVSQFLRVI 102
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRL----DGEDITKLPPHERA---RAGIAYVPQGREIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 103 PRISALEVvmqplLDTGVprEACAAKAARlltrlnVPERLWHLAPSTF----------SGGEQQRVNIARGFIVDYPILL 172
Cdd:TIGR03410 88 PRLTVEEN-----LLTGL--AALPRRSRK------IPDEIYELFPVLKemlgrrggdlSGGQQQQLAIARALVTRPKLLL 154
|
....*
gi 16131922 173 LDEPT 177
Cdd:TIGR03410 155 LDEPT 159
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
28-203 |
2.67e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.04 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGDEwVDLVT---APARKVV---EIRKTTvGWVSQF--- 98
Cdd:COG1129 272 SFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRL-DGKP-VRIRSprdAIRAGIAyvpEDRKGE-GLVLDLsir 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 99 ----LRVIPRISALevvmqPLLDTGvpREAcaAKAARLLTRLNV----PERLwhlaPSTFSGGEQQRVNIARGFIVDYPI 170
Cdd:COG1129 349 enitLASLDRLSRG-----GLLDRR--RER--ALAEEYIKRLRIktpsPEQP----VGNLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190
....*....|....*....|....*....|....*
gi 16131922 171 LLLDEPTASLD--AKnsAAVVELIREAKTRGAAIV 203
Cdd:COG1129 416 LILDEPTRGIDvgAK--AEIYRLIRELAAEGKAVI 448
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-182 |
3.66e-12 |
|
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: 63.08 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 27 ASLTVNaGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGDEWVDlvtapARKVVEI--RKTTVGWVSQFLRVIPR 104
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-NGTVLFD-----SRKKINLppQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 105 ISalevVMQPLLdTGVPREACAAK---AARLLTRLNVpERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLD 181
Cdd:cd03297 90 LN----VRENLA-FGLKRKRNREDrisVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
.
gi 16131922 182 A 182
Cdd:cd03297 164 R 164
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
4-221 |
4.69e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.05 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 4 VQNVSKTFILhQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYL--PDEGQIQIKHGDEWVDLvtapa 81
Cdd:COG2401 27 VAIVLEAFGV-ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGREA----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 rkvveirkttvgwvsqflrviprisalevvmqPLLDtGVPREACAAKAARLLTR--LNVPErLWHLAPSTFSGGEQQRVN 159
Cdd:COG2401 101 --------------------------------SLID-AIGRKGDFKDAVELLNAvgLSDAV-LWLRRFKELSTGQKFRFR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131922 160 IARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHdeavRNDVADRLHP 221
Cdd:COG2401 147 LALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKlARRAGITLVVATH----HYDVIDDLQP 205
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-218 |
5.66e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.58 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYLPDEGQIQIKHGDEWVDLVTA-PARKVVEIRKTtVGWVSQFLRV 101
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL--NRMNDKVSGYRYSGDVLLGGRSIfNYRDVLEFRRR-VGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPRISALEVVMQPLLDTGVPREACAAKAARLLTRLN----VPERLWHlAPSTFSGGEQQRVNIARGFIVDYPILLLDEPT 177
Cdd:PRK14271 113 FPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGlwdaVKDRLSD-SPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16131922 178 ASLDAKNSAAVVELIREAKTRGAAIVgIFHDEAVRNDVADR 218
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTVII-VTHNLAQAARISDR 231
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
22-207 |
5.75e-12 |
|
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: 62.43 E-value: 5.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgdEWVDLVTAPARKvveirkttvgwvsqfLRv 101
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI----DGIDISTIPLED---------------LR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 ipriSALEVVMQ-PLLDTGVPREACAA----KAARLLTRLNVPErlwhlAPSTFSGGEQQRVNIARGFIVDYPILLLDEP 176
Cdd:cd03369 82 ----SSLTIIPQdPTLFSGTIRSNLDPfdeySDEEIYGALRVSE-----GGLNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190
....*....|....*....|....*....|.
gi 16131922 177 TASLDAKNSAAVVELIREaKTRGAAIVGIFH 207
Cdd:cd03369 153 TASIDYATDALIQKTIRE-EFTNSTILTIAH 182
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-218 |
6.04e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 5 QNVSKTFilhqqNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSL-----YANYlpdEGQIqIKHGDE--WVDLV 77
Cdd:NF040905 5 RGITKTF-----PGVK--ALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvypHGSY---EGEI-LFDGEVcrFKDIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 78 TAPARKVVEIRkttvgwvsQFLRVIPRISALEVVM--QPLLDTGV-PREACAAKAARLLTRLNVPErlwhlAPSTFSG-- 152
Cdd:NF040905 74 DSEALGIVIIH--------QELALIPYLSIAENIFlgNERAKRGViDWNETNRRARELLAKVGLDE-----SPDTLVTdi 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 153 --GEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFH--DEAVRndVADR 218
Cdd:NF040905 141 gvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHklNEIRR--VADS 208
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-207 |
7.03e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 7.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 6 NVSKTFilhqqNGVRlpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEwVDLVTAParkvv 85
Cdd:PRK10982 3 NISKSF-----PGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQ-GKE-IDFKSSK----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 86 EIRKTTVGWVSQFLRVIPRISalevVMQPLLDTGVPREACAAKAARLL--TRLNVPERLWHLAP----STFSGGEQQRVN 159
Cdd:PRK10982 69 EALENGISMVHQELNLVLQRS----VMDNMWLGRYPTKGMFVDQDKMYrdTKAIFDELDIDIDPrakvATLSVSQMQMIE 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131922 160 IARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFH 207
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISH 192
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
28-203 |
8.80e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.74 E-value: 8.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIqikhgdEWVDlvtAPARKVVEIRKTTVGWVSQFLRVIPRISA 107
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV------LWQG---EPIRRQRDEYHQDLLYLGHQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 108 LEVV-----MQPLLDtgvpREACAAKAAR--LLTRLNVPERlwhlapsTFSGGEQQRVNIARGFIVDYPILLLDEPTASL 180
Cdd:PRK13538 92 LENLrfyqrLHGPGD----DEALWEALAQvgLAGFEDVPVR-------QLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|...
gi 16131922 181 DAKNSAAVVELIREAKTRGAAIV 203
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVI 183
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-208 |
1.15e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 62.41 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqnGvRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLrSLYANYLP-DEGQIQIkhgdEWVDLVTA 79
Cdd:COG4604 1 MIEIKNVSKRY------G-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLL-SMISRLLPpDSGEVLV----DGLDVATT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 80 PAR---KVVEIRKttvgwvsQFLRVIPRISALEVVM-------QplldtGVPREACAAKAARLLTRLNvperlwhLAP-- 147
Cdd:COG4604 69 PSRelaKRLAILR-------QENHINSRLTVRELVAfgrfpysK-----GRLTAEDREIIDEAIAYLD-------LEDla 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131922 148 ----STFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHD 208
Cdd:COG4604 130 drylDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRlADELGKTVVIVLHD 195
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-208 |
1.21e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.44 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHQQNgvrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHgdewvDLVTAp 80
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEK----YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-----DLLTE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 aRKVVEIRKTtVGWV-----SQFLRVipriSALEVVMQPLLDTGVPREACAAK---AARLLTRLNVPERlwhlAPSTFSG 152
Cdd:PRK13650 74 -ENVWDIRHK-IGMVfqnpdNQFVGA----TVEDDVAFGLENKGIPHEEMKERvneALELVGMQDFKER----EPARLSG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 153 GEQQRVNIArGFIVDYP-ILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHD 208
Cdd:PRK13650 144 GQKQRVAIA-GAVAMRPkIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHD 200
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-208 |
2.39e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHQQNgVRLP---VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHG--DEWVD 75
Cdd:PRK10575 2 QEYTNHSDTTFALRNVS-FRVPgrtLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplESWSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 76 lvTAPARKVveirkttvGWVSQFLRVIPRISALEVVM-------QPLLDTGVPREACAAKAARLLTRLNVPERLwhlaPS 148
Cdd:PRK10575 81 --KAFARKV--------AYLPQQLPAAEGMTVRELVAigrypwhGALGRFGAADREKVEEAISLVGLKPLAHRL----VD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131922 149 TFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELI-REAKTRGAAIVGIFHD 208
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVhRLSQERGLTVIAVLHD 207
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-208 |
3.32e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.90 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqqnGVRlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGdewvdLVTAP 80
Cdd:PRK09544 4 LVSLENVSVSF------GQR-RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK-----LRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 ARKVVEIRKTTVGWVSQFLRVIPRISALEVVmqPLLDTgvpreacaAKAARLLTrlnvperlwhlAP-STFSGGEQQRVN 159
Cdd:PRK09544 72 VPQKLYLDTTLPLTVNRFLRLRPGTKKEDIL--PALKR--------VQAGHLID-----------APmQKLSGGETQRVL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131922 160 IARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHD 208
Cdd:PRK09544 131 LARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHD 180
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-219 |
3.60e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNAG-----ECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhgdewVDLvtapARKVVEIRKTTVGWVSQFLRVI 102
Cdd:PRK13409 354 SLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-----LKI----SYKPQYIKPDYDGTVEDLLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 103 PRI---SALEV-VMQPL-LDtgvpreacaakaaRLLTRlNVPErlwhlapstFSGGEQQRVNIARGFIVDYPILLLDEPT 177
Cdd:PRK13409 425 TDDlgsSYYKSeIIKPLqLE-------------RLLDK-NVKD---------LSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131922 178 ASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:PRK13409 482 AHLDVEQRLAVAKAIRRiAEEREATALVVDHDIYMIDYISDRL 524
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-218 |
4.01e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.85 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 4 VQNVSKTFilhqqnGVRlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIqikhgdewvdlvTAPARK 83
Cdd:PRK11247 15 LNAVSKRY------GER-TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------------LAGTAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 84 VVEIRKTTvGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVperlWhlaPSTFSGGEQQRVNIARG 163
Cdd:PRK11247 76 LAEAREDT-RLMFQDARLLPWKKVIDNVGLGLKGQWRDAALQALAAVGLADRANE----W---PAALSGGQKQRVALARA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 164 FIVDYPILLLDEPTASLDAKNSAAVVELI-REAKTRGAAIVGIFHD--EAVRndVADR 218
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIeSLWQQHGFTVLLVTHDvsEAVA--MADR 203
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
28-217 |
4.16e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.95 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNAGECVVLHGHSGSGKSTLLRSLyaNYLPD-------EGQIqIKHGDEwvdlVTAPARKVVEIRKTtVGWVSQ--- 97
Cdd:PRK14243 30 WLDIPKNQITAFIGPSGCGKSTILRCF--NRLNDlipgfrvEGKV-TFHGKN----LYAPDVDPVEVRRR-IGMVFQkpn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 98 -FLRVI-------PRISALEVVMQPLLDTGVPREACAAKaarlltrlnVPERLwHLAPSTFSGGEQQRVNIARGFIVDYP 169
Cdd:PRK14243 102 pFPKSIydniaygARINGYKGDMDELVERSLRQAALWDE---------VKDKL-KQSGLSLSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131922 170 ILLLDEPTASLDAKNSAAVVELIREAKTRgAAIVGIFHDEAVRNDVAD 217
Cdd:PRK14243 172 VILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-208 |
4.33e-11 |
|
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: 60.42 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFILHQQNG--------------VRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQI 67
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPgligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 68 KHGDEWVDLVTAPAR-KVVEIRKTTVGW---VSQFLRVIPRIsalevvmqplldTGVPREACAAKAARLLTRLNVpERLW 143
Cdd:cd03267 81 AGLVPWKRRKKFLRRiGVVFGQKTQLWWdlpVIDSFYLLAAI------------YDLPPARFKKRLDELSELLDL-EELL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131922 144 HLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREA-KTRGAAIVGIFHD 208
Cdd:cd03267 148 DTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHY 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-208 |
4.50e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.05 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 24 LNRASLTVNAGECVVLHGHSGSGKSTLLRSLYanylpdeGQIQIKHGDewVDLVTAPARKVveIRKTTVGWVSQFLRV-- 101
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALM-------GFVRLASGK--ISILGQPTRQA--LQKNLVAYVPQSEEVdw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 -IPRISALEVVMQPLLDTGVPREACAAKAARL---LTRLNVPErLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPT 177
Cdd:PRK15056 92 sFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVtaaLARVDMVE-FRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190
....*....|....*....|....*....|.
gi 16131922 178 ASLDAKNSAAVVELIREAKTRGAAIVGIFHD 208
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
10-220 |
7.45e-11 |
|
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: 60.07 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 10 TFILHqqngvRLPVlnrasltVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGqiqiKHGDE--WVDLVTA-------- 79
Cdd:cd03236 14 SFKLH-----RLPV-------PREGQVLGLVGPNGIGKSTALKILAGKLKPNLG----KFDDPpdWDEILDEfrgselqn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 80 -----------PARK---VVEIRKTTVGWVSQFLRVIPRISALEVVMQPL-LDTGVPREAcaakaarlltrlnvperlwh 144
Cdd:cd03236 78 yftkllegdvkVIVKpqyVDLIPKAVKGKVGELLKKKDERGKLDELVDQLeLRHVLDRNI-------------------- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131922 145 lapSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRLH 220
Cdd:cd03236 138 ---DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIH 210
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-181 |
8.08e-11 |
|
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: 60.91 E-value: 8.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqnGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlvtapa 81
Cdd:TIGR01193 474 IVINDVSYSY------GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS---------- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 rkVVEIRKTTVgwvSQFLRVIPR--------------ISALEVVMQPLLDtgvprEACAAKAAR---------LLTRLNV 138
Cdd:TIGR01193 538 --LKDIDRHTL---RQFINYLPQepyifsgsilenllLGAKENVSQDEIW-----AACEIAEIKddienmplgYQTELSE 607
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131922 139 perlwhlAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLD 181
Cdd:TIGR01193 608 -------EGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
24-208 |
1.04e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.86 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 24 LNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhGDEWVDLvtaPARKVVEIRKTtVGWVSQ------ 97
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILF--DGKPIDY---SRKGLMKLRES-VGMVFQdpdnql 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 98 FlrvipRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVpERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPT 177
Cdd:PRK13636 96 F-----SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190
....*....|....*....|....*....|..
gi 16131922 178 ASLDAKNSAAVVELIRE-AKTRGAAIVGIFHD 208
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEmQKELGLTIIIATHD 201
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
24-208 |
1.30e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.75 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 24 LNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEwvdlVTAPARKvvEIRKTtVGWVSQ------ 97
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVM-GRE----VNAENEK--WVRSK-VGLVFQdpddqv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 98 FLRVIPRISALEVVMQPLLDTGVPREACAA-KAARLltrlnvpERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEP 176
Cdd:PRK13647 93 FSSTVWDDVAFGPVNMGLDKDEVERRVEEAlKAVRM-------WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190
....*....|....*....|....*....|..
gi 16131922 177 TASLDAKNSAAVVELIREAKTRGAAIVGIFHD 208
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLHNQGKTVIVATHD 197
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-207 |
1.50e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 60.12 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 21 LPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgDEwVDLVTAPA----RKVVEIRKTTVGWVS 96
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL---DG-VPLVQYDHhylhRQVALVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 97 QFLRVIP---RISALEVVMqplldtGVPREACAAKAARLLTR---LNVPErlwhlAPSTFSGGEQQRVNIARGFIVDYPI 170
Cdd:TIGR00958 570 SVRENIAyglTDTPDEEIM------AAAKAANAHDFIMEFPNgydTEVGE-----KGSQLSGGQKQRIAIARALVRKPRV 638
|
170 180 190
....*....|....*....|....*....|....*..
gi 16131922 171 LLLDEPTASLDAKNSAAVVELiREAKTRgaAIVGIFH 207
Cdd:TIGR00958 639 LILDEATSALDAECEQLLQES-RSRASR--TVLLIAH 672
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
28-208 |
2.19e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.84 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNA--GECVVLHGHSGSGKSTLLRSLYANYLPDEGQIqikhgdeWVD--LVTAPARKVVEIRkttVGWVSQFLRVIP 103
Cdd:PRK10253 25 NLTVEIpdGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-------WLDgeHIQHYASKEVARR---IGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 104 RISALEVVM------QPLLDTGVPREACAAKAARLLTRLNvperlwHLAPS---TFSGGEQQRVNIARGFIVDYPILLLD 174
Cdd:PRK10253 95 DITVQELVArgryphQPLFTRWRKEDEEAVTKAMQATGIT------HLADQsvdTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190
....*....|....*....|....*....|....*
gi 16131922 175 EPTASLDAKNSAAVVELIREA-KTRGAAIVGIFHD 208
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELnREKGYTLAAVLHD 203
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-222 |
2.43e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.56 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKS----TLLRSLYANYLPDEGQIQIKhGDEwvdlvTAPArkvvEIRKTTVGWVSQ 97
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLD-GKP-----VAPC----ALRGRKIATIMQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 98 FlrviPRiSALEVV-------MQPLLDTGVPREACAAKAARLLTRLNVPERLWHLAPSTFSGGEQQRVNIARGFIVDYPI 170
Cdd:PRK10418 87 N----PR-SAFNPLhtmhthaRETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131922 171 LLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESiVQKRALGMLLVTHDMGVVARLADDVAVM 214
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
24-214 |
3.58e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 58.57 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 24 LNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgdewvDLVTAPARKVVEIRKTtVGWV-----SQF 98
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI-------DGELLTAENVWNLRRK-IGMVfqnpdNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 99 LRVipriSALEVVMQPLLDTGVPREACAAKAARLLTRLNVPErLWHLAPSTFSGGEQQRVNIArGFIVDYP-ILLLDEPT 177
Cdd:PRK13642 95 VGA----TVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLD-FKTREPARLSGGQKQRVAVA-GIIALRPeIIILDEST 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16131922 178 ASLDAKNSAAVVELIREAKTR-GAAIVGIFH--DEAVRND 214
Cdd:PRK13642 169 SMLDPTGRQEIMRVIHEIKEKyQLTVLSITHdlDEAASSD 208
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-220 |
3.70e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 13 LHQQNGVRLpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyanylpdEGQIQIKHGDewvdlVTAPArkvveirKTTV 92
Cdd:PRK10636 7 LQIRRGVRV-LLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGS-----YTFPG-------NWQL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 93 GWVSQFLRVIPrISALEVVM----------QPLLDTGVPREACA-----------------AKAARLLTRLNVPERLWHL 145
Cdd:PRK10636 67 AWVNQETPALP-QPALEYVIdgdreyrqleAQLHDANERNDGHAiatihgkldaidawtirSRAASLLHGLGFSNEQLER 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131922 146 APSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKnsaAVVELIREAKTRGAAIVGIFHDEAVRNDVADR-LH 220
Cdd:PRK10636 146 PVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQGTLILISHDRDFLDPIVDKiIH 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-203 |
3.71e-10 |
|
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: 57.87 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQI--------QIKHgdewvdlvtaparkvvEIRKTTVG 93
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldgkpisQYEH----------------KYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 94 WVSQFLRVIPRiSALEVVMQPLldTGVPREACAAKAARLLTRLNVPErlWHLAPST--------FSGGEQQRVNIARGFI 165
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIAYGL--QSCSFECVKEAAQKAHAHSFISE--LASGYDTevgekgsqLSGGQKQRVAIARALI 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 16131922 166 VDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIV 203
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLV 204
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-188 |
4.82e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.49 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEWVDLVTAPA 81
Cdd:PRK11176 342 IEFRNVTFTY-----PGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLD-GHDLRDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVVEIrkttvgwVSQFLRVIPrisalevvmqpllDTGVPREACAA----------KAARLLTRLNVPERLWHLAPS--- 148
Cdd:PRK11176 416 RNQVAL-------VSQNVHLFN-------------DTIANNIAYARteqysreqieEAARMAYAMDFINKMDNGLDTvig 475
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131922 149 ----TFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAV 188
Cdd:PRK11176 476 engvLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAI 519
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
23-212 |
5.04e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.74 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyanylpdEGQIQikhGDEWVDLVTAPARKVVEIRKTTVGWVSQFLRVI 102
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQ---GNNFTGTILANNRKPTKQILKRTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 103 PRISALE-VVMQPLL--DTGVPREACAAKAARLLTRLNVPERLWHLAPSTF----SGGEQQRVNIARGFIVDYPILLLDE 175
Cdd:PLN03211 153 PHLTVREtLVFCSLLrlPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190
....*....|....*....|....*....|....*..
gi 16131922 176 PTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVR 212
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSR 269
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-68 |
7.35e-10 |
|
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: 56.77 E-value: 7.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTF---------------ILHQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQ 66
Cdd:cd03220 1 IELENVSKSYptykggssslkklgiLGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
..
gi 16131922 67 IK 68
Cdd:cd03220 81 VR 82
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-198 |
1.15e-09 |
|
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: 55.94 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVskTFILHQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGdewvdlvtapa 81
Cdd:cd03250 1 ISVEDA--SFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-PG----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 rkvveirktTVGWVSQflrviprisalevvmQPLLDTGVPRE------------------ACAAK------AARLLTRln 137
Cdd:cd03250 67 ---------SIAYVSQ---------------EPWIQNGTIREnilfgkpfdeeryekvikACALEpdleilPDGDLTE-- 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131922 138 VPERlwhlaPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVE-----LIREAKTR 198
Cdd:cd03250 121 IGEK-----GINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncilgLLLNNKTR 181
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-202 |
1.63e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.04 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 20 RLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIqIKHGDEWVDLVTAparkvvEIRKTTVGWVSQFL 99
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRI-VFDGKDITDWQTA------KIMREAVAIVPEGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 100 RVIPRISALE-VVMQPLLDTGVPREACAAKAARLLTRLNvpERLWHLApSTFSGGEQQRVNIARGFIVDYPILLLDEPTA 178
Cdd:PRK11614 90 RVFSRMTVEEnLAMGGFFAERDQFQERIKWVYELFPRLH--ERRIQRA-GTMSGGEQQMLAIGRALMSQPRLLLLDEPSL 166
|
170 180
....*....|....*....|....
gi 16131922 179 SLDAKNSAAVVELIREAKTRGAAI 202
Cdd:PRK11614 167 GLAPIIIQQIFDTIEQLREQGMTI 190
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
25-222 |
1.70e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.15 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 25 NRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEWVDLvtaPARKVVeiRKttvGWVSQF--LRVI 102
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLR-GQHIEGL---PGHQIA--RM---GVVRTFqhVRLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 103 PRISALE--VVMQPL-LDTGV-------------PREAcAAKAARLLTRLNVPErLWHLAPSTFSGGEQQRVNIARGFIV 166
Cdd:PRK11300 93 REMTVIEnlLVAQHQqLKTGLfsgllktpafrraESEA-LDRAATWLERVGLLE-HANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 167 DYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-203 |
1.74e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.96 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 21 LPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGdewVDLVTAPARkvvEIRKTTVGWVSQfLR 100
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL-DG---EDITGLSPR---ERRRLGVAYIPE-DR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 101 ----VIPRISALE-VVMQ----------PLLDtgvpREACAAKAARLLTRLNV-PERLWHLApSTFSGGEQQRVNIARGF 164
Cdd:COG3845 343 lgrgLVPDMSVAEnLILGryrrppfsrgGFLD----RKAIRAFAEELIEEFDVrTPGPDTPA-RSLSGGNQQKVILAREL 417
|
170 180 190
....*....|....*....|....*....|....*....
gi 16131922 165 IVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIV 203
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVL 456
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
29-182 |
2.32e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.19 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 29 LTVNAGECVVLHGHSGSGKSTLLRSLYAnyLPD--EGQIQIkhGDEWVDLVtAPArkvveirKTTVGWVSQFLRVIPRIS 106
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAG--LEDitSGDLFI--GEKRMNDV-PPA-------ERGVGMVFQSYALYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 107 ALEVVMQPLLDTGVPREACAAK---AARLLtrlnvpeRLWHL---APSTFSGGEQQRVNIARGFIVDYPILLLDEPTASL 180
Cdd:PRK11000 92 VAENMSFGLKLAGAKKEEINQRvnqVAEVL-------QLAHLldrKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
..
gi 16131922 181 DA 182
Cdd:PRK11000 165 DA 166
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-222 |
3.66e-09 |
|
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: 54.08 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyanylpdegqiqikhGDEWvdlvtaparkvvEIRKTTVGwvsqflrv 101
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL---------------AGLW------------PWGSGRIG-------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPRISALEVVMQ-PLLDTGVPREAcaakaarlltrLNVPerlWHlapSTFSGGEQQRVNIARGFIVDYPILLLDEPTASL 180
Cdd:cd03223 60 MPEGEDLLFLPQrPYLPLGTLREQ-----------LIYP---WD---DVLSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16131922 181 DAKNSAAVVELIREaktRGAAIVGIFHDEAVrndvaDRLHPM 222
Cdd:cd03223 123 DEESEDRLYQLLKE---LGITVISVGHRPSL-----WKFHDR 156
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-219 |
4.97e-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: 55.56 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 30 TVNAGECVVLHGHSGSGKSTLLRSLyANYL-PDEGQIqikhgDEWVDLVTAPARKVVEIRKTtvgwVSQFLR-VIPRI-- 105
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKIL-AGVLkPDEGEV-----DEDLKISYKPQYISPDYDGT----VEEFLRsANTDDfg 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 106 -SALEV-VMQPL-LDtgvpreacaakaaRLLTRlNVperlwhlapSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDA 182
Cdd:COG1245 432 sSYYKTeIIKPLgLE-------------KLLDK-NV---------KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
170 180 190
....*....|....*....|....*....|....*...
gi 16131922 183 KNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:COG1245 489 EQRLAVAKAIRRfAENRGKTAMVVDHDIYLIDYISDRL 526
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-224 |
5.05e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.13 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKStlLRSLYANYLPD-EGQIQIKHGD-EWVDLVT 78
Cdd:PRK11022 3 LLNVDKLSVHF---GDESAPFRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAIMGLIDyPGRVMAEKLEfNGQDLQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 79 APARKVVEIRKTTVGWVSQ--FLRVIPRISALEVVMQPL-LDTGVPREACAAKAARLLTRLNVPE---RLwHLAPSTFSG 152
Cdd:PRK11022 78 ISEKERRNLVGAEVAMIFQdpMTSLNPCYTVGFQIMEAIkVHQGGNKKTRRQRAIDLLNQVGIPDpasRL-DVYPHQLSG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131922 153 GEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTR-GAAIVGIFHDEAVRNDVADRLHPMGA 224
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYA 229
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-220 |
6.93e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 54.63 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIqIKHGDEwvdlVTAPARKVVEIRKTtVGWVSQ---- 97
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKP----LDYSKRGLLALRQQ-VATVFQdpeq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 98 --FLRVIPRISALEvvmqpLLDTGVPREACAAKAARLLTRLNVpERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDE 175
Cdd:PRK13638 89 qiFYTDIDSDIAFS-----LRNLGVPEAEITRRVDEALTLVDA-QHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131922 176 PTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRLH 220
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVY 207
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-183 |
7.00e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 54.85 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFilhqQNGVrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyanylpdEGQIQIKHGDEWVDlvtap 80
Cdd:PRK11650 3 GLKLQAVRKSY----DGKT--QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMV-------AGLERITSGEIWIG----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 aRKVV---EIRKTTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACA---AKAARLLTRlnvpERLWHLAPSTFSGGE 154
Cdd:PRK11650 65 -GRVVnelEPADRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEervAEAARILEL----EPLLDRKPRELSGGQ 139
|
170 180 190
....*....|....*....|....*....|
gi 16131922 155 QQRVNIARGfIVDYP-ILLLDEPTASLDAK 183
Cdd:PRK11650 140 RQRVAMGRA-IVREPaVFLFDEPLSNLDAK 168
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
23-222 |
1.67e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 53.65 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhgdewvdlvTAPARK--VVEIRKTtVGWVSQFL- 99
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR---------GEPITKenIREVRKF-VGLVFQNPd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 100 -RVIPRISALEVVMQPLlDTGVPREACAAKAARLLTRLNVpERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTA 178
Cdd:PRK13652 89 dQIFSPTVEQDIAFGPI-NLGLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131922 179 SLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:PRK13652 167 GLDPQGVKELIDFLNDlPETYGMTVIFSTHQLDLVPEMADYIYVM 211
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-198 |
1.80e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLrSL--------YANYLPDEGQiQIKHGDEWVDLvtaparkvveirKTTVG 93
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLL-SLitgdhpqgYSNDLTLFGR-RRGSGETIWDI------------KKHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 94 WVSQFLRVIPRIS--ALEVVMQPLLDT-GVPR---EACAAKAARLLTRLNVPERLwhlAPSTF---SGGEQQRVNIARGF 164
Cdd:PRK10938 340 YVSSSLHLDYRVStsVRNVILSGFFDSiGIYQavsDRQQKLAQQWLDILGIDKRT---ADAPFhslSWGQQRLALIVRAL 416
|
170 180 190
....*....|....*....|....*....|....*...
gi 16131922 165 IVDYPILLLDEPTASLDAKNSAAV---VE-LIREAKTR 198
Cdd:PRK10938 417 VKHPTLLILDEPLQGLDPLNRQLVrrfVDvLISEGETQ 454
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-208 |
3.22e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.46 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIqikhgdeWVDLVTAPA---RKVVEIRKtTVGWVSQF 98
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-------LFDGENIPAmsrSRLYTVRK-RMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 99 LRVIPRISALEVVMQPLldtgvpreacaakaaRLLTRLnvPERLWH-----------------LAPSTFSGGEQQRVNIA 161
Cdd:PRK11831 93 GALFTDMNVFDNVAYPL---------------REHTQL--PAPLLHstvmmkleavglrgaakLMPSELSGGMARRAALA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131922 162 RGFIVDYPILLLDEPTASLDAKNSAAVVELIREA-KTRGAAIVGIFHD 208
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHD 203
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-197 |
4.52e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.80 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSktFILHQQNgvrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEWVDLVTAPA 81
Cdd:PRK10790 341 IDIDNVS--FAYRDDN----LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLD-GRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RK-VVEIRKTTVGWVSQFLRVIP---RIS------ALEVVMQPLLDTGVPreacaakaARLLTRLNvpERlwhlaPSTFS 151
Cdd:PRK10790 414 RQgVAMVQQDPVVLADTFLANVTlgrDISeeqvwqALETVQLAELARSLP--------DGLYTPLG--EQ-----GNNLS 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131922 152 GGEQQRVNIARgFIVDYP-ILLLDEPTASLDAKNSAAV---VELIREAKT 197
Cdd:PRK10790 479 VGQKQLLALAR-VLVQTPqILILDEATANIDSGTEQAIqqaLAAVREHTT 527
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
132-181 |
4.79e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.57 E-value: 4.79e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 16131922 132 LLTRLnvperlwhlaPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLD 181
Cdd:PRK11144 121 LLDRY----------PGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-203 |
5.64e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 5.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhgdewvdlvTAPARKVVEIRKttVGWVSQFLRV 101
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQID---------GKTATRGDRSRF--MAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPRISALEVV-----MQPLLDTGVPREACA----AKAARLLTRlnvperlwhlapsTFSGGEQQRVNIARGFIVDYPILL 172
Cdd:PRK13543 94 KADLSTLENLhflcgLHGRRAKQMPGSALAivglAGYEDTLVR-------------QLSAGQKKRLALARLWLSPAPLWL 160
|
170 180 190
....*....|....*....|....*....|..
gi 16131922 173 LDEPTASLDAKNSAAVVELIR-EAKTRGAAIV 203
Cdd:PRK13543 161 LDEPYANLDLEGITLVNRMISaHLRGGGAALV 192
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-209 |
8.84e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSktFILHQQngvrlPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlvtap 80
Cdd:PRK13540 1 MLDVIELD--FDYHDQ-----PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 81 arkvveIRKTTVGWVSQFLRVIPRISalevvMQPLLDTgvpREACAAKAARLLTRLNVPE-----RLWHLAP---STFSG 152
Cdd:PRK13540 65 ------IKKDLCTYQKQLCFVGHRSG-----INPYLTL---RENCLYDIHFSPGAVGITElcrlfSLEHLIDypcGLLSS 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 153 GEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDE 209
Cdd:PRK13540 131 GQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQD 187
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-205 |
9.77e-08 |
|
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: 50.72 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 6 NVSKTFilhQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyANYLPDEGQIQ--IKHGDEwvdlvtaPARK 83
Cdd:cd03233 8 NISFTT---GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL-ANRTEGNVSVEgdIHYNGI-------PYKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 84 VVEIRKTTVGWVSQFLRVIPRISALEvvmqpLLDTgvpreACAAKAARLLtrlnvperlwhlapSTFSGGEQQRVNIARG 163
Cdd:cd03233 77 FAEKYPGEIIYVSEEDVHFPTLTVRE-----TLDF-----ALRCKGNEFV--------------RGISGGERKRVSIAEA 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131922 164 FIVDYPILLLDEPTASLDAKNSAAVVELIREA--KTRGAAIVGI 205
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMadVLKTTTFVSL 176
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
148-220 |
1.52e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.32 E-value: 1.52e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131922 148 STFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRLH 220
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVH 283
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-194 |
1.89e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.17 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTF-----ILHQQngvRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIK-HGDEWV 74
Cdd:PRK15112 4 LLEVRNLSKTFryrtgWFRRQ---TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 75 DLvtaparkvveirkttvGWVSQFLRVI---------PRISALEVVMQPL-LDTGVPREACAAKAARLLTRLNVPERLWH 144
Cdd:PRK15112 81 DY----------------SYRSQRIRMIfqdpstslnPRQRISQILDFPLrLNTDLEPEQREKQIIETLRQVGLLPDHAS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131922 145 LAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE 194
Cdd:PRK15112 145 YYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLE 194
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-223 |
2.10e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.24 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 17 NGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRS-LYAnylpdEGQIQIKHgdewvDLVTAPARKVVEIRKttvgwv 95
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEgLYA-----SGKARLIS-----FLPKFSRNKLIFIDQ------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 96 sqflrviprisalevvMQPLLDTGvpreacaakaarlLTRLNVPERLwhlapSTFSGGEQQRVNIARGFIVDYP--ILLL 173
Cdd:cd03238 68 ----------------LQFLIDVG-------------LGYLTLGQKL-----STLSGGELQRVKLASELFSEPPgtLFIL 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131922 174 DEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRnDVADRLHPMG 223
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVL-SSADWIIDFG 162
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-196 |
2.18e-07 |
|
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: 51.17 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 18 GVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyanylpdEGQIQIKHGDEWV---DLVTaparKVVEIRKTtVGW 94
Cdd:TIGR01257 1949 GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKML-------TGDTTVTSGDATVagkSILT----NISDVHQN-MGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 95 VSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLApSTFSGGEQQRVNIARGFIVDYPILLLD 174
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLA-GTYSGGNKRKLSTAIALIGCPPLVLLD 2095
|
170 180
....*....|....*....|....*.
gi 16131922 175 EPTASLDAKNSA----AVVELIREAK 196
Cdd:TIGR01257 2096 EPTTGMDPQARRmlwnTIVSIIREGR 2121
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-208 |
2.70e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.04 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyaNYLPD-EGQIQIKHGDEWVDlvtapaRKVVEIRKTTVGWVSQFLRV 101
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL--NRMNElESEVRVEGRVEFFN------QNIYERRVNLNRLRRQVSMV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPRISALEVVMQPLLDTGV------PR------EACAAKAARLLTRlnVPERLwHLAPSTFSGGEQQRVNIARGFIVDYP 169
Cdd:PRK14258 94 HPKPNLFPMSVYDNVAYGVkivgwrPKleiddiVESALKDADLWDE--IKHKI-HKSALDLSGGQQQRLCIARALAVKPK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16131922 170 ILLLDEPTASLDAKNSAAVVELIREAKTRGA-AIVGIFHD 208
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHN 210
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-194 |
3.22e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDewvdlvtaparkvveIRKTTVGWVSQFLRV 101
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD---------------VAKFGLTDLRRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPRisalevvmQPLLDTGVPR-------EACAAKAARLLTRLNVPERL----WHLAPSTFSGGE------QQRVNIARGF 164
Cdd:PLN03232 1315 IPQ--------SPVLFSGTVRfnidpfsEHNDADLWEALERAHIKDVIdrnpFGLDAEVSEGGEnfsvgqRQLLSLARAL 1386
|
170 180 190
....*....|....*....|....*....|
gi 16131922 165 IVDYPILLLDEPTASLDAKNSAAVVELIRE 194
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIRE 1416
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-207 |
4.08e-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: 48.78 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 18 GVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLrslyaNYLPDEGQIQIKHGDewvdlVTAPARKVVEIRKTTVGWVSQ 97
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLL-----DVLAGRKTAGVITGE-----ILINGRPLDKNFQRSTGYVEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 98 FLRVIPRISAlevvmqplldtgvpREACAAKAarLLTRLNVPERlwhlapstfsggeqQRVNIARGFIVDYPILLLDEPT 177
Cdd:cd03232 87 QDVHSPNLTV--------------REALRFSA--LLRGLSVEQR--------------KRLTIGVELAAKPSILFLDEPT 136
|
170 180 190
....*....|....*....|....*....|
gi 16131922 178 ASLDAKNSAAVVELIREAKTRGAAIVGIFH 207
Cdd:cd03232 137 SGLDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-222 |
5.75e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 18 GVRLPVlnraSLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQ--------------IKHGdewvdLVTAPA-R 82
Cdd:PRK11288 267 GLREPI----SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYldgkpidirsprdaIRAG-----IMLCPEdR 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 83 K---VVEIRKttvgwVSQFLRVIPRISALEVVMqpLLDTGvpREAcaAKAARLLTRLNVPERLWHLAPSTFSGGEQQRVN 159
Cdd:PRK11288 338 KaegIIPVHS-----VADNINISARRHHLRAGC--LINNR--WEA--ENADRFIRSLNIKTPSREQLIMNLSGGNQQKAI 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131922 160 IARGFIVDYPILLLDEPTASLD--AKNSaaVVELIREAKTRGAAIVGIFHDEAVRNDVADRLHPM 222
Cdd:PRK11288 407 LGRWLSEDMKVILLDEPTRGIDvgAKHE--IYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVM 469
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-219 |
8.10e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLyANYLPDEGQ---IQIKhGDEWVD---LVTAPARKVVEIRKTtvgwVS 96
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKAL-AGDLTGGGAprgARVT-GDVTLNgepLAAIDAPRLARLRAV----LP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 97 QFLRVIPRISALEVVM------------QPLLDTGVPREACAAKAARLLTRLNVperlwhlapSTFSGGEQQRVNIARGF 164
Cdd:PRK13547 90 QAAQPAFAFSAREIVLlgrypharragaLTHRDGEIAWQALALAGATALVGRDV---------TTLSGGELARVQFARVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131922 165 IVDYP---------ILLLDEPTASLDAKNSAAVVELIRE-AKTRGAAIVGIFHDEAVRNDVADRL 219
Cdd:PRK13547 161 AQLWPphdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRlARDWNLGVLAIVHDPNLAARHADRI 225
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-181 |
1.04e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.14 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYaNYLPDEGQIQIKhGDEWVDLVTAPARKVveirkttvgwvsqfLRVI 102
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQID-GVSWNSVTLQTWRKA--------------FGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 103 P-RISALEVVMQPLLDtgvPREACAakaarlltrlnvPERLWHLAPST-----------------------FSGGEQQRV 158
Cdd:TIGR01271 1298 PqKVFIFSGTFRKNLD---PYEQWS------------DEEIWKVAEEVglksvieqfpdkldfvlvdggyvLSNGHKQLM 1362
|
170 180
....*....|....*....|...
gi 16131922 159 NIARGFIVDYPILLLDEPTASLD 181
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLD 1385
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
132-220 |
1.15e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 132 LLTRLNVpERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAkTRGAAIVGIFHDEAV 211
Cdd:PRK13409 196 VVERLGL-ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIREL-AEGKYVLVVEHDLAV 273
|
....*....
gi 16131922 212 RNDVADRLH 220
Cdd:PRK13409 274 LDYLADNVH 282
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-223 |
1.15e-06 |
|
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: 48.67 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 24 LNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANY--------LPDEGQIQIKHGdewVDLVTAPARKVVEIRKTTvGWV 95
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpgkfegnvFINGKPVDIRNP---AQAIRAGIAMVPEDRKRH-GIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 96 SQF-------LRVIPRISALEVVmqpllDTGVPREACAAKAARLLTRLNVPErlwhLAPSTFSGGEQQRVNIARGFIVDY 168
Cdd:TIGR02633 352 PILgvgknitLSVLKSFCFKMRI-----DAAAELQIIGSAIQRLKVKTASPF----LPIGRLSGGNQQKAVLAKMLLTNP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131922 169 PILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRLHPMG 223
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIG 477
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
151-220 |
1.47e-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: 46.80 E-value: 1.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131922 151 SGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIF-HDEAVRNDVADRLH 220
Cdd:cd03222 73 SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVeHDLAVLDYLSDRIH 143
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
148-196 |
2.30e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 2.30e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 16131922 148 STFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAK 196
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLK 626
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
151-203 |
4.76e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.54 E-value: 4.76e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 16131922 151 SGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIV 203
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSII 449
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
149-207 |
4.98e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 4.98e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 149 TFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRG-AAIVGIFH 207
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAH 1417
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-198 |
5.63e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYlpdegqiQIKHGDEWVDLVTAPARKVVEIRKTTV-GWVSQF--- 98
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF-------EISEGRVWAERSIAYVPQQAWIMNATVrGNILFFdee 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 99 ----LRVIPRISALEVVMQpLLDTGVPREaCAAKAARLltrlnvperlwhlapstfSGGEQQRVNIARGFIVDYPILLLD 174
Cdd:PTZ00243 748 daarLADAVRVSQLEADLA-QLGGGLETE-IGEKGVNL------------------SGGQKARVSLARAVYANRDVYLLD 807
|
170 180
....*....|....*....|....*...
gi 16131922 175 EPTASLDAKNSAAVV-ELIREA---KTR 198
Cdd:PTZ00243 808 DPLSALDAHVGERVVeECFLGAlagKTR 835
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-66 |
6.12e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 6.12e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131922 4 VQNVSKTFilhqqngVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQ 66
Cdd:PRK15064 322 VENLTKGF-------DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
127-181 |
6.34e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 6.34e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 16131922 127 AKAARLLTRLNVPERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLD 181
Cdd:PLN03073 322 ARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-210 |
1.18e-05 |
|
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: 45.77 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDEWVDLvtaparkvvEIRKTTVGWVSQFLRV 101
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNL---------DAVRQSLGMCPQHNIL 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLApSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLD 181
Cdd:TIGR01257 1015 FHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEA-QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190
....*....|....*....|....*....|
gi 16131922 182 AKNSAAVVELIREAKTRGAAIVGIFH-DEA 210
Cdd:TIGR01257 1094 PYSRRSIWDLLLKYRSGRTIIMSTHHmDEA 1123
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-194 |
1.21e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgDEwvdlvtaparkvVEIRKTTVGWVSQFLRV 101
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILI---DG------------CDISKFGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPRisalevvmQPLLDTGVPR---------------EACAAKAARLLTRLN-------VPErlwhlAPSTFSGGEQQRVN 159
Cdd:PLN03130 1318 IPQ--------APVLFSGTVRfnldpfnehndadlwESLERAHLKDVIRRNslgldaeVSE-----AGENFSVGQRQLLS 1384
|
170 180 190
....*....|....*....|....*....|....*
gi 16131922 160 IARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE 194
Cdd:PLN03130 1385 LARALLRRSKILVLDEATAAVDVRTDALIQKTIRE 1419
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
41-216 |
1.41e-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: 45.31 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 41 GHSGSGKSTLLR-----------------SLYANYLPDEGQIQikhgdewvdlvtaPARKVVEIRKTTVGWVSQFLRVIP 103
Cdd:TIGR03719 38 GLNGAGKSTLLRimagvdkdfngearpqpGIKVGYLPQEPQLD-------------PTKTVRENVEEGVAEIKDALDRFN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 104 RISALevvmqpLLDTGVPREACAAKAARLLTRL------NVPERL-----------WHLAPSTFSGGEQQRVNIARGFIV 166
Cdd:TIGR03719 105 EISAK------YAEPDADFDKLAAEQAELQEIIdaadawDLDSQLeiamdalrcppWDADVTKLSGGERRRVALCRLLLS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131922 167 DYPILLLDEPTASLDAKNSAAVVELIREAKtrgAAIVGIFHDEAVRNDVA 216
Cdd:TIGR03719 179 KPDMLLLDEPTNHLDAESVAWLERHLQEYP---GTVVAVTHDRYFLDNVA 225
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-217 |
1.77e-05 |
|
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: 44.14 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 36 CVVLHGHSGSGKSTLLRSL-YAnyLPDEGQIQIKHGDEWVDLVTAPARKV-VEIR-KTTVGwvsQFLRVIPRISALE-VV 111
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALkYA--LTGELPPNSKGGAHDPKLIREGEVRAqVKLAfENANG---KKYTITRSLAILEnVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 112 MqplldtgVPREACAAKAARLLTRLnvperlwhlapstfSGGEQQ------RVNIARGFIVDYPILLLDEPTASLDAKN- 184
Cdd:cd03240 99 F-------CHQGESNWPLLDMRGRC--------------SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENi 157
|
170 180 190
....*....|....*....|....*....|....
gi 16131922 185 SAAVVELIREAK-TRGAAIVGIFHDEAVRnDVAD 217
Cdd:cd03240 158 EESLAEIIEERKsQKNFQLIVITHDEELV-DAAD 190
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-190 |
2.21e-05 |
|
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: 44.90 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGqiQIKHGDEwvdlvtaparkvveirkttVGWVSQFLRV 101
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG--KIKHSGR-------------------ISFSPQTSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPRISALEVVMQPLLDTGvpREACAAKAARLLTRLNV-PER---LWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPT 177
Cdd:TIGR01271 499 MPGTIKDNIIFGLSYDEY--RYTSVIKACQLEEDIALfPEKdktVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170
....*....|...
gi 16131922 178 ASLDAKNSAAVVE 190
Cdd:TIGR01271 577 THLDVVTEKEIFE 589
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-67 |
3.41e-05 |
|
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: 44.02 E-value: 3.41e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQI 67
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-222 |
3.72e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.89 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhGDEWVDLVTAP--ARKVV---EIRKTT-------VGWv 95
Cdd:PRK15439 283 SLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLN-GKEINALSTAQrlARGLVylpEDRQSSglyldapLAW- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 96 sqflrvipRISALEVVMQPL-LDTGVPREACAAKAARLLTRLNVPERlwhlAPSTFSGGEQQRVNIARGFIVDYPILLLD 174
Cdd:PRK15439 361 --------NVCALTHNRRGFwIKPARENAVLERYRRALNIKFNHAEQ----AARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131922 175 EPTASLDAKNSAAVVELIREAKTRGAAIVGIFHD--EAVRndVADRLHPM 222
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDleEIEQ--MADRVLVM 476
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-183 |
3.75e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 43.93 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkHGDEWVDLvtaparKVVEIRkttvgwvsqflrv 101
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF-HDIPLTKL------QLDSWR------------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 ipriSALEVVMQ-PLL--DT-------GVPrEACAAK---AARL------LTRL------NVPERLWHLapstfSGGEQQ 156
Cdd:PRK10789 389 ----SRLAVVSQtPFLfsDTvannialGRP-DATQQEiehVARLasvhddILRLpqgydtEVGERGVML-----SGGQKQ 458
|
170 180
....*....|....*....|....*..
gi 16131922 157 RVNIARGFIVDYPILLLDEPTASLDAK 183
Cdd:PRK10789 459 RISIARALLLNAEILILDDALSAVDGR 485
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
122-203 |
3.82e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 122 REACAAKAARLLTRLNVPERLWHlAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAA 201
Cdd:NF000106 118 RKDARARADELLERFSLTEAAGR-AAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGAT 196
|
..
gi 16131922 202 IV 203
Cdd:NF000106 197 VL 198
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-197 |
4.66e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 31 VNAGECVVLHGHSGSGKSTLLRSL----YANYLPDEGQIQIK-HGDEwvdlvtaparkvvEIRKTTVGWVSQflrviprI 105
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDgITPE-------------EIKKHYRGDVVY-------N 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 106 SALEV-----VMQPLLDTGVpreACAAKAAR--LLTRLNVPERLWHLAPSTF------------------SGGEQQRVNI 160
Cdd:TIGR00956 144 AETDVhfphlTVGETLDFAA---RCKTPQNRpdGVSREEYAKHIADVYMATYglshtrntkvgndfvrgvSGGERKRVSI 220
|
170 180 190
....*....|....*....|....*....|....*..
gi 16131922 161 ARGFIVDYPILLLDEPTASLDaknSAAVVELIREAKT 197
Cdd:TIGR00956 221 AEASLGGAKIQCWDNATRGLD---SATALEFIRALKT 254
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-102 |
5.84e-05 |
|
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: 41.98 E-value: 5.84e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131922 34 GECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDEWVDLVTAPARKVVEIRKTTVGWVSQFLRVI 102
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLA 70
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-208 |
6.01e-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: 43.39 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFilhqqnGVRLpVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIkhgDEWVDLvtapa 81
Cdd:TIGR03719 323 IEAENLTKAF------GDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI---GETVKL----- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 rkvveirkttvGWVSQFLRVI-PRISALEVVM--QPLLDTG---VP-REACAA---KAARLLTRLNVperlwhlapstFS 151
Cdd:TIGR03719 388 -----------AYVDQSRDALdPNKTVWEEISggLDIIKLGkreIPsRAYVGRfnfKGSDQQKKVGQ-----------LS 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 152 GGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKtrGAAIVgIFHD 208
Cdd:TIGR03719 446 GGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFA--GCAVV-ISHD 499
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
18-223 |
7.01e-05 |
|
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: 42.63 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 18 GVRLPVLNRASLTVNAGECVVLHGHSGSGKSTL-LRSLYAnylpdEGQIQI-------------KHGDEWVDLVT--APA 81
Cdd:cd03270 5 GAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLaFDTIYA-----EGQRRYveslsayarqflgQMDKPDVDSIEglSPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 82 RKVVEIR-----KTTVGWVSQ---FLRVIPRISALEVVMQPLLDTGVPreacaakaarLLTrlnvPERlwhlAPSTFSGG 153
Cdd:cd03270 80 IAIDQKTtsrnpRSTVGTVTEiydYLRLLFARVGIRERLGFLVDVGLG----------YLT----LSR----SAPTLSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131922 154 EQQRVNIAR--GFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDE-AVRNdvADRLHPMG 223
Cdd:cd03270 142 EAQRIRLATqiGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEdTIRA--ADHVIDIG 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-182 |
7.41e-05 |
|
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: 43.40 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKhgdewvdlvtaparkvveirkTTVGWVSQfLRV 101
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMK---------------------GSVAYVPQ-QAW 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPRISALEVVM--QPLLDtgvPREACAAKAARLLTRLNVperlwhlAPS-----------TFSGGEQQRVNIARGFIVDY 168
Cdd:TIGR00957 710 IQNDSLRENILfgKALNE---KYYQQVLEACALLPDLEI-------LPSgdrteigekgvNLSGGQKQRVSLARAVYSNA 779
|
170
....*....|....
gi 16131922 169 PILLLDEPTASLDA 182
Cdd:TIGR00957 780 DIYLFDDPLSAVDA 793
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
41-226 |
9.74e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 41.87 E-value: 9.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 41 GHSGSGKSTLLRSL-YANY-----LPDEGQI--QIKHGDE--WVDLVTAPARKVVEIRKTTVGWVSQFLRVIprisalev 110
Cdd:cd03279 35 GPTGAGKSTILDAItYALYgktprYGRQENLrsVFAPGEDtaEVSFTFQLGGKKYRVERSRGLDYDQFTRIV-------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 111 vmqpLLDTGvpreacaaKAARLLTRlnvperlwhlAPSTFSGGEQQRVNIA------------RGFIVDypILLLDEPTA 178
Cdd:cd03279 107 ----LLPQG--------EFDRFLAR----------PVSTLSGGETFLASLSlalalsevlqnrGGARLE--ALFIDEGFG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131922 179 SLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRL--HPMGASS 226
Cdd:cd03279 163 TLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRLevIKTPGGS 212
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-181 |
1.10e-04 |
|
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: 42.15 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 22 PVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGqiQIKHGDEwvdlvtaparkvveirkttVGWVSQFLRV 101
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG--KIKHSGR-------------------ISFSSQFSWI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 IPRISALEVVMQPLLDTgvPREACAAKAARLLTRL-NVPERLWHLAPS---TFSGGEQQRVNIARGFIVDYPILLLDEPT 177
Cdd:cd03291 110 MPGTIKENIIFGVSYDE--YRYKSVVKACQLEEDItKFPEKDNTVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPF 187
|
....
gi 16131922 178 ASLD 181
Cdd:cd03291 188 GYLD 191
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
9-68 |
1.51e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.18 E-value: 1.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 9 KTFILHQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIK 68
Cdd:PRK13545 25 KDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
148-205 |
1.82e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 1.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 148 STFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGI 205
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII 447
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-223 |
1.86e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 139 PERlwhlAPSTFSGGEQQRVNIARG-----FIVDYpilLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRN 213
Cdd:PRK00635 470 PER----ALATLSGGEQERTALAKHlgaelIGITY---ILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMIS 542
|
90
....*....|
gi 16131922 214 dVADRLHPMG 223
Cdd:PRK00635 543 -LADRIIDIG 551
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
37-196 |
2.47e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.76 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 37 VVLHGHSGSGKSTLLRSL-YANYLPDEGQIQ-----IKHGDE--WVDLVTAPARKVVEIRK----------TTVGWVSQF 98
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIrYALYGKARSRSKlrsdlINVGSEeaSVELEFEHGGKRYRIERrqgefaefleAKPSERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 99 LRVIPRISALEVVMQPLLDTGVPREACAAKAARLLT----RLNvpeRLWHLAP-STFSGGEQQRVNIARgfIVDypiLLL 173
Cdd:COG0419 106 LKRLLGLEIYEELKERLKELEEALESALEELAELQKlkqeILA---QLSGLDPiETLSGGERLRLALAD--LLS---LIL 177
|
170 180
....*....|....*....|...
gi 16131922 174 DepTASLDAKNSAAVVELIREAK 196
Cdd:COG0419 178 D--FGSLDEERLERLLDALEELA 198
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
133-205 |
2.63e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.45 E-value: 2.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131922 133 LTRLNVPERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGI 205
Cdd:PRK13549 389 IQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
28-222 |
2.66e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.50 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 28 SLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIqikhgdeWVDLVTAPARKVVEIRKttvgwvsqflrvipRISA 107
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI-------LLDGKPVTAEQPEDYRK--------------LFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 108 LEV---VMQPLLDTGvPREACAAKAARLLTRLNVPERL----WHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASL 180
Cdd:PRK10522 402 VFTdfhLFDQLLGPE-GKPANPALVEKWLERLKMAHKLeledGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQ 480
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131922 181 DAK-NSAAVVELIREAKTRGAAIVGIFHDEAVRnDVADRLHPM 222
Cdd:PRK10522 481 DPHfRREFYQVLLPLLQEMGKTIFAISHDDHYF-IHADRLLEM 522
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-208 |
3.66e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 1 MINVQNVSKTFILHQQNGVRLPvlnraSLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEG---------------QI 65
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLP-----SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshitrlsfeQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 66 QIKHGDEW----VDLVTAP----ARKVVEIrkttvgwvsqflrviprisalevvmqpLLDTGVPREACAAKAA-----RL 132
Cdd:PRK10938 76 QKLVSDEWqrnnTDMLSPGeddtGRTTAEI---------------------------IQDEVKDPARCEQLAQqfgitAL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131922 133 LTRlnvpeRLWHLapstfSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGI---FHD 208
Cdd:PRK10938 129 LDR-----RFKYL-----STGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVlnrFDE 197
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
2-71 |
3.73e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.57 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 2 INVQNVSKTFILHQQNGVRLP-------------VLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQiK 68
Cdd:PRK13546 5 VNIKNVTKEYRIYRTNKERMKdalipkhknktffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-R 83
|
...
gi 16131922 69 HGD 71
Cdd:PRK13546 84 NGE 86
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
151-223 |
6.17e-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: 39.27 E-value: 6.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 151 SGGEQQRVNIARGF----IVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVrNDVADRLHPMG 223
Cdd:cd03227 79 SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPEL-AELADKLIHIK 154
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
33-78 |
1.32e-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: 1.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 16131922 33 AGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDEWVDLVT 78
Cdd:pfam13191 23 RPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSP 68
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-207 |
1.33e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 39.32 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLrslyaNYLPDEGQIQIKHGDEwvDLVTAPARKVVEIRKTtvGWVSQ----- 97
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLL-----NVLAERVTTGVITGGD--RLVNGRPLDSSFQRSI--GYVQQqdlhl 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 98 -------------FLRVIPRISALE-----------VVMQPLLDT--GVPREAcaakaarlltrLNVPERlwhlapstfs 151
Cdd:TIGR00956 849 ptstvreslrfsaYLRQPKSVSKSEkmeyveeviklLEMESYADAvvGVPGEG-----------LNVEQR---------- 907
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131922 152 ggeqQRVNIARGfIVDYPILL--LDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFH 207
Cdd:TIGR00956 908 ----KRLTIGVE-LVAKPKLLlfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
145-219 |
1.62e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 145 LAPSTFSGGEQQRVNI----------ARGFIVDYPI--LLLDEPTASLDAKNSAAVVELIREAKTRGAA-IVGIFHDEAV 211
Cdd:PRK02224 777 LEPEQLSGGERALFNLslrcaiyrllAEGIEGDAPLppLILDEPTVFLDSGHVSQLVDLVESMRRLGVEqIVVVSHDDEL 856
|
....*...
gi 16131922 212 RnDVADRL 219
Cdd:PRK02224 857 V-GAADDL 863
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
23-195 |
1.63e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 38.68 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 23 VLNRASLTVNAGECVVLHGHSGSGKSTLLrSLYANYLPDEGQIQIKhGDEWVDLVTAPARKVVEIRKTTVGWVSQFLRV- 101
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLL-SAFLRLLNTEGDIQID-GVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 102 -----------IPRIsALEVVMQPLLDtgvpreacaakaarlltrlNVPERL-WHLAPS--TFSGGEQQRVNIARGFIVD 167
Cdd:cd03289 97 ldpygkwsdeeIWKV-AEEVGLKSVIE-------------------QFPGQLdFVLVDGgcVLSHGHKQLMCLARSVLSK 156
|
170 180
....*....|....*....|....*...
gi 16131922 168 YPILLLDEPTASLDAKNSAAVVELIREA 195
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQA 184
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
148-182 |
2.35e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.56 E-value: 2.35e-03
10 20 30
....*....|....*....|....*....|....*
gi 16131922 148 STFSGGEQQRVNIARGFIVDYPILLLDEPTASLDA 182
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-211 |
2.61e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 38.67 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 15 QQNGV---RLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSL----YANYLpdEGQIQI----KHGDEWVDL------- 76
Cdd:PLN03140 884 KEQGVtedRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagrkTGGYI--EGDIRIsgfpKKQETFARIsgyceqn 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 77 -VTAPArkvVEIRKTTVgwVSQFLRVIPRISALEVVMqpLLDtgvpreacaaKAARLLTRLNVPERLWHLAPSTFSGGEQ 155
Cdd:PLN03140 962 dIHSPQ---VTVRESLI--YSAFLRLPKEVSKEEKMM--FVD----------EVMELVELDNLKDAIVGLPGVTGLSTEQ 1024
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131922 156 -QRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAV 211
Cdd:PLN03140 1025 rKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
151-208 |
4.84e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 37.41 E-value: 4.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131922 151 SGGEQQRVNIARGFIVDYPILLLDEPTASLDaknsaavVELIR---EAKTR--GAAIVgIFHD 208
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLD-------VETLRaleEALLEfpGCAVV-ISHD 501
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
151-203 |
5.07e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 37.46 E-value: 5.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 16131922 151 SGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIV 203
Cdd:PRK09700 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
148-194 |
5.12e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 35.29 E-value: 5.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 148 STFSGGEQQ-------------RVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIRE 194
Cdd:pfam13558 31 GGLSGGEKQllaylplaaalaaQYGSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
37-124 |
6.77e-03 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 35.75 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131922 37 VVLHGHSGSGKSTLLRSLYANY-------------LPDEGQIQIKHGDEWVDLVTAPARKVVEIR---KTTVGWVSQFLR 100
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLEELgavrlssdderkrLFGEGRPSISYYTDATDRTYERLHELARIAlraGRPVILDATNLR 81
|
90 100
....*....|....*....|....
gi 16131922 101 VipriSALEVVMQPLLDTGVPREA 124
Cdd:pfam13671 82 R----DERARLLALAREYGVPVRI 101
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
151-182 |
7.09e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 37.26 E-value: 7.09e-03
10 20 30
....*....|....*....|....*....|..
gi 16131922 151 SGGEQQRVNIARGFIVDYPILLLDEPTASLDA 182
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
151-182 |
9.55e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 37.02 E-value: 9.55e-03
10 20 30
....*....|....*....|....*....|..
gi 16131922 151 SGGEQQRVNIARGFIVDYPILLLDEPTASLDA 182
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
|
| |
