|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
9-230 |
1.97e-113 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 323.92 E-value: 1.97e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYLHDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQ 88
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 89 IRRTDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANA 168
Cdd:COG1136 83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640481818 169 PRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHVIE 230
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
15-228 |
1.25e-102 |
|
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: 296.32 E-value: 1.25e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 15 DVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRTDI 94
Cdd:cd03255 5 NLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRRHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 95 GFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLA 174
Cdd:cd03255 85 GFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640481818 175 DEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHV 228
Cdd:cd03255 165 DEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
15-226 |
1.41e-84 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 250.73 E-value: 1.41e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 15 DVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRTDI 94
Cdd:TIGR02211 6 NLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 95 GFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLA 174
Cdd:TIGR02211 86 GFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 640481818 175 DEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDG 226
Cdd:TIGR02211 166 DEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDG 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
9-230 |
7.07e-82 |
|
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: 244.27 E-value: 7.07e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYLHDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQ 88
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 89 IRRTDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKEtvKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANA 168
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640481818 169 PRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHVIE 230
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
10-232 |
4.46e-74 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 223.78 E-value: 4.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVYLHDVRRRYKQGEatlTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQI 89
Cdd:COG2884 1 MIRFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 RRtDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAP 169
Cdd:COG2884 78 RR-RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640481818 170 RVLLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARMDRRV-SLQDGHVIELD 232
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVlELEDGRLVRDE 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-228 |
4.86e-71 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 216.61 E-value: 4.86e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 6 NGVPVVYLHDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVE 85
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 86 RTQIRRTDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAV 165
Cdd:PRK11629 81 KAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640481818 166 ANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHV 228
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
10-230 |
2.26e-64 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 199.62 E-value: 2.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVYLHDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQI 89
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 RRTDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAP 169
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640481818 170 RVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHVIE 230
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
9-219 |
4.11e-63 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 197.23 E-value: 4.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYLHDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLlEQADEGEVYVGGTATSGLSdvert 87
Cdd:COG1116 6 PALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRlIAGL-EKPTSGEVLVDGKPVTGPG----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 88 qirrTDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVAN 167
Cdd:COG1116 80 ----PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 640481818 168 APRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DR 219
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLaDR 208
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
13-230 |
1.09e-61 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 192.90 E-value: 1.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQgeatLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATsGLSDVERTQIRRt 92
Cdd:COG1126 4 IENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 DIGFVYQSHRLLPEFSALENVMLPQM-IRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRV 171
Cdd:COG1126 78 KVGMVFQQFNLFPHLTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 172 LLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:COG1126 158 MLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVaDRVVFMDGGRIVE 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-221 |
1.37e-61 |
|
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: 191.92 E-value: 1.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDvertqirrt 92
Cdd:cd03293 3 VRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 DIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVL 172
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 640481818 173 LADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRV 221
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRV 202
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
9-229 |
4.76e-61 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 191.81 E-value: 4.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYLHDVRRRYKQGEatlTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQ 88
Cdd:COG3638 1 PMLELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 89 IRRtDIGFVYQSHRLLPEFSALENVM--------LPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVA 160
Cdd:COG3638 78 LRR-RIGMIFQQFNLVPRLSVLTNVLagrlgrtsTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 161 IARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAAR-MDRRVSLQDGHVI 229
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-229 |
3.51e-59 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 197.25 E-value: 3.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRT 92
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 DIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVL 172
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 173 LADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARMDRRVSLQDGHVI 229
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
28-223 |
1.41e-56 |
|
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: 178.96 E-value: 1.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRTDIGFVYQSHRLLPEF 107
Cdd:TIGR03608 12 VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 108 SALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTAD 187
Cdd:TIGR03608 92 TVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRD 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 640481818 188 HVFKALTQLVRATRVaMLIATHNMDLAARMDRRVSL 223
Cdd:TIGR03608 172 EVLDLLLELNDEGKT-IIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-231 |
4.47e-56 |
|
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: 178.54 E-value: 4.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVYLHDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQI 89
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 RRtDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAP 169
Cdd:cd03258 81 RR-RIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640481818 170 RVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVS-LQDGHVIEL 231
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAvMEKGEVVEE 222
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
10-226 |
5.12e-55 |
|
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: 175.13 E-value: 5.12e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVYLHDVRRRYKQGEAtltILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQI 89
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVA---ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 RRTdIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAP 169
Cdd:TIGR02673 78 RRR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 640481818 170 RVLLADEPTGNLDPHTADHVFKALTQLVRATrVAMLIATHNMDLAARMDRRV-SLQDG 226
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKRG-TTVIVATHDLSLVDRVAHRViILDDG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
11-228 |
5.40e-55 |
|
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: 175.03 E-value: 5.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 11 VYLHDVRRRYKqgeaTLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGlsdvERTQIR 90
Cdd:cd03262 1 IEIKNLHKSFG----DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD----DKKNIN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 91 --RTDIGFVYQSHRLLPEFSALENVMLPQM-IRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVAN 167
Cdd:cd03262 73 elRQKVGMVFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640481818 168 APRVLLADEPTGNLDPHTADHVFKALTQLVRaTRVAMLIATHNMDLAARM-DRRVSLQDGHV 228
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
13-230 |
1.19e-53 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 175.65 E-value: 1.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRt 92
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 DIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVL 172
Cdd:COG1135 83 KIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 173 LADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVS-LQDGHVIE 230
Cdd:COG1135 163 LCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAvLENGRIVE 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-230 |
2.35e-53 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 171.81 E-value: 2.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVYLHDVRRRYKQgeatLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERtQI 89
Cdd:PRK09493 1 MIEFKNVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER-LI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 RRtDIGFVYQSHRLLPEFSALENVML-PQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANA 168
Cdd:PRK09493 76 RQ-EAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640481818 169 PRVLLADEPTGNLDPHTADHVFKALTQLVRATrVAMLIATHNMDLAARMDRRVSLQD-GHVIE 230
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDkGRIAE 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-230 |
3.29e-53 |
|
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: 170.39 E-value: 3.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGeatlTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLlEQADEGEVYVGGTatsglsDVERTQIRR 91
Cdd:cd03259 3 LKGLSKTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRlIAGL-ERPDSGEILIDGR------DVTGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 TDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRV 171
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 172 LLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALaDRIAVMNEGRIVQ 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-229 |
1.34e-52 |
|
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: 169.67 E-value: 1.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEatlTILDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLEqADEGEVYVGGTATSGLSDVERTQIRR 91
Cdd:cd03256 3 VENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLrCLNGLVE-PTSGSVLIDGTDINKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 tDIGFVYQSHRLLPEFSALENVM---LPQM-----IRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIAR 163
Cdd:cd03256 79 -QIGMIFQQFNLIERLSVLENVLsgrLGRRstwrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 164 AVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAAR-MDRRVSLQDGHVI 229
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-230 |
2.16e-52 |
|
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: 169.39 E-value: 2.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYLHDVRRRYkqgeATLTILDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLeQADEGEVYVGGTATSGLSDVERT 87
Cdd:COG1127 4 PMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLkLIIGLL-RPDSGEILVDGQDITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 88 QIRRtDIGFVYQSHRLlpeFSAL---ENVMLP-QMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIAR 163
Cdd:COG1127 79 ELRR-RIGMLFQGGAL---FDSLtvfENVAFPlREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640481818 164 AVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIaDRVAVLADGKIIA 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-228 |
2.89e-52 |
|
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: 167.97 E-value: 2.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 20 YKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRTdIGFVYQ 99
Cdd:cd03292 7 TKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK-IGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 100 SHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTG 179
Cdd:cd03292 86 DFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 640481818 180 NLDPHTADHVFKALTQlVRATRVAMLIATHNMDLAARMDRRV-SLQDGHV 228
Cdd:cd03292 166 NLDPDTTWEIMNLLKK-INKAGTTVVVATHAKELVDTTRHRViALERGKL 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
13-228 |
1.48e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.14 E-value: 1.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGeatlTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTAtsgLSDVERTQIRRt 92
Cdd:COG4619 3 LEGLSFRVGGK----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKP---LSAMPPPEWRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 DIGFVYQSHRLLPEfSALENVMLPQMIRGlpKKETVKRSKEILAYLGLAERVTHRPA-ELSGGEQQRVAIARAVANAPRV 171
Cdd:COG4619 75 QVAYVPQEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 640481818 172 LLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHV 228
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
13-232 |
2.43e-51 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 169.89 E-value: 2.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYkqgeATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLlEQADEGEVYVGGTatsglsDVERTQIRR 91
Cdd:COG3842 8 LENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRmIAGF-ETPDSGRILLDGR------DVTGLPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 TDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRV 171
Cdd:COG3842 77 RNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640481818 172 LLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIELD 232
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALaDRIAVMNDGRIEQVG 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-229 |
2.82e-51 |
|
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: 165.97 E-value: 2.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEatlTILDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLeQADEGEVYVGGTATSGLSdveRTQIRR 91
Cdd:COG1122 3 LENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLrLLNGLL-KPTSGEVLVDGKDITKKN---LRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 tDIGFVYQShrllPE---FSA--LENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVA 166
Cdd:COG1122 76 -KVGLVFQN----PDdqlFAPtvEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640481818 167 NAPRVLLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELaDRVIVLDDGRIV 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-230 |
6.91e-50 |
|
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: 170.08 E-value: 6.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 2 EQGENGVPVVYLHDVRRRYKQGEA-TLTILDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLEqADEGEVYVGGTATS 79
Cdd:COG1123 252 PAAAAAEPLLEVRNLSKRYPVRGKgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLArLLLGLLR-PTSGSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 80 GLSDVERTQIRRtDIGFVYQ--SHRLLPEFSALENVMLPQMIRG-LPKKETVKRSKEILAYLGLAERVTHR-PAELSGGE 155
Cdd:COG1123 331 KLSRRSLRELRR-RVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPDLADRyPHELSGGQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 156 QQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIaDRVAVMYDGRIVE 485
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-230 |
1.27e-49 |
|
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: 161.90 E-value: 1.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQADeGEVYVGGTATSGLSDVERtQIRR 91
Cdd:cd03257 4 VKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARaILGLLKPTS-GSIIFDGKDLLKLSRRLR-KIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 TDIGFVYQ--SHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAY--LGLAERVTHR-PAELSGGEQQRVAIARAVA 166
Cdd:cd03257 82 KEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLvgVGLPEEVLNRyPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640481818 167 NAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIaDRVAVMYAGKIVE 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-230 |
3.89e-48 |
|
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: 158.43 E-value: 3.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 11 VYLHDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERtqir 90
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 91 RTDIGFVYQSHR--LLPEFSALENVMLPQMIRGLPkkETVKRSKEILAYLGLAERVTHR-PAELSGGEQQRVAIARAVAN 167
Cdd:COG1124 78 RRRVQMVFQDPYasLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640481818 168 APRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVE 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
13-227 |
1.67e-47 |
|
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: 155.70 E-value: 1.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEATltILDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLeQADEGEVYVGGTATSGLSDVERtqirR 91
Cdd:cd03225 2 LKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLrLLNGLL-GPTSGEVLVDGKDLTKLSLKEL----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 TDIGFVYQShrllPE--FSAL---ENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVA 166
Cdd:cd03225 75 RKVGLVFQN----PDdqFFGPtveEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640481818 167 NAPRVLLADEPTGNLDPHTADHVFKALTQLVRAtRVAMLIATHNMDLAAR-MDRRVSLQDGH 227
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
28-229 |
5.83e-47 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 155.68 E-value: 5.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGT---ATSGLSDvERTQIR--RTDIGFVYQSHR 102
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItidTARSLSQ-QKGLIRqlRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 103 LLPEFSALENVML-PQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNL 181
Cdd:PRK11264 96 LFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 640481818 182 DPHTADHVFKALTQLVRATRvAMLIATHNMDLAARMDRRVSLQDGHVI 229
Cdd:PRK11264 176 DPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-231 |
7.67e-47 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 155.73 E-value: 7.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 5 ENGVPVVYLHDVRRRYKQGEatltILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGG-------TA 77
Cdd:COG4598 3 DTAPPALEVRDLHKSFGDLE----VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 78 TSGLSDVERTQIR--RTDIGFVYQSHRLLPEFSALENVML-PQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGG 154
Cdd:COG4598 79 DGELVPADRRQLQriRTRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 155 EQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRvAMLIATHNMDLAarmdRRVSlqdGHVIEL 231
Cdd:COG4598 159 QQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFA----RDVS---SHVVFL 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
28-230 |
2.25e-46 |
|
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: 153.81 E-value: 2.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLeQADEGEVYVGGTATSGLSDVERTQIRRTdIGFVYQSHRLLPE 106
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLrLIVGLL-RPDSGEVLIDGEDISGLSEAELYRLRRR-MGMLFQSGALFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 FSALENVMLP-QMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHT 185
Cdd:cd03261 92 LTVFENVAFPlREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 640481818 186 ADhvfkALTQLVRATRVAM----LIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:cd03261 172 SG----VIDDLIRSLKKELgltsIMVTHDLDTAFAIaDRIAVLYDGKIVA 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-232 |
3.32e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 153.30 E-value: 3.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEAtltiLDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLeQADEGEVYVGGTatsglsDV--ERTQI 89
Cdd:COG1131 3 VRGLTKRYGDKTA----LDGVSLTVEPGEIFGLLGPNGAGKTTTIrMLLGLL-RPTSGEVRVLGE------DVarDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 RRtDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAP 169
Cdd:COG1131 72 RR-RIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640481818 170 RVLLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARMDRRVS-LQDGHVIELD 232
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAiIDKGRIVADG 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
13-232 |
3.83e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 156.11 E-value: 3.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRt 92
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 DIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVL 172
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640481818 173 LADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVS-LQDGHVIELD 232
Cdd:PRK11153 163 LCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAvIDAGRLVEQG 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-227 |
1.56e-45 |
|
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: 149.64 E-value: 1.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQgeatLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDveRTQIRRT 92
Cdd:cd03229 3 LKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLED--ELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 DIGFVYQSHRLLPEFSALENVMLPqmirglpkketvkrskeilaylglaervthrpaeLSGGEQQRVAIARAVANAPRVL 172
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 173 LADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGH 227
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-230 |
1.76e-45 |
|
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: 158.14 E-value: 1.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYLHDVRRRYKQGEATltILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQADE--GEVYVGGTATSGLSDve 85
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALaLMGLLPHGGRisGEVLLDGRDLLELSE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 86 rtQIRRTDIGFVYQS--HRLLPEfSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIAR 163
Cdd:COG1123 79 --ALRGRRIGMVFQDpmTQLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640481818 164 AVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVE 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
11-228 |
3.29e-45 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 154.08 E-value: 3.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 11 VYLHDVRRRYKQGEAtltiLDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLlEQADEGEVYVGGTATSGLSDVERtqi 89
Cdd:COG3839 4 LELENVSKSYGGVEA----LKDIDLDIEDGEFLVLLGPSGCGKSTLLRmIAGL-EDPTSGEILIGGRDVTDLPPKDR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 rrtDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAP 169
Cdd:COG3839 76 ---NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640481818 170 RVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHN----MDLAarmDRRVSLQDGHV 228
Cdd:COG3839 153 KVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMTLA---DRIAVMNDGRI 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-230 |
3.79e-44 |
|
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: 147.71 E-value: 3.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEAtltiLDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQA----DEGEVYVGGTATSGLsDVERT 87
Cdd:cd03260 3 LRDLNVYYGDKHA----LKDISLDIPKGEITALIGPSGCGKSTLLRlLNRLNDLIpgapDEGEVLLDGKDIYDL-DVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 88 QIRRTdIGFVYQSHRLLPeFSALENVMLPQMIRG-LPKKETVKRSKEILAYLGLAERVTHR--PAELSGGEQQRVAIARA 164
Cdd:cd03260 78 ELRRR-VGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 165 VANAPRVLLADEPTGNLDPHTADHVFKALTQLvrATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVE 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
33-232 |
1.15e-42 |
|
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: 145.09 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 33 ASLALWEGQSVALVAPSGTGKSTLL-HIAGLLEqADEGEVYVGGTATSGLSDVERTQIRRTDIGFVYQSHRLLPEFSALE 111
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLrCINRLIE-PTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 112 NVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFK 191
Cdd:cd03294 122 NVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQD 201
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 640481818 192 ALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIELD 232
Cdd:cd03294 202 ELLRLQAELQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVG 243
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
32-230 |
2.14e-42 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 143.62 E-value: 2.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 32 GASLALW-------EGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIR--RTDIGFVYQSHR 102
Cdd:PRK11124 13 GAHQALFditldcpQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIRelRRNVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 103 LLPEFSALENVM-LPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNL 181
Cdd:PRK11124 93 LWPHLTVQQNLIeAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 640481818 182 DPHTADHVFKALTQLvRATRVAMLIATHNMDLAARMDRRV-SLQDGHVIE 230
Cdd:PRK11124 173 DPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVvYMENGHIVE 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
11-232 |
2.31e-42 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 146.45 E-value: 2.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 11 VYLHDVRRRYKQgeatLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLlEQADEGEVYVGG-TATSGLSdverTQ 88
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRiIAGL-ETPDSGRIVLNGrDLFTNLP----PR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 89 IRRtdIGFVYQSHRLLPEFSALENVM--LPqmIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVA 166
Cdd:COG1118 74 ERR--VGFVFQHYALFPHMTVAENIAfgLR--VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 167 NAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIELD 232
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELaDRVVVMNQGRIEQVG 216
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
39-230 |
2.77e-42 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 143.23 E-value: 2.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 39 EGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIR--RTDIGFVYQSHRLLPEFSALENVM-L 115
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIRllRQKVGMVFQQYNLWPHLTVMENLIeA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 116 PQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQ 195
Cdd:COG4161 107 PCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRE 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 640481818 196 LvRATRVAMLIATHNMDLAARMDRRVS-LQDGHVIE 230
Cdd:COG4161 187 L-SQTGITQVIVTHEVEFARKVASQVVyMEKGRIIE 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-214 |
2.93e-42 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 143.85 E-value: 2.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 15 DVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTATSGlSDVERtqirrtd 93
Cdd:COG4525 8 HVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNlIAGFL-APSSGEITLDGVPVTG-PGADR------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 94 iGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLL 173
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 640481818 174 ADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLA 214
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-229 |
3.69e-42 |
|
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: 143.26 E-value: 3.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGeatlTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTATSGLSDVERTQIrr 91
Cdd:COG1120 4 AENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRaLAGLL-KPSSGEVLLDGRDLASLSRRELARR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 tdIGFVYQSHRLLPEFSALENVML---PQM-IRGLPKKETVKRSKEILAYLGLAERVtHRP-AELSGGEQQRVAIARAVA 166
Cdd:COG1120 77 --IAYVPQEPPAPFGLTVRELVALgryPHLgLFGRPSAEDREAVEEALERTGLEHLA-DRPvDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640481818 167 NAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYaDRLVLLKDGRIV 217
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
14-229 |
3.25e-41 |
|
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: 140.51 E-value: 3.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 14 HDVRRRYKQGEatlTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRTd 93
Cdd:TIGR02315 5 ENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 94 IGFVYQSHRLLPEFSALENVMLP--------QMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAV 165
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGrlgykptwRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640481818 166 ANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAAR-MDRRVSLQDGHVI 229
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEIV 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-178 |
3.44e-41 |
|
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: 137.78 E-value: 3.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLeQADEGEVYVGGTAtsglSDVERTQIRRTDIGFVYQSHRLLPEFS 108
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLkLIAGLL-SPTEGTILLDGQD----LTDDERKSLRKEIGYVFQDPQLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640481818 109 ALENVMLPQMIRGLPKKETVKRSKEILAYLGL----AERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPT 178
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-232 |
3.81e-41 |
|
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: 139.70 E-value: 3.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 11 VYLHDVRRRYKqgeaTLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLlEQADEGEVYVGGTATSGLSDVERtqi 89
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRmIAGL-EEPTSGRIYIGGRDVTDLPPKDR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 rrtDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAP 169
Cdd:cd03301 73 ---DIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640481818 170 RVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIELD 232
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMaDRIAVMNDGQIQQIG 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
9-230 |
1.53e-40 |
|
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: 142.10 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYL--HDVRRRYKQgeatLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVER 86
Cdd:TIGR03265 1 SSPYLsiDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 87 tqirrtDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVA 166
Cdd:TIGR03265 77 ------DYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640481818 167 NAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHVIE 230
Cdd:TIGR03265 151 TSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIE 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
11-228 |
2.26e-40 |
|
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: 138.14 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 11 VYLHDVRRRYKQGeatlTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERtqir 90
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 91 rtDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPR 170
Cdd:cd03300 73 --PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 171 VLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHV 228
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMsDRIAVMNKGKI 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-232 |
1.85e-39 |
|
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: 136.28 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEatlTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVErtqIRRT 92
Cdd:cd03295 3 FENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 dIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGL--AERVTHRPAELSGGEQQRVAIARAVANAPR 170
Cdd:cd03295 77 -IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 171 VLLADEPTGNLDPHTADHV---FKALTQLVRATRVamlIATHNMDLAARM-DRRVSLQDGHVIELD 232
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLqeeFKRLQQELGKTIV---FVTHDIDEAFRLaDRIAIMKNGEIVQVG 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
30-228 |
7.43e-39 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 133.85 E-value: 7.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRtDIGFVYQSHRLLPEFSA 109
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR-QIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 110 LENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHV 189
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 640481818 190 FKALTQLVRATrVAMLIATHNMDLAARMDRRV-SLQDGHV 228
Cdd:PRK10908 177 LRLFEEFNRVG-VTVLMATHDIGLISRRSYRMlTLSDGHL 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-232 |
1.54e-38 |
|
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: 133.83 E-value: 1.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEAtltiLDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGTATsglsdVERTQIRR 91
Cdd:COG4555 4 VENLSKKYGKVPA----LKDVSFTAKDGEITGLLGPNGAGKTTLLRmLAGLLK-PDSGSILIDGEDV-----RKEPREAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 TDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRV 171
Cdd:COG4555 74 RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640481818 172 LLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIELD 232
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQG 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-226 |
1.61e-38 |
|
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: 133.33 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 22 QGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYV----GGTATSGLSDVERTQIRRTDIGF 96
Cdd:COG4778 19 QGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKcIYGNY-LPDSGSILVrhdgGWVDLAQASPREILALRRRTIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 97 VYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTH-RPAELSGGEQQRVAIARAVANAPRVLLAD 175
Cdd:COG4778 98 VSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDlPPATFSGGEQQRVNIARGFIADPPLLLLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 640481818 176 EPTGNLDPHTADHVfKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDG 226
Cdd:COG4778 178 EPTASLDAANRAVV-VELIEEAKARGTAIIGIFHDEEVREAVaDRVVDVTPF 228
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
33-231 |
3.04e-38 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 136.14 E-value: 3.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 33 ASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRTDIGFVYQSHRLLPEFSALEN 112
Cdd:TIGR01186 12 ADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRKKIGMVFQQFALFPHMTILQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 113 VMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKA 192
Cdd:TIGR01186 92 TSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSMQDE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 640481818 193 LTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIEL 231
Cdd:TIGR01186 172 LKKLQATLQKTIVFITHDLDEAIRIgDRIVIMKAGEIVQV 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-221 |
5.23e-38 |
|
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: 134.41 E-value: 5.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQA--DEGEVYVGGTATSGLSDVERTQI 89
Cdd:COG0444 4 VRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPgiTSGEILFDGEDLLKLSEKELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 RRTDIGFVYQShrllPeFSAL-------ENVMLPQMI-RGLPKKETVKRSKEILAYLGL--AERVTHR-PAELSGGEQQR 158
Cdd:COG0444 84 RGREIQMIFQD----P-MTSLnpvmtvgDQIAEPLRIhGGLSKAEARERAIELLERVGLpdPERRLDRyPHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640481818 159 VAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRV 221
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRV 221
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
13-232 |
8.38e-38 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 133.68 E-value: 8.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEatlTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVErtqIRRt 92
Cdd:COG1125 4 FENVTKRYPDGT---VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE---LRR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 DIGFVYQSHRLLPEFSALENVML-PQMiRGLPKKETVKRSKEILAYLGL-AERVTHR-PAELSGGEQQRVAIARAVANAP 169
Cdd:COG1125 77 RIGYVIQQIGLFPHMTVAENIATvPRL-LGWDKERIRARVDELLELVGLdPEEYRDRyPHELSGGQQQRVGVARALAADP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 170 RVLLADEPTGNLDPHTADHV---FKALTQLVRATRVamlIATHNMDLAARM-DRRVSLQDGHVIELD 232
Cdd:COG1125 156 PILLMDEPFGALDPITREQLqdeLLRLQRELGKTIV---FVTHDIDEALKLgDRIAVMREGRIVQYD 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
30-230 |
1.80e-37 |
|
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: 130.92 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGTATSGLSDVERtqirrtDIGFVYQSHRLLPEFS 108
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLEtIAGFIK-PDSGKILLNGKDITNLPPEKR------DISYVPQNYALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 109 ALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADH 188
Cdd:cd03299 88 VYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 640481818 189 VFKALTQLVRATRVAMLIATHNMDLAARMDRRVS-LQDGHVIE 230
Cdd:cd03299 168 LREELKKIRKEFGVTVLHVTHDFEEAWALADKVAiMLNGKLIQ 210
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-231 |
2.17e-37 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 131.24 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 5 ENGVPVVYLHdvrRRYKQGEatltILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATS----- 79
Cdd:PRK10619 3 ENKLNVIDLH---KRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 80 ----GLSDVERTQIRRTDIGFVYQSHRLLPEFSALENVM-LPQMIRGLPKKETVKRSKEILAYLGLAERVTHR-PAELSG 153
Cdd:PRK10619 76 dgqlKVADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640481818 154 GEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRvAMLIATHNMDLAarmdRRVSlqdGHVIEL 231
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFA----RHVS---SHVIFL 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-230 |
2.73e-37 |
|
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: 136.81 E-value: 2.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 6 NGVPVVYLHDVRRRYKQGEatlTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTAtsgLSDV 84
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNlLLGFL-PPYSGSILINGVD---LSDL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 85 ERTQIRRtDIGFVYQSHRLL------------PEFS------ALENVMLPQMIRGLPKketvkrskeilaylGLAERVTH 146
Cdd:COG4988 405 DPASWRR-QIAWVPQNPYLFagtirenlrlgrPDASdeeleaALEAAGLDEFVAALPD--------------GLDTPLGE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 147 RPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVamLIATHNMDLAARMDRRVSLQDG 226
Cdd:COG4988 470 GGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTV--ILITHRLALLAQADRILVLDDG 547
|
....
gi 640481818 227 HVIE 230
Cdd:COG4988 548 RIVE 551
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
28-229 |
4.90e-37 |
|
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: 127.94 E-value: 4.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGTATSGLSDVERTQIrrtdIGFVYQshrllpe 106
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKtLAGLLK-PSSGEILLDGKDLASLSPKELARK----IAYVPQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 fsALENVmlpqmirGLpkketvkrskeilayLGLAERVTHrpaELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTA 186
Cdd:cd03214 81 --ALELL-------GL---------------AHLADRPFN---ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 640481818 187 DHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLNLAARYaDRVILLKDGRIV 177
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
30-229 |
6.11e-37 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 130.65 E-value: 6.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLeQADEGEVYVGGTATSGLSDVERTQIRRTdIGFVYQ--SHRLLPE 106
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIqHLNGLL-KPTSGTVTIDGRDITAKKKKKLKDLRKK-VGLVFQfpEHQLFEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 fSALENVML-PQMIrGLPKKETVKRSKEILAYLGLAERVTHR-PAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPH 184
Cdd:TIGR04521 99 -TVYKDIAFgPKNL-GLSEEEAEERVKEALELVGLDEEYLERsPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 640481818 185 TADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:TIGR04521 177 GRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYaDRVIVMHKGKIV 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-228 |
8.12e-37 |
|
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: 127.13 E-value: 8.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEAtltiLDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLeQADEGEVYVGGTatsglsDV--ERTQI 89
Cdd:cd03230 3 VRNLSKRYGKKTA----LDDISLTVEKGEIYGLLGPNGAGKTTLIkIILGLL-KPDSGEIKVLGK------DIkkEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 RRtDIGFVYQSHRLLPEFSALENVmlpqmirglpkketvkrskeilaylglaervthrpaELSGGEQQRVAIARAVANAP 169
Cdd:cd03230 72 KR-RIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 170 RVLLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARM-DRRVSLQDGHV 228
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-232 |
8.50e-37 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 132.38 E-value: 8.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 1 MEQGENGVPVVYLHDVRRRYKqgeaTLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLlEQADEGEVYVGGTATS 79
Cdd:PRK09452 5 NKQPSSLSPLVELRGISKSFD----GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRlIAGF-ETPDSGRIMLDGQDIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 80 GLSDVERtqirrtDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRV 159
Cdd:PRK09452 80 HVPAENR------HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640481818 160 AIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHvIELD 232
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMsDRIVVMRDGR-IEQD 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
39-229 |
1.48e-36 |
|
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: 127.80 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 39 EGQSVALVAPSGTGKSTLLH-IAGLlEQADEGEVYVGGTAtsgLSDVER-----TQIRRtdIGFVYQSHRLLPEFSALEN 112
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRcIAGL-EKPDGGTIVLNGTV---LFDSRKkinlpPQQRK--IGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 113 VMLpqmirGLPKKETVK---RSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHV 189
Cdd:cd03297 96 LAF-----GLKRKRNREdriSVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 640481818 190 FKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQ 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
13-229 |
2.38e-36 |
|
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: 128.62 E-value: 2.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYkqgeATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTATSGLSDVERTQ--I 89
Cdd:COG0411 7 VRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNlITGFY-RPTSGRILFDGRDITGLPPHRIARlgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 RRTdigfvYQSHRLLPEFSALENVMLPQMIR----------GLPK-----KETVKRSKEILAYLGLAERVTHRPAELSGG 154
Cdd:COG0411 82 ART-----FQNPRLFPELTVLENVLVAAHARlgrgllaallRLPRarreeREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 155 EQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVS-LQDGHVI 229
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVvLDFGRVI 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-229 |
1.04e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.36 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYLHDVRRRYkQGEatlTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTatsglsDVERt 87
Cdd:COG1121 5 PAIELENLTVSY-GGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILGLL-PPTSGTVRLFGK------PPRR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 88 qiRRTDIGFVYQSHRLLPEF--SALENVML---PQM-IRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAI 161
Cdd:COG1121 73 --ARRRIGYVPQRAEVDWDFpiTVRDVVLMgryGRRgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640481818 162 ARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARMDRRVSLQDGHVI 229
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
15-230 |
1.20e-35 |
|
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: 126.30 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 15 DVRRRYKQGEAtltiLDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGtatsglSDVERTQIRRTDI 94
Cdd:cd03296 7 NVSKRFGDFVA----LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG------EDATDVPVQERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 95 GFVYQSHRLLPEFSALENVMLPQMIR----GLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPR 170
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640481818 171 VLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHN----MDLAarmDRRVSLQDGHVIE 230
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDqeeaLEVA---DRVVVMNKGRIEQ 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
11-229 |
5.09e-35 |
|
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: 124.15 E-value: 5.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 11 VYLHDVRRRYKQGeaTLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTatSGLSDveRTQIR 90
Cdd:cd03263 1 LQIRNLTKTYKKG--TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY--SIRTD--RKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 91 RtDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLaERVTHRPA-ELSGGEQQRVAIARAVANAP 169
Cdd:cd03263 75 Q-SLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGL-TDKANKRArTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640481818 170 RVLLADEPTGNLDPHTADHVFKALTQLVRATrvAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALcDRIAIMSDGKLR 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
18-229 |
6.93e-35 |
|
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: 123.63 E-value: 6.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 18 RRYKQGEAtltiLDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVggtatSGLSDVERTQIRRTDIGFV 97
Cdd:cd03265 8 KKYGDFEA----VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV-----AGHDVVREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 98 YQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEP 177
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 640481818 178 TGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQD-GHVI 229
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDhGRII 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-227 |
8.50e-35 |
|
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: 121.72 E-value: 8.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 11 VYLHDVRRRYKQGEATltILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGTAtsgLSDVERTQI 89
Cdd:cd03228 1 IEFKNVSFSYPGRPKP--VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKlLLRLYD-PTSGEILIDGVD---LRDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 RRTdIGFVYQSHRLlpeFSA--LENVmlpqmirglpkketvkrskeilaylglaervthrpaeLSGGEQQRVAIARAVAN 167
Cdd:cd03228 75 RKN-IAYVPQDPFL---FSGtiRENI-------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 168 APRVLLADEPTGNLDPHTADHVFKALTQLvrATRVAMLIATHNMDLAARMDRRVSLQDGH 227
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
45-232 |
8.87e-35 |
|
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: 126.07 E-value: 8.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 45 LVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTatsglsDVERTQIRRTDIGFVYQSHRLLPEFSALENVMLPQMIRGLPK 124
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGE------DVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 125 KETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAM 204
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180
....*....|....*....|....*....
gi 640481818 205 LIATHNMDLAARM-DRRVSLQDGHVIELD 232
Cdd:TIGR01187 155 VFVTHDQEEAMTMsDRIAIMRKGKIAQIG 183
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
34-221 |
1.99e-34 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 125.57 E-value: 1.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 34 SLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGtatsglSDVERTQIRRTDIGFVYQSHRLLPEFSALEN 112
Cdd:NF040840 20 SLEVKEGEYFIILGPSGAGKTVLLElIAGIWP-PDSGKIYLDG------KDITNLPPEKRGIAYVYQNYMLFPHKTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 113 VMLPQMIRGLPKKETVKRSKEILAYLGLaERVTHR-PAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFK 191
Cdd:NF040840 93 IAFGLKLRKVPKEEIERKVKEIMELLGI-SHLLHRkPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIR 171
|
170 180 190
....*....|....*....|....*....|
gi 640481818 192 ALTQLVRATRVAMLIATHNMDLAARMDRRV 221
Cdd:NF040840 172 EMKRWHREFGFTAIHVTHNFEEALSLADRV 201
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
27-229 |
2.29e-34 |
|
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: 122.55 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 27 LTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTATSGLSDVERTQ--IRRTdigfvYQSHRL 103
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNlISGFL-RPTSGSVLFDGEDITGLPPHEIARlgIGRT-----FQIPRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 104 LPEFSALENVMLP-QMIRGLP---------KKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLL 173
Cdd:cd03219 87 FPELTVLENVMVAaQARTGSGlllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 174 ADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:cd03219 167 LDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLaDRVTVLDQGRVI 222
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-229 |
4.29e-34 |
|
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: 122.92 E-value: 4.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 20 YKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTL-LHIAGLLeQADEGEVYVGGTATsgLSDVERTQIRRTdIGFVY 98
Cdd:TIGR04520 8 FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaKLLNGLL-LPTSGKVTVDGLDT--LDEENLWEIRKK-VGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 99 QShrllPE-------------FsALENvmlpqmiRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAV 165
Cdd:TIGR04520 84 QN----PDnqfvgatveddvaF-GLEN-------LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640481818 166 ANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHVI 229
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIV 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-230 |
4.41e-34 |
|
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: 128.80 E-value: 4.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEATltILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTAtsgLSDVERTQIRR 91
Cdd:COG2274 476 LENVSFRYPGDSPP--VLDNISLTIKPGERVAIVGRSGSGKSTLLKlLLGLY-EPTSGRILIDGID---LRQIDPASLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 tDIGFVYQSHRLL------------PEFS------ALENVMLPQMIRGLPkketvkrskeilayLGLAERVTHRPAELSG 153
Cdd:COG2274 550 -QIGVVLQDVFLFsgtirenitlgdPDATdeeiieAARLAGLHDFIEALP--------------MGYDTVVGEGGSNLSG 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640481818 154 GEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVR-ATRVamlIATHNMDLAARMDRRVSLQDGHVIE 230
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgRTVI---IIAHRLSTIRLADRIIVLDKGRIVE 689
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-230 |
4.71e-34 |
|
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: 127.96 E-value: 4.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYkqGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGTAtsgLSDVERTQIRR 91
Cdd:COG4987 336 LEDVSFRY--PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLAlLLRFLD-PQSGSITLGGVD---LRDLDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 TdIGFVYQSHRLL------------PEFS------ALENVMLPQMIRGLPKketvkrskeilaylGLAERVTHRPAELSG 153
Cdd:COG4987 410 R-IAVVPQRPHLFdttlrenlrlarPDATdeelwaALERVGLGDWLAALPD--------------GLDTWLGEGGRRLSG 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 154 GEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVamLIATHNMDLAARMDRRVSLQDGHVIE 230
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLERMDRILVLEDGRIVE 549
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
33-229 |
4.92e-34 |
|
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: 124.83 E-value: 4.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 33 ASLALWEGQSVALVAPSGTGKSTLLH-IAGLlEQADEGEVYVGGTAtsgLSDVER-----TQIRRtdIGFVYQSHRLLPE 106
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRaIAGL-ERPDSGRIRLGGEV---LQDSARgiflpPHRRR--IGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 FSALENVMLPQmiRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTA 186
Cdd:COG4148 92 LSVRGNLLYGR--KRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 640481818 187 DHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:COG4148 170 AEILPYLERLRDELDIPILYVSHSLDEVARLaDHVVLLEQGRVV 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
28-229 |
2.43e-33 |
|
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: 119.56 E-value: 2.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQAdEGEVYVGGtatsglsdvERTQIRRTDIGFVYQSHRLLPE 106
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLKPT-SGSIRVFG---------KPLEKERKRIGYVPQRRSIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 F--SALENVMLPQMIR----GLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGN 180
Cdd:cd03235 83 FpiSVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 640481818 181 LDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARMDRRVSLQDGHVI 229
Cdd:cd03235 163 VDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
27-229 |
3.14e-33 |
|
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: 119.46 E-value: 3.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 27 LTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQAdEGEVYVGGTATSGLSDVERTqirRTDIGFVYQSHRLLP 105
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMGLLPPR-SGSIRFDGRDITGLPPHERA---RAGIGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 106 EFSALENVMLPQMIRglPKKETVKRSKEILAYL-GLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPH 184
Cdd:cd03224 89 ELTVEENLLLGAYAR--RRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 640481818 185 TADHVFKALTQLvRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:cd03224 167 IVEEIFEAIREL-RDEGVTILLVEQNARFALEIaDRAYVLERGRVV 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
30-230 |
3.85e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 124.75 E-value: 3.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHI-AGLlEQADEGEVYVGGTATSGLSDVErtqIRRTDIGFVYQSHRLLPEFS 108
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKIlSGV-YQPDSGEILLDGEPVRFRSPRD---AQAAGIAIIHQELNLVPNLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 109 ALENVMLPQMIRGLP---KKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHT 185
Cdd:COG1129 96 VAENIFLGREPRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTERE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 640481818 186 ADHVFKALTQLvRATRVAMLIATHNMD----LAarmDRRVSLQDGHVIE 230
Cdd:COG1129 176 VERLFRIIRRL-KAQGVAIIYISHRLDevfeIA---DRVTVLRDGRLVG 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
13-227 |
6.31e-33 |
|
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: 116.58 E-value: 6.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGeatlTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERtqirRT 92
Cdd:cd00267 2 IENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----RR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 DIGFVYQshrllpefsalenvmlpqmirglpkketvkrskeilaylglaervthrpaeLSGGEQQRVAIARAVANAPRVL 172
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 173 LADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAAR-MDRRVSLQDGH 227
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-228 |
3.52e-32 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 117.86 E-value: 3.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 7 GVPVVyLHDVRRRYKQGeatlTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTAtsgLSDVer 86
Cdd:PRK11247 10 GTPLL-LNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP---LAEA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 87 tqirRTDIGFVYQSHRLLPEFSALENVMLpqmirGLpKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVA 166
Cdd:PRK11247 80 ----REDTRLMFQDARLLPWKKVIDNVGL-----GL-KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640481818 167 NAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSL-QDGHV 228
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLiEEGKI 212
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
30-230 |
3.91e-32 |
|
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: 117.40 E-value: 3.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQAD-----EGEVYVGG-TATSGLSDVERTqirRTDIGFVYQSHRL 103
Cdd:TIGR00972 17 LKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVpgvriEGKVLFDGqDIYDKKIDVVEL---RRRVGMVFQKPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 104 LPeFSALENVMLPQMIRGL-PKKETVKRSKEILAYLGLAERVTHR----PAELSGGEQQRVAIARAVANAPRVLLADEPT 178
Cdd:TIGR00972 94 FP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALWDEVKDRlhdsALGLSGGQQQRLCIARALAVEPEVLLLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 640481818 179 GNLDPHTADHVFKALTQLvrATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:TIGR00972 173 SALDPIATGKIEELIQEL--KKKYTIVIVTHNMQQAARIsDRTAFFYDGELVE 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
27-230 |
4.65e-32 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 121.83 E-value: 4.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 27 LTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQ--ADEGEV-----------YV-------------GGTATS- 79
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgYVerpskvgepcpvcGGTLEPe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 80 -----GLSDVERTQIRRTDIGFVYQSHRLLPEFSALENVM--LPQMirGLPKKETVKRSKEILAYLGLAERVTHRPAELS 152
Cdd:TIGR03269 93 evdfwNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLeaLEEI--GYEGKEAVGRAVDLIEMVQLSHRITHIARDLS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 153 GGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLsDKAIWLENGEIKE 249
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
28-182 |
5.62e-32 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 119.44 E-value: 5.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGtatsglSDVERTQIRRTDIGFVYQSHRLLPEF 107
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG------EDVTHRSIQQRDICMVFQSYALFPHM 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640481818 108 SALENVMLPQMIRGLPKKETVKRSKEILAYLGLA---ERVTHrpaELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:PRK11432 94 SLGENVGYGLKMLGVPKEERKQRVKEALELVDLAgfeDRYVD---QISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
16-228 |
1.81e-31 |
|
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: 117.91 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 16 VRRRYKQGEATLTildgASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRTDIG 95
Cdd:TIGR02142 3 ARFSKRLGDFSLD----ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 96 FVYQSHRLLPEFSALENvMLPQMIRGLPKkETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLAD 175
Cdd:TIGR02142 79 YVFQEARLFPHLSVRGN-LRYGMKRARPS-ERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640481818 176 EPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHV 228
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLaDRVVVLEDGRV 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
29-217 |
2.41e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 115.57 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGTATSGLSdVERtqirrtdiGFVYQSHRLLPEF 107
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNlIAGFVP-YQHGSITLDGKPVEGPG-AER--------GVVFQNEGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 108 SALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTAD 187
Cdd:PRK11248 86 NVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190
....*....|....*....|....*....|
gi 640481818 188 HVFKALTQLVRATRVAMLIATHNMDLAARM 217
Cdd:PRK11248 166 QMQTLLLKLWQETGKQVLLITHDIEEAVFM 195
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-230 |
3.86e-31 |
|
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: 119.40 E-value: 3.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYLHDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKS-TLLHIAGLLEQAD---EGEVYVGGTATSGLSDV 84
Cdd:COG4172 5 PLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 85 ERTQIRRTDIGFVYQshrllpE-FSAL-----------ENVMLpqmIRGLPKKETVKRSKEILAYLGLAE---RVTHRPA 149
Cdd:COG4172 85 ELRRIRGNRIAMIFQ------EpMTSLnplhtigkqiaEVLRL---HRGLSGAAARARALELLERVGIPDperRLDAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 150 ELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHV 228
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFaDRVAVMRQGEI 235
|
..
gi 640481818 229 IE 230
Cdd:COG4172 236 VE 237
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
30-229 |
4.00e-31 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 114.31 E-value: 4.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGtatSGLSDVERTQIRRtdIGFVYQSHRLLPEFSA 109
Cdd:TIGR03864 17 LDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAG---HDLRRAPRAALAR--LGVVFQQPTLDLDLSV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 110 LENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHV 189
Cdd:TIGR03864 92 RQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPTVGLDPASRAAI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 640481818 190 FKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHVI 229
Cdd:TIGR03864 172 TAHVRALARDQGLSVLWATHLVDEIEASDRLVVLHRGRVL 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
9-229 |
5.14e-31 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 114.41 E-value: 5.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYLHDVRRRYkqGEATltILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQADEGEVYVGGTaTSGLSDVErt 87
Cdd:COG1119 2 PLLELRNVTVRR--GGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSlITGDLPPTYGNDVRLFGE-RRGGEDVW-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 88 QIRRTdIGFVyqSHRLLPEFSALENVMlpQMIR-------GLPKK---ETVKRSKEILAYLGLAERVTHRPAELSGGEQQ 157
Cdd:COG1119 75 ELRKR-IGLV--SPALQLRFPRDETVL--DVVLsgffdsiGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640481818 158 RVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNM-DLAARMDRRVSLQDGHVI 229
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVeEIPPGITHVLLLKDGRVV 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
30-226 |
5.76e-31 |
|
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: 113.71 E-value: 5.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTatsglsdvertQIRRT--DIGFVYQSHRLLPEF 107
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK-----------QITEPgpDRMVVFQNYSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 108 SALENVMLP--QMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHT 185
Cdd:TIGR01184 70 TVRENIALAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 640481818 186 ADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDG 226
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLsDRVVMLTNG 191
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
28-225 |
1.17e-30 |
|
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: 112.19 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLHI-AGLLeQADEGEVYVGGTATSglsdvERTQIRRTDIGFVYQSHRLLPE 106
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRIlAGLL-PPSAGEVLWNGEPIR-----DAREDYRRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 FSALENVMLPQMIRGLPKKETvkRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTA 186
Cdd:COG4133 90 LTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 640481818 187 DHVFKALTQLVRATRVAmLIATHNmDLAARMDRRVSLQD 225
Cdd:COG4133 168 ALLAELIAAHLARGGAV-LLTTHQ-PLELAAARVLDLGD 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
11-229 |
1.22e-30 |
|
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: 112.37 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 11 VYLHDVRRRYkqgeATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGtatSGLSDVERTqi 89
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRmILGII-LPDSGEVLFDG---KPLDIAARN-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 rrtDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAP 169
Cdd:cd03269 71 ---RIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640481818 170 RVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLiATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARAGKTVIL-STHQMELVEELcDRVLLLNKGRAV 207
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-230 |
2.42e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.57 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYLHDVRRRYKQGEATltILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTAtsgLSDVERT 87
Cdd:PRK13635 4 EIIRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKlLNGLL-LPEAGTITVGGMV---LSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 88 QIRRTdIGFVYQShrllPE-------------FsALENvmlpqmiRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGG 154
Cdd:PRK13635 78 DVRRQ-VGMVFQN----PDnqfvgatvqddvaF-GLEN-------IGVPREEMVERVDQALRQVGMEDFLNREPHRLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 155 EQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHVIE 230
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-229 |
7.52e-30 |
|
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: 109.06 E-value: 7.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEAtltiLDGASLALWEGQSVALVAPSGTGKSTLLHI-AGLLeQADEGEVYVGGTATSGLSDVERtqiRR 91
Cdd:cd03216 3 LRGITKRFGGVKA----LDGVSLSVRRGEVHALLGENGAGKSTLMKIlSGLY-KPDSGEILVDGKEVSFASPRDA---RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 TDIGFVYQshrllpefsalenvmlpqmirglpkketvkrskeilaylglaervthrpaeLSGGEQQRVAIARAVANAPRV 171
Cdd:cd03216 75 AGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 172 LLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
29-229 |
9.93e-30 |
|
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: 110.46 E-value: 9.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTATSGLSdVERtqIRRTDIGFVYQSHRLLPEF 107
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLL-PPRSGSIRFDGEDITGLP-PHR--IARLGIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 108 SALENVMLPQMIRGlPKKETVKRSKEILAYL-GLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTA 186
Cdd:COG0410 94 TVEENLLLGAYARR-DRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 640481818 187 DHVFKALTQLvRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:COG0410 173 EEIFEIIRRL-NREGVTILLVEQNARFALEIaDRAYVLERGRIV 215
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-230 |
1.14e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 115.65 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEatlTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGTAtsgLSDVERTQIRR 91
Cdd:COG1132 342 FENVSFSYPGDR---PVLKDISLTIPPGETVALVGPSGSGKSTLVNlLLRFYD-PTSGRILIDGVD---IRDLTLESLRR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 TdIGFVYQSHRLL------------PEFS------ALENVMLPQMIRGLPKketvkrskeilaylGLAERVTHRPAELSG 153
Cdd:COG1132 415 Q-IGVVPQDTFLFsgtirenirygrPDATdeeveeAAKAAQAHEFIEALPD--------------GYDTVVGERGVNLSG 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 154 GEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIAtHNMDLAARMDRRVSLQDGHVIE 230
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIA-HRLSTIRNADRILVLDDGRIVE 554
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
29-232 |
2.21e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 110.13 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLL--------HIAGlleQADEGEVYVGGTATSGlSDVERTQIRRTdIGFVYQS 100
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmndLIPG---ARVEGEILLDGEDIYD-PDVDVVELRRR-VGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 101 HRLLPeFSALENVMLPQMIRGLPKK----ETVKRSkeiLAYLGLAERVTHR---PA-ELSGGEQQRVAIARAVANAPRVL 172
Cdd:COG1117 101 PNPFP-KSIYDNVAYGLRLHGIKSKseldEIVEES---LRKAALWDEVKDRlkkSAlGLSGGQQQRLCIARALAVEPEVL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640481818 173 LADEPTGNLDPHTADHVFKALTQLvrATRVAMLIATHNMDLAARM-DRRVSLQDGHVIELD 232
Cdd:COG1117 177 LMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQAARVsDYTAFFYLGELVEFG 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
29-228 |
2.23e-29 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 112.48 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTatsglsDVERTQIRRTDIGFVYQSHRLLPEFS 108
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT------DVSRLHARDRKVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 109 ALENV-----MLPQMIRglPKKETVKRS-KEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:PRK10851 91 VFDNIafgltVLPRRER--PNAAAIKAKvTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 640481818 183 PHTADHVFKALTQLVRATRVAMLIATHN----MDLAarmDRRVSLQDGHV 228
Cdd:PRK10851 169 AQVRKELRRWLRQLHEELKFTSVFVTHDqeeaMEVA---DRVVVMSQGNI 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
13-229 |
6.24e-29 |
|
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: 108.05 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEAtltiLDGASLALWEGQSvALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGtatsgLSDVERTQIRRT 92
Cdd:cd03264 3 LENLTKRYGKKRA----LDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDG-----QDVLKQPQKLRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 DIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVL 172
Cdd:cd03264 73 RIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 640481818 173 LADEPTGNLDPHTAdHVFKALTQLVRATRVaMLIATHNM-DLAARMDRRVSLQDGHVI 229
Cdd:cd03264 153 IVDEPTAGLDPEER-IRFRNLLSELGEDRI-VILSTHIVeDVESLCNQVAVLNKGKLV 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
28-229 |
8.08e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 108.66 E-value: 8.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTATSGLSDVERTQIRrtdiGFVYQSHRLLPE 106
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKlLTGEL-TPSSGEVRLNGRPLAAWSPWELARRR----AVLPQHSSLAFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 FSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARA-------VANAPRVLLADEPTG 179
Cdd:COG4559 90 FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVlaqlwepVDGGPRWLFLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 640481818 180 NLDPHTADHVFKALTQLVRAtRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:COG4559 170 ALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYaDRILLLHQGRLV 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
11-229 |
9.69e-29 |
|
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: 107.58 E-value: 9.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 11 VYLHDVRRRYkqGEATLTIldgaSLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTatsglsDVERTQIR 90
Cdd:cd03298 1 VRLDKIRFSY--GEQPMHF----DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV------DVTAAPPA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 91 RTDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPR 170
Cdd:cd03298 69 DRPVSMLFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 171 VLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRR-VSLQDGHVI 229
Cdd:cd03298 149 VLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRvVFLDNGRIA 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
33-231 |
1.01e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 111.66 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 33 ASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRTDIGFVYQSHRLLPEFSALEN 112
Cdd:PRK10070 47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 113 VMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKA 192
Cdd:PRK10070 127 TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDE 206
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 640481818 193 LTQLVRATRVAMLIATHNMDLAARMDRRVS-LQDGHVIEL 231
Cdd:PRK10070 207 LVKLQAKHQRTIVFISHDLDEAMRIGDRIAiMQNGEVVQV 246
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
10-228 |
1.71e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 108.18 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVYLHDVRRRYKQGEAtltiLDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLL--EQADEGEVYVGGTATSGLSDVER 86
Cdd:PRK09984 4 IIRVEKLAKTFNQHQA----LHAVDLNIHHGEMVALLGPSGSGKSTLLrHLSGLItgDKSAGSHIELLGRTVQREGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 87 tQIR--RTDIGFVYQSHRLLPEFSALENVMLPQM---------IRGLPKKETvKRSKEILAYLGLAERVTHRPAELSGGE 155
Cdd:PRK09984 80 -DIRksRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQK-QRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640481818 156 QQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHV 228
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYcERIVALRQGHV 231
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
28-229 |
2.79e-28 |
|
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: 106.86 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERtqiRRTDIGFVYQSHRLLPEF 107
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKR---ARLGIGYLPQEASIFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 108 SALENVMLPQMIRGLPKKETVKRSKEILAYLGLaERVTHRPA-ELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPhTA 186
Cdd:cd03218 91 TVEENILAVLEIRGLSKKEREEKLEELLEEFHI-THLRKSKAsSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP-IA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 640481818 187 DHVFKALTQLVRATRVAMLIATHNM-DLAARMDRRVSLQDGHVI 229
Cdd:cd03218 169 VQDIQKIIKILKDRGIGVLITDHNVrETLSITDRAYIIYEGKVL 212
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-226 |
3.07e-28 |
|
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: 105.80 E-value: 3.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEatlTILDGASLALWEGQSVALVAPSGTGKSTLLHI-AGLLEQADeGEVYVGGtatsglSDVERTQIRR 91
Cdd:cd03226 2 IENISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKIlAGLIKESS-GSILLNG------KPIKAKERRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 TdIGFVYQ-SHRLLPEFSALENVMLPqmIRGLPKKETVKRskEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPR 170
Cdd:cd03226 72 S-IGYVMQdVDYQLFTDSVREELLLG--LKELDAGNEQAE--TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 171 VLLADEPTGNLDPHTADHVFKALTQLVRATrVAMLIATHNMDLAARM-DRRVSLQDG 226
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQG-KAVIVITHDYEFLAKVcDRVLLLANG 202
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
29-214 |
3.14e-28 |
|
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: 105.58 E-value: 3.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLeQADEGEVYVGGTAT----SGLSDvertqiRRTDIGFVYQShrl 103
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLlHLNGLL-RPQSGAVLIDGEPLdysrKGLLE------RRQRVGLVFQD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 104 lPE---FSA--LENVMLPQMIRGLPKKETVKRSKEILAYLG---LAERVTHrpaELSGGEQQRVAIARAVANAPRVLLAD 175
Cdd:TIGR01166 77 -PDdqlFAAdvDQDVAFGPLNLGLSEAEVERRVREALTAVGasgLRERPTH---CLSGGEKKRVAIAGAVAMRPDVLLLD 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 640481818 176 EPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLA 214
Cdd:TIGR01166 153 EPTAGLDPAGREQMLAILRRL-RAEGMTVVISTHDVDLA 190
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-230 |
4.25e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 107.08 E-value: 4.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 14 HDVRRRYKQG-----EATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQ 88
Cdd:PRK10419 7 SGLSHHYAHGglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 89 IRRtDIGFVYQSH--RLLPEFSALENVMLP-QMIRGLPKKETVKRSKEILAYLGLAERVTHR-PAELSGGEQQRVAIARA 164
Cdd:PRK10419 87 FRR-DIQMVFQDSisAVNPRKTVREIIREPlRHLLSLDKAERLARASEMLRAVDLDDSVLDKrPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 165 VANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQD-GHVIE 230
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDnGQIVE 232
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
15-216 |
5.75e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.41 E-value: 5.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 15 DVRRRYKQGE--ATLTILDgASLALWEGQSVALVAPSGTGKSTLL-HIAGLLeQADEGEVYVGGTATSGLSDVERTQIRR 91
Cdd:PRK13634 7 KVEHRYQYKTpfERRALYD-VNVSIPSGSYVAIIGHTGSGKSTLLqHLNGLL-QPTSGTVTIGERVITAGKKNKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 TDIGFVYQ--SHRLLPEfSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHR-PAELSGGEQQRVAIARAVANA 168
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLAME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 640481818 169 PRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAAR 216
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAAR 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
28-224 |
8.54e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.57 E-value: 8.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSdverTQIRRTDIGFVYQSHRLLPEf 107
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK----PEIYRQQVSYCAQTPTLFGD- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 108 SALENVMLPQMIRGlpKKETVKRSKEILAYLGLAERVTHRP-AELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTA 186
Cdd:PRK10247 96 TVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 640481818 187 DHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQ 224
Cdd:PRK10247 174 HNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQ 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
30-223 |
1.11e-27 |
|
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: 109.68 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGTATSGLSdverTQIRRTDIGFVYQsHRLLPEFS 108
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNlLLGFVD-PTEGSIAVNGVPLADAD----ADSWRDQIAWVPQ-HPFLFAGT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 109 ALENVmlpQMIRGLPKKETVKRSKEiLAYL---------GLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTG 179
Cdd:TIGR02857 412 IAENI---RLARPDASDAEIREALE-RAGLdefvaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 640481818 180 NLDPHTADHVFKALTQLvrATRVAMLIATHNMDLAARMDRRVSL 223
Cdd:TIGR02857 488 HLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAALADRIVVL 529
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
15-229 |
1.56e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 105.93 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 15 DVRRRYKQGEATLtilDGASLALWEGQSVALVAPSGTGKSTL-LHIAGLLEqADEGEVYVGGTA----TSGLSDVERTqi 89
Cdd:PRK13639 6 DLKYSYPDGTEAL---KGINFKAEKGEMVALLGPNGAGKSTLfLHFNGILK-PTSGEVLIKGEPikydKKSLLEVRKT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 rrtdIGFVYQS---HRLLPefSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVA 166
Cdd:PRK13639 80 ----VGIVFQNpddQLFAP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640481818 167 NAPRVLLADEPTGNLDPHTADHVFKALTQLVRATrVAMLIATHNMDLAARMDRRVS-LQDGHVI 229
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVYADKVYvMSDGKII 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
30-232 |
2.40e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 105.68 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLEQAdEGEVYVGG-TATSGLSDVERTQIRRtDIGFVYQ-SHRLLPE 106
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMqHFNALLKPS-SGTITIAGyHITPETGNKNLKKLRK-KVSLVFQfPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 FSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERV-THRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHT 185
Cdd:PRK13641 101 NTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 640481818 186 ADHVFKALTQLVRATRVAMLIaTHNM-DLAARMDRRVSLQDGHVIELD 232
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILV-THNMdDVAEYADDVLVLEHGKLIKHA 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
30-225 |
2.41e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.23 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTqirrtdIGFVYQSHRLLPEFSA 109
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP------INMMFQSYALFPHMTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 110 LENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHV 189
Cdd:PRK11607 109 EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRM 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 640481818 190 FKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQD 225
Cdd:PRK11607 189 QLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
13-228 |
2.57e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 106.85 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYkqgEATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLlEQADEGEVYVGGTATSGLSDVERtqirr 91
Cdd:PRK11650 6 LQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRmVAGL-ERITSGEIWIGGRVVNELEPADR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 tDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRV 171
Cdd:PRK11650 77 -DIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640481818 172 LLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHN----MDLAarmDRRVSLQDGHV 228
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDqveaMTLA---DRVVVMNGGVA 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-229 |
3.43e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.58 E-value: 3.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYkqgeATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIA-GLLEqADEGEVYVGGtatsglSDVERTQIRR 91
Cdd:COG4152 4 LKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIIlGILA-PDSGEVLWDG------EPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 tdIGFvyqshrlLPEfsalENVMLPQM-----------IRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVA 160
Cdd:COG4152 73 --IGY-------LPE----ERGLYPKMkvgeqlvylarLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 161 IARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELcDRIVIINKGRKV 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-230 |
3.61e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 104.22 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLL-----EQADEGEVYVGGTATSGLSDVErtqIRRTdIGFVYQSHRL 103
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIE---LRRR-VQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 104 LPEFSALENVMLPQMIRGL--PKKETVKRSKEILAYLGLAERVTHR---PA-ELSGGEQQRVAIARAVANAPRVLLADEP 177
Cdd:PRK14247 94 IPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRldaPAgKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640481818 178 TGNLDPHTADHVFKALTQLVRatRVAMLIATHNMDLAARMDRRVS-LQDGHVIE 230
Cdd:PRK14247 174 TANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAfLYKGQIVE 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
39-228 |
4.04e-27 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 106.65 E-value: 4.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 39 EGQSVALVAPSGTGKSTLLH-IAGLlEQADEGEVYVGGTATSGLSDVERTqirrtdIGFVYQSHRLLPEFSALENVMLPQ 117
Cdd:PRK11000 28 EGEFVVFVGPSGCGKSTLLRmIAGL-EDITSGDLFIGEKRMNDVPPAERG------VGMVFQSYALYPHLSVAENMSFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 118 MIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLV 197
Cdd:PRK11000 101 KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLH 180
|
170 180 190
....*....|....*....|....*....|....*
gi 640481818 198 RATRVAMLIATHN----MDLAarmDRRVSLQDGHV 228
Cdd:PRK11000 181 KRLGRTMIYVTHDqveaMTLA---DKIVVLDAGRV 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
15-229 |
4.06e-27 |
|
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: 103.60 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 15 DVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGlsdvERTQIRRtDI 94
Cdd:cd03266 6 ALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK----EPAEARR-RL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 95 GFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLA 174
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 175 DEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLcDRVVVLHRGRVV 215
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
14-230 |
4.93e-27 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 104.50 E-value: 4.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 14 HDVRRRYKQG-----EATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQ 88
Cdd:TIGR02769 6 RDVTHTYRTGglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 89 IRRtDIGFVYQS--HRLLPEFSALENVMLP-QMIRGLPKKETVKRSKEILAYLGL-AERVTHRPAELSGGEQQRVAIARA 164
Cdd:TIGR02769 86 FRR-DVQLVFQDspSAVNPRMTVRQIIGEPlRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 165 VANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQD-GHVIE 230
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDkGQIVE 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
19-229 |
6.55e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 103.30 E-value: 6.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 19 RYKQGEATLTildgASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTATSGLSDVERTqirrtdIGFV 97
Cdd:COG3840 8 TYRYGDFPLR----FDLTIAAGERVAILGPSGAGKSTLLNlIAGFL-PPDSGRILWNGQDLTALPPAERP------VSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 98 YQSHRLLPEFSALENVMLpqmirGL-PK----KETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVL 172
Cdd:COG3840 77 FQENNLFPHLTVAQNIGL-----GLrPGlkltAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 640481818 173 LADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSL-QDGHVI 229
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLvADGRIA 209
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
30-232 |
1.04e-26 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 104.39 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTatsglsDVERT--QIRRTdIGFVYQSHRLLPEF 107
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGY------DVVREprKVRRS-IGIVPQYASVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 108 SALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTAD 187
Cdd:TIGR01188 82 TGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 640481818 188 HVFKALTQLVRAtRVAMLIATHNMDLAARMDRRVSLQD-GHVIELD 232
Cdd:TIGR01188 162 AIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDhGRIIAEG 206
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
28-229 |
1.60e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.93 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLeQADEGEVYVGGTATSGLSDVERTQIRrtdiGFVYQSHRLLPE 106
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLrALSGEL-SPDSGEVRLNGRPLADWSPAELARRR----AVLPQHSSLSFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 FSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVA------NAPRVLLADEPTGN 180
Cdd:PRK13548 91 FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 640481818 181 LDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:PRK13548 171 LDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYaDRIVLLHQGRLV 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
9-232 |
1.94e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.55 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYLHDVRRRYKQGEAtltiLDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEgEVYVGGTATSGLSDV--ER 86
Cdd:PRK14239 4 PILQVSDLSVYYNKKKA----LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNP-EVTITGSIVYNGHNIysPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 87 T---QIRRtDIGFVYQSHRLLPeFSALENVMLPQMIRGLPKK----ETVKRS-KEILAYLGLAERVTHRPAELSGGEQQR 158
Cdd:PRK14239 79 TdtvDLRK-EIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKqvldEAVEKSlKGASIWDEVKDRLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640481818 159 VAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLvrATRVAMLIATHNMDLAARM-DRRVSLQDGHVIELD 232
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRIsDRTGFFLDGDLIEYN 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
15-229 |
2.10e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 103.63 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 15 DVRRRYKQGEAT-LTILDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLL-----------------EQADEGEVY--- 72
Cdd:PRK13651 7 NIVKIFNKKLPTeLKALDNVSVEINQGEFIAIIGQTGSGKTTFIeHLNALLlpdtgtiewifkdeknkKKTKEKEKVlek 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 73 --VGGTATSGLSDVErtQIRRTdIGFVYQ-SHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHR-P 148
Cdd:PRK13651 87 lvIQKTRFKKIKKIK--EIRRR-VGVVFQfAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRsP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 149 AELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRvAMLIATHNMDLA-ARMDRRVSLQDGH 227
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVlEWTKRTIFFKDGK 242
|
..
gi 640481818 228 VI 229
Cdd:PRK13651 243 II 244
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
30-232 |
2.60e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.82 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLEqADEGEVYVGGTATSGlSDVERTQIRRtDIGFVYQshrlLPEFS 108
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIqHLNGLLK-PTSGKIIIDGVDITD-KKVKLSDIRK-KVGLVFQ----YPEYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 109 ALENVMLPQMI-----RGLPKKETVKRSKEILAYLGLA-ERVTHR-PAELSGGEQQRVAIARAVANAPRVLLADEPTGNL 181
Cdd:PRK13637 96 LFEETIEKDIAfgpinLGLSEEEIENRVKRAMNIVGLDyEDYKDKsPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 640481818 182 DPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHVIELD 232
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQ 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
28-223 |
3.31e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 100.63 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQA--DEGEVYVGGTATSGLSdverTQIRRtdIGFVYQSHRLL 104
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALP----AEQRR--IGILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 105 PEFSALENVM--LPqmiRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:COG4136 89 PHLSVGENLAfaLP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 640481818 183 PHTADHvFKALT-QLVRATRVAMLIATHNMDLAARMDRRVSL 223
Cdd:COG4136 166 AALRAQ-FREFVfEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-230 |
3.57e-26 |
|
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: 105.54 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 5 ENGVPVVYLHDVRRRY-------KQGEATLTILDGASLALWEGQSVALVAPSGTGKSTL-LHIAGLLEQadEGEVYVGGT 76
Cdd:COG4172 270 PDAPPLLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLIPS--EGEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 77 ATSGLSDVERTQIRRtDIGFVYQ----ShrLLPEFSALENVMLPQMI--RGLPKKETVKRSKEILAYLGLAERVTHR-PA 149
Cdd:COG4172 348 DLDGLSRRALRPLRR-RMQVVFQdpfgS--LSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPAARHRyPH 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 150 ELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHV 228
Cdd:COG4172 425 EFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALaHRVMVMKDGKV 504
|
..
gi 640481818 229 IE 230
Cdd:COG4172 505 VE 506
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-228 |
9.12e-26 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 98.44 E-value: 9.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEATltILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQAdEGEVYVGGTAtsgLSDVERTQIRR 91
Cdd:cd03246 3 VENVSFRYPGAEPP--VLRNVSFSIEPGESLAIIGPSGSGKSTLARlILGLLRPT-SGRVRLDGAD---ISQWDPNELGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 TdIGFVYQSHRLLPEfSALENVmlpqmirglpkketvkrskeilaylglaervthrpaeLSGGEQQRVAIARAVANAPRV 171
Cdd:cd03246 77 H-VGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 172 LLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARMDRRVSLQDGHV 228
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
10-229 |
1.28e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.97 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVYLHDVRRRYKQGEATLtilDGASLALWEGQSVALVAPSGTGKST-LLHIAGLlEQADEGEVYVGGTATSGlsdvERTQ 88
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKAL---KGLSLSIPEGSKTALLGPNGAGKSTlLLHLNGI-YLPQRGRVKVMGREVNA----ENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 89 IRRTDIGFVYQShrllPE---FSA--LENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIAR 163
Cdd:PRK13647 76 WVRSKVGLVFQD----PDdqvFSStvWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 164 AVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRvAMLIATHNMDLAAR-MDRRVSLQDGHVI 229
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEwADQVIVLKEGRVL 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-229 |
2.20e-25 |
|
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: 99.33 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 3 QGENGVPVVYLHDVRRRYKQGEAtltiLDGASLALWEGQSVALVAPSGTGKSTLLHI-AGLLeQADEGEVYVGGtatsgL 81
Cdd:cd03267 14 SKEPGLIGSLKSLFKRKYREVEA----LKGISFTIEKGEIVGFIGPNGAGKTTTLKIlSGLL-QPTSGEVRVAG-----L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 82 SDVERTQIRRTDIGFVY-QSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLaERVTHRPA-ELSGGEQQRV 159
Cdd:cd03267 84 VPWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDL-EELLDTPVrQLSLGQRMRA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640481818 160 AIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNM-DLAARMDRRVSLQDGHVI 229
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMkDIEALARRVLVIDKGRLL 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-229 |
4.53e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.00 E-value: 4.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGTATSGLSDVERTQirrtDIGFVYQSHRL--L 104
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNaIAGSLP-PDSGSILIDGKDVTKLPEYKRAK----YIGRVFQDPMMgtA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 105 PEFSALENVMLPQM-------IRGLPKKETvKRSKEILAYL--GLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLAD 175
Cdd:COG1101 95 PSMTIEENLALAYRrgkrrglRRGLTKKRR-ELFRELLATLglGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 640481818 176 EPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:COG1101 174 EHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYgNRLIMMHEGRII 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
30-229 |
4.67e-25 |
|
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: 98.05 E-value: 4.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTATSGLSDVErtqIRRtDIGFVYQSHRLLpeFS 108
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKlLAGLY-KPTSGSVLLDGTDIRQLDPAD---LRR-NIGYVPQDVTLF--YG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 109 AL-ENVMLpqmirGLP--KKETVKRSKEILAYL--------GLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEP 177
Cdd:cd03245 93 TLrDNITL-----GAPlaDDERILRAAELAGVTdfvnkhpnGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 640481818 178 TGNLDPHTADHVFKALTQLVRATrvAMLIATHNMDLAARMDRRVSLQDGHVI 229
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
30-231 |
5.52e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 99.70 E-value: 5.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTAT-SGLSDVERTQIRRTDIGFVYQshrlLPEFS 108
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKIKEVKRLRKEIGLVFQ----FPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 109 ALE-----NVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHR-PAELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:PRK13645 103 LFQetiekDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 640481818 183 PHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIEL 231
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIaDEVIVMHEGKVISI 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-230 |
5.94e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 98.84 E-value: 5.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYLHDVRRRYKQGEAtltiLDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEV-YVGGTAT----SGLS 82
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNaLSARL-APDAGEVhYRMRDGQlrdlYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 83 DVERTQIRRTDIGFVYQSHR--LLPEFSALENVMLPQMIRGLPKKETVKRskEILAYLGLAE----RVTHRPAELSGGEQ 156
Cdd:PRK11701 80 EAERRRLLRTEWGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHYGDIRA--TAGDWLERVEidaaRIDDLPTTFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 157 QRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHnmDLA-ARM--DRRVSLQDGHVIE 230
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTH--DLAvARLlaHRLLVMKQGRVVE 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
30-182 |
1.12e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 99.42 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRtDIGFVYQ----ShrLLP 105
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRR-RMQMVFQdpyaS--LNP 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 106 EFSALENVMLPQMIRGL-PKKETVKRSKEILAYLGLAERVTHR-PAELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:COG4608 111 RMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEHADRyPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-212 |
1.31e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.87 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 6 NGVPVVYLHDVRRRYkqgeATLTILDGASLALWEGQSVALVAPSGTGKSTLLHI-AGLLeQADEGEVYVGGtatsglsdv 84
Cdd:COG3845 1 MMPPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKIlYGLY-QPDSGEILIDG--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 85 ERTQIR------RTDIGFVYQSHRLLPEFSALENVML---PQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGE 155
Cdd:COG3845 67 KPVRIRsprdaiALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGE 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 156 QQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMD 212
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLR 202
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-230 |
1.99e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 97.43 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 44 ALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQI--RRTDIGFVYQSHRLLPEFSALENVMLPQMIRG 121
Cdd:PRK14246 40 GIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAikLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 122 LPKKETVKR-SKEILAYLGLAERVTHR---PA-ELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQL 196
Cdd:PRK14246 120 IKEKREIKKiVEECLRKVGLWKEVYDRlnsPAsQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL 199
|
170 180 190
....*....|....*....|....*....|....*
gi 640481818 197 vrATRVAMLIATHNMDLAARMDRRVS-LQDGHVIE 230
Cdd:PRK14246 200 --KNEIAIVIVSHNPQQVARVADYVAfLYNGELVE 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
10-229 |
2.01e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.00 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVYLHDVRRRYKQGEATLtilDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLEQAdEGEVYVGGTATsglsDVERTQ 88
Cdd:PRK13636 5 ILKVEELNYNYSDGTHAL---KGININIKKGEVTAILGGNGAGKSTLFqNLNGILKPS-SGRILFDGKPI----DYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 89 IR--RTDIGFVYQS--HRLlpeFSA--LENVMLPQMIRGLPKKETVKRSKEILAYLGLaERVTHRPAE-LSGGEQQRVAI 161
Cdd:PRK13636 77 LMklRESVGMVFQDpdNQL---FSAsvYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 162 ARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAA-RMDRRVSLQDGHVI 229
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
5-230 |
2.04e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.51 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 5 ENGVPVVYLHDVRRRYkQGEATLTiLDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATS--GLS 82
Cdd:PRK13648 2 EDKNSIIVFKNVSFQY-QSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITddNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 83 DVertqirRTDIGFVYQShrllPEFS------------ALENVMLPQmirglpkKETVKRSKEILAYLGLAERVTHRPAE 150
Cdd:PRK13648 80 KL------RKHIGIVFQN----PDNQfvgsivkydvafGLENHAVPY-------DEMHRRVSEALKQVDMLERADYEPNA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 151 LSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHVIE 230
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYK 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-205 |
2.44e-24 |
|
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: 96.19 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 15 DVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQAD--EGEVYVGGtatsglSDVERTQIRR 91
Cdd:cd03234 8 DVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDaISGRVEGGGttSGQILFNG------QPRKPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 TdIGFVYQSHRLLPEFSALENVMLPQMIRgLPKKETVKRSKEILAYLGLAE----RVTHRPAE-LSGGEQQRVAIARAVA 166
Cdd:cd03234 82 C-VAYVRQDDILLPGLTVRETLTYTAILR-LPRKSSDAIRKKRVEDVLLRDlaltRIGGNLVKgISGGERRRVSIAVQLL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 640481818 167 NAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAML 205
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVIL 198
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
35-229 |
2.48e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.88 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 35 LALWEGQSVALVAPSGTGKSTLL-HIAGLLeQADEGEVYVGGTATSGLSDVERTQIRRTDIGFVYQshrlLPEFSALENV 113
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLqHLNGLL-QPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQ----FPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 114 ML------PQMIrGLPKKETVKRSKEILAYLGLAERVTHR-PAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTA 186
Cdd:PRK13643 102 VLkdvafgPQNF-GIPKEKAEKIAAEKLEMVGLADEFWEKsPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 640481818 187 DHVFKaLTQLVRATRVAMLIATHNM-DLAARMDRRVSLQDGHVI 229
Cdd:PRK13643 181 IEMMQ-LFESIHQSGQTVVLVTHLMdDVADYADYVYLLEKGHII 223
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-231 |
2.69e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.83 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLH----IAGLLEQAD-EGEVYVGGTATSGlSDVERTQIRRtDIGFVYQSHRL 103
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNEEARvEGEVRLFGRNIYS-PDVDPIEVRR-EVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 104 LPEFSALENVMLPQMIRGL--PKKETVKRSKEILAYLGLAERVTHR----PAELSGGEQQRVAIARAVANAPRVLLADEP 177
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRlndyPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 640481818 178 TGNLDPHTADHVFKALTQLvrATRVAMLIATHNMDLAARMDRRVS-LQDGHVIEL 231
Cdd:PRK14267 177 TANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAfLYLGKLIEV 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-230 |
2.85e-24 |
|
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: 96.53 E-value: 2.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 15 DVRRRYKQGeatLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGtatSGLSDVERTQIRRTdI 94
Cdd:cd03253 5 NVTFAYDPG---RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG---QDIREVTLDSLRRA-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 95 GFVYQSHRLLPEfSALENVML-------PQMIRGLPK---KETVKRSKEilaylGLAERVTHRPAELSGGEQQRVAIARA 164
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRYgrpdatdEEVIEAAKAaqiHDKIMRFPD-----GYDTIVGERGLKLSGGEKQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 165 VANAPRVLLADEPTGNLDPHTADHVFKALTQlVRATRVAMLIAtHNMDLAARMDRRVSLQDGHVIE 230
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRD-VSKGRTTIVIA-HRLSTIVNADKIIVLKDGRIVE 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-229 |
4.69e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.98 E-value: 4.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYkQGEAtltILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGlsdveRTQIRRT 92
Cdd:PRK13536 44 LAGVSKSY-GDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-----RARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 DIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVL 172
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 640481818 173 LADEPTGNLDPHTADHVFKALTQLVrATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLcDRLCVLEAGRKI 251
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-230 |
5.86e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.53 E-value: 5.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 27 LTIL--DGASLA------LWEGQSVALVAPSGTGKSTLLH-IAGLLeqADEGEVYVGGTAtsgLSDVERTQIRRTdIGFV 97
Cdd:PRK11174 355 LEILspDGKTLAgplnftLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIE---LRELDPESWRKH-LSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 98 YQShRLLPEFSALENVML--PQM----IRGLPKKETVKrskEILAYL--GLAERVTHRPAELSGGEQQRVAIARAVANAP 169
Cdd:PRK11174 429 GQN-PQLPHGTLRDNVLLgnPDAsdeqLQQALENAWVS---EFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPC 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640481818 170 RVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLiaTHNMDLAARMDRRVSLQDGHVIE 230
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMV--THQLEDLAQWDQIWVMQDGQIVQ 563
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-229 |
6.34e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 96.31 E-value: 6.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 15 DVRRRYKQGEAT--LTILDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLEQAdEGEVYVGGTATSGLSDVerTQIRR 91
Cdd:PRK13633 9 NVSYKYESNEESteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAkHMNALLIPS-EGKVYVDGLDTSDEENL--WDIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 TdIGFVYQShrllPEFSAL-----ENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVA 166
Cdd:PRK13633 86 K-AGMVFQN----PDNQIVativeEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640481818 167 NAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHVI 229
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-230 |
7.33e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 96.32 E-value: 7.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 23 GEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQA-----DEGEVYVGGTATSGLSDVerTQIRRTdIGFV 97
Cdd:PRK14271 30 GFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDV--LEFRRR-VGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 98 YQSHRLLPeFSALENVMLPQMIRGL-PKKETVKRSKEILAYLGL----AERVTHRPAELSGGEQQRVAIARAVANAPRVL 172
Cdd:PRK14271 107 FQRPNPFP-MSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 173 LADEPTGNLDPHTADHVFKALTQLvrATRVAMLIATHNMDLAARMDRRVSL-QDGHVIE 230
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALfFDGRLVE 242
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-231 |
7.47e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 97.08 E-value: 7.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 22 QGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGTATSGLSDVERTQIRRtDIGFVYQS 100
Cdd:PRK15079 29 QPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARaIIGLVK-ATDGEVAWLGKDLLGMKDDEWRAVRS-DIQMIFQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 101 hrllPEFSalenvMLPQMIRG-------------LPKKETVKRSKEILAYLGLAERVTHR-PAELSGGEQQRVAIARAVA 166
Cdd:PRK15079 107 ----PLAS-----LNPRMTIGeiiaeplrtyhpkLSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640481818 167 NAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHnmDLAARM---DRRVSLQDGHVIEL 231
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAH--DLAVVKhisDRVLVMYLGHAVEL 243
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-229 |
8.26e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.80 E-value: 8.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 8 VPVVYLHDVRRRYkqGEATltILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGlsdveRT 87
Cdd:PRK13537 5 VAPIDFRNVEKRY--GDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-----RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 88 QIRRTDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVAN 167
Cdd:PRK13537 76 RHARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640481818 168 APRVLLADEPTGNLDPHTADHVFKALTQLVRATRvAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLcDRLCVIEEGRKI 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-230 |
1.34e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.54 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 22 QGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQAdEGEVYVGGTATSGlsdvERTQIRRTDIGFVYQS 100
Cdd:PRK13642 15 EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARlIDGLFEEF-EGKVKIDGELLTA----ENVWNLRRKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 101 -HRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTG 179
Cdd:PRK13642 90 pDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 640481818 180 NLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHVIE 230
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIK 220
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
15-230 |
1.41e-23 |
|
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: 93.82 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 15 DVRRRYKQGEAtltiLDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTqirrtdI 94
Cdd:cd03268 5 DLTKTYGKKRV----LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR------I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 95 GFVYQSHRLLPEFSALENVMLPQMIRGLPKKetvkRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLA 174
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640481818 175 DEPTGNLDPhtaDHVfKALTQLVRATR---VAMLIATH---NMDLAArmDRRVSLQDGHVIE 230
Cdd:cd03268 151 DEPTNGLDP---DGI-KELRELILSLRdqgITVLISSHllsEIQKVA--DRIGIINKGKLIE 206
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-209 |
1.75e-23 |
|
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: 93.38 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 21 KQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHI-AGLLE-QADEGEVYVGGTatsglsDVERTQIRRTdIGFVY 98
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNAlAGRRTgLGVSGEVLINGR------PLDKRSFRKI-IGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 99 QSHRLLPEFSALENVMLPQMIRGLpkketvkrskeilaylglaervthrpaelSGGEQQRVAIARAVANAPRVLLADEPT 178
Cdd:cd03213 89 QDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190
....*....|....*....|....*....|.
gi 640481818 179 GNLDPHTADHVFKALTQLVRATRVAMLIaTH 209
Cdd:cd03213 140 SGLDSSSALQVMSLLRRLADTGRTIICS-IH 169
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
28-232 |
2.02e-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: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLHI-AGLLEqADEGEVYVGGTATsglsdvertqirrtdIGFVYQSHRLLPE 106
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKIlAGELE-PDSGEVSIPKGLR---------------IGYLPQEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 FSALENVM-----LPQMIRGLPKKETVK---------------------------RSKEILAYLGLAERVTHRP-AELSG 153
Cdd:COG0488 76 LTVLDTVLdgdaeLRALEAELEELEAKLaepdedlerlaelqeefealggweaeaRAEEILSGLGFPEEDLDRPvSELSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 154 GEQQRVAIARAVANAPRVLLADEPTGNLDPHTADhvfkALTQLVRATRVAMLIATHnmdlaarmDR----RVSlqdGHVI 229
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLESIE----WLEEFLKNYPGTVLVVSH--------DRyfldRVA---TRIL 220
|
...
gi 640481818 230 ELD 232
Cdd:COG0488 221 ELD 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
11-230 |
2.36e-23 |
|
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: 94.14 E-value: 2.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 11 VYLHDVRRRYKQgEATLTILDGASLALWEGQSVALVAPSGTGKSTllhIAGLLEQ---ADEGEVYVGGtatsglSDVERT 87
Cdd:cd03249 1 IEFKNVSFRYPS-RPDVPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERfydPTSGEILLDG------VDIRDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 88 QIR--RTDIGFVYQSHRLLpEFSALENVMLpqmirGLPK---KETVKRSKEILAYL-------GLAERVTHRPAELSGGE 155
Cdd:cd03249 71 NLRwlRSQIGLVSQEPVLF-DGTIAENIRY-----GKPDatdEEVEEAAKKANIHDfimslpdGYDTLVGERGSQLSGGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640481818 156 QQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRAtRVAMLIAtHNMDLAARMDRRVSLQDGHVIE 230
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKG-RTTIVIA-HRLSTIRNADLIAVLQNGQVVE 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
10-228 |
2.64e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.80 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVYLHDVRRRYKQGEATLTiLDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGTAtsgLSDVERTQ 88
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRlIDGLLE-AESGQIIIDGDL---LTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 89 IRRTdIGFVYQShrllPEFS------------ALENvmlpqmiRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQ 156
Cdd:PRK13650 79 IRHK-IGMVFQN----PDNQfvgatveddvafGLEN-------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640481818 157 QRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHV 228
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-217 |
3.34e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 94.33 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 26 TLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQAdEGEVYVGGTATS-GLSDVER----TQIRRtDIGFVYQS 100
Cdd:PRK14258 19 TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRVEFfNQNIYERrvnlNRLRR-QVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 101 HRLLPeFSALENVMLPQMIRGL-PKKETVKRSKEILAYLGLAERVTHR----PAELSGGEQQRVAIARAVANAPRVLLAD 175
Cdd:PRK14258 97 PNLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKHKihksALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 640481818 176 EPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM 217
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRL 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
11-230 |
1.00e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 93.31 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 11 VYLHDVRRRYKQG-----EAtltiLDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLEQADeGEVYVGG-TATSGLSD 83
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyehQA----IHDVNTEFEQGKYYAIVGQTGSGKSTLIqNINALLKPTT-GTVTVDDiTITHKTKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 84 VERTQIRRTdIGFVYQshrlLPEFSALENVMLPQMIRGlPKK-----ETVK-RSKEILAYLGLAERV-THRPAELSGGEQ 156
Cdd:PRK13646 78 KYIRPVRKR-IGMVFQ----FPESQLFEDTVEREIIFG-PKNfkmnlDEVKnYAHRLLMDLGFSRDVmSQSPFQMSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640481818 157 QRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNM-DLAARMDRRVSLQDGHVIE 230
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMnEVARYADEVIVMKEGSIVS 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-230 |
1.06e-22 |
|
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: 95.64 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 5 ENGVPVVYLHDVRRRYKQGE-ATLTILDGASLALWEGQSVALVAPSGTGKSTLLHI-AGLLEQAdEGEVYVG-GTATSGL 81
Cdd:TIGR03269 274 EVGEPIIKVRNVSKRYISVDrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIiAGVLEPT-SGEVNVRvGDEWVDM 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 82 SD---VERTQIRRTdIGFVYQSHRLLPEFSALENvmLPQMIR-GLPKKETVKRSKEILAYLGL----AERVTHR-PAELS 152
Cdd:TIGR03269 353 TKpgpDGRGRAKRY-IGILHQEYDLYPHRTVLDN--LTEAIGlELPDELARMKAVITLKMVGFdeekAEEILDKyPDELS 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 153 GGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSL-QDGHVIE 230
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALmRDGKIVK 508
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
28-228 |
1.93e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.14 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTATSGLSdvERTQIRRtdIGFVYQSHRLLPE 106
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRaINGTL-TPTAGTVLVAGDDVEALS--ARAASRR--VASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 FSALENVML---PQMIRGLPKKETVKRS-KEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:PRK09536 92 FDVRQVVEMgrtPHRSRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 640481818 183 PHTADHVFKALTQLVRATRVAmLIATHNMDLAARM-DRRVSLQDGHV 228
Cdd:PRK09536 172 INHQVRTLELVRRLVDDGKTA-VAAIHDLDLAARYcDELVLLADGRV 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
20-229 |
2.23e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 91.98 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 20 YKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHI-AGLLeQADEGEVYVGGTAtsgLSDVERTQIRrTDIGFVY 98
Cdd:PRK13632 15 FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKIlTGLL-KPQSGEIKIDGIT---ISKENLKEIR-KKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 99 QShrllPE-------------FSaLENVMLPqmirglPKKetvkrSKEILAYL----GLAERVTHRPAELSGGEQQRVAI 161
Cdd:PRK13632 90 QN----PDnqfigatveddiaFG-LENKKVP------PKK-----MKDIIDDLakkvGMEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 162 ARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIA-THNMDLAARMDRRVSLQDGHVI 229
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDL-RKTRKKTLISiTHDMDEAILADKVIVFSEGKLI 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
30-216 |
3.83e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.38 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLH----IAGLLEQAD-EGEVYVGGTATSGlSDVERTQIRRTdIGFVYQSHRLL 104
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrLNDLIPGFRvEGKVTFHGKNLYA-PDVDPVEVRRR-IGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 105 PEfSALENVMLPQMIRGLPKK--ETVKRS----------KEILAYLGLAervthrpaeLSGGEQQRVAIARAVANAPRVL 172
Cdd:PRK14243 104 PK-SIYDNIAYGARINGYKGDmdELVERSlrqaalwdevKDKLKQSGLS---------LSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 640481818 173 LADEPTGNLDPHTADHVFKALTQLVRatRVAMLIATHNMDLAAR 216
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAAR 215
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-196 |
4.18e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.34 E-value: 4.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 26 TLTILDGASLALWEGQSVALVAPSGTGKSTLLHIaglLEQADEGEVYVGGTATSGLSDVERTQIRRTDiGFVYQSHRLLP 105
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNA---LAFRSPKGVKGSGSVLLNGMPIDAKEMRAIS-AYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 106 EFSALENVMLPQMIR---GLPKKETVKRSKEILAYLGL---AERVTHRPAE---LSGGEQQRVAIARAVANAPRVLLADE 176
Cdd:TIGR00955 113 TLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLrkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180
....*....|....*....|
gi 640481818 177 PTGNLDPHTADHVFKALTQL 196
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGL 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
7-182 |
6.28e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 91.95 E-value: 6.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 7 GVPVVYLHDVRRRY--KQG----EATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSG 80
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvKRGlfkpERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 81 LSDVERTQiRRTDIGFVYQS--HRLLPEF---SALENvmlPQMIR-GLPKKETVKRSKEILAYLGL-AERVTHRPAELSG 153
Cdd:PRK11308 82 ADPEAQKL-LRQKIQIVFQNpyGSLNPRKkvgQILEE---PLLINtSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSG 157
|
170 180
....*....|....*....|....*....
gi 640481818 154 GEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
28-230 |
6.88e-22 |
|
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: 89.89 E-value: 6.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQADeGEVYVGGTATSGLSDVERTqirRTDIGFVYQSHRLLPE 106
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKtLMGLLPVKS-GSIRLDGEDITKLPPHERA---RAGIAYVPQGREIFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 FSALENVMLpqMIRGLPKKETvKRSKEILAYLGLAERVTHRPA-ELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHT 185
Cdd:TIGR03410 90 LTVEENLLT--GLAALPRRSR-KIPDEIYELFPVLKEMLGRRGgDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 640481818 186 ADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:TIGR03410 167 IKDIGRVIRRLRAEGGMAILLVEQYLDFARELaDRYYVMERGRVVA 212
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
30-229 |
8.19e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.96 E-value: 8.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTA-TSGLSDVERTQIRRTdIGFVYQshrlLPEFS 108
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTSKNKDIKQIRKK-VGLVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 109 ALENVML------PQMIrGLPKKETVKRSKEILAYLGLAERVTHR-PAELSGGEQQRVAIARAVANAPRVLLADEPTGNL 181
Cdd:PRK13649 98 LFEETVLkdvafgPQNF-GVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 640481818 182 DPHTADHVFKALTQLVRATRVAMLIaTHNM-DLAARMDRRVSLQDGHVI 229
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLV-THLMdDVANYADFVYVLEKGKLV 224
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
9-230 |
1.38e-21 |
|
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: 89.50 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYLHDVRRRYKQGEATLTIldgaSLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYV-----GGTATSGLS 82
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRDV----SFDLYPGEVLGIVGESGSGKSTLLGcLAGRL-APDHGTATYimrsgAELELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 83 DVERTQIRRTDIGFVYQSHR--LLPEFSALENVMLPQMIRGLPKKETVKRSKEilAYLGLAE----RVTHRPAELSGGEQ 156
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPRdgLRMRVSAGANIGERLMAIGARHYGNIRATAQ--DWLEEVEidptRIDDLPRAFSGGMQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640481818 157 QRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:TIGR02323 155 QRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLaQRLLVMQQGRVVE 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-232 |
1.52e-21 |
|
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: 88.74 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEA-TLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLsdvertqirr 91
Cdd:cd03220 20 LKKLGILGRKGEVgEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 tDIGfvyqsHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRV 171
Cdd:cd03220 90 -GLG-----GGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640481818 172 LLADEPTGNLDPHTADHVFKALTQLVRATRvAMLIATHNMDLAARM-DRRVSLQDGHVIELD 232
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
34-231 |
1.54e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 92.61 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 34 SLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRtDIGFVYQS--HRLLPEFSALE 111
Cdd:PRK10261 344 SFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQDpyASLDPRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 112 NVMLPQMIRGL-PKKETVKRSKEILAYLGL-AERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHV 189
Cdd:PRK10261 423 SIMEPLRVHGLlPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 640481818 190 FKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQD-GHVIEL 231
Cdd:PRK10261 503 INLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYlGQIVEI 545
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
34-228 |
2.30e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.49 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 34 SLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGtatsglSDVERTQIRRTDIGFVYQSHRLLPEFSALEN 112
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNlIAGFL-TPASGSLTLNG------QDHTTTPPSRRPVSMLFQENNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 113 VML---PQMIRGLPKKETVKrskEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHV 189
Cdd:PRK10771 92 IGLglnPGLKLNAAQREKLH---AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 640481818 190 FKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHV 228
Cdd:PRK10771 169 LTLVSQVCQERQLTLLMVSHSLEDAARIaPRSLVVADGRI 208
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-230 |
3.35e-21 |
|
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: 88.31 E-value: 3.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 11 VYLHDVRRRYKQGEATltILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGtatSGLSDVERTQIR 90
Cdd:cd03252 1 ITFEHVRFRYKPDGPV--ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG---HDLALADPAWLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 91 RtDIGFVYQSHRLLPEfSALENVMLPQmiRGLPKKETVKRSKEILAY-------LGLAERVTHRPAELSGGEQQRVAIAR 163
Cdd:cd03252 76 R-QVGVVLQENVLFNR-SIRDNIALAD--PGMSMERVIEAAKLAGAHdfiselpEGYDTIVGEQGAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 164 AVANAPRVLLADEPTGNLDpHTADHVFKALTQLVRATRVAMLIAtHNMDLAARMDRRVSLQDGHVIE 230
Cdd:cd03252 152 ALIHNPRILIFDEATSALD-YESEHAIMRNMHDICAGRTVIIIA-HRLSTVKNADRIIVMEKGRIVE 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
29-230 |
4.80e-21 |
|
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: 91.34 E-value: 4.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTAtsgLSDVERTQIRRTdIGFVYQSHRLLpEFS 108
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS---LKDIDRHTLRQF-INYLPQEPYIF-SGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 109 ALENVMLpQMIRGLPKKEtVKRSKEILAY--------LGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGN 180
Cdd:TIGR01193 564 ILENLLL-GAKENVSQDE-IWAACEIAEIkddienmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSN 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 640481818 181 LDPHTADHVFKALTQLVRATrvaMLIATHNMDLAARMDRRVSLQDGHVIE 230
Cdd:TIGR01193 642 LDTITEKKIVNNLLNLQDKT---IIFVAHRLSVAKQSDKIIVLDHGKIIE 688
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-232 |
5.77e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 5.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 7 GVPVVYLHDVRRRYkqGEatLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGTatsglsdve 85
Cdd:COG0488 312 GKKVLELEGLSKSY--GD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKlLAGELE-PDSGTVKLGET--------- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 86 rtqirrTDIGFVYQSHRLL-PEFSALENVMlpqmiRGLPKKetvkRSKEILAYLGL----AERVTHRPAELSGGEQQRVA 160
Cdd:COG0488 378 ------VKIGYFDQHQEELdPDKTVLDELR-----DGAPGG----TEQEVRGYLGRflfsGDDAFKPVGVLSGGEKARLA 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640481818 161 IARAVANAPRVLLADEPTGNLDPHTADhvfkALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIELD 232
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLDIETLE----ALEEALDDFPGTVLLVSHDRYFLDRVaTRILEFEDGGVREYP 511
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
29-230 |
7.28e-21 |
|
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: 87.28 E-value: 7.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTAtsgLSDVERTQIRRTdIGFVYQSHRLLPEfS 108
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGID---IRDISRKSLRSM-IGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 109 ALENVMLPqmiRGLPKKETVKRSKEILAYL--------GLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGN 180
Cdd:cd03254 93 IMENIRLG---RPNATDEEVIEAAKEAGAHdfimklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 640481818 181 LDPHTADHVFKALtQLVRATRVAMLIAtHNMDLAARMDRRVSLQDGHVIE 230
Cdd:cd03254 170 IDTETEKLIQEAL-EKLMKGRTSIIIA-HRLSTIKNADKILVLDDGKIIE 217
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-230 |
1.64e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.67 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 14 HDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLEqADEGEVYVGGTATS--GLSdvertqir 90
Cdd:COG1134 26 ELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLkLIAGILE-PTSGRVEVNGRVSAllELG-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 91 rtdIGFVyqshrllPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLaERVTHRPAE-LSGGEQQRVAIARAVANAP 169
Cdd:COG1134 97 ---AGFH-------PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAEL-GDFIDQPVKtYSSGMRARLAFAVATAVDP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 170 RVLLADEPTGnldphTADHVF--KALTQL--VRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:COG1134 166 DILLVDEVLA-----VGDAAFqkKCLARIreLRESGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVM 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-210 |
1.83e-20 |
|
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: 89.34 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 7 GVPVVYLHDVRRRYKQGEAtltILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGTAtsgLSDVE 85
Cdd:TIGR02868 331 GKPTLELRDLSAGYPGAPP---VLDGVSLDLPPGERVAILGPSGSGKSTLLAtLAGLLD-PLQGEVTLDGVP---VSSLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 86 RTQIRRTdIGFVYQSHRLL------------PEFS------ALENVMLPQMIRGLPKketvkrskeilaylGLAERVTHR 147
Cdd:TIGR02868 404 QDEVRRR-VSVCAQDAHLFdttvrenlrlarPDATdeelwaALERVGLADWLRALPD--------------GLDTVLGEG 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640481818 148 PAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVamLIATHN 210
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTV--VLITHH 529
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
15-230 |
1.93e-20 |
|
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: 86.17 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 15 DVRRRYKQGeatlTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTATSGLSDVERTqirRTD 93
Cdd:TIGR04406 6 NLIKSYKKR----KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYmIVGLV-RPDAGKILIDGQDITHLPMHERA---RLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 94 IGFVYQSHRLLPEFSALENVMLPQMIRG-LPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVL 172
Cdd:TIGR04406 78 IGYLPQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 173 LADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNM-DLAARMDRRVSLQDGHVIE 230
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVrETLDICDRAYIISDGKVLA 215
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
49-229 |
3.42e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 87.24 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 49 SGTGKSTLLHIAGLLEQADEGEVYVGGTAtsgLSDVER-----TQIRRtdIGFVYQSHRLLPEFSALENVMLpqmirGLP 123
Cdd:PRK11144 33 SGAGKTSLINAISGLTRPQKGRIVLNGRV---LFDAEKgiclpPEKRR--IGYVFQDARLFPHYKVRGNLRY-----GMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 124 KKETVKRSKeILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVA 203
Cdd:PRK11144 103 KSMVAQFDK-IVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIP 181
|
170 180
....*....|....*....|....*..
gi 640481818 204 MLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:PRK11144 182 ILYVSHSLDEILRLaDRVVVLEQGKVK 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
28-223 |
3.68e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.21 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQAdEGEVYVGGTATSGLSdVERTQIRRTdigfvyqshrlLPe 106
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKvLAGVLRPT-SGTVRRAGGARVAYV-PQRSEVPDS-----------LP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 FSALENVML----PQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:NF040873 72 LTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 640481818 183 PHTADHVFKALTQLvRATRVAMLIATHNMDLAARMDRRVSL 223
Cdd:NF040873 152 AESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
29-232 |
4.40e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.01 E-value: 4.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLL--EQADEGEVYVGGTATSG--LSDVertqirRTDIGFVYQShrl 103
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKlINGLLlpDDNPNSKITVDGITLTAktVWDI------REKVGIVFQN--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 104 lPEFS------------ALENvmlpqmiRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRV 171
Cdd:PRK13640 93 -PDNQfvgatvgddvafGLEN-------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640481818 172 LLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHVIELD 232
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-230 |
4.42e-20 |
|
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: 85.36 E-value: 4.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 11 VYLHDVRRRYkqGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTAtsgLSDVERTQIR 90
Cdd:cd03251 1 VEFKNVTFRY--PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD---VRDYTLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 91 RtDIGFVYQSHRLLPEfSALENVMLPQmiRGLPKKETVKRSKEILAY-------LGLAERVTHRPAELSGGEQQRVAIAR 163
Cdd:cd03251 76 R-QIGLVSQDVFLFND-TVAENIAYGR--PGATREEVEEAARAANAHefimelpEGYDTVIGERGVKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 164 AVANAPRVLLADEPTGNLDPHTADHVFKALTQLVrATRVAMLIAtHNMDLAARMDRRVSLQDGHVIE 230
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIA-HRLSTIENADRIVVLEDGKIVE 216
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
10-229 |
7.02e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.42 E-value: 7.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVYLHDVRRRYKQGEATLTILDgasLALWEGQSVALVAPSGTGKSTL-LHIAGLLeQADEGEVYVGGTATSglsDVERTQ 88
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENIN---LVIKKGEYIGIIGKNGSGKSTLaLHLNGLL-RPQKGKVLVSGIDTG---DFSKLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 89 IRRTDIGFVYQShrllPEFSALENVMLPQMIRG-----LPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIAR 163
Cdd:PRK13644 74 GIRKLVGIVFQN----PETQFVGRTVEEDLAFGpenlcLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 164 AVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIaTHNMDLAARMDRRVSLQDGHVI 229
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYI-THNLEELHDADRIIVMDRGKIV 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
14-183 |
7.13e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 84.70 E-value: 7.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 14 HDVRRRYKQgeatLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTATSGLSDVERTqirRT 92
Cdd:COG1137 7 ENLVKSYGK----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYmIVGLV-KPDSGRIFLDGEDITHLPMHKRA---RL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 DIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLaERVTHRPA-ELSGGEQQRVAIARAVANAPRV 171
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGI-THLRKSKAySLSGGERRRVEIARALATNPKF 157
|
170
....*....|..
gi 640481818 172 LLADEPTGNLDP 183
Cdd:COG1137 158 ILLDEPFAGVDP 169
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
30-217 |
7.45e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.62 E-value: 7.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLeQADEGEVYVGGTAtsgLSDVERTQIRRTdIGFVYQShrllPE-- 106
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFrHFNGIL-KPTSGSVLIRGEP---ITKENIREVRKF-VGLVFQN----PDdq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 -FSAL--ENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDP 183
Cdd:PRK13652 91 iFSPTveQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190
....*....|....*....|....*....|....
gi 640481818 184 HTADHVFKALTQLVRATRVAMLIATHNMDLAARM 217
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEM 204
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
28-213 |
7.80e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.24 E-value: 7.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLEqadegevyvgGTATSGLSDVERTQIRRtdigfvyqshrllpE 106
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLrLLAGALK----------GTPVAGCVDVPDNQFGR--------------E 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 FSALENVmlpqmirglPKKETVKRSKEILAYLGLAERVTHR--PAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPH 184
Cdd:COG2401 100 ASLIDAI---------GRKGDFKDAVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*....
gi 640481818 185 TADHVFKALTQLVRATRVAMLIATHNMDL 213
Cdd:COG2401 171 TAKRVARNLQKLARRAGITLVVATHHYDV 199
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-230 |
8.08e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 83.13 E-value: 8.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKqgEATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTATSGLSDVERTQIrr 91
Cdd:cd03247 3 INNVSFSYP--EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQlLTGDL-KPQQGEITLDGVPVSDLEKALSSLI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 tdiGFVYQSHRLlpeFSAlenvmlpqmirglpkketvkrskEILAYLGlaervthrpAELSGGEQQRVAIARA-VANAPR 170
Cdd:cd03247 78 ---SVLNQRPYL---FDT-----------------------TLRNNLG---------RRFSGGERQRLALARIlLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 171 VLLaDEPTGNLDPHTADHVFKALTQLVRATRVAMLiaTHNMDLAARMDRRVSLQDGHVIE 230
Cdd:cd03247 120 VLL-DEPTVGLDPITERQLLSLIFEVLKDKTLIWI--THHLTGIEHMDKILFLENGKIIM 176
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
27-213 |
1.80e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.89 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 27 LTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSD--VERTQIRRTdigfvYQSHRLL 104
Cdd:PRK11300 18 LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqIARMGVVRT-----FQHVRLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 105 PEFSALENVMLPQ-------MIRGLPK--------KETVKRSKEILAYLGLAErVTHRPA-ELSGGEQQRVAIARAVANA 168
Cdd:PRK11300 93 REMTVIENLLVAQhqqlktgLFSGLLKtpafrraeSEALDRAATWLERVGLLE-HANRQAgNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 640481818 169 PRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDL 213
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL 216
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
27-212 |
3.91e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.13 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 27 LTILDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLEQAdEGEVYVGGTATSGLSDVERT-------------QIRRT 92
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVtHFNGLIKSK-YGTIQVGDIYIGDKKNNHELitnpyskkiknfkELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 dIGFVYQshrlLPEFSALE-----NVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHR-PAELSGGEQQRVAIARAVA 166
Cdd:PRK13631 118 -VSMVFQ----FPEYQLFKdtiekDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERsPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 640481818 167 NAPRVLLADEPTGNLDPhTADHVFKALTQLVRATRVAMLIATHNMD 212
Cdd:PRK13631 193 IQPEILIFDEPTAGLDP-KGEHEMMQLILDAKANNKTVFVITHTME 237
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
9-229 |
4.49e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.62 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYLHDVRRRYKQGEAtltiLDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTAtsgLSDVERTQ 88
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQA----LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD---ITDWQTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 89 IRRTDIGFVYQSHRLLPEFSALENVMLPQMIRGLPK-KETVKRSKEILAYLglAERVTHRPAELSGGEQQRVAIARAVAN 167
Cdd:PRK11614 77 IMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQfQERIKWVYELFPRL--HERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640481818 168 APRVLLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLaDRGYVLENGHVV 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-228 |
6.14e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.72 E-value: 6.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 2 EQGENGVPVVYLHDVRRRYkqgeATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGL 81
Cdd:PRK15439 3 TSDTTAPPLLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 82 SDVERTQIrrtDIGFVYQSHRLLPEFSALENVMLpqmirGLPKKE-TVKRSKEILAYLGLAERVTHRPAELSGGEQQRVA 160
Cdd:PRK15439 79 TPAKAHQL---GIYLVPQEPLLFPNLSVKENILF-----GLPKRQaSMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 161 IARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARMDRRVS-LQDGHV 228
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISvMRDGTI 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
30-230 |
8.14e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.58 E-value: 8.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQirrTDIGFVYQSHRLLPEFSA 109
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA---AGVAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 110 LENVMLPQmirgLP-------KKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:PRK11288 97 AENLYLGQ----LPhkggivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 640481818 183 PHTADHVFKALTQLvRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:PRK11288 173 AREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALcDAITVFKDGRYVA 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-230 |
1.12e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.11 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYKQGEatLTILDGASLALWEGQSVALVAPSGTGKSTLLHiagLLE---QADEGEVYVGGTAtsgLSDVERTQI 89
Cdd:PRK11160 341 LNNVSFTYPDQP--QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ---LLTrawDPQQGEILLNGQP---IADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 RRTdIGFVYQSHRLlpeFSAL--ENVMLPQmirglpKKETVKRSKEILAYLGLAERVTH------------RPaeLSGGE 155
Cdd:PRK11160 413 RQA-ISVVSQRVHL---FSATlrDNLLLAA------PNASDEALIEVLQQVGLEKLLEDdkglnawlgeggRQ--LSGGE 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 156 QQRVAIARA-VANAPRVLLaDEPTGNLDPHTADHVFKALTQLvrATRVAMLIATHNMDLAARMDRRVSLQDGHVIE 230
Cdd:PRK11160 481 QRRLGIARAlLHDAPLLLL-DEPTEGLDAETERQILELLAEH--AQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
13-229 |
1.38e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 81.28 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRRRYkqgeATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTatsglsDVERTQIR-- 90
Cdd:COG4604 4 IKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGL------DVATTPSRel 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 91 -------RTDIGFVyqsHRL----LPEF-----SalenvmlpqmiRGLPKKETVKRSKEILAYLGLAErVTHRPA-ELSG 153
Cdd:COG4604 74 akrlailRQENHIN---SRLtvreLVAFgrfpyS-----------KGRLTAEDREIIDEAIAYLDLED-LADRYLdELSG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 154 GEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYaDHIVAMKDGRVV 215
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
29-228 |
2.90e-18 |
|
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: 82.87 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTAtsgLSDVERTQIRRTdIGFVYQSHRLLPEF 107
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARlLVGVW-PPTAGSVRLDGAD---LSQWDREELGRH-IGYLPQDVELFDGT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 108 SAlENV-MLPQ-----------------MIRGLPKketvkrskeilaylGLAERVTHRPAELSGGEQQRVAIARAVANAP 169
Cdd:COG4618 422 IA-ENIaRFGDadpekvvaaaklagvheMILRLPD--------------GYDTRIGEGGARLSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 170 RVLLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARMDRRVSLQDGHV 228
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-230 |
5.06e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.06 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 20 YKQGEATLTILDGASLALWEGQSVALVAPSGTGKS-TLLHIAGLLEQADEgeVYVGG----TATSGLSDVERT--QIRRT 92
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPV--VYPSGdirfHGESLLHASEQTlrGVRGN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 DIGFVYQS--------HRL---LPEFSALENVMLPQMIRGlpkketvkrskEILAYL---GL---AERVTHRPAELSGGE 155
Cdd:PRK15134 93 KIAMIFQEpmvslnplHTLekqLYEVLSLHRGMRREAARG-----------EILNCLdrvGIrqaAKRLTDYPHQLSGGE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 156 QQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVS-LQDGHVIE 230
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAvMQNGRCVE 237
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
28-210 |
6.11e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 6.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGTAtSGLSDVeRTQIrrtdigfVYQSHR--LL 104
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRlIAGLLP-PAAGTIKLDGGD-IDDPDV-AEAC-------HYLGHRnaMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 105 PEFSALENVMLPQMIRGLPKKETVkrskEILAYLGLAeRVTHRPA-ELSGGEQQRVAIAR-AVANAPrVLLADEPTGNLD 182
Cdd:PRK13539 86 PALTVAENLEFWAAFLGGEELDIA----AALEAVGLA-PLAHLPFgYLSAGQKRRVALARlLVSNRP-IWILDEPTAALD 159
|
170 180
....*....|....*....|....*...
gi 640481818 183 PHtADHVFKALTQLVRATRVAMLIATHN 210
Cdd:PRK13539 160 AA-AVALFAELIRAHLAQGGIVIAATHI 186
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
29-211 |
6.62e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.19 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRTdIGFVYQSHRLLPEFS 108
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 109 ALENVMLPqmIR---GLPK---KETVKRSKEILAYLGLAERVthrPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:PRK11831 101 VFDNVAYP--LRehtQLPApllHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180
....*....|....*....|....*....
gi 640481818 183 PHTADHVFKALTQLVRATRVAMLIATHNM 211
Cdd:PRK11831 176 PITMGVLVKLISELNSALGVTCVVVSHDV 204
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
14-183 |
8.08e-18 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 78.98 E-value: 8.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 14 HDVRRRYKQGeatlTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQaDEGEVYVGGtatsglSDVERTQIRrt 92
Cdd:TIGR03740 4 KNLSKRFGKQ----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKmITGILRP-TSGEIIFDG------HPWTRKDLH-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 DIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKetvkRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVL 172
Cdd:TIGR03740 71 KIGSLIESPPLYENLTARENLKVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLL 146
|
170
....*....|.
gi 640481818 173 LADEPTGNLDP 183
Cdd:TIGR03740 147 ILDEPTNGLDP 157
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
29-223 |
8.69e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 80.33 E-value: 8.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQ-----ADEgeVYVGGTATSGLSDVERTQIRRTDIGFVYQ--S 100
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKDnwhvtADR--FRWNGIDLLKLSPRERRKIIGREIAMIFQepS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 101 HRLLPEfsalENVMlPQMIRGLP-----------KKETVKRSKEILAYLGLAErvtHR------PAELSGGEQQRVAIAR 163
Cdd:COG4170 100 SCLDPS----AKIG-DQLIEAIPswtfkgkwwqrFKWRKKRAIELLHRVGIKD---HKdimnsyPHELTEGECQKVMIAM 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 164 AVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSL 223
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITV 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-215 |
1.34e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 80.15 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 1 MEQGENGVPVVYLHDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKS-TLLHIAGLLeqADEGEVyvGGTATS 79
Cdd:PRK09473 3 PLAQQQADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLL--AANGRI--GGSATF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 80 ------GLSDVERTQIRRTDIGFVYQS--HRLLPEFSALENVMLPQMI-RGLPKKETVKRSKEILAYLGLAE---RVTHR 147
Cdd:PRK09473 79 ngreilNLPEKELNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEarkRMKMY 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640481818 148 PAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAA 215
Cdd:PRK09473 159 PHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVA 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
28-230 |
4.91e-17 |
|
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: 79.48 E-value: 4.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTllhIAGLLEQ---ADEGEVYVGGTAtsgLSDVERTQIRRtDIGFVYQSHRLL 104
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKST---LARLLFRfydVTSGRILIDGQD---IRDVTQASLRA-AIGIVPQDTVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 105 ------------PEFS------ALENVMLPQMIRGLPKketvkrskeilaylGLAERVTHRPAELSGGEQQRVAIARAVA 166
Cdd:COG5265 445 ndtiayniaygrPDASeeeveaAARAAQIHDFIESLPD--------------GYDTRVGERGLKLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640481818 167 NAPRVLLADEPTGNLDPHTADHVFKALTQlVRATRVAMLIAtHNMDLAARMDRRVSLQDGHVIE 230
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALRE-VARGRTTLVIA-HRLSTIVDADEILVLEAGRIVE 572
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
28-229 |
5.98e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.98 E-value: 5.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQADeGEVYVGGTATSGLSDverTQIRRTdIGFVYQSHrLLPE 106
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKcFARLLTPQS-GTVFLGDKPISMLSS---RQLARR-LALLPQHH-LTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 FSALENVM-------LPQMIRGLPK-KETVKRSKEILAYLGLAERvthRPAELSGGEQQRVAIARAVA-NAPRVLLaDEP 177
Cdd:PRK11231 90 GITVRELVaygrspwLSLWGRLSAEdNARVNQAMEQTRINHLADR---RLTDLSGGQRQRAFLAMVLAqDTPVVLL-DEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 178 TGNLD-PHTADhVFKALTQLVRA--TRVAMLiatHNMDLAARM-DRRVSLQDGHVI 229
Cdd:PRK11231 166 TTYLDiNHQVE-LMRLMRELNTQgkTVVTVL---HDLNQASRYcDHLVVLANGHVM 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-228 |
7.29e-17 |
|
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: 76.36 E-value: 7.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVYLHDVRRRYKQGEATLtILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTAtsgLSDVERTQI 89
Cdd:cd03248 11 IVKFQNVTFAYPTRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKP---ISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 RRTdIGFVYQSHRLLPEfSALENVMLpqmirGLPKKETVKRSKEILAY----------LGLAERVTHRPAELSGGEQQRV 159
Cdd:cd03248 87 HSK-VSLVGQEPVLFAR-SLQDNIAY-----GLQSCSFECVKEAAQKAhahsfiselaSGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 160 AIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVamLIATHNMDLAARMDRRVSLQDGHV 228
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTV--LVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
28-229 |
7.74e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.47 E-value: 7.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTqirRTDIGFVYQSHRLLPEF 107
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA---RRGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 108 SALENVMLPQMIR-GLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTA 186
Cdd:PRK10895 94 SVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 640481818 187 DHVfKALTQLVRATRVAMLIATHNM-DLAARMDRRVSLQDGHVI 229
Cdd:PRK10895 174 IDI-KRIIEHLRDSGLGVLITDHNVrETLAVCERAYIVSQGHLI 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
30-230 |
1.10e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 78.46 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLhiaGLLEQA---DEGEVYVGGTATsglSDVERTQIRRTdIGFVYQSHRLLPE 106
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLI---NLLQRVfdpQSGRILIDGTDI---RTVTRASLRRN-IAVVFQDAGLFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 fSALENVMLpqmirGLP--KKETVKRSKEILAYLGLAER--------VTHRPAELSGGEQQRVAIARAVANAPRVLLADE 176
Cdd:PRK13657 424 -SIEDNIRV-----GRPdaTDEEMRAAAERAQAHDFIERkpdgydtvVGERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640481818 177 PTGNLDPHTADHVFKALTQlVRATRVAMLIAtHNMDLAARMDRRVSLQDGHVIE 230
Cdd:PRK13657 498 ATSALDVETEAKVKAALDE-LMKGRTTFIIA-HRLSTVRNADRILVFDNGRVVE 549
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
28-226 |
1.36e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.93 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeqadegevyvggTATSGlsdvertQIRRtdigfvyqshrllPe 106
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRaIAGLW------------PYGSG-------RIAR-------------P- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 fsALENVM-LPQ---MIRG-------LPKKETVKRSKEILAYL------GLAER---VTHRPAELSGGEQQRVAIARAVA 166
Cdd:COG4178 424 --AGARVLfLPQrpyLPLGtlreallYPATAEAFSDAELREALeavglgHLAERldeEADWDQVLSLGEQQRLAFARLLL 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 167 NAPRVLLADEPTGNLDPHTADHVFKALTQLVRATrvAMLIATHNMDLAARMDRRVSLQDG 226
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLREELPGT--TVISVGHRSTLAAFHDRVLELTGD 559
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
30-230 |
1.59e-16 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 77.83 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTAtsgLSDVERTQIRRtDIGFVYQsHRLLPEFSA 109
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHD---LADYTLASLRR-QVALVSQ-DVVLFNDTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 110 LENVMLPQMiRGLPKKETvkRSKEILAYL---------GLAERVTHRPAELSGGEQQRVAIARAV-ANAPrVLLADEPTG 179
Cdd:TIGR02203 423 ANNIAYGRT-EQADRAEI--ERALAAAYAqdfvdklplGLDTPIGENGVLLSGGQRQRLAIARALlKDAP-ILILDEATS 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 640481818 180 NLDPHTADHVFKALTQLVRAtRVAMLIAtHNMDLAARMDRRVSLQDGHVIE 230
Cdd:TIGR02203 499 ALDNESERLVQAALERLMQG-RTTLVIA-HRLSTIEKADRIVVMDDGRIVE 547
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
30-199 |
2.00e-16 |
|
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: 74.01 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGTATSGLSDVERtqiRRTDIGFV---YQSHRLLP 105
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEaLFGLRP-PASGEITLDGKPVTRRSPRDA---IRAGIAYVpedRKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 106 EFSALENVMLPQMirglpkketvkrskeilaylglaervthrpaeLSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHT 185
Cdd:cd03215 92 DLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170
....*....|....
gi 640481818 186 ADHVFKALTQLVRA 199
Cdd:cd03215 140 KAEIYRLIRELADA 153
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
30-230 |
2.23e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 76.70 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKS-TLLHIAGLLE-----QADEGEVyvGGTATSGLSDVERTQIRRTDIGFVYQS--H 101
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgrvMAEKLEF--NGQDLQRISEKERRNLVGAEVAMIFQDpmT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 102 RLLPEFSALENVMLPQMI-RGLPKKETVKRSKEILAYLGL---AERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEP 177
Cdd:PRK11022 101 SLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640481818 178 TGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRV-SLQDGHVIE 230
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIiVMYAGQVVE 234
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-232 |
7.20e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 74.35 E-value: 7.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 24 EATLTILDGASLALWEGQSVALVAPSGTGKStlLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRTDIGFVYQSHRl 103
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQNPR- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 104 lPEFSALENVM--LPQMIRGLPKKETVKRSKEILAYLGLAE--RVTHR-PAELSGGEQQRVAIARAV-ANAPrVLLADEP 177
Cdd:PRK10418 90 -SAFNPLHTMHthARETCLALGKPADDATLTAALEAVGLENaaRVLKLyPFEMSGGMLQRMMIALALlCEAP-FIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 178 TGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVS-LQDGHVIELD 232
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAvMSHGRIVEQG 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
30-196 |
9.18e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 9.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSgLSDVERTQirRTDIGFVYQSHRLLPEFSA 109
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-FNGPKSSQ--EAGIGIIHQELNLIPQLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 110 LENVMLPQMIR----GLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNL-DPH 184
Cdd:PRK10762 97 AENIFLGREFVnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTE 176
|
170
....*....|..
gi 640481818 185 TADhVFKALTQL 196
Cdd:PRK10762 177 TES-LFRVIREL 187
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-223 |
1.08e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 75.82 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGtatsglSDVERT-QIRRTDIGFVYQSHRLLPEFS 108
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG------KDIETNlDAVRQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 109 ALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADH 188
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190
....*....|....*....|....*....|....*
gi 640481818 189 VFKALTQLvRATRvAMLIATHNMDLAARMDRRVSL 223
Cdd:TIGR01257 1100 IWDLLLKY-RSGR-TIIMSTHHMDEADLLGDRIAI 1132
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-230 |
1.27e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.28 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVYLHDVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKS-TLLHIAGLLEQADeGEVYVGG----------TAT 78
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAG-GLVQCDKmllrrrsrqvIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 79 SGLSDVERTQIRRTDIGFVYQS--HRLLPEFSALENVmlPQMIR---GLPKKETVKRSKEILAYLGLAER---VTHRPAE 150
Cdd:PRK10261 91 SEQSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQI--AESIRlhqGASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 151 LSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVI 229
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIaDRVLVMYQGEAV 248
|
.
gi 640481818 230 E 230
Cdd:PRK10261 249 E 249
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
30-226 |
1.50e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.82 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIrrtDIGFVYQSHRLLPEFSA 109
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL---GIGIIYQELSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 110 LENV----MLPQMIRGLPK---KETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:PRK09700 98 LENLyigrHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 640481818 183 PHTADHVFKALTQLvRATRVAMLIATHNMDLAARM-DRRVSLQDG 226
Cdd:PRK09700 178 NKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-229 |
1.51e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.16 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVYLHDVRRRYKQGEAtltiLDGASLALWEGQSVALVAPSGTGKSTLLH-IAGL--LEQadeGEVYV-GGtatsglsDVE 85
Cdd:NF033858 1 VARLEGVSHRYGKTVA----LDDVSLDIPAGCMVGLIGPDGVGKSSLLSlIAGArkIQQ---GRVEVlGG-------DMA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 86 RTQIRRT---DIGFVYQ--SHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAeRVTHRPA-ELSGGEQQRV 159
Cdd:NF033858 67 DARHRRAvcpRIAYMPQglGKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLA-PFADRPAgKLSGGMKQKL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640481818 160 AIARAVANAPRVLLADEPTGNLDPhTADHVFKALTQLVRATRVAM--LIATHNMDLAARMDRRVSLQDGHVI 229
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDP-LSRRQFWELIDRIRAERPGMsvLVATAYMEEAERFDWLVAMDAGRVL 216
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
28-228 |
2.03e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 74.69 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTAtsgLSDVERTQIRRTdIGFVYQSHRLLPEF 107
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGAD---LKQWDRETFGKH-IGYLPQDVELFPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 108 SAlENVmlPQMIRGLPKKETVKRSK-----EILAYL--GLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGN 180
Cdd:TIGR01842 408 VA-ENI--ARFGENADPEKIIEAAKlagvhELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 640481818 181 LDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARMDRRVSLQDGHV 228
Cdd:TIGR01842 485 LDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-229 |
2.58e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHI-AGLLEQAD-EGEVYVGGT--ATSGLSDVERTqirrtDIGFVYQSHRLLP 105
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVlSGVYPHGTyEGEIIFEGEelQASNIRDTERA-----GIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 106 EFSALENVML-PQMIRG--LPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:PRK13549 96 ELSVLENIFLgNEITPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 640481818 183 PHTADHVFKALTQLvRATRVAMLIATHNMD-LAARMDRRVSLQDGHVI 229
Cdd:PRK13549 176 ESETAVLLDIIRDL-KAHGIACIYISHKLNeVKAISDTICVIRDGRHI 222
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-232 |
2.95e-15 |
|
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: 71.76 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 14 HDVRRRYKQGEATltILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGG--TATSGLSDVertqir 90
Cdd:cd03244 6 KNVSLRYRPNLPP--VLKNISFSIKPGEKVGIVGRTGSGKSSLLLaLFRLVE-LSSGSILIDGvdISKIGLHDL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 91 RTDIGFVYQSHRLLP-----------EFS------ALENVMLPQMIRGLPKketvkrskeilaylGLAERVTHRPAELSG 153
Cdd:cd03244 77 RSRISIIPQDPVLFSgtirsnldpfgEYSdeelwqALERVGLKEFVESLPG--------------GLDTVVEEGGENLSV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 154 GEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKAL-TQLVRATrvaMLIATHNMDLAARMDRRVSLQDGHVIELD 232
Cdd:cd03244 143 GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIrEAFKDCT---VLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-206 |
4.25e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.52 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 5 ENGVPVVYLHDVRRRykqGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVYVGGTATSGLSd 83
Cdd:COG3845 252 EPGEVVLEVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEaLAGLR-PPASGSIRLDGEDITGLS- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 84 veRTQIRRTDIGFV---YQSHRLLPEFSALENVML-----PQMIRG--LPKKETVKRSKEILAYLGLAERVTHRPAE-LS 152
Cdd:COG3845 327 --PRERRRLGVAYIpedRLGRGLVPDMSVAENLILgryrrPPFSRGgfLDRKAIRAFAEELIEEFDVRTPGPDTPARsLS 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640481818 153 GGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLvRATRVAMLI 206
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLL 457
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
29-231 |
6.05e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.22 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTllhIAGLLE---QADEGEVYVGGTAtsgLSDVERTQIRRtDIGFVYQSHRLLP 105
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQnlyQPTGGQVLLDGVP---LVQYDHHYLHR-QVALVGQEPVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 106 EfSALENVMLPqmIRGLPKKETVKRSKEILAY-------LGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPT 178
Cdd:TIGR00958 569 G-SVRENIAYG--LTDTPDEEIMAAAKAANAHdfimefpNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640481818 179 GNLDPhtadHVFKALTQLV-RATRVAMLIAtHNMDLAARMDRRVSLQDGHVIEL 231
Cdd:TIGR00958 646 SALDA----ECEQLLQESRsRASRTVLLIA-HRLSTVERADQILVLKKGSVVEM 694
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
28-230 |
6.49e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 6.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLlHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRTdIGFVYQ--SHRLLP 105
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTT-GLALLRLINSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQdpNSSLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 106 EFSALENVM--LPQMIRGLPKKETVKRSKEILAYLGLAERVTHR-PAELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:PRK15134 378 RLNVLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 640481818 183 PHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRV-SLQDGHVIE 230
Cdd:PRK15134 458 KTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQViVLRQGEVVE 506
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-228 |
6.64e-15 |
|
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: 72.94 E-value: 6.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 27 LTILDGASLALWEGQSVALVAPSGTGKSTLLHI-AGLLEQAD-EGEVYVGGT--ATSGLSDVERTqirrtDIGFVYQSHR 102
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKIlSGVYPHGTwDGEIYWSGSplKASNIRDTERA-----GIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 103 LLPEFSALENVMLPQMIRgLPKK-----ETVKRSKEILAYLGL-AERVTHRPAELSGGEQQRVAIARAVANAPRVLLADE 176
Cdd:TIGR02633 89 LVPELSVAENIFLGNEIT-LPGGrmaynAMYLRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640481818 177 PTGNLDPHTADHVFKALTQLvRATRVAMLIATHNMD-LAARMDRRVSLQDG-HV 228
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNeVKAVCDTICVIRDGqHV 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
40-226 |
1.42e-14 |
|
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: 69.81 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 40 GQSVALVAPSGTGKSTLLhiAGLL-E-QADEGEVYVGGTatsglsdvertqirrtdIGFVYQSHRLLPEfSALENVmlpq 117
Cdd:cd03250 31 GELVAIVGPVGSGKSSLL--SALLgElEKLSGSVSVPGS-----------------IAYVSQEPWIQNG-TIRENI---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 118 mIRGLP-----KKETVK-----RSKEILAyLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTAD 187
Cdd:cd03250 87 -LFGKPfdeerYEKVIKacalePDLEILP-DGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 640481818 188 HVF-KALTQLVRATRVAMLIaTHNMDLAARMDRRVSLQDG 226
Cdd:cd03250 165 HIFeNCILGLLLNNKTRILV-THQLQLLPHADQIVVLDNG 203
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
43-230 |
2.88e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.29 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 43 VALVAPSGTGKSTLlhiAGLLE---QADEGEVYVGGTATSGLSDvertQIRRTDIGFVYQSHRLLPE------------- 106
Cdd:PRK10790 370 VALVGHTGSGKSTL---ASLLMgyyPLTEGEIRLDGRPLSSLSH----SVLRQGVAMVQQDPVVLADtflanvtlgrdis 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 ----FSALENVMLPQMIRGLPKketvkrskeilaylGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:PRK10790 443 eeqvWQALETVQLAELARSLPD--------------GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 640481818 183 PHTADHVFKALtQLVRATRVAMLIAtHNMDLAARMDRRVSLQDGHVIE 230
Cdd:PRK10790 509 SGTEQAIQQAL-AAVREHTTLVVIA-HRLSTIVEADTILVLHRGQAVE 554
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
50-232 |
3.10e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 71.31 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 50 GTGKST---LLhiAGLLEqADEGEVYVGGTATSGlSDVErtqIRRTdIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKE 126
Cdd:NF033858 302 GCGKSTtmkML--TGLLP-ASEGEAWLFGQPVDA-GDIA---TRRR-VGYMSQAFSLYGELTVRQNLELHARLFHLPAAE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 127 TVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLI 206
Cdd:NF033858 374 IAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFI 453
|
170 180
....*....|....*....|....*..
gi 640481818 207 ATHNMDLAARMDrRVSLQD-GHVIELD 232
Cdd:NF033858 454 STHFMNEAERCD-RISLMHaGRVLASD 479
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
28-209 |
3.37e-14 |
|
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: 67.09 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVyvggtatsglsdverTQIRRTDIGFVYQshrllpe 106
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTLLKlIAGELE-PDEGIV---------------TWGSTVKIGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 fsalenvmlpqmirglpkketvkrskeilaylglaervthrpaeLSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTA 186
Cdd:cd03221 71 --------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI 106
|
170 180
....*....|....*....|...
gi 640481818 187 DhvfkALTQLVRATRVAMLIATH 209
Cdd:cd03221 107 E----ALEEALKEYPGTVILVSH 125
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
9-211 |
4.67e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.53 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYLHDVRRRYKQGEatlTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATsglsdveRTQ 88
Cdd:PRK15056 5 AGIVVNDVTVTWRNGH---TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-------RQA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 89 IRRTDIGFVYQSHRLLPEFSAL--ENVMLPQ-----MIRgLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAI 161
Cdd:PRK15056 75 LQKNLVAYVPQSEEVDWSFPVLveDVVMMGRyghmgWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 640481818 162 ARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIATHNM 211
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNL 202
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-212 |
5.09e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.73 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 16 VRRRYKQGEAtltiLDGASLALWEGQSVALVAPSGTGKSTLLHI-AGLLeQADEGEVYVGGTatsglsdV---ERTQIRR 91
Cdd:COG4586 28 FRREYREVEA----VDDISFTIEPGEIVGFIGPNGAGKSTTIKMlTGIL-VPTSGEVRVLGY-------VpfkRRKEFAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 92 tDIGFVY-QSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAErVTHRPA-ELSGGEQQRVAIARAVANAP 169
Cdd:COG4586 96 -RIGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGE-LLDTPVrQLSLGQRMRCELAAALLHRP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 640481818 170 RVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMD 212
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMD 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-223 |
5.43e-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: 68.29 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 27 LTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATsglsDVERTQIRRtdiGFVYQSHR--LL 104
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL----DFQRDSIAR---GLLYLGHApgIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 105 PEFSALENVmlpQMIRGLPKKETVkrsKEILAYLGLAErVTHRP-AELSGGEQQRVAIARAVANAPRVLLADEPTGNLDP 183
Cdd:cd03231 86 TTLSVLENL---RFWHADHSDEQV---EEALARVGLNG-FEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 640481818 184 HTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSL 223
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-196 |
6.17e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.29 E-value: 6.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqadeGEVYVGGTATSGLSDVERTqIRRTdiGFVYQSHRLLPE 106
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNaLAGRIQ----GNNFTGTILANNRKPTKQI-LKRT--GFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 FSALENVMLPQMIR---GLPKKETVKRSKEILAYLGLAERVTHRPAE-----LSGGEQQRVAIARAVANAPRVLLADEPT 178
Cdd:PLN03211 155 LTVRETLVFCSLLRlpkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170
....*....|....*...
gi 640481818 179 GNLDPHTADHVFKALTQL 196
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSL 252
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-229 |
1.21e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 15 DVRRRYKqgeatlTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQ--ADEGEVYVGGTATSG--LSDVERTQI 89
Cdd:PRK13547 8 HVARRHR------AILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGggAPRGARVTGDVTLNGepLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 RRTDIGFVYQSHRLLPeFSALENVMLPQMIRGLPKKETVKRSKEI----LAYLGLAERVTHRPAELSGGEQQRVAIARAV 165
Cdd:PRK13547 82 ARLRAVLPQAAQPAFA-FSAREIVLLGRYPHARRAGALTHRDGEIawqaLALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640481818 166 AN---------APRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAAR-MDRRVSLQDGHVI 229
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIV 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-212 |
1.27e-13 |
|
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: 69.66 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 4 GENGVPVVYLHDVRRRYKqGEATLTIlDGASLALWEGQSVALVAPSGTGKSTLLhiaglleqadegEVYVGGTA-TSGLS 82
Cdd:TIGR01257 1931 GGNKTDILRLNELTKVYS-GTSSPAV-DRLCVGVRPGECFGLLGVNGAGKTTTF------------KMLTGDTTvTSGDA 1996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 83 DVERTQIRrTDIGFVYQSHRLLPEFSAL-------ENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGE 155
Cdd:TIGR01257 1997 TVAGKSIL-TNISDVHQNMGYCPQFDAIddlltgrEHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGN 2075
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 156 QQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRvAMLIATHNMD 212
Cdd:TIGR01257 2076 KRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSME 2131
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
13-223 |
1.38e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 68.68 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 13 LHDVRR---RYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqaDEGEVyvggTATS--------- 79
Cdd:PRK15093 3 LLDIRNltiEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKaICGVTK--DNWRV----TADRmrfddidll 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 80 GLSDVERTQIRRTDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKET--------VKRSKEILAYLGLAErvtHR---- 147
Cdd:PRK15093 77 RLSPRERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGRwwqrfgwrKRRAIELLHRVGIKD---HKdamr 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640481818 148 --PAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSL 223
Cdd:PRK15093 154 sfPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINV 231
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
40-229 |
1.43e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.56 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 40 GQSVALVAPSGTGKSTLLH-IAGLLEQadEGEVYVGGTATSGLSDVERTQIRrtdiGFVYQSHRLLPefsalenvMLP-- 116
Cdd:COG4138 22 GELIHLIGPNGAGKSTLLArMAGLLPG--QGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPF--------AMPvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 117 QMIR-GLPKKETVKRSKEILAY----LGLAERVTHRPAELSGGEQQRVAIARAV------ANA-PRVLLADEPTGNLDPH 184
Cdd:COG4138 88 QYLAlHQPAGASSEAVEQLLAQlaeaLGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINPeGQLLLLDEPMNSLDVA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 640481818 185 ---TADHVFKALTQLVRATrvamLIATHNMDLAAR-MDRRVSLQDGHVI 229
Cdd:COG4138 168 qqaALDRLLRELCQQGITV----VMSSHDLNHTLRhADRVWLLKQGKLV 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-231 |
3.72e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.43 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLhiAGLLEQAD--EGEVYVGGTatsglsdvertqirrtdIGFVYQsHRLLPEF 107
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLL--SALLAEMDkvEGHVHMKGS-----------------VAYVPQ-QAWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 108 SALENVMLPQMIRGlPKKETVKRSKEILAYL-----GLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:TIGR00957 714 SLRENILFGKALNE-KYYQQVLEACALLPDLeilpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 640481818 183 PHTADHVFKALT----QLVRATRVamlIATHNMDLAARMDRRVSLQDGHVIEL 231
Cdd:TIGR00957 793 AHVGKHIFEHVIgpegVLKNKTRI---LVTHGISYLPQVDVIIVMSGGKISEM 842
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
27-226 |
4.01e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 66.20 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 27 LTILDGASLALWEGQSVALVAPSGTGKSTLLhIAGLLE-QADEGEVYVGGTATSGLSDVERTQIRRTDIGFVYQSHRLLp 105
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLL-LAILGEmQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 106 EFSALENVML-----PQMIRGLPKKETVKRSKEILAYlGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGN 180
Cdd:cd03290 92 NATVEENITFgspfnKQRYKAVTDACSLQPDIDLLPF-GDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 640481818 181 LDPHTADHVFKA-LTQLVRATRVAMLIATHNMDLAARMDRRVSLQDG 226
Cdd:cd03290 171 LDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-229 |
1.03e-12 |
|
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: 64.59 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 15 DVRRRYKQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLL-HIAGLLEqadeGEVYVGGTAT-SGLSDVERTQIRRT 92
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLkALANRTE----GNVSVEGDIHyNGIPYKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 93 DIGFVYQSHRLLP--------EFSALENVmlPQMIRGLpkketvkrskeilaylglaervthrpaelSGGEQQRVAIARA 164
Cdd:cd03233 84 EIIYVSEEDVHFPtltvretlDFALRCKG--NEFVRGI-----------------------------SGGERKRVSIAEA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 165 VANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATH--NMDLAARMDRRVSLQDGHVI 229
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYqaSDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-229 |
1.49e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.19 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVertqirrtdiGFVYQSHRLLPEF 107
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK----------AFARKVAYLPQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 108 SALENVMLPQMIR----------GLPKKETVKRSKEILAYLGLaERVTHRPAE-LSGGEQQRVAIARAVANAPRVLLADE 176
Cdd:PRK10575 95 PAAEGMTVRELVAigrypwhgalGRFGAADREKVEEAISLVGL-KPLAHRLVDsLSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 177 PTGNLD-PHTADHVfkALTQLVRATRVAMLIAT-HNMDLAARM-DRRVSLQDGHVI 229
Cdd:PRK10575 174 PTSALDiAHQVDVL--ALVHRLSQERGLTVIAVlHDINMAARYcDYLVALRGGEMI 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
30-230 |
2.02e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.81 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTllhIAGLLEQ---ADEGEVYVGGTatsGLSDVERTQIRRtDIGFVYQSHRLLPE 106
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKST---IANLLTRfydIDEGEILLDGH---DLRDYTLASLRN-QVALVSQNVHLFND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 FSAlENVmlpqmirGLPKKETVKRsKEI-----LAYL---------GLAERVTHRPAELSGGEQQRVAIARAV-ANAPrV 171
Cdd:PRK11176 432 TIA-NNI-------AYARTEQYSR-EQIeeaarMAYAmdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALlRDSP-I 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 172 LLADEPTGNLDPHTADHVFKALTQLvRATRVAMLIAtHNMDLAARMDRRVSLQDGHVIE 230
Cdd:PRK11176 502 LILDEATSALDTESERAIQAALDEL-QKNRTSLVIA-HRLSTIEKADEILVVEDGEIVE 558
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-232 |
3.03e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.77 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 5 ENGVPV--------VYLHDVRRRYKQGEATltILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGG- 75
Cdd:PLN03232 1221 ENNRPVsgwpsrgsIKFEDVHLRYRPGLPP--VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDc 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 76 -TATSGLSDVER--TQIRRTDIGFVYQSHRLLPEFSALENVMLPQMIRGLPKKETVKRSKeilayLGLAERVTHRPAELS 152
Cdd:PLN03232 1299 dVAKFGLTDLRRvlSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNP-----FGLDAEVSEGGENFS 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 153 GGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRAtrVAMLIATHNMDLAARMDRRVSLQDGHVIELD 232
Cdd:PLN03232 1374 VGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS--CTMLVIAHRLNTIIDCDKILVLSSGQVLEYD 1451
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
40-182 |
3.12e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.80 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 40 GQSVALVAPSGTGKSTLLH-IAGLLEQadEGEVYVGGTATSGLSDVERTQIRrtdiGFVYQSHR---LLPEFSALEnVML 115
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLArMAGLLPG--SGSIQFAGQPLEAWSAAELARHR----AYLSQQQTppfAMPVFQYLT-LHQ 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640481818 116 PQmirGLPKKETVKRSKEILAYLGLAERVtHRPA-ELSGGEQQRVAIARAV-----ANAP--RVLLADEPTGNLD 182
Cdd:PRK03695 95 PD---KTRTEAVASALNEVAEALGLDDKL-GRSVnQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLD 165
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-187 |
3.76e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.97 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEV-----------------YVGGTA----TSGLSDV--- 84
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdlivarlqqdpprNVEGTVydfvAEGIEEQaey 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 85 --ERTQIRR---TDigfvyQSHRLLPEFSALENVMlpqMIRGLPKKETvkRSKEILAYLGL-AERvthRPAELSGGEQQR 158
Cdd:PRK11147 98 lkRYHDISHlveTD-----PSEKNLNELAKLQEQL---DHHNLWQLEN--RINEVLAQLGLdPDA---ALSSLSGGWLRK 164
|
170 180
....*....|....*....|....*....
gi 640481818 159 VAIARAVANAPRVLLADEPTGNLDPHTAD 187
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLDIETIE 193
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-213 |
4.29e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.87 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTL-LHIAGLLeQADEGEVYVGGTAtsgLSDVERTQIR-RTDIGFVYQSHRLLPE 106
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLL-RPQKGAVLWQGKP---LDYSKRGLLAlRQQVATVFQDPEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 FSALE-NVMLPQMIRGLPKKETVKRSKEILAYLGlAERVTHRPAE-LSGGEQQRVAIARAVANAPRVLLADEPTGNLDPH 184
Cdd:PRK13638 92 YTDIDsDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180
....*....|....*....|....*....
gi 640481818 185 TADHVFKALTQLVRATRvAMLIATHNMDL 213
Cdd:PRK13638 171 GRTQMIAIIRRIVAQGN-HVIISSHDIDL 198
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-178 |
5.95e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.27 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 17 RRRYKQGEATLTI--------LDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLlEQADEGEVYVGGTATSGLSDVERt 87
Cdd:COG1129 247 KRAAAPGEVVLEVeglsvggvVRDVSFSVRAGEILGIAGLVGAGRTELARaLFGA-DPADSGEIRLDGKPVRIRSPRDA- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 88 qIRRtdiGFVY-----QSHRLLPEFSALENVMLPQMiRGLPKKETVKRSKEILAYLGLAERVTHRPA-------ELSGGE 155
Cdd:COG1129 325 -IRA---GIAYvpedrKGEGLVLDLSIRENITLASL-DRLSRGGLLDRRRERALAEEYIKRLRIKTPspeqpvgNLSGGN 399
|
170 180
....*....|....*....|...
gi 640481818 156 QQRVAIARAVANAPRVLLADEPT 178
Cdd:COG1129 400 QQKVVLAKWLATDPKVLILDEPT 422
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
107-231 |
1.26e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.22 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 FSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTA 186
Cdd:NF000106 101 FSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR 180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 640481818 187 DHVFKALTQLVRATrVAMLIATHNMDLAARM-------DRRVSLQDGHVIEL 231
Cdd:NF000106 181 NEVWDEVRSMVRDG-ATVLLTTQYMEEAEQLaheltviDRGRVIADGKVDEL 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
29-213 |
1.70e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.05 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVyvggtatsglsdvERTQIRRtdIGFVYQSHRLLPefs 108
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKLR--IGYVPQKLYLDT--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 109 alenvMLPQMIRGLPKKETVKRSKEILAYLGL--AERVTHRPAE-LSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHT 185
Cdd:PRK09544 81 -----TLPLTVNRFLRLRPGTKKEDILPALKRvqAGHLIDAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*...
gi 640481818 186 ADHVFKALTQLVRATRVAMLIATHNMDL 213
Cdd:PRK09544 156 QVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
29-232 |
3.56e-11 |
|
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: 60.50 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTL-LHIAGLLEqADEGEVYVGG--TATSGLSDVertqirRTDIGFVYQshrllp 105
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLiLALFRFLE-AEEGKIEIDGidISTIPLEDL------RSSLTIIPQ------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 106 efsalENVMLPQMIRGLPKKETVKRSKEILAYLglaeRVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHT 185
Cdd:cd03369 90 -----DPTLFSGTIRSNLDPFDEYSDEEIYGAL----RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 640481818 186 aDHvfkALTQLVRA--TRVAMLIATHNMDLAARMDRRVSLQDGHVIELD 232
Cdd:cd03369 161 -DA---LIQKTIREefTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-226 |
5.85e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.50 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 23 GEATLTILDGAslaLWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGGTATSglsdvertqirrtdigfvYQSH 101
Cdd:cd03237 11 GEFTLEVEGGS---ISESEVIGILGPNGIGKTTFIKmLAGVLK-PDEGDIEIELDTVS------------------YKPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 102 RLLPEFSALENVMLPQMIRGLPKKETVKrsKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNL 181
Cdd:cd03237 69 YIKADYEGTVRDLLSSITKDFYTHPYFK--TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 640481818 182 DPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDG 226
Cdd:cd03237 147 DVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
34-196 |
5.87e-11 |
|
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: 59.09 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 34 SLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqadegevYVGGTatsglsdVERTqiRRTDIGFVYQshrllpefsalen 112
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRaLAGLWP-------WGSGR-------IGMP--EGEDLLFLPQ------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 113 vmLPQMIRG-LpkketvkrsKEILAYlglaervthrP--AELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHV 189
Cdd:cd03223 72 --RPYLPLGtL---------REQLIY----------PwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL 130
|
....*..
gi 640481818 190 FKALTQL 196
Cdd:cd03223 131 YQLLKEL 137
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
29-182 |
7.15e-11 |
|
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: 61.10 E-value: 7.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATsglsdvertqirrtdIGFVYQSHRLLPEFS 108
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIK---------------VGYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 109 ALENVMLpqmirGL-PKKETVKRSKEILAYLG---------------LAERVTHRPA----------------------- 149
Cdd:TIGR03719 85 VRENVEE-----GVaEIKDALDRFNEISAKYAepdadfdklaaeqaeLQEIIDAADAwdldsqleiamdalrcppwdadv 159
|
170 180 190
....*....|....*....|....*....|....
gi 640481818 150 -ELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:TIGR03719 160 tKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-182 |
8.40e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.90 E-value: 8.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVY-LHDVRRRYKQGEatlTILDGASLALWEGQSVALVAPSGTGKSTLLHI-AGLlEQADEGEVyvggTATSGLSdvert 87
Cdd:PRK11819 5 YIYtMNRVSKVVPPKK---QILKDISLSFFPGAKIGVLGLNGAGKSTLLRImAGV-DKEFEGEA----RPAPGIK----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 88 qirrtdIGFVYQSHRLLPEFSALENVMLpqmirGL-PKKETVKRSKEILAYLG--------LAER--------------- 143
Cdd:PRK11819 72 ------VGYLPQEPQLDPEKTVRENVEE-----GVaEVKAALDRFNEIYAAYAepdadfdaLAAEqgelqeiidaadawd 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 144 --------------------VTHrpaeLSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:PRK11819 141 ldsqleiamdalrcppwdakVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
30-230 |
1.20e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.57 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHI-AGLLEQAD-EGE-VYVGGTAT-SGLSDVERtqirrtdIGFV--YQSHRL 103
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVlSGVYPHGSyEGEiLFDGEVCRfKDIRDSEA-------LGIViiHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 104 LPEFSALENVML--PQMIRGLPK-KETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGN 180
Cdd:NF040905 90 IPYLSIAENIFLgnERAKRGVIDwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 640481818 181 LDPHTADHVFKALTQLvRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:NF040905 170 LNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVaDSITVLRDGRTIE 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
34-230 |
1.95e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 59.08 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 34 SLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQ-IR------------RTDIGfvyqs 100
Cdd:COG4167 33 SFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKhIRmifqdpntslnpRLNIG----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 101 hRLLPEFSALENVMLPQmirglpkkETVKRSKEILAYLGL-AERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTG 179
Cdd:COG4167 108 -QILEEPLRLNTDLTAE--------EREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 640481818 180 NLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:COG4167 179 ALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHIsDKVLVMHQGEVVE 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-185 |
2.43e-10 |
|
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: 59.56 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVYLHDVRRRYkqGEATLtiLDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTatsglsdvertqi 89
Cdd:TIGR03719 322 VIEAENLTKAF--GDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET------------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 90 rrTDIGFVYQSHRLL-PEFSALENVMLPQMIRGLPKKETVKRskeilAYLGL--------AERVthrpAELSGGEQQRVA 160
Cdd:TIGR03719 385 --VKLAYVDQSRDALdPNKTVWEEISGGLDIIKLGKREIPSR-----AYVGRfnfkgsdqQKKV----GQLSGGERNRVH 453
|
170 180
....*....|....*....|....*
gi 640481818 161 IARAVANAPRVLLADEPTGNLDPHT 185
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVET 478
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
29-230 |
6.48e-10 |
|
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: 56.77 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLE-QADEGEVYVGGTATSGLSDVERTqirRTDIGFVYQShrllpe 106
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKtIMGHPKyEVTEGEILFKGEDITDLPPEERA---RLGIFLAFQY------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 fsalenvmlPQMIRGLpkketvkRSKEILAYLGLAervthrpaeLSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTA 186
Cdd:cd03217 86 ---------PPEIPGV-------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 640481818 187 DHVFKALTQLVRATRvAMLIATHNMDLAARM--DRRVSLQDGHVIE 230
Cdd:cd03217 141 RLVAEVINKLREEGK-SVLIITHYQRLLDYIkpDRVHVLYDGRIVK 185
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-231 |
6.82e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.26 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 34 SLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTqirRTDIGFVYQSHR---LLPEFSAL 110
Cdd:PRK09700 283 SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAV---KKGMAYITESRRdngFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 111 ENVMLPQMIR--------GL--PKKE--TVKRSKEILAYLglAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPT 178
Cdd:PRK09700 360 QNMAISRSLKdggykgamGLfhEVDEqrTAENQRELLALK--CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 640481818 179 GNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHVIEL 231
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-229 |
1.08e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.92 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 23 GEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTqiRRtdIGFVYQSHR 102
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--RR--IGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 103 LLPEFSALENVML------PQMIRGlpKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADE 176
Cdd:PRK10253 92 TPGDITVQELVARgryphqPLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640481818 177 PTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRR-VSLQDGHVI 229
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHlIALREGKIV 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
31-223 |
1.88e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.58 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 31 DGASLALWEGQSVALVAPSGTGKSTLLHI-AGLLeQADEGEVYVGGTAtsglsdvertqIRRTDIGF----VYQSHR--L 103
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRIlAGLA-RPDAGEVLWQGEP-----------IRRQRDEYhqdlLYLGHQpgI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 104 LPEFSALENVMLPQMIRGLPKKETVkrsKEILAYLGLAERvTHRPAE-LSGGEQQRVAIAR-AVANAPRVLLaDEPTGNL 181
Cdd:PRK13538 86 KTELTALENLRFYQRLHGPGDDEAL---WEALAQVGLAGF-EDVPVRqLSAGQQRRVALARlWLTRAPLWIL-DEPFTAI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 640481818 182 DPHTAdhvfKALTQLVR--ATRVAMLIAT--HNMDLAARMDRRVSL 223
Cdd:PRK13538 161 DKQGV----ARLEALLAqhAEQGGMVILTthQDLPVASDKVRKLRL 202
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-219 |
2.11e-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: 56.72 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 39 EGQSVALVAPSGTGKSTLLHI-AGLLEqADEGEVYvggtatsglsdvertqirrTDIGFVYQSHRLLPEFSALENVMLPQ 117
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKIlAGVLK-PDEGEVD-------------------EDLKISYKPQYISPDYDGTVEEFLRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 118 MIrglpkKETVKRSK---EILAYLGLaERVTHRP-AELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKAL 193
Cdd:COG1245 425 AN-----TDDFGSSYyktEIIKPLGL-EKLLDKNvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498
|
170 180
....*....|....*....|....*....
gi 640481818 194 TQLVRATRVAMLIATHN---MDLAArmDR 219
Cdd:COG1245 499 RRFAENRGKTAMVVDHDiylIDYIS--DR 525
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
8-228 |
2.95e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.71 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 8 VPVVYLHDVRRRYKQGEatLTILDGASlalwegqsvalvapsGTGKSTLLHiaGLLEQAD--EGEVYVggtatsglsdvE 85
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGK--LTVVLGAT---------------GSGKSTLLQ--SLLSQFEisEGRVWA-----------E 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 86 RTqirrtdIGFVyqshrllPEFSALENVMLPQMIRGLPKKETVKRSKEI--------LAYL--GLAERVTHRPAELSGGE 155
Cdd:PTZ00243 721 RS------IAYV-------PQQAWIMNATVRGNILFFDEEDAARLADAVrvsqleadLAQLggGLETEIGEKGVNLSGGQ 787
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640481818 156 QQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKA--LTQLVRATRVamlIATHNMDLAARMDRRVSLQDGHV 228
Cdd:PTZ00243 788 KARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEcfLGALAGKTRV---LATHQVHVVPRADYVVALGDGRV 859
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-184 |
4.76e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.02 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 33 ASLALWEGQSVALVAPSGTGKSTLLHIAGLleQADEG----------EVYVGGTATSGL-----SDVERTQIRRTDIGFV 97
Cdd:PLN03073 196 ASVTLAFGRHYGLVGRNGTGKTTFLRYMAM--HAIDGipkncqilhvEQEVVGDDTTALqcvlnTDIERTQLLEEEAQLV 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 98 yQSHRLLPEFSALENVMLPQmIRGLPKKETVKRSKEI-------------------LAYLGLAERVTHRPAE-LSGGEQQ 157
Cdd:PLN03073 274 -AQQRELEFETETGKGKGAN-KDGVDKDAVSQRLEEIykrlelidaytaearaasiLAGLSFTPEMQVKATKtFSGGWRM 351
|
170 180
....*....|....*....|....*..
gi 640481818 158 RVAIARAVANAPRVLLADEPTGNLDPH 184
Cdd:PLN03073 352 RIALARALFIEPDLLLLDEPTNHLDLH 378
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
40-209 |
5.33e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.47 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 40 GQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSglsDVERTQIrrtdigFVYQSH--RLLPEFSALENVmlpQ 117
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT---RGDRSRF------MAYLGHlpGLKADLSTLENL---H 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 118 MIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLV 197
Cdd:PRK13543 105 FLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHL 184
|
170
....*....|..
gi 640481818 198 RaTRVAMLIATH 209
Cdd:PRK13543 185 R-GGGAALVTTH 195
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
34-207 |
5.90e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 34 SLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTatSGLSDVErTQIRRTDIGFVYQSHRL---------- 103
Cdd:PTZ00265 405 NFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS--HNLKDIN-LKWWRSKIGVVSQDPLLfsnsiknnik 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 104 -----LPEFSALENVM------------------------LPQMIRG---------------LPKKETVKRSKEILAY-- 137
Cdd:PTZ00265 482 yslysLKDLEALSNYYnedgndsqenknkrnscrakcagdLNDMSNTtdsneliemrknyqtIKDSEVVDVSKKVLIHdf 561
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 138 -LGLAER----VTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLV-RATRVAMLIA 207
Cdd:PTZ00265 562 vSALPDKyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIA 637
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-214 |
8.68e-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: 55.18 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 39 EGQSVALVAPSGTGKSTLLHI-AGLL--------EQADEGEVyvggtatsglsdvertqIRRtdigfvYQSHRLLPEFSA 109
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKIlSGELkpnlgdydEEPSWDEV-----------------LKR------FRGTELQDYFKK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 110 LEN-----VMLPQMIRGLPK--KETVK----------RSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVL 172
Cdd:COG1245 155 LANgeikvAHKPQYVDLIPKvfKGTVRellekvdergKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 640481818 173 LADEPTGNLDPHTADHVFKALTQLVRATRvAMLIATHnmDLA 214
Cdd:COG1245 235 FFDEPSSYLDIYQRLNVARLIRELAEEGK-YVLVVEH--DLA 273
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-182 |
9.27e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 9.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 39 EGQSVALVAPSGTGKSTLLHI-AGLL--------EQADEGEVyvggtatsglsdVERtqIRRTDIgfvyQSHrllpeFSA 109
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKIlSGELipnlgdyeEEPSWDEV------------LKR--FRGTEL----QNY-----FKK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 110 LEN-----VMLPQMIRGLPK--KETVK----------RSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVL 172
Cdd:PRK13409 155 LYNgeikvVHKPQYVDLIPKvfKGKVRellkkvdergKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170
....*....|
gi 640481818 173 LADEPTGNLD 182
Cdd:PRK13409 235 FFDEPTSYLD 244
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
29-226 |
1.42e-08 |
|
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: 53.71 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEqADEGEVYVGG--TATSGLSDVERTQIRRTDI-GFVYQSHRLL 104
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELE-PSEGKIKHSGriSFSSQFSWIMPGTIKENIIfGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 105 pefSALENVMLPQMIRGLPKKEtvkrsKEILAYLGLAervthrpaeLSGGEQQRVAIARAVANAPRVLLADEPTGNLDPH 184
Cdd:cd03291 131 ---SVVKACQLEEDITKFPEKD-----NTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 640481818 185 TADHVFKALTQLVRATRVAMLIaTHNMDLAARMDRRVSLQDG 226
Cdd:cd03291 194 TEKEIFESCVCKLMANKTRILV-TSKMEHLKKADKILILHEG 234
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-226 |
1.55e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 26 TLTILDGASLALWEGQSVALVAPSGTGKSTLLHIagLLEQADEGeVYVGGTATSGLSDVERTQIRRtdIGFVYQSHRLLP 105
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNV--LAERVTTG-VITGGDRLVNGRPLDSSFQRS--IGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 106 EFSALENVMLPQMIR---GLPKKETVKRSKEILAYLGL---AERVTHRPAE-LSGGEQQRVAIARAVANAPRVLL-ADEP 177
Cdd:TIGR00956 850 TSTVRESLRFSAYLRqpkSVSKSEKMEYVEEVIKLLEMesyADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 640481818 178 TGNLDPHTADHVFKALTQLVRATRvAMLIATH--NMDLAARMDRRVSLQDG 226
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLADHGQ-AILCTIHqpSAILFEEFDRLLLLQKG 979
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-195 |
1.90e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.15 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 21 KQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLhiAGLLEQAD-EGEVYVGGTATSGLSdverTQIRRTDIGFVYQ 99
Cdd:TIGR01271 1226 KYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLL--SALLRLLStEGEIQIDGVSWNSVT----LQTWRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 100 S---------HRLLPE--------FSALENVMLPQMIRGLPKKetvkrskeilaylgLAERVTHRPAELSGGEQQRVAIA 162
Cdd:TIGR01271 1300 KvfifsgtfrKNLDPYeqwsdeeiWKVAEEVGLKSVIEQFPDK--------------LDFVLVDGGYVLSNGHKQLMCLA 1365
|
170 180 190
....*....|....*....|....*....|...
gi 640481818 163 RAVANAPRVLLADEPTGNLDPHTADHVFKALTQ 195
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
40-230 |
5.15e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 40 GQSVALVAPSGTGKSTLLH-IAGLLEQADEGEVYVGGTAT--SGLSDVERTQIRRTDI-GFVYQSHRLlpeFSALENVML 115
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVAyvPQVSWIFNATVRENILfGSDFESERY---WRAIDVTAL 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 116 PQMIRGLPKKETVKrskeilaylglaerVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQ 195
Cdd:PLN03232 720 QHDLDLLPGRDLTE--------------IGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK 785
|
170 180 190
....*....|....*....|....*....|....*..
gi 640481818 196 --LVRATRVamlIATHNMDLAARMDRRVSLQDGHVIE 230
Cdd:PLN03232 786 deLKGKTRV---LVTNQLHFLPLMDRIILVSEGMIKE 819
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
29-227 |
5.44e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQAdEGEVYVGG--TATSGLSDVERTQIRRTDI-GFVYQSHRLL 104
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPS-EGKIKHSGriSFSPQTSWIMPGTIKDNIIfGLSYDEYRYT 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 105 pefSALENVMLPQMIRGLPKKEtvkrsKEILAYLGLAervthrpaeLSGGEQQRVAIARAVANAPRVLLADEPTGNLDPH 184
Cdd:TIGR01271 520 ---SVIKACQLEEDIALFPEKD-----KTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 640481818 185 TADHVFKA--LTQLVRATRVamlIATHNMDLAARMDRRVSLQDGH 227
Cdd:TIGR01271 583 TEKEIFESclCKLMSNKTRI---LVTSKLEHLKKADKILLLHEGV 624
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-182 |
5.99e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLeQADEGEVyvggtatsGLSdvertqiRRTDIGFVYQsHRLlpE 106
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKlLAGEL-APVSGEI--------GLA-------KGIKLGYFAQ-HQL--E 386
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640481818 107 FSALENVMLPQMIRgLPKKETVKRSKEILAYLGL-AERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:PRK10636 387 FLRADESPLQHLAR-LAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-230 |
6.58e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 51.71 E-value: 6.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 19 RYKQG---EATLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQADeGEVYVGGTATSGLSDVERTQirRTDI 94
Cdd:PRK15112 15 RYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKmLAGMIEPTS-GELLIDDHPLHFGDYSYRSQ--RIRM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 95 GFVYQSHRLLPEFSALENVMLP-QMIRGLPKKETVKRSKEILAYLGL-AERVTHRPAELSGGEQQRVAIARAVANAPRVL 172
Cdd:PRK15112 92 IFQDPSTSLNPRQRISQILDFPlRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 173 LADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHVIE 230
Cdd:PRK15112 172 IADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHIsDQVLVMHQGEVVE 230
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
26-226 |
6.70e-08 |
|
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: 51.09 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 26 TLTILDGASLALWEGQSVALVAPSGTGKSTLLHI-AGLLEQAD-EGEVYVGGTatsglsdvERTQIRRTDIGFVYQSHRL 103
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVlAGRKTAGViTGEILINGR--------PLDKNFQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 104 LPEFSALENVMLPQMIRGlpkketvkrskeilayLGLAERvthrpaelsggeqQRVAIARAVANAPRVLLADEPTGNLDP 183
Cdd:cd03232 91 SPNLTVREALRFSALLRG----------------LSVEQR-------------KRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 640481818 184 HTADHVFKALTQLVRATRvAMLIATH--NMDLAARMDRRVSLQDG 226
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQ-AILCTIHqpSASIFEKFDRLLLLKRG 185
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
147-230 |
8.00e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.43 E-value: 8.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 147 RPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALT--QLVRATRVamlIATHNMDLAARMDRRVSLQ 224
Cdd:PLN03130 737 RGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIkdELRGKTRV---LVTNQLHFLSQVDRIILVH 813
|
....*.
gi 640481818 225 DGHVIE 230
Cdd:PLN03130 814 EGMIKE 819
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-185 |
8.78e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 8.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLHIagLLEQ--ADEGEVYVGgtatsglsdverTQIrrtDIGFVYQsHR--L 103
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKL--MLGQlqADSGRIHCG------------TKL---EVAYFDQ-HRaeL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 104 LPEFSALENVmlpqmirGLPKKE-TVK-RSKEILAYLG---LAERVTHRPAE-LSGGEQQRVAIARAVANAPRVLLADEP 177
Cdd:PRK11147 395 DPEKTVMDNL-------AEGKQEvMVNgRPRHVLGYLQdflFHPKRAMTPVKaLSGGERNRLLLARLFLKPSNLLILDEP 467
|
....*...
gi 640481818 178 TGNLDPHT 185
Cdd:PRK11147 468 TNDLDVET 475
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
30-212 |
1.28e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQirrTDIGFVYQSHRLLPEFSA 109
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE---NGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 110 LENVMLPQMirglPKK-------ETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:PRK10982 91 MDNMWLGRY----PTKgmfvdqdKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190
....*....|....*....|....*....|
gi 640481818 183 PHTADHVFKALTQLvRATRVAMLIATHNMD 212
Cdd:PRK10982 167 EKEVNHLFTIIRKL-KERGCGIVYISHKME 195
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-214 |
1.44e-07 |
|
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: 50.83 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 39 EGQSVALVAPSGTGKSTLLHIaglleqadegevyVGGTATSGLSDVERTQIRRTDIGFvYQSHRLLPEFSALEN-----V 113
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKI-------------LAGKLKPNLGKFDDPPDWDEILDE-FRGSELQNYFTKLLEgdvkvI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 114 MLPQMIRGLPK----------KETVKRSK--EILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNL 181
Cdd:cd03236 91 VKPQYVDLIPKavkgkvgellKKKDERGKldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190
....*....|....*....|....*....|...
gi 640481818 182 DPHTADHVFKALTQLVRATRvAMLIATHnmDLA 214
Cdd:cd03236 171 DIKQRLNAARLIRELAEDDN-YVLVVEH--DLA 200
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-185 |
1.47e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVYLHDVRRRYkqGEATLtiLDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLlEQADEGEVYVGGTAtsglsdvertq 88
Cdd:PRK11819 324 VIEAENLSKSF--GDRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKmITGQ-EQPDSGTIKIGETV----------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 89 irrtDIGFVYQSH-RLLPEFSALENVMLPQMIRGLPKKETVKRskeilAYLGL--------AERVthrpAELSGGEQQRV 159
Cdd:PRK11819 388 ----KLAYVDQSRdALDPNKTVWEEISGGLDIIKVGNREIPSR-----AYVGRfnfkggdqQKKV----GVLSGGERNRL 454
|
170 180
....*....|....*....|....*.
gi 640481818 160 AIARAVANAPRVLLADEPTGNLDPHT 185
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
151-221 |
1.85e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 1.85e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640481818 151 LSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLV-RATRVAMLIAtHNMDLAARMDRRV 221
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIA-HRIASIKRSDKIV 1429
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
40-221 |
2.03e-07 |
|
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: 48.91 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 40 GQSVALVAPSGTGKSTLLH-IAGLLEQADEGEVYVGGTatsglsdvertqirrtdigfvyqshrllpefsalenvmlpqm 118
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGE------------------------------------------ 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 119 irglpkketvkRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFK-----AL 193
Cdd:smart00382 40 -----------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrLL 108
|
170 180 190
....*....|....*....|....*....|....
gi 640481818 194 TQLVRATRVAMLIATHN------MDLAARMDRRV 221
Cdd:smart00382 109 LLLKSEKNLTVILTTNDekdlgpALLRRRFDRRI 142
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-219 |
2.12e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 39 EGQSVALVAPSGTGKSTLLHI-AGLLEqADEGEVYvggtatsglsdvertqirrTDIGFVYQSHRLLPEFSA-----LEN 112
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLlAGVLK-PDEGEVD-------------------PELKISYKPQYIKPDYDGtvedlLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 113 VmlPQMIRGLPKKEtvkrskEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKA 192
Cdd:PRK13409 424 I--TDDLGSSYYKS------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 495
|
170 180 190
....*....|....*....|....*....|
gi 640481818 193 LTQLVRATRVAMLIATHN---MDLAArmDR 219
Cdd:PRK13409 496 IRRIAEEREATALVVDHDiymIDYIS--DR 523
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
28-210 |
2.69e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 49.68 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 28 TILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLE-QADEGEVYVGGTATSGLSDVERTqirRTDIGFVYQSHrllP 105
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKvLMGHPKyEVTSGSILLDGEDILELSPDERA---RAGIFLAFQYP---V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 106 EF----------SALENVMLPQMirglPKKETVKRSKEILAYLGLAERVTHRP--AELSGGEQQRVAIARAVANAPRVLL 173
Cdd:COG0396 88 EIpgvsvsnflrTALNARRGEEL----SAREFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 640481818 174 ADEPTGNLDphtADhVFKALTQLVRATR---VAMLIATHN 210
Cdd:COG0396 164 LDETDSGLD---ID-ALRIVAEGVNKLRspdRGILIITHY 199
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-230 |
1.64e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.17 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 24 EATLTILDGASLALWEGQSVALVAPSGTGKSTLLhiAGLLEQAD--EGEVYvggtatsgLSDVERTQIR----RTDIGFV 97
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLL--SLIQRHFDvsEGDIR--------FHDIPLTKLQldswRSRLAVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 98 YQSHRLLPEfSALENVML------PQMIRGLPKKETVKrsKEILAY-LGLAERVTHRPAELSGGEQQRVAIARAVANAPR 170
Cdd:PRK10789 395 SQTPFLFSD-TVANNIALgrpdatQQEIEHVARLASVH--DDILRLpQGYDTEVGERGVMLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 171 VLLADEPTGNLDPHTADHVFKALTQLVRATRVamLIATHNMDLAARMDRRVSLQDGHVIE 230
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGEGRTV--IISAHRLSALTEASEILVMQHGHIAQ 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
151-182 |
2.23e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 2.23e-06
10 20 30
....*....|....*....|....*....|..
gi 640481818 151 LSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
44-218 |
2.43e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.45 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 44 ALVAPSGTGKSTLLHIaglLEQADEGEVYVGGTATSGLSDV-----ERTQIR---RTDIGFVYQSHRllpEFSALENV-M 114
Cdd:cd03240 26 LIVGQNGAGKTTIIEA---LKYALTGELPPNSKGGAHDPKLiregeVRAQVKlafENANGKKYTITR---SLAILENViF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 115 LPQmirglpkketvkrsKEILAYLgLAERVThrpaeLSGGEQQ------RVAIARAV-ANAPrVLLADEPTGNLDPhtaD 187
Cdd:cd03240 100 CHQ--------------GESNWPL-LDMRGR-----CSGGEKVlasliiRLALAETFgSNCG-ILALDEPTTNLDE---E 155
|
170 180 190
....*....|....*....|....*....|....*
gi 640481818 188 HVFKALTQLVRATRVA----MLIATHNMDLAARMD 218
Cdd:cd03240 156 NIEESLAEIIEERKSQknfqLIVITHDEELVDAAD 190
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
29-209 |
3.14e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQADEGEVYV-GGTATSG--LSDVERtqirrtDIGFVyqSHRLL 104
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSlITGDHPQGYSNDLTLfGRRRGSGetIWDIKK------HIGYV--SSSLH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 105 PEF---SALENVMLPQMIRGLPKKETV-----KRSKEILAYLGLAERVTHRP-AELSGGEQQRVAIARAVANAPRVLLAD 175
Cdd:PRK10938 347 LDYrvsTSVRNVILSGFFDSIGIYQAVsdrqqKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILD 426
|
170 180 190
....*....|....*....|....*....|....
gi 640481818 176 EPTGNLDPHTADHVFKALTQLVRATRVAMLIATH 209
Cdd:PRK10938 427 EPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-207 |
3.23e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 26 TLTILDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQADEGevyVGGTAT-SGLSDVERTQIRRTDIGFVYQSHRL 103
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKtIASNTDGFHIG---VEGVITyDGITPEEIKKHYRGDVVYNAETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 104 LP--------EFSALenVMLPQM-IRGLPKKETVKRSKE-ILAYLGLAE-RVTHRPAEL----SGGEQQRVAIARAVANA 168
Cdd:TIGR00956 150 FPhltvgetlDFAAR--CKTPQNrPDGVSREEYAKHIADvYMATYGLSHtRNTKVGNDFvrgvSGGERKRVSIAEASLGG 227
|
170 180 190
....*....|....*....|....*....|....*....
gi 640481818 169 PRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIA 207
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA 266
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-232 |
3.64e-06 |
|
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: 46.77 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 21 KQGEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHiAGLLEQADEGEVYVGGTATSGLSdverTQIRRTDIGFV--- 97
Cdd:cd03289 11 KYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLS-AFLRLLNTEGDIQIDGVSWNSVP----LQKWRKAFGVIpqk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 98 --------------YQSHRLLPEFSALENVMLPQMIRGLPKKETVkrskeILAYLGLAervthrpaeLSGGEQQRVAIAR 163
Cdd:cd03289 86 vfifsgtfrknldpYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDF-----VLVDGGCV---------LSHGHKQLMCLAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 164 AVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVamLIATHNMDLAARMDRRVSLQDGHVIELD 232
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTV--ILSEHRIEAMLECQRFLVIEENKVRQYD 218
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-182 |
5.92e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 26 TLTILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVERTQIRRTDIGFVYQSHRllp 105
Cdd:PRK10636 13 VRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIDGDR--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 106 EFSALENVMLPQMIRG--------LPKKETVK------RSKEILAYLGLAERVTHRP-AELSGGEQQRVAIARAVANAPR 170
Cdd:PRK10636 90 EYRQLEAQLHDANERNdghaiatiHGKLDAIDawtirsRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSD 169
|
170
....*....|..
gi 640481818 171 VLLADEPTGNLD 182
Cdd:PRK10636 170 LLLLDEPTNHLD 181
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
29-232 |
7.32e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 29 ILDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGG--TATSGLSDVertqirRTDIGFVYQSHRL--- 103
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdISKFGLMDL------RKVLGIIPQAPVLfsg 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 104 -----LPEFSALENVMLPQMIRGLPKKETVKRSKeilayLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPT 178
Cdd:PLN03130 1328 tvrfnLDPFNEHNDADLWESLERAHLKDVIRRNS-----LGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640481818 179 GNLDPHTADHVFKALTQLVRAtrVAMLIATHNMDLAARMDRRVSLQDGHVIELD 232
Cdd:PLN03130 1403 AAVDVRTDALIQKTIREEFKS--CTMLIIAHRLNTIIDCDRILVLDAGRVVEFD 1454
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-232 |
8.07e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.48 E-value: 8.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 19 RYKQGEATltILDGASLALWEGQSVALVAPSGTGKSTL-LHIAGLLEQAdEGEVYVGG--TATSGLSDV--ERTQIRRTD 93
Cdd:TIGR00957 1293 RYREDLDL--VLRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDGlnIAKIGLHDLrfKITIIPQDP 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 94 IGFVYQSHRLLPEFS---------ALENVMLPQMIRGLPKKetvkrskeilaylglaerVTHRPAE----LSGGEQQRVA 160
Cdd:TIGR00957 1370 VLFSGSLRMNLDPFSqysdeevwwALELAHLKTFVSALPDK------------------LDHECAEggenLSVGQRQLVC 1431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640481818 161 IARAVANAPRVLLADEPTGNLDPHTADHVFKAL-TQLVRATrvaMLIATHNMDLAARMDRRVSLQDGHVIELD 232
Cdd:TIGR00957 1432 LARALLRKTKILVLDEATAAVDLETDNLIQSTIrTQFEDCT---VLTIAHRLNTIMDYTRVIVLDKGEVAEFG 1501
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-228 |
1.16e-05 |
|
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: 45.59 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 30 LDGASLALWEGQSVALVAPSGTGKSTLLH-IAGLLEQADEGEVYVGGTATSGLSDVertQIRRTDIGFV---YQSHRLLP 105
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPA---QAIRAGIAMVpedRKRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 106 EFSALENVMLPQMIRgLPKKETVKRSKEILAYLGLAERVTHRPAE-------LSGGEQQRVAIARAVANAPRVLLADEPT 178
Cdd:TIGR02633 353 ILGVGKNITLSVLKS-FCFKMRIDAAAELQIIGSAIQRLKVKTASpflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 640481818 179 GNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHV 228
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
26-176 |
1.41e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 26 TLTILDGASLALWEGQSVALVAPSGTGKSTLLHIaglleqadegevyVGGTATSGLSDVErtqiRRTDIGFVYQSHRLLP 105
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNI-------------IGGSLSPTVGKVD----RNGEVSVIAISAGLSG 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640481818 106 EFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADE 176
Cdd:PRK13546 99 QLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
9-176 |
2.30e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.88 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 9 PVVYLHDVRRRYKQGEATLTiLDGASLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTAT-----SGLSD 83
Cdd:PRK13545 20 PFDKLKDLFFRSKDGEYHYA-LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAliaisSGLNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 84 vertqirrtdigfvyqshrllpEFSALENVMLPQMIRGLPKKETVKRSKEILAYLGLAERVTHRPAELSGGEQQRVAIAR 163
Cdd:PRK13545 99 ----------------------QLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAI 156
|
170
....*....|...
gi 640481818 164 AVANAPRVLLADE 176
Cdd:PRK13545 157 SVHINPDILVIDE 169
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
135-231 |
2.40e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.14 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 135 LAYLGLAERVThrpaELSGGEQQRVAIARAVANAPR---VLLADEPTGNLDPHTADHVFKALTQLVRATRvAMLIATHNM 211
Cdd:cd03271 158 LGYIKLGQPAT----TLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNL 232
|
90 100
....*....|....*....|
gi 640481818 212 DLAARMDrrvslqdgHVIEL 231
Cdd:cd03271 233 DVIKCAD--------WIIDL 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
151-228 |
3.22e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.27 E-value: 3.22e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 151 LSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKaLTQLVRATRVAMLIATHNMDLAARM-DRRVSLQDGHV 228
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQ-LIRSIAAQNVAVLFISSDLEEIEQMaDRVLVMHQGEI 481
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
143-226 |
3.23e-05 |
|
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: 42.94 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 143 RVTHRPA--ELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRR 220
Cdd:cd03222 62 TPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDR 141
|
....*.
gi 640481818 221 VSLQDG 226
Cdd:cd03222 142 IHVFEG 147
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
43-182 |
3.25e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 43 VALVAPSGTGKSTLLH-IAGLLEqadegevyvggtATSGlsDVERTQIRRtdIGFVYQSHRLLPEFSALENVMLPQMIRG 121
Cdd:PLN03073 538 IAMVGPNGIGKSTILKlISGELQ------------PSSG--TVFRSAKVR--MAVFSQHHVDGLDLSSNPLLYMMRCFPG 601
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640481818 122 LPKKetvkRSKEILAYLGLAERVTHRPA-ELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:PLN03073 602 VPEQ----KLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
149-198 |
4.94e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 4.94e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 640481818 149 AELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVR 198
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ 453
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
39-224 |
5.89e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.58 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 39 EGQSVALVAPSGTGKSTLLHIAGLLeqadeGEVYvGGTatsglsdveRTQIRRTDIGFVYQShrllPEFSA---LENVML 115
Cdd:TIGR00954 477 SGNNLLICGPNGCGKSSLFRILGEL-----WPVY-GGR---------LTKPAKGKLFYVPQR----PYMTLgtlRDQIIY 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 116 P----QMI-RGLPKKETVKRSKEI-LAYL----GLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHT 185
Cdd:TIGR00954 538 PdsseDMKrRGLSDKDLEQILDNVqLTHIlereGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 640481818 186 ADHVFKALTQ----LVRATRVAMLIATHNMDLaaRMDRRVSLQ 224
Cdd:TIGR00954 618 EGYMYRLCREfgitLFSVSHRKSLWKYHEYLL--YMDGRGGYQ 658
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
10-229 |
6.38e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 10 VVYLHDVRRRYKQ---GEATLTILDGASLALWEGQSVALVAPSGTGKSTLLHIaglLEQADEGEVYVGGTATSGLSDVER 86
Cdd:PLN03140 873 VNYFVDMPAEMKEqgvTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDV---LAGRKTGGYIEGDIRISGFPKKQE 949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 87 TQIRRTdiGFVYQSHRLLPEFSALENVMLPQMIRgLPkKETVKRSK--------EILAYLGLAERVTHRPA--ELSGGEQ 156
Cdd:PLN03140 950 TFARIS--GYCEQNDIHSPQVTVRESLIYSAFLR-LP-KEVSKEEKmmfvdevmELVELDNLKDAIVGLPGvtGLSTEQR 1025
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 157 QRVAIA-RAVANaPRVLLADEPTGNLDPHTADHVFKALTQLVRATR-VAMLIATHNMDLAARMDRRVSLQ-DGHVI 229
Cdd:PLN03140 1026 KRLTIAvELVAN-PSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRtVVCTIHQPSIDIFEAFDELLLMKrGGQVI 1100
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
151-228 |
7.78e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 7.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640481818 151 LSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHV 228
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-231 |
1.31e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 133 EILAYLGLAERVTHRP-AELSGGEQQRVAIARAVANA---PRVLLADEPTGNLdpHTAD-----HVFKALTQLVRatrvA 203
Cdd:PRK00635 791 HALCSLGLDYLPLGRPlSSLSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGL--HTHDikaliYVLQSLTHQGH----T 864
|
90 100
....*....|....*....|....*...
gi 640481818 204 MLIATHNMDLAARMDrrvslqdgHVIEL 231
Cdd:PRK00635 865 VVIIEHNMHVVKVAD--------YVLEL 884
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
151-219 |
1.88e-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: 40.81 E-value: 1.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640481818 151 LSGGEQQRVAIARAVANA---PRVLLA-DEPTGNLDPHTAdhvfKALTQLVRATRVA---MLIATHNMDLAARMDR 219
Cdd:cd03227 78 LSGGEKELSALALILALAslkPRPLYIlDEIDRGLDPRDG----QALAEAILEHLVKgaqVIVITHLPELAELADK 149
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
40-232 |
4.82e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 40.28 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 40 GQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSdverTQIRRTDIGFVYQSHRLL---------PE---- 106
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP----LHTLRSRLSIILQDPILFsgsirfnldPEckct 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 107 ----FSALENVMLPQMIRGLPKketvkrskeilaylGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLD 182
Cdd:cd03288 123 ddrlWEALEIAQLKNMVKSLPG--------------GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASID 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 640481818 183 PHTaDHVFKALTQLVRATRVAMLIAtHNMDLAARMDRRVSLQDGHVIELD 232
Cdd:cd03288 189 MAT-ENILQKVVMTAFADRTVVTIA-HRVSTILDADLVLVLSRGILVECD 236
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
135-231 |
5.26e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 135 LAYLGLAERVThrpaELSGGEQQRVAIAR---AVANAPRVLLADEPTGNLdpHTAD--HVFKALTQLVRATRVAMLIaTH 209
Cdd:TIGR00630 818 LGYIRLGQPAT----TLSGGEAQRIKLAKelsKRSTGRTLYILDEPTTGL--HFDDikKLLEVLQRLVDKGNTVVVI-EH 890
|
90 100
....*....|....*....|..
gi 640481818 210 NMDLAARMDrrvslqdgHVIEL 231
Cdd:TIGR00630 891 NLDVIKTAD--------YIIDL 904
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
11-232 |
7.52e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.96 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 11 VYLHDVRRRYKQGEATLTILDgasLALWEGQSVALVAPSGTGKSTLLHIAGLLEQADEGEVYVGGTATSGLSDVErtqir 90
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPIN---LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED----- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 91 rtdigfvYQSHrllpeFSAL-ENVMLPQMIRGlPKKETV--KRSKEILAYLGLAERVTHRPAE-----LSGGEQQRVAIA 162
Cdd:PRK10522 395 -------YRKL-----FSAVfTDFHLFDQLLG-PEGKPAnpALVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALL 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 163 RAVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIATHNMDLAARMDRRVSLQDGHVIELD 232
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELT 531
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
130-209 |
1.04e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 130 RSKEILAYLGLAERVTHRP-AELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTadhvFKALTQLVRATRVAMLIAT 208
Cdd:PRK15064 134 RAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIIS 209
|
.
gi 640481818 209 H 209
Cdd:PRK15064 210 H 210
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
49-187 |
1.21e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.70 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 49 SGTGKSTLLHIAGLLEQADEGEVYVGGTATSglsdvertQIRRTDIGFVYQSHRLLPEFSALENVMLPQMIRGlpKKETV 128
Cdd:PRK13541 35 NGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN--------NIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYN--SAETL 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 640481818 129 KRSkeiLAYLGLAERVTHRPAELSGGEQQRVAIARAVANAPRVLLADEPTGNLDPHTAD 187
Cdd:PRK13541 105 YAA---IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
151-219 |
1.95e-03 |
|
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: 37.69 E-value: 1.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640481818 151 LSGGEQQRVAIAR--AVANAPRVLLADEPTGNLDPHTADHVFKALTQLVRATRVAMLIaTHNMDLAARMDR 219
Cdd:cd03238 88 LSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILI-EHNLDVLSSADW 157
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
141-231 |
9.01e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 37.05 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640481818 141 AERVTHRPAELSGG--EQ----QRVAIARAVANAPRVLLADEPTGNLDPHTADHVFKALTQLvrATRVAMLIATHNMDLA 214
Cdd:COG4717 549 EDGRTRPVEELSRGtrEQlylaLRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAEL--AKGRQVIYFTCHEELV 626
|
90
....*....|....*..
gi 640481818 215 ARMDRrvslQDGHVIEL 231
Cdd:COG4717 627 ELFQE----EGAHVIEL 639
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
7-66 |
9.02e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 35.98 E-value: 9.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640481818 7 GVPVVYLHDvrrryKQGEATLTILdgaslALWEGQSVALVAPSGTGKSTLL-HIAGLLEQA 66
Cdd:pfam03193 83 GYPVLFVSA-----KTGEGIEALK-----ELLKGKTTVLAGQSGVGKSTLLnALLPELDLR 133
|
|
| |
