|
Name |
Accession |
Description |
Interval |
E-value |
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-210 |
3.24e-114 |
|
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: 326.31 E-value: 3.24e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTFDMHVLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIDLASC 81
Cdd:COG4778 3 TLLEVENLSKTFTLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 82 PDRTVIDLRGDSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLWQAYPATFSGGERQRVN 161
Cdd:COG4778 83 SPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493478021 162 LAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHD 211
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
4-210 |
9.81e-83 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 246.53 E-value: 9.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDMHVLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIDLASCPD 83
Cdd:TIGR02324 2 LEVEDLSKTFTLHQQGGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEGAWVDLAQASP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RTVIDLRGDSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLWQAYPATFSGGERQRVNLA 163
Cdd:TIGR02324 82 REVLEVRRKTIGYVSQFLRVIPRVSALEVVAEPLLERGVPREAARARARELLARLNIPERLWHLPPATFSGGEQQRVNIA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493478021 164 QALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:TIGR02324 162 RGFIADYPILLLDEPTASLDAANRQVVVELIAEAKARGAALIGIFHD 208
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-210 |
2.21e-54 |
|
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: 174.22 E-value: 2.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDMhvlGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPD 83
Cdd:cd03255 1 IELKNLSKTYGG---GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRV----DGTDISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RTVIDLRGDSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLwQAYPATFSGGERQRVNLA 163
Cdd:cd03255 74 KELAAFRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRL-NHYPSELSGGQQQRVAIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493478021 164 QALAPKPDLLLLDEPTSALDPDTRRAAIDLL-STYLGSETTVVGVFHN 210
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVTHD 200
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-194 |
3.68e-51 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 165.99 E-value: 3.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTFDMhvlGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASC 81
Cdd:COG1136 3 PLLELRNLTKSYGT---GEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLI----DGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 82 PDRTVIDLRGDSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLwQAYPATFSGGERQRVN 161
Cdd:COG1136 76 SERELARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRL-DHRPSQLSGGQQQRVA 154
|
170 180 190
....*....|....*....|....*....|...
gi 493478021 162 LAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELL 187
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-194 |
9.61e-51 |
|
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: 172.78 E-value: 9.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTFDMHVLGDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLASC 81
Cdd:COG1123 259 PLLEVRNLSKRYPVRGKGGVRAV--DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF---DG-KDLTKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 82 PDRTVIDLRGDsIGY-----TSQFldeIPRVPAVDVVARPLIEQGV-DREDARSVARDLLSALSVPESLWQAYPATFSGG 155
Cdd:COG1123 333 SRRSLRELRRR-VQMvfqdpYSSL---NPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLADRYPHELSGG 408
|
170 180 190
....*....|....*....|....*....|....*....
gi 493478021 156 ERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLL 447
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-194 |
1.03e-48 |
|
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: 159.98 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDmhvLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdgDIDLAScP 82
Cdd:cd03257 1 LLEVKNLSVSFP---TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD----GKDLLK-L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTVIDLRGDSIGYTSQ----FLDeiPRVPAVDVVARPLIEQGVDR--EDARSVARDLLSALSVPESLWQAYPATFSGGE 156
Cdd:cd03257 73 SRRLRKIRRKEIQMVFQdpmsSLN--PRMTIGEQIAEPLRIHGKLSkkEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQ 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 493478021 157 RQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLL 188
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-194 |
1.32e-48 |
|
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: 162.53 E-value: 1.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDMHVlGDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDP---SSGEVVYHspdgDIDLA 79
Cdd:COG0444 1 LLEVRNLKVYFPTRR-GVVKAV--DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFD----GEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 80 SCPDRTVIDLRGDSIG------YTSqfLDeiPRVPAVDVVARPLIE-QGVDREDARSVARDLLSA--LSVPESLWQAYPA 150
Cdd:COG0444 74 KLSEKELRKIRGREIQmifqdpMTS--LN--PVMTVGDQIAEPLRIhGGLSKAEARERAIELLERvgLPDPERRLDRYPH 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493478021 151 TFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLL 193
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-210 |
3.18e-42 |
|
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: 143.00 E-value: 3.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDmhvLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdidlascpd 83
Cdd:cd03293 1 LEVRNVSKTYG---GGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLV---DG--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 rTVIDLRGDSIGYTSQ----FldeiPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLwQAYPATFSGGERQR 159
Cdd:cd03293 66 -EPVTGPGPDRGYVFQqdalL----PWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFE-NAYPHQLSGGMRQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493478021 160 VNLAQALAPKPDLLLLDEPTSALDPDTRRAAID-LLSTYLGSETTVVGVFHN 210
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEeLLDIWRETGKTVLLVTHD 191
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-194 |
1.13e-41 |
|
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: 143.17 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTF--------DMHVLGDT---------QVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGE 66
Cdd:cd03294 1 IKIKGLYKIFgknpqkafKLLAKGKSkeeilkktgQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 67 VVYhspDGDiDLASCPDRTVIDLRGDSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVpESLWQ 146
Cdd:cd03294 81 VLI---DGQ-DIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGL-EGWEH 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493478021 147 AYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:cd03294 156 KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDEL 203
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-229 |
3.32e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 139.95 E-value: 3.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDMHVLgdtqvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdgDIDLASCPd 83
Cdd:COG4619 1 LELEGLSFRVGGKPI-------LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLD----GKPLSAMP- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 rtVIDLRGdSIGY---TSQFLDEIPRvpavDVVARPLieQGVDREDARSVARDLLSALSVPESLWQAYPATFSGGERQRV 160
Cdd:COG4619 69 --PPEWRR-QVAYvpqEPALWGGTVR----DNLPFPF--QLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 161 NLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSE-TTVVGVFHNTDVVDAVADRVVVLDDGRL 229
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-237 |
9.51e-41 |
|
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: 146.20 E-value: 9.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MT-VLSVDGLSKTFdmhvlGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRtYDPSSGEVVYHSPDGDIDLA 79
Cdd:COG1123 1 MTpLLEVRDLSVRY-----PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRISGEVLLDGRDLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 80 SCPDRtvidLRGDSIGYTSQ-FLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQ 158
Cdd:COG1123 75 ELSEA----LRGRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 159 RVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTyLGSE--TTVVGVFHNTDVVDAVADRVVVLDDGRLQRVVPTE 236
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRE-LQRErgTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
.
gi 493478021 237 A 237
Cdd:COG1123 229 E 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-194 |
1.52e-40 |
|
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: 139.11 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTFDmhvLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLASC 81
Cdd:COG4181 7 PIIELRGLTKTVG---TGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRL---AG-QDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 82 PDRTVIDLRGDSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDreDARSVARDLLSALSVPESLwQAYPATFSGGERQRVN 161
Cdd:COG4181 80 DEDARARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRL-DHYPAQLSGGEQQRVA 156
|
170 180 190
....*....|....*....|....*....|...
gi 493478021 162 LAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLL 189
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-194 |
3.71e-40 |
|
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: 138.40 E-value: 3.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDMHvlGDTQVVgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdgDIDLASCPD 83
Cdd:COG1124 2 LEVRNLSVSYGQG--GRRVPV-LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD----GRPVTRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RtviDLRGDsIG------YTSqfLDeiPRVPAVDVVARPLIEQGVDREDARsvARDLLSALSVPESLWQAYPATFSGGER 157
Cdd:COG1124 75 K---AFRRR-VQmvfqdpYAS--LH--PRHTVDRILAEPLRIHGLPDREER--IAELLEQVGLPPSFLDRYPHQLSGGQR 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 493478021 158 QRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLL 181
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-184 |
5.20e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 137.82 E-value: 5.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLAScP 82
Cdd:COG1126 1 MIEIENLHKSF-----GDLEV--LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITV----DGEDLTD-S 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTVIDLRGDsIGYTSQ----FldeiPRVPAVDVVARPLIE-QGVDREDARSVARDLLSALSVPESLwQAYPATFSGGER 157
Cdd:COG1126 69 KKDINKLRRK-VGMVFQqfnlF----PHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKA-DAYPAQLSGGQQ 142
|
170 180
....*....|....*....|....*..
gi 493478021 158 QRVNLAQALAPKPDLLLLDEPTSALDP 184
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDP 169
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-183 |
7.29e-40 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 139.87 E-value: 7.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDMH--VLGDT--QVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDL 78
Cdd:COG4608 7 LLEVRDLKKHFPVRggLFGRTvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILF---DG-QDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 79 ASCPDRTVIDLRG-------DSigYTSqfLDeiPRVPAVDVVARPLIEQGV-DREDARSVARDLLSALSVPESLWQAYPA 150
Cdd:COG4608 83 TGLSGRELRPLRRrmqmvfqDP--YAS--LN--PRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEHADRYPH 156
|
170 180 190
....*....|....*....|....*....|...
gi 493478021 151 TFSGGERQRVNLAQALAPKPDLLLLDEPTSALD 183
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-234 |
1.22e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 136.34 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDmhvlgdTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCP 82
Cdd:COG2884 1 MIRFENVSKRYP------GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLV----NGQDLSRLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTVIDLRgDSIGYTSQ-F-LdeIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLwQAYPATFSGGERQRV 160
Cdd:COG2884 71 RREIPYLR-RRIGVVFQdFrL--LPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKA-KALPHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493478021 161 NLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTY--LGseTTVVGVFHNTDVVDAVADRVVVLDDGRLQRVVP 234
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInrRG--TTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
2.35e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 136.76 E-value: 2.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFDmHVLGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYH-----SPDGD 75
Cdd:COG1116 5 APALELRGVSKRFP-TGGGGVTA--LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDgkpvtGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 76 I-----DLASCPDRTVIDlrgdsigytsqfldeiprvpavdVVARPLIEQGVDREDARSVARDLLSA--LSvpeSLWQAY 148
Cdd:COG1116 82 RgvvfqEPALLPWLTVLD-----------------------NVALGLELRGVPKAERRERARELLELvgLA---GFEDAY 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493478021 149 PATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSE-TTVVGVFHN 210
Cdd:COG1116 136 PHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgKTVLFVTHD 198
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-209 |
1.02e-38 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 133.81 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDG-DIDLascP 82
Cdd:cd03262 1 IEIKNLHKSF-----GDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII---DGlKLTD---D 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTVIDLRgDSIGYTSQFLDEIPRVPAVDVVARPLIE-QGVDREDARSVARDLLSALSVPESLwQAYPATFSGGERQRVN 161
Cdd:cd03262 68 KKNINELR-QKVGMVFQQFNLFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKA-DAYPAQLSGGQQQRVA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493478021 162 LAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFH 209
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-205 |
3.52e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 132.88 E-value: 3.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmhvlGDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdgDIDLASCPD 83
Cdd:COG1131 1 IEVRGLTKRY-----GDKTAL--DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL----GEDVARDPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RtvidLRGdSIGYTSQFLDEIPRVPA---VDVVARpLieQGVDREDARSVARDLLSALSVPESLwQAYPATFSGGERQRV 160
Cdd:COG1131 70 E----VRR-RIGYVPQEPALYPDLTVrenLRFFAR-L--YGLPRKEARERIDELLELFGLTDAA-DRKVGTLSGGMKQRL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493478021 161 NLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:COG1131 141 GLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVL 185
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-180 |
5.28e-38 |
|
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: 130.08 E-value: 5.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDgdidlascPDRTVIDLRGDSIGYTSQFLDEIP 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD--------LTDDERKSLRKEIGYVFQDPQLFP 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493478021 106 RVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPE---SLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTS 180
Cdd:pfam00005 73 RLTVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-194 |
1.09e-37 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 132.10 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTFDmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASC 81
Cdd:COG3638 1 PMLELRNLSKRYP----GGTPA--LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILV----DGQDVTAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 82 PDRTVIDLRGDsIGYTSQFLDEIPRVPAVDVV------ARPLIE---QGVDREDaRSVARDLLSALSVPESLWQayPA-T 151
Cdd:COG3638 71 RGRALRRLRRR-IGMIFQQFNLVPRLSVLTNVlagrlgRTSTWRsllGLFPPED-RERALEALERVGLADKAYQ--RAdQ 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493478021 152 FSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLL 189
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-209 |
5.10e-37 |
|
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: 129.18 E-value: 5.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPd 83
Cdd:cd03259 1 LELKGLSKTY-----GSVRA--LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI----DGRDVTGVP- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 rtvIDLRGdsIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLwQAYPATFSGGERQRVNLA 163
Cdd:cd03259 69 ---PERRN--IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLL-NRYPHELSGGQQQRVALA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493478021 164 QALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGS-ETTVVGVFH 209
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTH 189
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-194 |
6.09e-37 |
|
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: 130.00 E-value: 6.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPD 83
Cdd:cd03256 1 IEVENLSKTYP----NGKKA--LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLI----DGTDINKLKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RTVIDLRGDsIGYTSQFLDEIPRVPAVDVV------ARPLIE---QGVDREDaRSVARDLLSALSVPESLWQAyPATFSG 154
Cdd:cd03256 71 KALRQLRRQ-IGMIFQQFNLIERLSVLENVlsgrlgRRSTWRslfGLFPKEE-KQRALAALERVGLLDKAYQR-ADQLSG 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493478021 155 GERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLL 187
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-188 |
1.47e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 131.76 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFdmhvlGDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspdgdIDlas 80
Cdd:COG3842 3 MPALELENVSKRY-----GDVTAL--DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIL-------LD--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 cpDRTVIDL----RGdsIGYTSQ----FldeiprvPAVDV---VARPLIEQGVDREDARSVARDLLSALSVpESLWQAYP 149
Cdd:COG3842 66 --GRDVTGLppekRN--VGMVFQdyalF-------PHLTVaenVAFGLRMRGVPKAEIRARVAELLELVGL-EGLADRYP 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 493478021 150 ATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRR 188
Cdd:COG3842 134 HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLRE 172
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-194 |
3.79e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 130.58 E-value: 3.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDMhvlGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLASCPD 83
Cdd:COG1135 2 IELENLSKTFPT---KGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLV---DG-VDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RTVIDLRGDsIGYTSQ-F--LDEipRVpAVDVVARPLIEQGVDREDARSVARDLLS-------AlsvpeslwQAYPATFS 153
Cdd:COG1135 75 RELRAARRK-IGMIFQhFnlLSS--RT-VAENVALPLEIAGVPKAEIRKRVAELLElvglsdkA--------DAYPSQLS 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493478021 154 GGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLL 183
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-194 |
6.19e-36 |
|
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: 127.31 E-value: 6.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDmhvLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdgDIDLASCP 82
Cdd:cd03258 1 MIELKNVSKVFG---DTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVD----GTDLTLLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTVIDLRGDsIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNL 162
Cdd:cd03258 74 GKELRKARRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGI 151
|
170 180 190
....*....|....*....|....*....|..
gi 493478021 163 AQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALL 183
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-194 |
1.09e-35 |
|
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: 132.50 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFDMHVlGDTQVVglDDVSFDVREGEFLAVVGESGSGKS----SLLKCLYRTYDPSSGEVVYHspdgDI 76
Cdd:COG4172 4 MPLLSVEDLSVAFGQGG-GTVEAV--KGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFD----GQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 77 DLASCPDRTVIDLRGDSIGY------TSqfLDEIPRVpaVDVVARPL-IEQGVDREDARSVARDLLSA--LSVPESLWQA 147
Cdd:COG4172 77 DLLGLSERELRRIRGNRIAMifqepmTS--LNPLHTI--GKQIAEVLrLHRGLSGAAARARALELLERvgIPDPERRLDA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493478021 148 YPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:COG4172 153 YPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLL 199
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-210 |
1.10e-35 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 125.66 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 5 SVDGLSKTFdmhvlGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLAscpDR 84
Cdd:cd03225 1 ELKNLSFSY-----PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV----DGKDLT---KL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 85 TVIDLRGDsIGYT-----SQFL-----DEiprvpavdvVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSG 154
Cdd:cd03225 69 SLKELRRK-VGLVfqnpdDQFFgptveEE---------VAFGLENLGLPEEEIEERVEEALELVGL-EGLRDRSPFTLSG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493478021 155 GERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:cd03225 138 GQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHD 193
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-210 |
1.50e-35 |
|
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: 125.93 E-value: 1.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDMhvlGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDiDLASCP 82
Cdd:TIGR02211 1 LLKCENLGKRYQE---GKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLF---NGQ-SLSKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTVIDLRGDSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLwQAYPATFSGGERQRVNL 162
Cdd:TIGR02211 74 SNERAKLRNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRI-NHRPSELSGGERQRVAI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493478021 163 AQALAPKPDLLLLDEPTSALDPDTRRAAIDLLsTYLGSE--TTVVGVFHN 210
Cdd:TIGR02211 153 ARALVNQPSLVLADEPTGNLDNNNAKIIFDLM-LELNRElnTSFLVVTHD 201
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-205 |
2.43e-35 |
|
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: 123.66 E-value: 2.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDgdidlascPD 83
Cdd:cd03230 1 IEVRNLSKRY-----GKKTA--LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD--------IK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RTVIDLRGDsIGYtsqfldeiprVPavdvvarplieqgvdrEDARsvardLLSALSVPESLwqaypaTFSGGERQRVNLA 163
Cdd:cd03230 66 KEPEEVKRR-IGY----------LP----------------EEPS-----LYENLTVRENL------KLSGGMKQRLALA 107
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493478021 164 QALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTIL 149
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-205 |
3.73e-35 |
|
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: 125.14 E-value: 3.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLAscpD 83
Cdd:COG1122 1 IELENLSFSYP----GGTPA--LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV----DGKDIT---K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RTVIDLRGDsIGYT-----SQFLDEIPRvpavDVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQ 158
Cdd:COG1122 68 KNLRELRRK-VGLVfqnpdDQLFAPTVE----EDVAFGPENLGLPREEIRERVEEALELVGL-EHLADRPPHELSGGQKQ 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493478021 159 RVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVI 188
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-210 |
5.67e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.82 E-value: 5.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFDMHVLgdtqvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDgdidlas 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPV-------LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 cpdrtvIDLRGDSIGYTSQFLDEIPRVPA-V-DVVA------RPLIeQGVDREDaRSVARDLLSALSVpESLWQAYPATF 152
Cdd:COG1121 70 ------PRRARRRIGYVPQRAEVDWDFPItVrDVVLmgrygrRGLF-RRPSRAD-REAVDEALERVGL-EDLADRPIGEL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493478021 153 SGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHD 198
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-188 |
2.97e-34 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 126.37 E-value: 2.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTF--------DMH--------VLGDT-QVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPS 63
Cdd:COG4175 1 MPKIEVRNLYKIFgkrperalKLLdqgkskdeILEKTgQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 64 SGEVVYHspdgDIDLASCPDRTVIDLRGDSIGYTSQ-FldeiprvpA-------VDVVARPLIEQGVDREDARSVARDLL 135
Cdd:COG4175 81 AGEVLID----GEDITKLSKKELRELRRKKMSMVFQhF--------AllphrtvLENVAFGLEIQGVPKAERRERAREAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493478021 136 SA--LSVPEslwQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRR 188
Cdd:COG4175 149 ELvgLAGWE---DSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRR 200
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
26-205 |
3.33e-34 |
|
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: 120.95 E-value: 3.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPDRtviDLRgDSIGYTSQfldeip 105
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI----DGVDLRDLDLE---SLR-KNIAYVPQ------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 rvpavdvvaRPLIEQGvdredarSVARDLLSalsvpeslwqaypatfsGGERQRVNLAQALAPKPDLLLLDEPTSALDPD 185
Cdd:cd03228 84 ---------DPFLFSG-------TIRENILS-----------------GGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180
....*....|....*....|
gi 493478021 186 TRRAAIDLLSTYLGSETTVV 205
Cdd:cd03228 131 TEALILEALRALAKGKTVIV 150
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-209 |
5.48e-34 |
|
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: 122.40 E-value: 5.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDiDLASCP 82
Cdd:COG1127 5 MIEVRNLTKSF-----GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV---DGQ-DITGLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTVIDLRgDSIGYTSQF---LDEIPrvpavdV---VARPLIEQG-VDREDARSVARDLLSALSVPESLWQaYPATFSGG 155
Cdd:COG1127 74 EKELYELR-RRIGMLFQGgalFDSLT------VfenVAFPLREHTdLSEAEIRELVLEKLELVGLPGAADK-MPSELSGG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493478021 156 ERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTY---LGseTTVVGVFH 209
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELrdeLG--LTSVVVTH 200
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-209 |
7.83e-34 |
|
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: 122.07 E-value: 7.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCP 82
Cdd:COG1120 1 MLEAENLSVGY-----GGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLL----DGRDLASLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTvidlRGDSIGYTSQFLDEIPRVPAVDVVAR---PLIE--QGVDREDaRSVARDLLSALSVpESLWQAYPATFSGGER 157
Cdd:COG1120 70 RRE----LARRIAYVPQEPPAPFGLTVRELVALgryPHLGlfGRPSAED-REAVEEALERTGL-EHLADRPVDELSGGER 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493478021 158 QRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSE-TTVVGVFH 209
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgRTVVMVLH 196
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-205 |
8.71e-34 |
|
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: 121.89 E-value: 8.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDmhvlgdtQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdgDIDLASCP 82
Cdd:COG4555 1 MIEVENLSKKYG-------KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID----GEDVRKEP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTVidlrgDSIGYtsqFLDEIPRVPAVDVvaRPLIE-----QGVDREDARSVARDLLSALSVPESLWQAYpATFSGGER 157
Cdd:COG4555 70 REAR-----RQIGV---LPDERGLYDRLTV--RENIRyfaelYGLFDEELKKRIEELIELLGLEEFLDRRV-GELSTGMK 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493478021 158 QRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:COG4555 139 KKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVL 186
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-209 |
2.06e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.97 E-value: 2.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 10 SKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLAScPDRTVIDL 89
Cdd:PRK09493 8 SKHF-----GPTQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIV---DG-LKVND-PKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 90 RGDSiGYTSQFLDEIPRVPAVDVVA-RPLIEQGVDREDARSVARDLLSALSVPESLwQAYPATFSGGERQRVNLAQALAP 168
Cdd:PRK09493 76 RQEA-GMVFQQFYLFPHLTALENVMfGPLRVRGASKEEAEKQARELLAKVGLAERA-HHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493478021 169 KPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFH 209
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
26-205 |
5.01e-33 |
|
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: 126.10 E-value: 5.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPDRtviDLRgDSIGYTSQ----F- 100
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI----DGIDLRQIDPA---SLR-RQIGVVLQdvflFs 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 101 ---LDEIprvpavdVVARPlieqGVDREDARSVARdLLSALSVPESLWQAYP-------ATFSGGERQRVNLAQALAPKP 170
Cdd:COG2274 563 gtiRENI-------TLGDP----DATDEEIIEAAR-LAGLHDFIEALPMGYDtvvgeggSNLSGGQRQRLAIARALLRNP 630
|
170 180 190
....*....|....*....|....*....|....*
gi 493478021 171 DLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:COG2274 631 RILILDEATSALDAETEAIILENLRRLLKGRTVII 665
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-229 |
5.74e-33 |
|
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: 119.05 E-value: 5.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 23 VVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdgDIDLASCPDRTVIDLRgDSIGYTSQFLD 102
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVN----GQDVSDLRGRAIPYLR-RKIGVVFQDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 103 EIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSAL 182
Cdd:cd03292 89 LLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493478021 183 DPDTRRAAIDLLSTYLGSETTVVGVFHNTDVVDAVADRVVVLDDGRL 229
Cdd:cd03292 168 DPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
26-232 |
8.39e-33 |
|
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: 119.33 E-value: 8.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPdrtVIDLRgDSIGYTSQFLDEIP 105
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFI----DGEDIREQD---PVELR-RKIGYVIQQIGLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 -RVPAVDVVARPLIEqGVDREDARSVARDLLSALSV-PESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALD 183
Cdd:cd03295 89 hMTVEENIALVPKLL-KWPKEKIRERADELLALVGLdPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493478021 184 PDTRRAAIDL---LSTYLGSetTVVGVFHNTDVVDAVADRVVVLDDGRLQRV 232
Cdd:cd03295 168 PITRDQLQEEfkrLQQELGK--TIVFVTHDIDEAFRLADRIAIMKNGEIVQV 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-194 |
1.05e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 118.76 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDMhvlGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPdgdiDLASCP 82
Cdd:PRK11629 5 LLQCDNLCKRYQE---GSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ----PMSKLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTVIDLRGDSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNL 162
Cdd:PRK11629 78 SAAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGL-EHRANHRPSELSGGERQRVAI 156
|
170 180 190
....*....|....*....|....*....|..
gi 493478021 163 AQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLL 188
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-194 |
1.24e-32 |
|
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: 124.03 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTFDMH--VLGDT--QVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRtYDPSSGEVVYHspdgDID 77
Cdd:COG4172 274 PLLEARDLKVWFPIKrgLFRRTvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFD----GQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 78 LASCPDRTVIDLRGDsIG------YTSqfLDeiPRVPAVDVVARPLI--EQGVDREDARSVARDLLSALSVPESLWQAYP 149
Cdd:COG4172 349 LDGLSRRALRPLRRR-MQvvfqdpFGS--LS--PRMTVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDPAARHRYP 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493478021 150 ATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:COG4172 424 HEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLL 468
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
9-228 |
4.37e-32 |
|
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: 116.58 E-value: 4.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 9 LSKTFDMHVLGdtqvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDiDLASCPDRTVID 88
Cdd:TIGR02673 7 VSKAYPGGVAA------LHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRI---AGE-DVNRLRGRQLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 89 LRgDSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLwQAYPATFSGGERQRVNLAQALAP 168
Cdd:TIGR02673 77 LR-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKA-DAFPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 169 KPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHNTDVVDAVADRVVVLDDGR 228
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-194 |
5.35e-32 |
|
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: 117.40 E-value: 5.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDmhvlgdTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdgdidlascp 82
Cdd:TIGR02315 1 MLEVENLSKVYP------NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLE------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTVIDLRGDS-------IGYTSQFLDEIPRVPAVDVV------ARPLIEQGVDR--EDARSVARDLLSALSVPEslwQA 147
Cdd:TIGR02315 63 GTDITKLRGKKlrklrrrIGMIFQHYNLIERLTVLENVlhgrlgYKPTWRSLLGRfsEEDKERALSALERVGLAD---KA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493478021 148 Y--PATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:TIGR02315 140 YqrADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYL 188
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
26-228 |
1.20e-31 |
|
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: 113.88 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdgDIDLASCPDRTVIDLrgdsIGYTSQFldeip 105
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID----GKDIAKLPLEELRRR----IGYVPQL----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 rvpavdvvarplieqgvdredarsvardllsalsvpeslwqaypatfSGGERQRVNLAQALAPKPDLLLLDEPTSALDPD 185
Cdd:cd00267 82 -----------------------------------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493478021 186 TRRAAIDLLSTYLGSETTVVGVFHNTDVVDAVADRVVVLDDGR 228
Cdd:cd00267 115 SRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-236 |
1.31e-31 |
|
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: 115.74 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYD-----PSSGEVVYhspDGDIDL 78
Cdd:cd03260 1 IELRDLNVYY-----GDKHA--LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLL---DGKDIY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 79 AscPDRTVIDLRgDSIGYTSQFLDEIPrVPAVDVVARPLIEQGV-DREDARSVARDLLS--ALSvPESLWQAYPATFSGG 155
Cdd:cd03260 71 D--LDVDVLELR-RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRkaALW-DEVKDRLHALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 156 ERQRVNLAQALAPKPDLLLLDEPTSALDPdTRRAAIDLLSTYLGSETTVVGVFHNTDVVDAVADRVVVLDDGRLQRVVPT 235
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
.
gi 493478021 236 E 236
Cdd:cd03260 225 E 225
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
22-210 |
1.83e-31 |
|
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: 116.78 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 22 QVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPDRTVIDLRGDsIGYTSQF- 100
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTI----DGRDITAKKKKKLKDLRKK-VGLVFQFp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 101 ---------LDEI---PRvpavdvvarpliEQGVDREDARSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAP 168
Cdd:TIGR04521 92 ehqlfeetvYKDIafgPK------------NLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493478021 169 KPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSE-TTVVGVFHN 210
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKgLTVILVTHS 202
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-188 |
5.76e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 116.78 E-value: 5.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIDLaSCPD 83
Cdd:COG1118 3 IEVRNISKRF-----GSFTL--LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNL-PPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RtvidlrgdSIGYTSQ----F-----LDEI---PRVpavdvvarplieQGVDREDARSVARDLLSALSVpESLWQAYPAT 151
Cdd:COG1118 75 R--------RVGFVFQhyalFphmtvAENIafgLRV------------RPPSKAEIRARVEELLELVQL-EGLADRYPSQ 133
|
170 180 190
....*....|....*....|....*....|....*..
gi 493478021 152 FSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRR 188
Cdd:COG1118 134 LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRK 170
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-195 |
7.10e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 116.44 E-value: 7.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 8 GLSKTFDmhvLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLASCPDRTVI 87
Cdd:PRK11153 6 NISKVFP---QGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLV---DG-QDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 88 DLRgDSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLsALSVPESLWQAYPATFSGGERQRVNLAQALA 167
Cdd:PRK11153 79 KAR-RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELL-ELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180
....*....|....*....|....*...
gi 493478021 168 PKPDLLLLDEPTSALDPDTRRAAIDLLS 195
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLK 184
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
19-209 |
1.02e-30 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 112.14 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 19 GDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPDRTvidlRGDSIGYTS 98
Cdd:cd03214 10 GGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL----DGKDLASLSPKE----LARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 99 QFLDeiprvpAVDVvaRPLIEQGVDredarsvardllsalsvpeslwqaypaTFSGGERQRVNLAQALAPKPDLLLLDEP 178
Cdd:cd03214 80 QALE------LLGL--AHLADRPFN---------------------------ELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190
....*....|....*....|....*....|..
gi 493478021 179 TSALDPDTRRAAIDLLSTYLGSE-TTVVGVFH 209
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERgKTVVMVLH 156
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
26-210 |
1.73e-30 |
|
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: 112.24 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEvvyhspdgdIDLASCPdrtvIDLRGDSIGYTSQFLDEIP 105
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGS---------IRVFGKP----LEKERKRIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPAV--DVVA-----------------RPLIEQGVDREDARSVARDLLSALSvpeslwqaypatfsGGERQRVNLAQAL 166
Cdd:cd03235 82 DFPISvrDVVLmglyghkglfrrlskadKAKVDEALERVGLSELADRQIGELS--------------GGQQQRVLLARAL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493478021 167 APKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHD 191
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-209 |
2.28e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.56 E-value: 2.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFdmhvlGDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspdgdIDlas 80
Cdd:COG3839 1 MASLELENVSKSY-----GGVEAL--KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIL-------IG--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 cpDRTVIDL----RGdsIGYTSQFldeiprvPAV-------DVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYP 149
Cdd:COG3839 64 --GRDVTDLppkdRN--IAMVFQS-------YALyphmtvyENIAFPLKLRKVPKAEIDRRVREAAELLGL-EDLLDRKP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493478021 150 ATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTR---RAAIDLLSTYLGseTTVVGVFH 209
Cdd:COG3839 132 KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRvemRAEIKRLHRRLG--TTTIYVTH 192
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-185 |
3.27e-30 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 112.92 E-value: 3.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFDmhvlGDTQVVGLDdvsFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDL-A 79
Cdd:PRK11264 1 MSAIEVKNLVKKFH----GQTVLHGID---LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV----GDITIdT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 80 SCP----DRTVIDLRgDSIGYTSQFLDEIPRVPAVD-VVARPLIEQGVDREDARSVARDLLS--ALSVPESlwqAYPATF 152
Cdd:PRK11264 70 ARSlsqqKGLIRQLR-QHVGFVFQNFNLFPHRTVLEnIIEGPVIVKGEPKEEATARARELLAkvGLAGKET---SYPRRL 145
|
170 180 190
....*....|....*....|....*....|...
gi 493478021 153 SGGERQRVNLAQALAPKPDLLLLDEPTSALDPD 185
Cdd:PRK11264 146 SGGQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-194 |
4.50e-30 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 112.65 E-value: 4.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFDMhvlGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyhSPDGDIDLAS 80
Cdd:COG4525 1 MSMLTVRHVSVRYPG---GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI---TLDGVPVTGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 CPDRTVIdlrgdsigytsqFLDE--IPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQ 158
Cdd:COG4525 75 GADRGVV------------FQKDalLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGL-ADFARRRIWQLSGGMRQ 141
|
170 180 190
....*....|....*....|....*....|....*.
gi 493478021 159 RVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELL 177
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-210 |
6.87e-30 |
|
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: 109.97 E-value: 6.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIDLASCPD 83
Cdd:cd03229 1 LELKNVSKRY-----GQKTV--LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RTvidlrgDSIGYtsqfldeiprvpavdvvarpLIEQGVdredarsvardLLSALSVPESLwqAYPatFSGGERQRVNLA 163
Cdd:cd03229 74 LR------RRIGM--------------------VFQDFA-----------LFPHLTVLENI--ALG--LSGGQQQRVALA 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493478021 164 QALAPKPDLLLLDEPTSALDPDTRRAAIDLLST-YLGSETTVVGVFHN 210
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSlQAQLGITVVLVTHD 160
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-205 |
2.17e-29 |
|
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: 115.25 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDmhvlGDTQVVgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPD 83
Cdd:COG4987 334 LELEDVSFRYP----GAGRPV-LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL----GGVDLRDLDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RtviDLRgDSIGYTSQfldeipRVPAVD-------VVARPlieqGVDREDARSVAR-----DLLSALsvPESL--W-QAY 148
Cdd:COG4987 405 D---DLR-RRIAVVPQ------RPHLFDttlrenlRLARP----DATDEELWAALErvglgDWLAAL--PDGLdtWlGEG 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493478021 149 PATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:COG4987 469 GRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLL 525
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-209 |
3.16e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.39 E-value: 3.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 6 VDGLSKTFDMHVLgdtqvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyHSPDGDI-----DLAS 80
Cdd:COG0488 1 LENLSKSFGGRPL-------LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS-IPKGLRIgylpqEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 CPDRTVID--LRGDS-IGYTSQFLDEI---PRVPAVDVVARPLIEQGVDRED---ARSVARDLLSALSVPESLWQAYPAT 151
Cdd:COG0488 73 DDDLTVLDtvLDGDAeLRALEAELEELeakLAEPDEDLERLAELQEEFEALGgweAEARAEEILSGLGFPEEDLDRPVSE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493478021 152 FSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTrraaIDLLSTYL-GSETTVVGVFH 209
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLkNYPGTVLVVSH 207
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-209 |
6.23e-29 |
|
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: 109.13 E-value: 6.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDG-DIDLASCP 82
Cdd:cd03261 1 IELRGLTKSF-----GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI---DGeDISGLSEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTVIDLRgdsIGYTSQFldeiprvPA-------VDVVARPLIEQGV-DREDARSVARDLLSALSVPESLwQAYPATFSG 154
Cdd:cd03261 71 ELYRLRRR---MGMLFQS-------GAlfdsltvFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAE-DLYPAELSG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493478021 155 GERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTY---LGseTTVVGVFH 209
Cdd:cd03261 140 GMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkeLG--LTSIMVTH 195
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-210 |
1.34e-28 |
|
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: 108.19 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTfdmhvLGDTQvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDG-DIDLAScP 82
Cdd:cd03299 1 LKVENLSKD-----WKEFK---LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL---NGkDITNLP-P 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRtvidlRGDSIGYTSQFLdeIPRVPAVDVVARPLIEQGVDR-EDARSVaRDLLSALSVpESLWQAYPATFSGGERQRVN 161
Cdd:cd03299 69 EK-----RDISYVPQNYAL--FPHMTVYKNIAYGLKKRKVDKkEIERKV-LEIAEMLGI-DHLLNRKPETLSGGEQQRVA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493478021 162 LAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYL-GSETTVVGVFHN 210
Cdd:cd03299 140 IARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRkEFGVTVLHVTHD 189
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-205 |
1.63e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 112.95 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 19 GDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDG----DIDLAScpdrtvidLRgDSI 94
Cdd:COG1132 351 GDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI---DGvdirDLTLES--------LR-RQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 95 GYTSQfldeiprvpavDVV------------ARPlieqGVDREDARSVAR-----DLLSALsvPESLwqAYP-----ATF 152
Cdd:COG1132 417 GVVPQ-----------DTFlfsgtireniryGRP----DATDEEVEEAAKaaqahEFIEAL--PDGY--DTVvgergVNL 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493478021 153 SGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIV 530
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-194 |
3.51e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 107.70 E-value: 3.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDmhvlgdtQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDG-DIDLA--S 80
Cdd:PRK11701 7 LSVRGLTKLYG-------PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGqLRDLYalS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 CPDRTVIdLRGDsIGYTSQF-LDEI-PRVPAVDVVARPLIEQGVDR-EDARSVARDLLSALSVPESLWQAYPATFSGGER 157
Cdd:PRK11701 80 EAERRRL-LRTE-WGFVHQHpRDGLrMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQ 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 493478021 158 QRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLL 194
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-240 |
1.21e-27 |
|
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: 105.40 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDmhvlgdtQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPd 83
Cdd:cd03300 1 IELENVSKFYG-------GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL----DGKDITNLP- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 rtvIDLRGDSIGYTSQFLdeIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNLA 163
Cdd:cd03300 69 ---PHKRPVNTVFQNYAL--FPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 164 QALAPKPDLLLLDEPTSALDPDTR---RAAIDLLSTYLGseTTVVGVFHNTDVVDAVADRVVVLDDGRLQRV-VPTEAYD 239
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDLKLRkdmQLELKRLQKELG--ITFVFVTHDQEEALTMSDRIAVMNKGKIQQIgTPEEIYE 220
|
.
gi 493478021 240 E 240
Cdd:cd03300 221 E 221
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-184 |
1.78e-27 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 105.65 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHS------PDGDI 76
Cdd:COG4598 8 ALEVRDLHKSF-----GDLEV--LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkPDRDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 77 DLASCPDRTVIDLRGdSIGYTSQ-F--------LDEIPRVPaVDVvarplieQGVDREDARSVARDLLSALSVPESLwQA 147
Cdd:COG4598 81 ELVPADRRQLQRIRT-RLGMVFQsFnlwshmtvLENVIEAP-VHV-------LGRPKAEAIERAEALLAKVGLADKR-DA 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 493478021 148 YPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDP 184
Cdd:COG4598 151 YPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP 187
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-205 |
2.66e-27 |
|
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: 103.71 E-value: 2.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDMHVLgdtqvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIDLASCP 82
Cdd:COG4133 2 MLEAENLSCRRGERLL-------FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRtvidlrgdsIGYTSQFLDEIPRVPAVD--VVARPLIEQGVDREDARsvarDLLSALSVpESLWQAYPATFSGGERQRV 160
Cdd:COG4133 75 RR---------LAYLGHADGLKPELTVREnlRFWAALYGLRADREAID----EALEAVGL-AGLADLPVRQLSAGQKRRV 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493478021 161 NLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVL 185
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-232 |
3.55e-27 |
|
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: 103.87 E-value: 3.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDmhvlgdtQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCP- 82
Cdd:cd03301 1 VELENVTKRFG-------NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYI----GGRDVTDLPp 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 -DRtvidlrgdSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVN 161
Cdd:cd03301 70 kDR--------DIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQI-EHLLDRKPKQLSGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493478021 162 LAQALAPKPDLLLLDEPTSALDPDTR---RAAIDLLSTYLGseTTVVGVFHNTDVVDAVADRVVVLDDGRLQRV 232
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRvqmRAELKRLQQRLG--TTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-209 |
1.02e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.46 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTFDMHVLgdtqvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSpdgdidlasc 81
Cdd:COG0488 314 KVLELEGLSKSYGDKTL-------LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE---------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 82 pdrTVidlrgdSIGYTSQFLDEI-PRVPAVDVVARplieqgVDREDARSVARDLLSALSVPESLWQAYPATFSGGERQRV 160
Cdd:COG0488 377 ---TV------KIGYFDQHQEELdPDKTVLDELRD------GAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARL 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493478021 161 NLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGsetTVVGVFH 209
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPG---TVLLVSH 487
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-239 |
3.23e-26 |
|
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: 102.03 E-value: 3.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLsVDGLSKTFDmhvlgdtQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGdidlas 80
Cdd:cd03296 1 MSIE-VRNVSKRFG-------DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 cpdrTVIDLRGDSIGYTSQFLDEIPRVPAVDVVA-----RPLIEQGVDREDARSVaRDLLSALSVpESLWQAYPATFSGG 155
Cdd:cd03296 67 ----TDVPVQERNVGFVFQHYALFRHMTVFDNVAfglrvKPRSERPPEAEIRAKV-HELLKLVQL-DWLADRYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 156 ERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTyLGSETTVVGVF--HNTDVVDAVADRVVVLDDGRLQRV- 232
Cdd:cd03296 141 QRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRR-LHDELHVTTVFvtHDQEEALEVADRVVVMNKGRIEQVg 219
|
....*..
gi 493478021 233 VPTEAYD 239
Cdd:cd03296 220 TPDEVYD 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
26-210 |
3.82e-26 |
|
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: 101.54 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDG----DIDLAS-------CPDRTVidLRGDSI 94
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI---DGqdirEVTLDSlrraigvVPQDTV--LFNDTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 95 GYTSQFldeiPRVPAVDVvarplieqgvDREDARSVARDLLSALSVPEslwqAYpAT--------FSGGERQRVNLAQAL 166
Cdd:cd03253 92 GYNIRY----GRPDATDE----------EVIEAAKAAQIHDKIMRFPD----GY-DTivgerglkLSGGEKQRVAIARAI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493478021 167 APKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVgVFHN 210
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIV-IAHR 195
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-205 |
4.59e-26 |
|
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: 106.00 E-value: 4.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 14 DMHVLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPDRtviDLRgDS 93
Cdd:COG4988 341 DVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI----NGVDLSDLDPA---SWR-RQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 94 IGYTSQFldeiPRVPAVDV-----VARPlieqGVDREDARSVAR-----DLLSALsvPESLwqAYP-----ATFSGGERQ 158
Cdd:COG4988 413 IAWVPQN----PYLFAGTIrenlrLGRP----DASDEELEAALEaagldEFVAAL--PDGL--DTPlgeggRGLSGGQAQ 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493478021 159 RVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVIL 527
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-184 |
5.51e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 101.73 E-value: 5.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSktfdmHVLGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdgDIDLASCPD 83
Cdd:COG4559 2 LEAENLS-----VRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLN----GRPLAAWSP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 ------RTVidLRGDSigyTSQFldeiPrVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLWQAYPaTFSGGER 157
Cdd:COG4559 71 welarrRAV--LPQHS---SLAF----P-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQ-TLSGGEQ 139
|
170 180 190
....*....|....*....|....*....|....
gi 493478021 158 QRVNLAQALA-------PKPDLLLLDEPTSALDP 184
Cdd:COG4559 140 QRVQLARVLAqlwepvdGGPRWLFLDEPTSALDL 173
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
19-184 |
7.92e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.86 E-value: 7.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 19 GDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyHSPDGDIDLASCPD-RTVIDLRGDsIGYT 97
Cdd:COG4161 13 GSHQA--LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL--NIAGHQFDFSQKPSeKAIRLLRQK-VGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 98 SQFLDEIPRVPAVD-VVARPLIEQGVDREDARSVARDLLSALSVPESLwQAYPATFSGGERQRVNLAQALAPKPDLLLLD 176
Cdd:COG4161 88 FQQYNLWPHLTVMEnLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKA-DRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
....*...
gi 493478021 177 EPTSALDP 184
Cdd:COG4161 167 EPTAALDP 174
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-183 |
1.13e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 102.35 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFDMH---VLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdID 77
Cdd:PRK11308 3 QPLLQAIDLKKHYPVKrglFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYY---QG-QD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 78 LASCPDRTVIDLRGD-SIGYTSQFLDEIPRVPAVDVVARPL-IEQGVDREDARSVARDLLSALSVPESLWQAYPATFSGG 155
Cdd:PRK11308 79 LLKADPEAQKLLRQKiQIVFQNPYGSLNPRKKVGQILEEPLlINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGG 158
|
170 180
....*....|....*....|....*...
gi 493478021 156 ERQRVNLAQALAPKPDLLLLDEPTSALD 183
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-205 |
1.52e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 99.50 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmhvlGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDgdidlascpD 83
Cdd:cd03263 1 LQIRNLTKTY-----KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS---------I 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RTVIDLRGDSIGYTSQF--LDEiprvpavDVVARPLIE-----QGVDREDARSVARDLLSALSVpESLWQAYPATFSGGE 156
Cdd:cd03263 67 RTDRKAARQSLGYCPQFdaLFD-------ELTVREHLRfyarlKGLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGM 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493478021 157 RQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTyLGSETTVV 205
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILE-VRKGRSII 186
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-210 |
1.60e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 99.85 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKtfdmHV-LGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDgdidLASC 81
Cdd:PRK10584 6 IVEVHHLKK----SVgQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP----LHQM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 82 PDRTVIDLRGDSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLWQaYPATFSGGERQRVN 161
Cdd:PRK10584 78 DEEARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDH-LPAQLSGGEQQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493478021 162 LAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL-STYLGSETTVVGVFHN 210
Cdd:PRK10584 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfSLNREHGTTLILVTHD 206
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-211 |
1.73e-25 |
|
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: 99.23 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 8 GLSKTFDMHVLgdtqvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDiDLASCPDRTVI 87
Cdd:TIGR03608 3 NISKKFGDKVI-------LDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYL---NGQ-ETPPLNSKKAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 88 DLRGDSIGYTSQ---FLDEIPRVPAVDVvarPLIEQGVDREDARSVARDLLSALSVPESLWQaYPATFSGGERQRVNLAQ 164
Cdd:TIGR03608 72 KFRREKLGYLFQnfaLIENETVEENLDL---GLKYKKLSKKEKREKKKEALEKVGLNLKLKQ-KIYELSGGEQQRVALAR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493478021 165 ALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHNT 211
Cdd:TIGR03608 148 AILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP 194
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-194 |
2.08e-25 |
|
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: 100.11 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFDmhvlGdtqVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDG-DID-- 77
Cdd:COG0411 2 DPLLEVRGLTKRFG----G---LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILF---DGrDITgl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 78 ----------------LASCPDRTVID--LRGDSIGYTSQFLDEIPRVPAVdvvarplieqGVDREDARSVARDLLSALS 139
Cdd:COG0411 72 pphriarlgiartfqnPRLFPELTVLEnvLVAAHARLGRGLLAALLRLPRA----------RREEREARERAEELLERVG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493478021 140 VpESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:COG0411 142 L-ADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELI 195
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-210 |
2.92e-25 |
|
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: 99.43 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDmhvlgdtQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDG-DIDLAScP 82
Cdd:cd03219 1 LEVRGLTKRFG-------GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLF---DGeDITGLP-P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTVidLRGdsIGYTSQfldeIPRV-PAVDV-----VARPLIEQGV--------DREDARSVARDLLSALSVPEsLWQAY 148
Cdd:cd03219 70 HEIA--RLG--IGRTFQ----IPRLfPELTVlenvmVAAQARTGSGlllararrEEREARERAEELLERVGLAD-LADRP 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493478021 149 PATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:cd03219 141 AGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHD 202
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-185 |
3.50e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 99.32 E-value: 3.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 19 GDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyHSPDGDIDLASCPD-RTVIDLRGDsIGYT 97
Cdd:PRK11124 13 GAHQA--LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL--NIAGNHFDFSKTPSdKAIRELRRN-VGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 98 SQFLDEIPRVpavdVVARPLIE-----QGVDREDARSVARDLLSALSVPEsLWQAYPATFSGGERQRVNLAQALAPKPDL 172
Cdd:PRK11124 88 FQQYNLWPHL----TVQQNLIEapcrvLGLSKDQALARAEKLLERLRLKP-YADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170
....*....|...
gi 493478021 173 LLLDEPTSALDPD 185
Cdd:PRK11124 163 LLFDEPTAALDPE 175
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-196 |
4.37e-25 |
|
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: 99.43 E-value: 4.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDmhvlgDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLAScpD 83
Cdd:TIGR04520 1 IEVENVSFSYP-----ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTV---DG-LDTLD--E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RTVIDLRgDSIGY-----TSQFldeiprVPAV--DVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGE 156
Cdd:TIGR04520 70 ENLWEIR-KKVGMvfqnpDNQF------VGATveDDVAFGLENLGVPREEMRKRVDEALKLVGM-EDFRDREPHLLSGGQ 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493478021 157 RQRVNLAQALAPKPDLLLLDEPTSALDPDTRRaaiDLLST 196
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRK---EVLET 178
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
26-209 |
8.25e-25 |
|
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: 97.33 E-value: 8.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDgdidlasCPDRTvidlRGDSIGYTSQFLDeip 105
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP-------IKAKE----RRKSIGYVMQDVD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPAVDVVARPLIEQGVDREDARSVARDLLSALSvPESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPD 185
Cdd:cd03226 82 YQLFTDSVREELLLGLKELDAGNEQAETVLKDLD-LYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180
....*....|....*....|....
gi 493478021 186 TRRAAIDLLSTYLGSETTVVGVFH 209
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITH 184
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-192 |
9.96e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 98.93 E-value: 9.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTFDmhvlgDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLAsc 81
Cdd:PRK13635 4 EIIRVEHISFRYP-----DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV----GGMVLS-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 82 pDRTVIDLRgDSIGYT-----SQFLDEIPRvpavDVVARPLIEQGVDREDARSVARDLLSALSVPESLWQAyPATFSGGE 156
Cdd:PRK13635 73 -EETVWDVR-RQVGMVfqnpdNQFVGATVQ----DDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNRE-PHRLSGGQ 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 493478021 157 RQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAID 192
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLE 181
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-209 |
1.28e-24 |
|
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: 97.85 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 19 GDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVY--HSPDGDIDLAscpdrtviDLRGdSIGY 96
Cdd:COG1119 14 GGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfGERRGGEDVW--------ELRK-RIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 97 TSQFLDE--IPRVPAVDVVA--------RPlieQGVDREDaRSVARDLLSALSVpESLWQAYPATFSGGERQRVNLAQAL 166
Cdd:COG1119 83 VSPALQLrfPRDETVLDVVLsgffdsigLY---REPTDEQ-RERARELLELLGL-AHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493478021 167 APKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGS-ETTVVGVFH 209
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEgAPTLVLVTH 201
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-194 |
1.37e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.22 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFDMHVL---GDTQVVgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYH-SPDGDI 76
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLsgkHQHQTV-LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRgEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 77 DLASCPD--RTVIDLRGDSIGYTSqfldeiPRVPAVDVVARPLIE-QGVDREDARSVARDLLSALSVPESLWQAYPATFS 153
Cdd:PRK10419 80 NRAQRKAfrRDIQMVFQDSISAVN------PRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493478021 154 GGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLL 194
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-210 |
1.41e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 98.19 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYD--PS---SGEVVYHspdgDI 76
Cdd:COG1117 10 PKIEVRNLNVYY-----GDKQA--LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLD----GE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 77 DLAScPDRTVIDLRgDSIGY---------TSQFldeiprvpavDVVARPLIEQGV-DRE--DARsVARDLLSAlsvpeSL 144
Cdd:COG1117 79 DIYD-PDVDVVELR-RRVGMvfqkpnpfpKSIY----------DNVAYGLRLHGIkSKSelDEI-VEESLRKA-----AL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493478021 145 W-------QAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTyLGSETTVVGVFHN 210
Cdd:COG1117 141 WdevkdrlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILE-LKKDYTIVIVTHN 212
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-229 |
1.61e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 98.75 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 22 QVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVV---YHSPdgdidlASCPDRTVIDLRgDSIGYTS 98
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagYHIT------PETGNKNLKKLR-KKVSLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 99 QFLDEIPRVPAV--DVVARPLiEQGVDREDARSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLD 176
Cdd:PRK13641 92 QFPEAQLFENTVlkDVEFGPK-NFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493478021 177 EPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHNTDVVDAVADRVVVLDDGRL 229
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
26-210 |
1.97e-24 |
|
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: 95.95 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIDlascpDRTVIDLRgDSIGYTSQFLDEIP 105
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYS-----RKGLLERR-QRVGLVFQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPAVDV-VARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDP 184
Cdd:TIGR01166 82 FAADVDQdVAFGPLNLGLSEAEVERRVREALTAVGA-SGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180
....*....|....*....|....*.
gi 493478021 185 DTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
26-209 |
2.03e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.15 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdgdidlascpdrtvidlRGDSIGYTSQFLDEIP 105
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA-------------------GGARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPA--VDVVA----RPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPT 179
Cdd:NF040873 69 SLPLtvRDLVAmgrwARRGLWRRLTRDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|
gi 493478021 180 SALDPDTRRAAIDLLSTYLGSETTVVGVFH 209
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTH 177
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-210 |
2.78e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 99.72 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 8 GLSKTFDMHVLGDTqvVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLASCPDRTVI 87
Cdd:PRK10070 28 GLSKEQILEKTGLS--LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI---DG-VDIAKISDAELR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 88 DLRGDSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNLAQALA 167
Cdd:PRK10070 102 EVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493478021 168 PKPDLLLLDEPTSALDPDTRRAAID-LLSTYLGSETTVVGVFHN 210
Cdd:PRK10070 181 INPDILLMDEAFSALDPLIRTEMQDeLVKLQAKHQRTIVFISHD 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-187 |
2.89e-24 |
|
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: 96.21 E-value: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 28 DVSFDVrEGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDIDLASCPDrtvIDL--RGDSIGYTSQfldEIP 105
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL---NGTVLFDSRKK---INLppQQRKIGLVFQ---QYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPAVDVvaRPLIEQGVdREDARSVARDLLSALSVP---ESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSAL 182
Cdd:cd03297 86 LFPHLNV--RENLAFGL-KRKRNREDRISVDELLDLlglDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
....*
gi 493478021 183 DPDTR 187
Cdd:cd03297 163 DRALR 167
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
26-205 |
3.16e-24 |
|
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: 96.53 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLAscpDRTVIDLRgDSIGYTSQ----FL 101
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI---DG-HDVR---DYTLASLR-RQIGLVSQdvflFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 102 DEIPRVPAvdvVARPlieqGVDREDARSVARdLLSALSVPESLWQAYPA-------TFSGGERQRVNLAQALAPKPDLLL 174
Cdd:cd03251 90 DTVAENIA---YGRP----GATREEVEEAAR-AANAHEFIMELPEGYDTvigergvKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190
....*....|....*....|....*....|.
gi 493478021 175 LDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLMKNRTTFV 192
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-209 |
4.49e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 96.96 E-value: 4.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDMHVLgdtqvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHS--------PDGD 75
Cdd:PRK10619 6 LNVIDLHKRYGEHEV-------LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdKDGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 76 IDLAscpDRTVIDLRGDSIGYTSQFLDEIPRVPAVD-VVARPLIEQGVDREDARSVARDLLSALSVPESLWQAYPATFSG 154
Cdd:PRK10619 79 LKVA---DKNQLRLLRTRLTMVFQHFNLWSHMTVLEnVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493478021 155 GERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFH 209
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTH 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-210 |
6.00e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.46 E-value: 6.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 6 VDGLSKTFDMHVlgDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIDLAscPDRT 85
Cdd:PRK13651 5 VKNIVKIFNKKL--PTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKK--TKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 86 VIDLRGDSIGYTS----QFLDEI-PRVPAV---------------DVVARPlIEQGVDREDARSVARDLLSALSVPESLW 145
Cdd:PRK13651 81 EKVLEKLVIQKTRfkkiKKIKEIrRRVGVVfqfaeyqlfeqtiekDIIFGP-VSMGVSKEEAKKRAAKYIELVGLDESYL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478021 146 QAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-236 |
9.29e-24 |
|
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: 99.11 E-value: 9.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 23 VVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIDLAS---------------------- 80
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKpgpdgrgrakryigilhqeydl 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 CPDRTVIDLRGDSIGYtsQFLDEIPRVPAVDVvarpLIEQGVDREDARSVArdllsalsvpeslwQAYPATFSGGERQRV 160
Cdd:TIGR03269 377 YPHRTVLDNLTEAIGL--ELPDELARMKAVIT----LKMVGFDEEKAEEIL--------------DKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478021 161 NLAQALAPKPDLLLLDEPTSALDPDTRRAAID-LLSTYLGSETTVVGVFHNTDVVDAVADRVVVLDDGRLQRVVPTE 236
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-210 |
1.01e-23 |
|
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: 94.65 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmhvlGDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdidlascpd 83
Cdd:cd03269 1 LEVENVTKRF-----GRVTAL--DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF---DG--------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RTVIDLRGDSIGYtsqfLDE----IPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPEsLWQAYPATFSGGERQR 159
Cdd:cd03269 62 KPLDIAARNRIGY----LPEerglYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSE-YANKRVEELSKGNQQK 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493478021 160 VNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:cd03269 137 VQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-189 |
1.51e-23 |
|
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: 98.74 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyhSPDG----DIDLAS-------CPDRTVidLRGDSI 94
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRI---LIDGqdirDVTQASlraaigiVPQDTV--LFNDTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 95 GYTSQFldeiprvpavdvvARPlieqGVDREDARSVARdlLSALS--VpESLWQAYpAT--------FSGGERQRVNLAQ 164
Cdd:COG5265 449 AYNIAY-------------GRP----DASEEEVEAAAR--AAQIHdfI-ESLPDGY-DTrvgerglkLSGGEKQRVAIAR 507
|
170 180
....*....|....*....|....*
gi 493478021 165 ALAPKPDLLLLDEPTSALDPDTRRA 189
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERA 532
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-185 |
2.47e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVY----HSPDGDID- 77
Cdd:COG1129 4 LLEMRGISKSF-----GGVKA--LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdgepVRFRSPRDa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 78 -----------LASCPDRTVidlrGDSIgytsqFLDEIPRvpavdvvARPLIeqgvDREDARSVARDLLSALSVPESLWQ 146
Cdd:COG1129 77 qaagiaiihqeLNLVPNLSV----AENI-----FLGREPR-------RGGLI----DWRAMRRRARELLARLGLDIDPDT 136
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493478021 147 ayP-ATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPD 185
Cdd:COG1129 137 --PvGDLSVAQQQLVEIARALSRDARVLILDEPTASLTER 174
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-210 |
4.45e-23 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 97.05 E-value: 4.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 14 DMHVLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLAScpdrtvidLRGDS 93
Cdd:TIGR02868 339 DLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTL----DGVPVSS--------LDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 94 IGYTSQFLDEIPRVPAVDV-----VARPlieqGVDREDARSVAR-----DLLSALSVPESLW-QAYPATFSGGERQRVNL 162
Cdd:TIGR02868 407 VRRRVSVCAQDAHLFDTTVrenlrLARP----DATDEELWAALErvglaDWLRALPDGLDTVlGEGGARLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493478021 163 AQALAPKPDLLLLDEPTSALDPDTRRAAI-DLLSTylGSETTVVGVFHN 210
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLeDLLAA--LSGRTVVLITHH 529
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-209 |
5.07e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.80 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 25 GLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPDRTVIDLRGDSIGYTSQFLDE- 103
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV----GDIVVSSTSKQKEIKPVRKKVGVVFQFPESq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 104 -IPRVPAVDVVARPLiEQGVDREDARSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSAL 182
Cdd:PRK13643 97 lFEETVLKDVAFGPQ-NFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180
....*....|....*....|....*..
gi 493478021 183 DPDTRRAAIDLLSTYLGSETTVVGVFH 209
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-194 |
5.44e-23 |
|
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: 94.10 E-value: 5.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTFDMHVL----GDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPD-GDI 76
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGGLfgakQRAPV--LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDlYQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 77 DLASCP--DRTVIDLRGDSIGYTSqfldeiPRVPAVDVVARPLiEQGVDREDARSVAR--DLLSALSVPESLWQAYPATF 152
Cdd:TIGR02769 79 DRKQRRafRRDVQLVFQDSPSAVN------PRMTVRQIIGEPL-RHLTSLDESEQKARiaELLDMVGLRSEDADKLPRQL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493478021 153 SGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELL 193
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-205 |
9.51e-23 |
|
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: 92.27 E-value: 9.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 20 DTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPdrtVIDLRGDsIGYTSQ 99
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL----DGTDIRQLD---PADLRRN-IGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 100 --FL------DEIprvpavdVVARPLIEqgvdreDARsvardLLSA--LSVPESLWQAYPATF-----------SGGERQ 158
Cdd:cd03245 86 dvTLfygtlrDNI-------TLGAPLAD------DER-----ILRAaeLAGVTDFVNKHPNGLdlqigergrglSGGQRQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493478021 159 RVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLII 194
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-206 |
1.39e-22 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 95.82 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmhvlGDTQVVgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPD 83
Cdd:TIGR02857 322 LEFSGVSVAY-----PGRRPA-LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV----NGVPLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 rtviDLRGDSIGYTSQfldeIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLWQAY-------PATFSGGE 156
Cdd:TIGR02857 392 ----DSWRDQIAWVPQ----HPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLdtpigegGAGLSGGQ 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493478021 157 RQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVG 206
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLV 513
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-183 |
1.42e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.93 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFDMhvlGDTQVVGLDDVSFDVREGEFLAVVGESGSGKS----SLLKCLyrtydPSSgEVVYhsPDGDI 76
Cdd:PRK15134 3 QPLLAIENLSVAFRQ---QQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSP-PVVY--PSGDI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 77 -----DLASCPDRTVIDLRGDSIGYTSQfldeiprVPAVDV-----VARPLIE-----QGVDREDARSVARDLLSALSV- 140
Cdd:PRK15134 72 rfhgeSLLHASEQTLRGVRGNKIAMIFQ-------EPMVSLnplhtLEKQLYEvlslhRGMRREAARGEILNCLDRVGIr 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493478021 141 -PESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALD 183
Cdd:PRK15134 145 qAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALD 188
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-210 |
1.99e-22 |
|
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: 90.35 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSktfdmHVLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLascpD 83
Cdd:cd03246 1 LEVENVS-----FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL---DG-ADI----S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RTVIDLRGDSIGYTSQfldeiprvpavdvvarplieqgvdredarsvaRDLLSALSVPESLwqaypatFSGGERQRVNLA 163
Cdd:cd03246 68 QWDPNELGDHVGYLPQ--------------------------------DDELFSGSIAENI-------LSGGQRQRLGLA 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493478021 164 QALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:cd03246 109 RALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR 155
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
26-209 |
2.55e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.26 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhsPDGDidlascpdrtvidlrgdsigyTSQFLDEIP 105
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--PAGA---------------------RVLFLPQRP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPAV---DVVARPLIEQGVDREDARSVAR-----DLLSALSVpESLWQAypaTFSGGERQRVNLAQALAPKPDLLLLDE 177
Cdd:COG4178 436 YLPLGtlrEALLYPATAEAFSDAELREALEavglgHLAERLDE-EADWDQ---VLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|..
gi 493478021 178 PTSALDPDTRRAAIDLLSTYLgSETTVVGVFH 209
Cdd:COG4178 512 ATSALDEENEAALYQLLREEL-PGTTVISVGH 542
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-205 |
3.14e-22 |
|
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: 94.78 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 19 GDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLAscpDRTVIDLRgDSIGYTS 98
Cdd:TIGR02203 341 PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL---DG-HDLA---DYTLASLR-RQVALVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 99 Q----FLDEIprvpaVDVVARPLIEQgVDREDARSVAR-----DLLSALsvPESLWQAY---PATFSGGERQRVNLAQAL 166
Cdd:TIGR02203 413 QdvvlFNDTI-----ANNIAYGRTEQ-ADRAEIERALAaayaqDFVDKL--PLGLDTPIgenGVLLSGGQRQRLAIARAL 484
|
170 180 190
....*....|....*....|....*....|....*....
gi 493478021 167 APKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQGRTTLV 523
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-205 |
3.27e-22 |
|
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: 90.72 E-value: 3.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDmhvlgdtQVVGLDDVSFDVREGeFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdgDIDLASCPD 83
Cdd:cd03264 1 LQLENLTKRYG-------KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRID----GQDVLKQPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RtvidLRGdSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLWQaYPATFSGGERQRVNLA 163
Cdd:cd03264 69 K----LRR-RIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKK-KIGSLSGGMRRRVGIA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493478021 164 QALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTyLGSETTVV 205
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSE-LGEDRIVI 183
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-209 |
4.52e-22 |
|
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: 89.92 E-value: 4.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDmHVLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCL--YRTYDPSSGEVVYHSPDGDIDLAS 80
Cdd:cd03213 3 TLSFRNLTVTVK-SSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 CpdrtvidlrgdSIGYtsqfldeiprvpavdvvarplieqgVDREDArsvardLLSALSVPESLWqaYPA---TFSGGER 157
Cdd:cd03213 82 K-----------IIGY-------------------------VPQDDI------LHPTLTVRETLM--FAAklrGLSGGER 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493478021 158 QRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFH 209
Cdd:cd03213 118 KRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
26-209 |
5.48e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.73 E-value: 5.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPDRTVIDLRGDSIGYTSQFldeip 105
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRV----DDTLITSTSKNKDIKQIRKKVGLVFQF----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 rvPAVDVVARPLIEQ--------GVDREDARSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDE 177
Cdd:PRK13649 94 --PESQLFEETVLKDvafgpqnfGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190
....*....|....*....|....*....|..
gi 493478021 178 PTSALDPDTRRAAIDLLSTYLGSETTVVGVFH 209
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-184 |
5.99e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.99 E-value: 5.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTfdmhvLGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdgDIDLASC 81
Cdd:PRK13548 1 AMLEARNLSVR-----LGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLN----GRPLADW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 82 PDRTVIDLRG---DSIGYTSQFldeiprvPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLWQAYPaTFSGGERQ 158
Cdd:PRK13548 70 SPAELARRRAvlpQHSSLSFPF-------TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYP-QLSGGEQQ 141
|
170 180 190
....*....|....*....|....*....|..
gi 493478021 159 RVNLAQALA------PKPDLLLLDEPTSALDP 184
Cdd:PRK13548 142 RVQLARVLAqlwepdGPPRWLLLDEPTSALDL 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
26-209 |
6.25e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 88.91 E-value: 6.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspdgdidLASCPDRTVIDLRGDSIGYTSQfldeip 105
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT---------LDGVPVSDLEKALSSLISVLNQ------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 rvpavdvvaRPLieqgvdredarsvardLLSAlsvpeSLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPD 185
Cdd:cd03247 83 ---------RPY----------------LFDT-----TLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180
....*....|....*....|....
gi 493478021 186 TRRAAIDLLSTYLgSETTVVGVFH 209
Cdd:cd03247 133 TERQLLSLIFEVL-KDKTLIWITH 155
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
26-205 |
9.54e-22 |
|
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: 89.91 E-value: 9.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDG-DI-DLASCpdrtviDLRgDSIGYTSQ---- 99
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILL---DGvDIrDLNLR------WLR-SQIGLVSQepvl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 100 ----FLDEIP--RVPAVDvvarplieqgvdrEDARSVARdLLSALSVPESLWQAYP-------ATFSGGERQRVNLAQAL 166
Cdd:cd03249 89 fdgtIAENIRygKPDATD-------------EEVEEAAK-KANIHDFIMSLPDGYDtlvgergSQLSGGQKQRIAIARAL 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 493478021 167 APKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIV 193
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-184 |
1.40e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.94 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFdmhvlGDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDidlascp 82
Cdd:COG4152 1 MLELKGLTKRF-----GDKTAV--DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW---DGE------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTVIDLRGdsIGYtsqfLDE----IPRVPAVDVV---ARpLieQGVDREDARSVARDLLSALSVPEslWQAYPA-TFSG 154
Cdd:COG4152 64 PLDPEDRRR--IGY----LPEerglYPKMKVGEQLvylAR-L--KGLSKAEAKRRADEWLERLGLGD--RANKKVeELSK 132
|
170 180 190
....*....|....*....|....*....|
gi 493478021 155 GERQRVNLAQALAPKPDLLLLDEPTSALDP 184
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDP 162
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-188 |
1.69e-21 |
|
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: 88.97 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 6 VDGLSKTFDmhvlgdtQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDgdidlASCPDRT 85
Cdd:cd03265 3 VENLVKKYG-------DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHD-----VVREPRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 86 VidlrGDSIGYTSQFL---DEIPRVPAVDVVARPlieQGVDREDARSVARDLLSALSvpesLWQA---YPATFSGGERQR 159
Cdd:cd03265 71 V----RRRIGIVFQDLsvdDELTGWENLYIHARL---YGVPGAERRERIDELLDFVG----LLEAadrLVKTYSGGMRRR 139
|
170 180
....*....|....*....|....*....
gi 493478021 160 VNLAQALAPKPDLLLLDEPTSALDPDTRR 188
Cdd:cd03265 140 LEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-209 |
1.84e-21 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 86.73 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDMHVLgdtqvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSpdgdidlascpd 83
Cdd:cd03221 1 IELENLSKTYGGKLL-------LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 rtvidlrGDSIGYTSQFldeiprvpavdvvarplieqgvdredarsvardllsalsvpeslwqaypatfSGGERQRVNLA 163
Cdd:cd03221 62 -------TVKIGYFEQL----------------------------------------------------SGGEKMRLALA 82
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493478021 164 QALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGsetTVVGVFH 209
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG---TVILVSH 125
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-183 |
2.07e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 92.61 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDMHvlgDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEV------VYHSPDGDI 76
Cdd:PRK10261 12 VLAVENLNIAFMQE---QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmlLRRRSRQVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 77 DLASCPDRTVIDLRGDSIGYTSQ--FLDEIPRVPAVDVVARPL-IEQGVDREDARSVARDLLSALSVPES--LWQAYPAT 151
Cdd:PRK10261 89 ELSEQSAAQMRHVRGADMAMIFQepMTSLNPVFTVGEQIAESIrLHQGASREEAMVEAKRMLDQVRIPEAqtILSRYPHQ 168
|
170 180 190
....*....|....*....|....*....|..
gi 493478021 152 FSGGERQRVNLAQALAPKPDLLLLDEPTSALD 183
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALD 200
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-184 |
2.61e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.01 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFdmhvlGDtqVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDG-DIDLA 79
Cdd:COG3845 3 PPALELRGITKRF-----GG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI---DGkPVRIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 80 ScPdRTVIDLRgdsIGYTSQ-FLDeiprVPAVDVV------ARPLIEQGVDREDARSVARDLLSA--LSVPeslWQAYPA 150
Cdd:COG3845 73 S-P-RDAIALG---IGMVHQhFML----VPNLTVAenivlgLEPTKGGRLDRKAARARIRELSERygLDVD---PDAKVE 140
|
170 180 190
....*....|....*....|....*....|....
gi 493478021 151 TFSGGERQRVNLAQALAPKPDLLLLDEPTSALDP 184
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEPTAVLTP 174
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-187 |
4.33e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.58 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspDGDIDLASC 81
Cdd:PRK11247 11 TPLLLNAVSKRY-----GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL----AGTAPLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 82 PDRTVIdlrgdsigytsQFLDE--IPRVPAVDVVARPLieqgvdREDARSVARDLLSALSVPESLwQAYPATFSGGERQR 159
Cdd:PRK11247 80 REDTRL-----------MFQDArlLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRA-NEWPAALSGGQKQR 141
|
170 180
....*....|....*....|....*...
gi 493478021 160 VNLAQALAPKPDLLLLDEPTSALDPDTR 187
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDALTR 169
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-204 |
5.80e-21 |
|
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: 87.27 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDgDIDLASCPD 83
Cdd:cd03268 1 LKTNDLTKTY-----GKKRV--LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-YQKNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 R--TVID-------LRGDSIGYTSQFLDEIPRvPAVDVVarpLIEQGVDREDARSVArdllsalsvpeslwqaypaTFSG 154
Cdd:cd03268 73 RigALIEapgfypnLTARENLRLLARLLGIRK-KRIDEV---LDVVGLKDSAKKKVK-------------------GFSL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493478021 155 GERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTV 204
Cdd:cd03268 130 GMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITV 179
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-188 |
6.09e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 89.76 E-value: 6.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 6 VDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspDGDIDLASCPDRT 85
Cdd:PRK10851 5 IANIKKSF-----GRTQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH--GTDVSRLHARDRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 86 VidlrgdsiGYTSQFLDEIPRVPAVDVVA----------RPlieqgvDREDARSVARDLLSALSVPEsLWQAYPATFSGG 155
Cdd:PRK10851 76 V--------GFVFQHYALFRHMTVFDNIAfgltvlprreRP------NAAAIKAKVTQLLEMVQLAH-LADRYPAQLSGG 140
|
170 180 190
....*....|....*....|....*....|...
gi 493478021 156 ERQRVNLAQALAPKPDLLLLDEPTSALDPDTRR 188
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-210 |
7.52e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.94 E-value: 7.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 19 GDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEvvYHSPDGDIdlASCPDRTVIDLRGDSIGYTS 98
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGT--YRVAGQDV--ATLDADALAQLRREHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 99 QFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLwQAYPATFSGGERQRVNLAQALAPKPDLLLLDEP 178
Cdd:PRK10535 93 QRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRV-EYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190
....*....|....*....|....*....|..
gi 493478021 179 TSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:PRK10535 172 TGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
18-229 |
1.19e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.85 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 18 LGDTQvvGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPDRTVIDLRgDSIGYT 97
Cdd:PRK10908 12 LGGRQ--ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWF----SGHDITRLKNREVPFLR-RQIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 98 SQFLDEIPRVPAVDVVARPLIEQGVDREDAR---SVARDLLSALSVPESlwqaYPATFSGGERQRVNLAQALAPKPDLLL 174
Cdd:PRK10908 85 FQDHHLLMDRTVYDNVAIPLIIAGASGDDIRrrvSAALDKVGLLDKAKN----FPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493478021 175 LDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHNTDVVDAVADRVVVLDDGRL 229
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-210 |
1.27e-20 |
|
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: 85.17 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDmhvlgdtQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspdgdidlascpd 83
Cdd:cd03216 1 LELRGITKRFG-------GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL--------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 rtvidLRGDSIGYTSqfldeiPRvpavdvvarplieqgvdreDARsvardllsALSVpESLWQaypatFSGGERQRVNLA 163
Cdd:cd03216 59 -----VDGKEVSFAS------PR-------------------DAR--------RAGI-AMVYQ-----LSVGERQMVEIA 94
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493478021 164 QALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHR 141
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
24-210 |
1.32e-20 |
|
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: 88.22 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 24 VGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSpdgdIDLASCPDRtvidLRgDSIGYTSQF--L 101
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAG----YDVVREPRK----VR-RSIGIVPQYasV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 102 DEiprvpavDVVARPLIE-----QGVDREDARSVARDLLSALSvpesLWQA---YPATFSGGERQRVNLAQALAPKPDLL 173
Cdd:TIGR01188 78 DE-------DLTGRENLEmmgrlYGLPKDEAEERAEELLELFE----LGEAadrPVGTYSGGMRRRLDIAASLIHQPDVL 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 493478021 174 LLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:TIGR01188 147 FLDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHY 183
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-186 |
2.64e-20 |
|
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: 89.09 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDmhvlgdtQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRT--YDPSSGEVVYH----------- 70
Cdd:TIGR03269 1 IEVKNLTKKFD-------GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyve 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 71 --SPDG-------------DIDLASCPDRTVIDLRGD-SIGYTSQF-LDEIPRVpaVDVVARPLIEQGVDREDARSVARD 133
Cdd:TIGR03269 74 rpSKVGepcpvcggtlepeEVDFWNLSDKLRRRIRKRiAIMLQRTFaLYGDDTV--LDNVLEALEEIGYEGKEAVGRAVD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493478021 134 LLSALSVPESLWQAyPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDT 186
Cdd:TIGR03269 152 LIEMVQLSHRITHI-ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQT 203
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-244 |
2.69e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.16 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDmhvlgDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGdIDLAScp 82
Cdd:PRK13640 5 IVEFKHVSFTYP-----DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDG-ITLTA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 dRTVIDLRgDSIGYTSQFLDEiPRVPAV--DVVARPLIEQGVDREDARSVARDLLSALSVPESLwQAYPATFSGGERQRV 160
Cdd:PRK13640 77 -KTVWDIR-EKVGIVFQNPDN-QFVGATvgDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYI-DSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 161 NLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYL-GSETTVVGVFHNTdVVDAVADRVVVLDDGR-LQRVVPTEAY 238
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDI-DEANMADQVLVLDDGKlLAQGSPVEIF 231
|
....*.
gi 493478021 239 DEEVVL 244
Cdd:PRK13640 232 SKVEML 237
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-210 |
3.11e-20 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 85.56 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspDGDIDLASCPD 83
Cdd:cd03224 1 LEVENLNAGY-----GKSQI--LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD--GRDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RTvidLRGdsIGYtsqfldeiprVPavdvvarplieQGvdredarsvaRDLLSALSV-------------------PESL 144
Cdd:cd03224 72 RA---RAG--IGY----------VP-----------EG----------RRIFPELTVeenlllgayarrrakrkarLERV 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493478021 145 WQAYPA----------TFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:cd03224 116 YELFPRlkerrkqlagTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQN 191
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
26-191 |
3.17e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.71 E-value: 3.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDIdlasCPDRTVIDLRgDSIGYTSQFLDEiP 105
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII---DGDL----LTEENVWDIR-HKIGMVFQNPDN-Q 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPAV--DVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALD 183
Cdd:PRK13650 94 FVGATveDDVAFGLENKGIPHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
....*...
gi 493478021 184 PDTRRAAI 191
Cdd:PRK13650 173 PEGRLELI 180
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-194 |
3.74e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 87.45 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 27 DDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDgdidLASCPDRTVIDLRGD--SIgytsqFLDEI 104
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKD----LLGMKDDEWRAVRSDiqMI-----FQDPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 105 ----PRVPAVDVVARPLI--EQGVDREDARSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEP 178
Cdd:PRK15079 109 aslnPRMTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170
....*....|....*.
gi 493478021 179 TSALDPDTRRAAIDLL 194
Cdd:PRK15079 189 VSALDVSIQAQVVNLL 204
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
26-194 |
3.76e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.29 E-value: 3.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDIDLASCPDRTVIdlrgdsigytsqFLDE-- 103
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITL---DGKPVEGPGAERGVV------------FQNEgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 104 IPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALD 183
Cdd:PRK11248 82 LPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170
....*....|.
gi 493478021 184 PDTRRAAIDLL 194
Cdd:PRK11248 161 AFTREQMQTLL 171
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-192 |
6.45e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.91 E-value: 6.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 20 DTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdgdiDLASCPDRTVIDLRgDSIGYTSQ 99
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVD------GLDTSDEENLWDIR-NKAGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 100 FLDE--IPRVPAVDVVARPliEQ-GVDREDARSVARDLLSALSVPESLWQAyPATFSGGERQRVNLAQALAPKPDLLLLD 176
Cdd:PRK13633 93 NPDNqiVATIVEEDVAFGP--ENlGIPPEEIRERVDESLKKVGMYEYRRHA-PHLLSGGQKQRVAIAGILAMRPECIIFD 169
|
170
....*....|....*.
gi 493478021 177 EPTSALDPDTRRAAID 192
Cdd:PRK13633 170 EPTAMLDPSGRREVVN 185
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-210 |
8.83e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 86.32 E-value: 8.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFDMHvlgDTQVVGLDDVSFDVREGEFLAVVGESGSGKSS-------LLKCLYRTydpsSGEVVYhspD 73
Cdd:PRK09473 10 DALLDVKDLRVTFSTP---DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQtafalmgLLAANGRI----GGSATF---N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 74 GDiDLASCPDRTVIDLRGDSIGYTsqFLDEIPRVPAVDVVARPLIE-----QGVDREDARSVARDLLSALSVPESL--WQ 146
Cdd:PRK09473 80 GR-EILNLPEKELNKLRAEQISMI--FQDPMTSLNPYMRVGEQLMEvlmlhKGMSKAEAFEESVRMLDAVKMPEARkrMK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493478021 147 AYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPdTRRAAIDLLSTYLGSE--TTVVGVFHN 210
Cdd:PRK09473 157 MYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAQIMTLLNELKREfnTAIIMITHD 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-187 |
9.31e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.81 E-value: 9.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDmhvlGDTQVvglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLASCP 82
Cdd:PRK11607 19 LLEIRNLTKSFD----GQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML---DG-VDLSHVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRtvidLRGDSIGYTSQFLdeIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPEsLWQAYPATFSGGERQRVNL 162
Cdd:PRK11607 88 PY----QRPINMMFQSYAL--FPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQE-FAKRKPHQLSGGQRQRVAL 160
|
170 180
....*....|....*....|....*
gi 493478021 163 AQALAPKPDLLLLDEPTSALDPDTR 187
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLR 185
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-205 |
9.50e-20 |
|
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: 84.85 E-value: 9.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 19 GDTQVVgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPD-GDIDLASCpDRTVIDLRGDSIGYT 97
Cdd:cd03252 12 PDGPVI-LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAWL-RRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 98 SQFLDEIPrvpavdvvarpLIEQGVDREDARSVARdLLSALSVPESLWQAYP-------ATFSGGERQRVNLAQALAPKP 170
Cdd:cd03252 90 RSIRDNIA-----------LADPGMSMERVIEAAK-LAGAHDFISELPEGYDtivgeqgAGLSGGQRQRIAIARALIHNP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 493478021 171 DLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVII 192
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-194 |
1.09e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.60 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 22 QVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDidlaSCPDRTVIDLRGDsIGYTSQ-- 99
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID----TLSPGKLQALRRD-IQFIFQdp 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 100 --FLDeiPRVPAVDVVARPLIEQGV-DREDARSVARDLLSALSV-PESLWQaYPATFSGGERQRVNLAQALAPKPDLLLL 175
Cdd:PRK10261 411 yaSLD--PRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLlPEHAWR-YPHEFSGGQRQRICIARALALNPKVIIA 487
|
170
....*....|....*....
gi 493478021 176 DEPTSALDPDTRRAAIDLL 194
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLL 506
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-210 |
1.24e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.46 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 25 GLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDL-ASCPDRTVIDLRgDSIGYTSQF--- 100
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI----GERVItAGKKNKKLKPLR-KKVGIVFQFpeh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 101 -LDEipRVPAVDVVARPlIEQGVDREDARSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPT 179
Cdd:PRK13634 97 qLFE--ETVEKDICFGP-MNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190
....*....|....*....|....*....|...
gi 493478021 180 SALDPDTRRAAIDLLSTyLGSET--TVVGVFHN 210
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYK-LHKEKglTTVLVTHS 205
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-210 |
1.48e-19 |
|
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: 84.05 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDIDLASCPDRTVIdLRGDSIGYTSQFLDEIp 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL---EGKQITEPGPDRMVV-FQNYSLLPWLTVRENI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 rVPAVDVVARPLieqgvDREDARSVARDLLSALSVPESLwQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPD 185
Cdd:TIGR01184 76 -ALAVDRVLPDL-----SKSERRAIVEEHIALVGLTEAA-DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180
....*....|....*....|....*.
gi 493478021 186 TRRAAID-LLSTYLGSETTVVGVFHN 210
Cdd:TIGR01184 149 TRGNLQEeLMQIWEEHRVTVLMVTHD 174
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-197 |
3.14e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 83.22 E-value: 3.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 14 DMHVLGDTQVVgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDiDLASCPDRTVidlrGDS 93
Cdd:PRK10247 12 NVGYLAGDAKI-LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF---EGE-DISTLKPEIY----RQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 94 IGYTSQfldeiprVPAV--DVVARPLI---EQGVDREDARSVARDLlSALSVPESLWQAYPATFSGGERQRVNLAQALAP 168
Cdd:PRK10247 83 VSYCAQ-------TPTLfgDTVYDNLIfpwQIRNQQPDPAIFLDDL-ERFALPDTILTKNIAELSGGEKQRISLIRNLQF 154
|
170 180
....*....|....*....|....*....
gi 493478021 169 KPDLLLLDEPTSALDPDTRRAAIDLLSTY 197
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRY 183
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-187 |
3.61e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 82.53 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDMHVLgdtqvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDP---SSGEVVYhspdGDIDLAS 80
Cdd:COG4136 2 LSLENLTITLGGRPL-------LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLL----NGRRLTA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 CPdrtvIDLRGdsIGYTSQfldeiprvpavDV-------VARPL---IEQGVDREDARSVARDLLSALSVPeSLWQAYPA 150
Cdd:COG4136 71 LP----AEQRR--IGILFQ-----------DDllfphlsVGENLafaLPPTIGRAQRRARVEQALEEAGLA-GFADRDPA 132
|
170 180 190
....*....|....*....|....*....|....*..
gi 493478021 151 TFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTR 187
Cdd:COG4136 133 TLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-191 |
4.73e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 83.21 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmHVLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPD 83
Cdd:COG1101 2 LELKNLSKTF--NPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILI----DGKDVTKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 rtviDLRGDSIGytsqfldeipRV---PAVDVVARPLIEQ----------------GVDREDaRSVARDLLSA------- 137
Cdd:COG1101 76 ----YKRAKYIG----------RVfqdPMMGTAPSMTIEEnlalayrrgkrrglrrGLTKKR-RELFRELLATlglglen 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493478021 138 -LSVPESLwqaypatFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPdtRRAAI 191
Cdd:COG1101 141 rLDTKVGL-------LSGGQRQALSLLMATLTKPKLLLLDEHTAALDP--KTAAL 186
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-210 |
6.59e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.79 E-value: 6.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYR---TYDPS---SGEVVYHSPD-GDIDlascpdrtVIDLRGDsIGYTS 98
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieIYDSKikvDGKVLYFGKDiFQID--------AIKLRKE-VGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 99 QFLDEIPRVPAVDVVARPLIEQGV-DREDARSVARDLLSALSVPESLWQAY--PAT-FSGGERQRVNLAQALAPKPDLLL 174
Cdd:PRK14246 97 QQPNPFPHLSIYDNIAYPLKSHGIkEKREIKKIVEECLRKVGLWKEVYDRLnsPASqLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 493478021 175 LDEPTSALDPDTRRaAIDLLSTYLGSETTVVGVFHN 210
Cdd:PRK14246 177 MDEPTSMIDIVNSQ-AIEKLITELKNEIAIVIVSHN 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-194 |
7.72e-19 |
|
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: 84.80 E-value: 7.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSktfdMHVLGDTQVVgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLASCPD 83
Cdd:COG4618 331 LSVENLT----VVPPGSKRPI-LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL---DG-ADLSQWDR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 rtviDLRGDSIGYTSQ---FLD----E-IPRVPAVD---VVarplieqgvdrEDARSV-ARDLLsaLSVPeslwQAY--- 148
Cdd:COG4618 402 ----EELGRHIGYLPQdveLFDgtiaEnIARFGDADpekVV-----------AAAKLAgVHEMI--LRLP----DGYdtr 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493478021 149 ----PATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRA---AIDLL 194
Cdd:COG4618 461 igegGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAlaaAIRAL 513
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
41-240 |
9.59e-19 |
|
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: 83.31 E-value: 9.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 41 VVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPDrtviDLRGdsIGYTSQFLDEIPRVPAVDVVARPLIEQ 120
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIML----DGEDVTNVPP----HLRH--INMVFQSYALFPHMTVEENVAFGLKMR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 121 GVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTR---RAAIDLLSTY 197
Cdd:TIGR01187 71 KVPRAEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRdqmQLELKTIQEQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493478021 198 LGseTTVVGVFHNTDVVDAVADRVVVLDDGRLQRV-VPTEAYDE 240
Cdd:TIGR01187 150 LG--ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIgTPEEIYEE 191
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
26-190 |
1.07e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.54 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTY--DPSSGEVVYhsPDGDIDlascPDRTVIDlrgdsigytsqflde 103
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV--PDNQFG----REASLID--------------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 104 iprvpavdvvarplieqGVDREDARSVARDLLSA--LSVPeSLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSA 181
Cdd:COG2401 105 -----------------AIGRKGDFKDAVELLNAvgLSDA-VLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170
....*....|
gi 493478021 182 LDPDT-RRAA 190
Cdd:COG2401 167 LDRQTaKRVA 176
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-229 |
1.07e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 83.36 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDMHVlgDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEV----VYHSPDGDIDL 78
Cdd:PRK13631 21 ILRVKNLYCVFDEKQ--ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 79 ASCPDRT-----VIDLRgDSIGYTSQF------LDEIPRvpavDVVARPlIEQGVDREDARSVARDLLSALSVPESLWQA 147
Cdd:PRK13631 99 LITNPYSkkiknFKELR-RRVSMVFQFpeyqlfKDTIEK----DIMFGP-VALGVKKSEAKKLAKFYLNKMGLDDSYLER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 148 YPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHNTDVVDAVADRVVVLDDG 227
Cdd:PRK13631 173 SPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
..
gi 493478021 228 RL 229
Cdd:PRK13631 253 KI 254
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-236 |
1.45e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.45 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGevvyHSPDGDIDLAScpdRTVIDLRG-----DSIGYTSQF 100
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG----YRYSGDVLLGG---RSIFNYRDvlefrRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 101 LDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSvpesLWQAY-------PATFSGGERQRVNLAQALAPKPDLL 173
Cdd:PRK14271 110 PNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVG----LWDAVkdrlsdsPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493478021 174 LLDEPTSALDPDTRRAAIDLLSTyLGSETTVVGVFHNTDVVDAVADRVVVLDDGRLQRVVPTE 236
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRS-LADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTE 247
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-196 |
1.56e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 84.24 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 25 GLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyhSPDG----DIDLASCP-------------DRTVI 87
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI---LIDGtdirTVTRASLRrniavvfqdaglfNRSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 88 D-LRgdsIGYTSQFLDEIpRVPAVDVVARPLIEQGVDREDARSVARDllSALSvpeslwqaypatfsGGERQRVNLAQAL 166
Cdd:PRK13657 427 DnIR---VGRPDATDEEM-RAAAERAQAHDFIERKPDGYDTVVGERG--RQLS--------------GGERQRLAIARAL 486
|
170 180 190
....*....|....*....|....*....|...
gi 493478021 167 APKPDLLLLDEPTSALDPDTRR---AAIDLLST 196
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAkvkAALDELMK 519
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
26-186 |
1.85e-18 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 81.12 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLAscpDRTVIDLRgDSIGYTSQ------ 99
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILI---DG-IDIR---DISRKSLR-SMIGVVLQdtflfs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 100 --FLDEIprvpavdVVARPLIEQGVDREDARSV-ARDLLSALsvPESLwQAYP----ATFSGGERQRVNLAQALAPKPDL 172
Cdd:cd03254 91 gtIMENI-------RLGRPNATDEEVIEAAKEAgAHDFIMKL--PNGY-DTVLgengGNLSQGERQLLAIARAMLRDPKI 160
|
170
....*....|....
gi 493478021 173 LLLDEPTSALDPDT 186
Cdd:cd03254 161 LILDEATSNIDTET 174
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-210 |
2.58e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLAS 80
Cdd:PRK09536 1 MPMIDVSDLSVEF-----GDTTV--LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLV----AGDDVEA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 CPDRTVidlrgdsigytSQFLDEIPRVPAV--DVVARPLIEQGVDREDARSVARDLLSALSVPESLWQAYPATF------ 152
Cdd:PRK09536 70 LSARAA-----------SRRVASVPQDTSLsfEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFadrpvt 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 153 --SGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:PRK09536 139 slSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHD 198
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-194 |
3.41e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 82.10 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFdmhvlGD--TQVVGLDDVSFDVREGEFLAVVGESGSGKS-SLLKCLYRTYDPssGEVVYHSPDGD-I 76
Cdd:PRK11022 1 MALLNVDKLSVHF-----GDesAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLEFNgQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 77 DLASCPDRTVIDLRGDSIGYTsqFLDEIPRVPAVDVVARPLIE-----QGVDREDARSVARDLLSALSVP--ESLWQAYP 149
Cdd:PRK11022 74 DLQRISEKERRNLVGAEVAMI--FQDPMTSLNPCYTVGFQIMEaikvhQGGNKKTRRQRAIDLLNQVGIPdpASRLDVYP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493478021 150 ATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:PRK11022 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELL 196
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-210 |
4.78e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.44 E-value: 4.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 19 GDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdgDIDLASCPDRtvidlrgdSIGYTS 98
Cdd:PRK11231 13 GTKRIL--NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLG----DKPISMLSSR--------QLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 99 QFLDEIPRVPAvDVVARPLIEQGvdredaRSVARDLLSALSVP--ESLWQAYPAT------------FSGGERQRVNLAQ 164
Cdd:PRK11231 79 ALLPQHHLTPE-GITVRELVAYG------RSPWLSLWGRLSAEdnARVNQAMEQTrinhladrrltdLSGGQRQRAFLAM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493478021 165 ALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD 197
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
26-209 |
5.54e-18 |
|
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: 79.46 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLASCPDRtviDLRgdsigytsQFLDEIP 105
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI---DG-VDISKIGLH---DLR--------SRISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RvpavdvvaRPLIEQGVDRE--DARSVARDllsalsvpESLWQAY-----------------------PATFSGGERQRV 160
Cdd:cd03244 85 Q--------DPVLFSGTIRSnlDPFGEYSD--------EELWQALervglkefveslpggldtvveegGENLSVGQRQLL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493478021 161 NLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLgSETTVVGVFH 209
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIREAF-KDCTVLTIAH 196
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
26-194 |
7.22e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 80.42 E-value: 7.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyhspdgDIDLASCPDRTVIDLRgDSIGYT-----SQF 100
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI-------KIDGITISKENLKEIR-KKIGIIfqnpdNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 101 LDeiprVPAVDVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTS 180
Cdd:PRK13632 97 IG----ATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTS 171
|
170
....*....|....
gi 493478021 181 ALDPDTRRAAIDLL 194
Cdd:PRK13632 172 MLDPKGKREIKKIM 185
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
16-191 |
1.03e-17 |
|
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: 80.93 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 16 HVLGDTQVvgldDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDIdLASCPDRTVIDLRGDSIG 95
Cdd:TIGR02142 7 KRLGDFSL----DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVL---NGRT-LFDSRKGIFLPPEKRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 96 YTSQfldEIPRVPAVDVvaRPLIEQGVDREDA--RSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPKPDLL 173
Cdd:TIGR02142 79 YVFQ---EARLFPHLSV--RGNLRYGMKRARPseRRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170
....*....|....*...
gi 493478021 174 LLDEPTSALDpDTRRAAI 191
Cdd:TIGR02142 154 LMDEPLAALD-DPRKYEI 170
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
26-211 |
1.29e-17 |
|
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: 78.28 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSpdgdidlascpdrtvidlrgdSIGYTSQF----- 100
Cdd:cd03250 21 LKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG---------------------SIAYVSQEpwiqn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 101 ---LDEIprvpavdVVARPLIEQGVDRE-DARSVARDLlsalsvpeslwQAYPA-----------TFSGGERQRVNLAQA 165
Cdd:cd03250 80 gtiRENI-------LFGKPFDEERYEKViKACALEPDL-----------EILPDgdlteigekgiNLSGGQKQRISLARA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493478021 166 LAPKPDLLLLDEPTSALDPDTRRAAID-LLSTYLGSETTVVGVFHNT 211
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQL 188
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
14-211 |
1.35e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.96 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 14 DMHV-LGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCL--YRTYDPSSGEVVYhspDG-DI-DLAscpdrtvID 88
Cdd:COG0396 5 NLHVsVEGKEI--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILL---DGeDIlELS-------PD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 89 LR---GdsIGYTSQFLDEIPRVPAVD-----VVARPLIEqgVDREDARSVARDLLSALSVPESLWQAY-PATFSGGERQR 159
Cdd:COG0396 73 ERaraG--IFLAFQYPVEIPGVSVSNflrtaLNARRGEE--LSAREFLKLLKEKMKELGLDEDFLDRYvNEGFSGGEKKR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493478021 160 VNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHNT 211
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQ 200
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
11-211 |
1.55e-17 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 78.84 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 11 KTFDMHV-LGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCL--YRTYDPSSGEVVYhspdGDIDLASCPdrtvI 87
Cdd:TIGR01978 2 KIKDLHVsVEDKEI--LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILF----KGQDLLELE----P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 88 DLR-GDSIGYTSQFLDEIPRVP-------AVDVVARPLIEQGVDREDARSVARDLLSALSVPESLWQAYPAT-FSGGERQ 158
Cdd:TIGR01978 72 DERaRAGLFLAFQYPEEIPGVSnleflrsALNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEgFSGGEKK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493478021 159 RVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHNT 211
Cdd:TIGR01978 152 RNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQ 204
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-189 |
2.27e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 79.99 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFDmhvlgDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDG-DIDLA 79
Cdd:PRK09452 12 SPLVELRGISKSFD-----GKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML---DGqDITHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 80 SCPDR---TVidlrgdsigYTSQFLdeIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGE 156
Cdd:PRK09452 82 PAENRhvnTV---------FQSYAL--FPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQL-EEFAQRKPHQLSGGQ 149
|
170 180 190
....*....|....*....|....*....|...
gi 493478021 157 RQRVNLAQALAPKPDLLLLDEPTSALDPDTRRA 189
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDYKLRKQ 182
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-210 |
3.79e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 78.67 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 22 QVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDL-ASCPDRTVIDLRgDSIGYTSQF 100
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV----DDITItHKTKDKYIRPVR-KRIGMVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 101 ----LDEiprvpavDVVARPLI----EQGVDREDARSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPKPDL 172
Cdd:PRK13646 94 pesqLFE-------DTVEREIIfgpkNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 493478021 173 LLLDEPTSALDPDTRRAAIDLLSTY-LGSETTVVGVFHN 210
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHD 205
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
26-209 |
4.42e-17 |
|
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: 76.04 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLyrtydpsSGevVYHSPDGDIDLASCPDrtvidlrgdsigytSQFLdeiP 105
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-------AG--LWPWGSGRIGMPEGED--------------LLFL---P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RvpavdvvaRPLIEQGVDREdarsvardllsALSVPeslWQAypaTFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPD 185
Cdd:cd03223 71 Q--------RPYLPLGTLRE-----------QLIYP---WDD---VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180
....*....|....*....|....
gi 493478021 186 TRRAAIDLLSTYLgseTTVVGVFH 209
Cdd:cd03223 126 SEDRLYQLLKELG---ITVISVGH 146
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-184 |
6.03e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 76.81 E-value: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmhvlGDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPd 83
Cdd:cd03218 1 LRAENLSKRY-----GKRKVV--NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL----DGQDITKLP- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 rtvIDLR-GDSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNL 162
Cdd:cd03218 69 ---MHKRaRLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEI 144
|
170 180
....*....|....*....|..
gi 493478021 163 AQALAPKPDLLLLDEPTSALDP 184
Cdd:cd03218 145 ARALATNPKFLLLDEPFAGVDP 166
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
26-184 |
6.19e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.51 E-value: 6.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYD--PS---SGEVVY-----HSPDGDidlascpdrtVIDLRGDsIG 95
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYnghniYSPRTD----------TVDLRKE-IG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 96 YTSQFLDEIPRVPAVDVVARPLIEQGVDRE--DArSVARDLLSAlsvpeSLW-------QAYPATFSGGERQRVNLAQAL 166
Cdd:PRK14239 90 MVFQQPNPFPMSIYENVVYGLRLKGIKDKQvlDE-AVEKSLKGA-----SIWdevkdrlHDSALGLSGGQQQRVCIARVL 163
|
170
....*....|....*...
gi 493478021 167 APKPDLLLLDEPTSALDP 184
Cdd:PRK14239 164 ATSPKIILLDEPTSALDP 181
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
28-191 |
7.55e-17 |
|
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: 78.60 E-value: 7.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 28 DVSFDVREGEFLAVVGESGSGKSSLLKC---LYRtydPSSGEVVYhspDGDI--DlascpDRTVIDL----RgdSIGYTS 98
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRL---GGEVlqD-----SARGIFLpphrR--RIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 99 Q----FldeiprvPAVDVvaRPLIEQGVDREDARSVARDLLSALSVP--ESLWQAYPATFSGGERQRVNLAQALAPKPDL 172
Cdd:COG4148 84 QearlF-------PHLSV--RGNLLYGRKRAPRAERRISFDEVVELLgiGHLLDRRPATLSGGERQRVAIGRALLSSPRL 154
|
170
....*....|....*....
gi 493478021 173 LLLDEPTSALDpDTRRAAI 191
Cdd:COG4148 155 LLMDEPLAALD-LARKAEI 172
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-187 |
7.97e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 77.78 E-value: 7.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 24 VGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLAscpDRTV--IDLRgDSIGYTSQ-- 99
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII----DGVDIT---DKKVklSDIR-KKVGLVFQyp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 100 ----FLDEIPRVPAVDVVARPLIEQGVDREDARSVArdlLSALSVpESLWQAYPATFSGGERQRVNLAQALAPKPDLLLL 175
Cdd:PRK13637 93 eyqlFEETIEKDIAFGPINLGLSEEEIENRVKRAMN---IVGLDY-EDYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170
....*....|..
gi 493478021 176 DEPTSALDPDTR 187
Cdd:PRK13637 169 DEPTAGLDPKGR 180
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-194 |
8.38e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.14 E-value: 8.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTFDMH--VLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspdgdIDla 79
Cdd:PRK15112 3 TLLEVRNLSKTFRYRtgWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL-------ID-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 80 scpDRTVIdlRGDsIGYTSQFLDEIPRVPAVDVVARPLIEQGVDredarsVARDLLSALSVPE-------SLWQA----- 147
Cdd:PRK15112 74 ---DHPLH--FGD-YSYRSQRIRMIFQDPSTSLNPRQRISQILD------FPLRLNTDLEPEQrekqiieTLRQVgllpd 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493478021 148 ----YPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:PRK15112 142 hasyYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLM 192
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-229 |
8.67e-17 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 76.38 E-value: 8.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 24 VGLDDVSF-----------DVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSpdgdIDLASCP--DRTVidlr 90
Cdd:cd03298 1 VRLDKIRFsygeqpmhfdlTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING----VDVTAAPpaDRPV---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 91 gdsigyTSQFLDEiprvpavDVVARPLIEQGVD---------REDARSVARDLLSALSVPEsLWQAYPATFSGGERQRVN 161
Cdd:cd03298 73 ------SMLFQEN-------NLFAHLTVEQNVGlglspglklTAEDRQAIEVALARVGLAG-LEKRLPGELSGGERQRVA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 162 LAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTyLGSET--TVVGVFHNTDVVDAVADRVVVLDDGRL 229
Cdd:cd03298 139 LARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD-LHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
26-194 |
1.02e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.10 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVY-HSPDGDIDLAscpdrtviDLRGDsIGYT-----SQ 99
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYnNQAITDDNFE--------KLRKH-IGIVfqnpdNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 100 FLDEIPRVPavdvVARPLIEQGVDREDARSVARDLLS-------ALSVPESLwqaypatfSGGERQRVNLAQALAPKPDL 172
Cdd:PRK13648 96 FVGSIVKYD----VAFGLENHAVPYDEMHRRVSEALKqvdmlerADYEPNAL--------SGGQKQRVAIAGVLALNPSV 163
|
170 180
....*....|....*....|..
gi 493478021 173 LLLDEPTSALDPDTRRAAIDLL 194
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLV 185
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-184 |
1.90e-16 |
|
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: 75.79 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLsktfdmHV-LGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDG-DIDL 78
Cdd:COG0410 1 MPMLEVENL------HAgYGGIHV--LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRF---DGeDITG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 79 AScPDRTVidLRGdsIGYtsqfldeiprVPavdvvarplieQG--------VD---------REDARSVARDLLSALSV- 140
Cdd:COG0410 70 LP-PHRIA--RLG--IGY----------VP-----------EGrrifpsltVEenlllgayaRRDRAEVRADLERVYELf 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493478021 141 P---ESLWQayPA-TFSGGERQRVNLAQALAPKPDLLLLDEPTSALDP 184
Cdd:COG0410 124 PrlkERRRQ--RAgTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAP 169
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-179 |
1.95e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.75 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTfdmhvlgdtqvVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYH-------SPDG 74
Cdd:COG1129 255 VVLEVEGLSVG-----------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgkpvrirSPRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 75 DID--LASCP-DRtvidlRGDSIgytsqFLDE-IPR---VPAVDVVARPLIeqgVDREDARSVARDLLSALSV-PESLWQ 146
Cdd:COG1129 324 AIRagIAYVPeDR-----KGEGL-----VLDLsIREnitLASLDRLSRGGL---LDRRRERALAEEYIKRLRIkTPSPEQ 390
|
170 180 190
....*....|....*....|....*....|...
gi 493478021 147 AYpATFSGGERQRVNLAQALAPKPDLLLLDEPT 179
Cdd:COG1129 391 PV-GNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
26-183 |
2.82e-16 |
|
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: 77.39 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyhspdgDIDLAscpdrtviDLR-------GDSIGYTS 98
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV-------RLDGA--------DLKqwdretfGKHIGYLP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 99 QFLDEIPRVPAVDVvARplIEQGVDREDARSVARdLLSALSVPESLWQAYP-------ATFSGGERQRVNLAQALAPKPD 171
Cdd:TIGR01842 399 QDVELFPGTVAENI-AR--FGENADPEKIIEAAK-LAGVHELILRLPDGYDtvigpggATLSGGQRQRIALARALYGDPK 474
|
170
....*....|..
gi 493478021 172 LLLLDEPTSALD 183
Cdd:TIGR01842 475 LVVLDEPNSNLD 486
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-197 |
3.32e-16 |
|
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: 75.00 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLkclyrtyDPSSGEVVYHS-PDGDIDLASCPDRtvIDLRGDSIGYTSQFLDEI 104
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLL-------DAISGRVEGGGtTSGQILFNGQPRK--PDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 105 PRVPAVDVVA----RPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTS 180
Cdd:cd03234 94 PGLTVRETLTytaiLRLPRKSSDAIRKKRVEDVLLRDLAL-TRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170
....*....|....*..
gi 493478021 181 ALDPDTRRAAIDLLSTY 197
Cdd:cd03234 173 GLDSFTALNLVSTLSQL 189
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
26-186 |
3.46e-16 |
|
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: 74.37 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyhSPDGdIDLASCPdrtVIDLRgDSIGYtsqfldeIP 105
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI---EIDG-IDISTIP---LEDLR-SSLTI-------IP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPavdVVARPLIEQGVDREDARSvARDLLSALSVPESlwqayPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPD 185
Cdd:cd03369 89 QDP---TLFSGTIRSNLDPFDEYS-DEEIYGALRVSEG-----GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
.
gi 493478021 186 T 186
Cdd:cd03369 160 T 160
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-184 |
3.55e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.50 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 20 DTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIDlascpDRTVIDLRgDSIGYTSQ 99
Cdd:PRK13639 14 GTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYD-----KKSLLEVR-KTVGIVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 100 FLDEIPRVPAV--DVVARPLiEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDE 177
Cdd:PRK13639 86 NPDDQLFAPTVeeDVAFGPL-NLGLSKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
....*..
gi 493478021 178 PTSALDP 184
Cdd:PRK13639 164 PTSGLDP 170
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
26-183 |
4.22e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.05 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYdPSSGE------------------------VVYHSPDGDIDlasc 81
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEiwfdgqplhnlnrrqllpvrhriqVVFQDPNSSLN---- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 82 PDRTVIdlrgdsigytsQFLDEIPRV--PAVDVVARpliEQGVdREDARSVARDllsalsvPESLwQAYPATFSGGERQR 159
Cdd:PRK15134 377 PRLNVL-----------QIIEEGLRVhqPTLSAAQR---EQQV-IAVMEEVGLD-------PETR-HRYPAEFSGGQRQR 433
|
170 180
....*....|....*....|....
gi 493478021 160 VNLAQALAPKPDLLLLDEPTSALD 183
Cdd:PRK15134 434 IAIARALILKPSLIILDEPTSSLD 457
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-210 |
4.42e-16 |
|
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: 74.10 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 14 DMHV-LGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCL--YRTYDPSSGEVVYhspDG-DIDLASCPDRTvidL 89
Cdd:cd03217 5 DLHVsVGGKEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILF---KGeDITDLPPEERA---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 90 RGdsIGYTSQfldEIPRVPAVDVvarplieqgvdredarsvaRDLLSALSVpeslwqaypaTFSGGERQRVNLAQALAPK 169
Cdd:cd03217 77 LG--IFLAFQ---YPPEIPGVKN-------------------ADFLRYVNE----------GFSGGEKKRNEILQLLLLE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493478021 170 PDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY 163
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
26-210 |
6.29e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.82 E-value: 6.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYD--PS---SGEVVYHSP---DGDIDLASCPDRtvidlrgdsIGYT 97
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKnlyAPDVDPVEVRRR---------IGMV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 98 SQFLDEIPRVPAVDVVARPLIeQGVDREDARSVARDLLSAL---SVPESLWQAyPATFSGGERQRVNLAQALAPKPDLLL 174
Cdd:PRK14243 97 FQKPNPFPKSIYDNIAYGARI-NGYKGDMDELVERSLRQAAlwdEVKDKLKQS-GLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 493478021 175 LDEPTSALDP-DTRRaaIDLLSTYLGSETTVVGVFHN 210
Cdd:PRK14243 175 MDEPCSALDPiSTLR--IEELMHELKEQYTIIIVTHN 209
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-194 |
6.44e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.66 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTFDMHVlgdtqvvGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLyrtydpsSGEVVY-HSPDGDIDL-- 78
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQ-------ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGdKSAGSHIELlg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 79 --ASCPDRTVIDLRGD--SIGYTSQFLDEIPRVPAVDVV------ARPLIEQGVdREDARSVARDLLSALSVPESLWQAY 148
Cdd:PRK09984 69 rtVQREGRLARDIRKSraNTGYIFQQFNLVNRLSVLENVligalgSTPFWRTCF-SWFTREQKQRALQALTRVGMVHFAH 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493478021 149 P--ATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:PRK09984 148 QrvSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTL 195
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-210 |
7.43e-16 |
|
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: 73.94 E-value: 7.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDmhvLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLASCPd 83
Cdd:cd03266 2 ITADALTKRFR---DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV---DG-FDVVKEP- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 rtvIDLRgDSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLwQAYPATFSGGERQRVNLA 163
Cdd:cd03266 74 ---AEAR-RRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELL-DRRVGGFSTGMRQKVAIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493478021 164 QALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHI 195
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-194 |
8.81e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.21 E-value: 8.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLAscpDRTVIDLRgDSIGYTSQ----FL 101
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL---DG-HDLR---DYTLASLR-NQVALVSQnvhlFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 102 DEIPRVPAVdvvARpliEQGVDREDARSVARdLLSALSVPESLWQAYP-------ATFSGGERQRVNLAQALAPKPDLLL 174
Cdd:PRK11176 431 DTIANNIAY---AR---TEQYSREQIEEAAR-MAYAMDFINKMDNGLDtvigengVLLSGGQRQRIAIARALLRDSPILI 503
|
170 180
....*....|....*....|...
gi 493478021 175 LDEPTSALDPDTRRA---AIDLL 194
Cdd:PRK11176 504 LDEATSALDTESERAiqaALDEL 526
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-209 |
9.05e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.18 E-value: 9.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYD--PS---SGEVVYhspDGD 75
Cdd:PRK14247 1 MNKIEIRDLKVSF-----GQVEV--LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYL---DGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 76 iDLASCPdrtVIDLRgDSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARdLLSALSVPEsLWQ-------AY 148
Cdd:PRK14247 71 -DIFKMD---VIELR-RRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQER-VRWALEKAQ-LWDevkdrldAP 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493478021 149 PATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTrRAAIDLLSTYLGSETTVVGVFH 209
Cdd:PRK14247 144 AGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPEN-TAKIESLFLELKKDMTIVLVTH 203
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-236 |
1.07e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.11 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 11 KTFDMHV-LGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspDGDIDLAS----CPDRT 85
Cdd:PRK14267 6 ETVNLRVyYGSNHV--IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARV----EGEVRLFGrniySPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 86 VIDLRgDSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDR---EDARSVARDLLSAlsvpeSLWQA-------YPATFSGG 155
Cdd:PRK14267 80 PIEVR-REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKskkELDERVEWALKKA-----ALWDEvkdrlndYPSNLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 156 ERQRVNLAQALAPKPDLLLLDEPTSALDPdTRRAAIDLLSTYLGSETTVVGVFHNTDVVDAVADRVVVLDDGRLQRVVPT 235
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPT 232
|
.
gi 493478021 236 E 236
Cdd:PRK14267 233 R 233
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-210 |
1.31e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.58 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MT-VLSVDGLSKTFDMH---------------VLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSS 64
Cdd:COG1134 1 MSsMIEVENVSKSYRLYhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 65 GEVVYH----SPdgdIDLASC--PDRTVID---LRGDSIGYTSQFLDEipRVPAV-------DVVARPLieqgvdredar 128
Cdd:COG1134 81 GRVEVNgrvsAL---LELGAGfhPELTGREniyLNGRLLGLSRKEIDE--KFDEIvefaelgDFIDQPV----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 129 svardllsalsvpeslwqaypATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVF 208
Cdd:COG1134 145 ---------------------KTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVS 203
|
..
gi 493478021 209 HN 210
Cdd:COG1134 204 HS 205
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
25-195 |
1.42e-15 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 75.31 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 25 GLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyhSPDGdIDLASCP------------------DRTV 86
Cdd:TIGR01192 350 GVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQI---LIDG-IDINTVTreslrksiatvfqdaglfNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 87 IDlrGDSIGYTSQFLDEIPRVPAVdVVARPLIEQGVDREDARSVARDllsalsvpeslwqaypATFSGGERQRVNLAQAL 166
Cdd:TIGR01192 426 RE--NIRLGREGATDEEVYEAAKA-AAAHDFILKRSNGYDTLVGERG----------------NRLSGGERQRLAIARAI 486
|
170 180 190
....*....|....*....|....*....|..
gi 493478021 167 APKPDLLLLDEPTSALDPDTR---RAAIDLLS 195
Cdd:TIGR01192 487 LKNAPILVLDEATSALDVETEarvKNAIDALR 518
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-182 |
1.47e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.33 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFdmhvlgdTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspdgdIDLAS 80
Cdd:PRK11288 2 SPYLSFDGIGKTF-------PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL-------IDGQE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 CPDRTVIDLRGDSIGYTSQfldEIPRVPAVDVVARPLIEQ-----G-VDREDARSVARDLLSALSV---PeslwQAYPAT 151
Cdd:PRK11288 68 MRFASTTAALAAGVAIIYQ---ELHLVPEMTVAENLYLGQlphkgGiVNRRLLNYEAREQLEHLGVdidP----DTPLKY 140
|
170 180 190
....*....|....*....|....*....|.
gi 493478021 152 FSGGERQRVNLAQALAPKPDLLLLDEPTSAL 182
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-194 |
2.96e-15 |
|
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: 71.31 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSktfdmhvLGDTqvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDG-DIDLAS 80
Cdd:cd03215 3 PVLEVRGLS-------VKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITL---DGkPVTRRS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 CPDRtvIDLRgdsIGYtsqfldeiprVPavdvvarplieqgvdrEDARSVArdLLSALSVPESLwqAYPATFSGGERQRV 160
Cdd:cd03215 69 PRDA--IRAG---IAY----------VP----------------EDRKREG--LVLDLSVAENI--ALSSLLSGGNQQKV 113
|
170 180 190
....*....|....*....|....*....|....
gi 493478021 161 NLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:cd03215 114 VLARWLARDPRVLILDEPTRGVDVGAKAEIYRLI 147
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-194 |
2.98e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.44 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFdmhvlgdTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCL-----YRTYDpssGEVVYhspDGDId 77
Cdd:NF040905 1 ILEMRGITKTF-------PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvypHGSYE---GEILF---DGEV- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 78 lasCPDRTVIDLRGDSIGYTSQFLDEIPRVPavdvVARPLI---EQG----VDREDARSVARDLLSALSVPESlwqayPA 150
Cdd:NF040905 67 ---CRFKDIRDSEALGIVIIHQELALIPYLS----IAENIFlgnERAkrgvIDWNETNRRARELLAKVGLDES-----PD 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493478021 151 TFSG----GERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:NF040905 135 TLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLL 182
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
3-184 |
4.23e-15 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 71.92 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFdmhvlGDTQVVglDDVSFDVREGEFLAVVGESGSGKSSllkCLYRT---YDPSSGEVVYhspdGDIDLA 79
Cdd:TIGR04406 1 TLVAENLIKSY-----KKRKVV--NDVSLSVKSGEIVGLLGPNGAGKTT---SFYMIvglVRPDAGKILI----DGQDIT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 80 SCPdrtvIDLRGDS-IGYTSQfldE--IPRVPAV--DVVARPLIEQGVDREDARSVARDLLSALSVPESLWQAyPATFSG 154
Cdd:TIGR04406 67 HLP----MHERARLgIGYLPQ---EasIFRKLTVeeNIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNK-AMSLSG 138
|
170 180 190
....*....|....*....|....*....|
gi 493478021 155 GERQRVNLAQALAPKPDLLLLDEPTSALDP 184
Cdd:TIGR04406 139 GERRRVEIARALATNPKFILLDEPFAGVDP 168
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
30-237 |
4.60e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 71.71 E-value: 4.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 30 SFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspdgdidlascpdrtvidLRGDSIGYTSqfldeiprvPA 109
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIL--------------------WNGQDLTALP---------PA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 110 vdvvARPL--------------IEQGV----------DREDARSVArDLLSALSVpESLWQAYPATFSGGERQRVNLAQA 165
Cdd:COG3840 70 ----ERPVsmlfqennlfphltVAQNIglglrpglklTAEQRAQVE-QALERVGL-AGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493478021 166 LAPKPDLLLLDEPTSALDPDTRRAAIDLLSTyLGSET--TVVGVFHNTDVVDAVADRVVVLDDGRLQRVVPTEA 237
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDE-LCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-210 |
4.67e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.38 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 20 DTQVVgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDpSSGEVvyhSPDGDIDL--ASCPDRTVI--DLRG---- 91
Cdd:PRK14258 18 DTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEV---RVEGRVEFfnQNIYERRVNlnRLRRqvsm 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 92 -------------DSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARdllSALSVpeslwqaypatfSGGERQ 158
Cdd:PRK14258 93 vhpkpnlfpmsvyDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHK---SALDL------------SGGQQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493478021 159 RVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL-STYLGSETTVVGVFHN 210
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqSLRLRSELTMVIVSHN 210
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-210 |
4.95e-15 |
|
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: 71.98 E-value: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 6 VDGLSKTFDMHV----LGDT----------QVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyhS 71
Cdd:cd03267 3 VSNLSKSYRVYSkepgLIGSlkslfkrkyrEVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV---R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 72 PDGDIdlascPDRTVIDLR---GDSIGYTSQFLDEIPRVPAVDVVARPLieqGVDREDARSVARDLLSALSVPESLWQay 148
Cdd:cd03267 80 VAGLV-----PWKRRKKFLrriGVVFGQKTQLWWDLPVIDSFYLLAAIY---DLPPARFKKRLDELSELLDLEELLDT-- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493478021 149 PA-TFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGS-ETTVVGVFHN 210
Cdd:cd03267 150 PVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHY 213
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-209 |
7.40e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.43 E-value: 7.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVV--------YHSPDG 74
Cdd:TIGR03719 4 IYTMNRVSKVVP----PKKEI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARpqpgikvgYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 75 DIDlascPDRTVIDLRGDSIGYTSQFLDEIPRVPA--------VDVVARpliEQG-----VDREDARSVARDL---LSAL 138
Cdd:TIGR03719 78 QLD----PTKTVRENVEEGVAEIKDALDRFNEISAkyaepdadFDKLAA---EQAelqeiIDAADAWDLDSQLeiaMDAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493478021 139 SVPEslWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTrraaIDLLSTYLGS-ETTVVGVFH 209
Cdd:TIGR03719 151 RCPP--WDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEyPGTVVAVTH 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-210 |
7.97e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 73.32 E-value: 7.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDmhvlGDTQVVgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLASCPD 83
Cdd:PRK11160 339 LTLNNVSFTYP----DQPQPV-LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL----NGQPIADYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RTvidLRgDSIGYTSQfldeiprvpavdvvaRPLIEQGVDRED---ARSVARD-----------LLSALSVPESL--W-- 145
Cdd:PRK11160 410 AA---LR-QAISVVSQ---------------RVHLFSATLRDNlllAAPNASDealievlqqvgLEKLLEDDKGLnaWlg 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493478021 146 ----QaypatFSGGERQRVNLAQAL---APkpdLLLLDEPTSALDPDTRRAAIDLLSTYlGSETTVVGVFHN 210
Cdd:PRK11160 471 eggrQ-----LSGGEQRRLGIARALlhdAP---LLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHR 533
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-238 |
2.03e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.60 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFdmhvlGDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDIDLAS 80
Cdd:PRK11000 1 MASVTLRNVTKAY-----GDVVIS--KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI----GEKRMND 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 CP--DRtvidlrgdSIGYTSQFLDEIPRVPAVDVVARPLIEQGVDREDARS----VARDLLSAlsvpeSLWQAYPATFSG 154
Cdd:PRK11000 70 VPpaER--------GVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQrvnqVAEVLQLA-----HLLDRKPKALSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 155 GERQRVNLAQALAPKPDLLLLDEPTSALDPDTR---RAAIDLLSTYLGSetTVVGVFHNTDVVDAVADRVVVLDDGRLQR 231
Cdd:PRK11000 137 GQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRvqmRIEISRLHKRLGR--TMIYVTHDQVEAMTLADKIVVLDAGRVAQ 214
|
....*...
gi 493478021 232 V-VPTEAY 238
Cdd:PRK11000 215 VgKPLELY 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-183 |
3.46e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.21 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSktfdmhVLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDG-DIDLAS 80
Cdd:COG3845 256 VVLEVENLS------VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL---DGeDITGLS 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 CpdRTVIDLRgdsIGYtsqfldeIP--R-----VPAVDVV--------ARPLIEQG--VDREDARSVARDLLSALSV-PE 142
Cdd:COG3845 327 P--RERRRLG---VAY-------IPedRlgrglVPDMSVAenlilgryRRPPFSRGgfLDRKAIRAFAEELIEEFDVrTP 394
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493478021 143 SLWQAyPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALD 183
Cdd:COG3845 395 GPDTP-ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-194 |
3.86e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.76 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGeVVYHSPDgdidlas 80
Cdd:PRK09544 2 TSLVSLENVSVSF-----GQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-VIKRNGK------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 cpdrtvidLRgdsIGYTSQFLDEIPRVPAVdvVARPL-IEQGVDREDarsvardLLSALSVPES--LWQAYPATFSGGER 157
Cdd:PRK09544 67 --------LR---IGYVPQKLYLDTTLPLT--VNRFLrLRPGTKKED-------ILPALKRVQAghLIDAPMQKLSGGET 126
|
170 180 190
....*....|....*....|....*....|....*..
gi 493478021 158 QRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLI 163
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-184 |
5.78e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 68.90 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFdmhvlGDTQVVglDDVSFDVREGEFLAVVGESGSGKSS-------LLKclyrtydPSSGEVVYhspd 73
Cdd:COG1137 1 MMTLEAENLVKSY-----GKRTVV--KDVSLEVNQGEIVGLLGPNGAGKTTtfymivgLVK-------PDSGRIFL---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 74 GDIDLASCPdrtvIDLR---GdsIGYTSQfldE--IPR-------VPAVdvvarpLIEQGVDREDARSVARDLLSALSVp 141
Cdd:COG1137 63 DGEDITHLP----MHKRarlG--IGYLPQ---EasIFRkltvednILAV------LELRKLSKKEREERLEELLEEFGI- 126
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493478021 142 ESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDP 184
Cdd:COG1137 127 THLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDP 169
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-210 |
6.36e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 69.25 E-value: 6.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDiDLASCPD-RTVIDL-----RGDSIGYTSQ 99
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG-DFSKLQGiRKLVGIvfqnpETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 100 ----FLDEIPRVPAVDV---VARPLIEQGVDREDARSvardllsalsvpeslwqayPATFSGGERQRVNLAQALAPKPDL 172
Cdd:PRK13644 97 edlaFGPENLCLPPIEIrkrVDRALAEIGLEKYRHRS-------------------PKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 493478021 173 LLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHN 195
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-205 |
1.02e-13 |
|
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: 68.27 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 20 DTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGD--IDLASCPDRTVIDLRG------ 91
Cdd:cd03248 26 DTLV--LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL---DGKpiSQYEHKYLHSKVSLVGqepvlf 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 92 -----DSIGYTSQFLdEIPRVPAVDVVAR-----PLIEQGVDREdarsvardllsalsVPESlwqayPATFSGGERQRVN 161
Cdd:cd03248 101 arslqDNIAYGLQSC-SFECVKEAAQKAHahsfiSELASGYDTE--------------VGEK-----GSQLSGGQKQRVA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493478021 162 LAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLV 204
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
26-229 |
1.11e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 68.68 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspdgdidlascpdrtvidLRGDSIgyTSQFLDEIP 105
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVL--------------------IRGEPI--TKENIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPAV------DVVARPLIEQ---------GVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNLAQALAPKP 170
Cdd:PRK13652 78 KFVGLvfqnpdDQIFSPTVEQdiafgpinlGLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493478021 171 DLLLLDEPTSALDPDTRRAAIDLLSTYlgSET---TVVGVFHNTDVVDAVADRVVVLDDGRL 229
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDL--PETygmTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-182 |
1.54e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.43 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmhvlgdTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspdgdIDLASCPD 83
Cdd:PRK09700 6 ISMAGIGKSF-------GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT-------INNINYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RTVIDLRGDSIGYTSQFL---DE--------IPRVPAVDVVARPLieqgVDREDARSVARDLLSALSVPESLwQAYPATF 152
Cdd:PRK09700 72 LDHKLAAQLGIGIIYQELsviDEltvlenlyIGRHLTKKVCGVNI----IDWREMRVRAAMMLLRVGLKVDL-DEKVANL 146
|
170 180 190
....*....|....*....|....*....|
gi 493478021 153 SGGERQRVNLAQALAPKPDLLLLDEPTSAL 182
Cdd:PRK09700 147 SISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
26-194 |
1.70e-13 |
|
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: 69.38 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEV-VYHSPDGDIDLAScpdrtvidLRGdSIGYTSQ----- 99
Cdd:TIGR01193 490 LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIlLNGFSLKDIDRHT--------LRQ-FINYLPQepyif 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 100 ---FLDEIpRVPAVDVVARPLIEQGVD----REDARSVARDLLSALSVPESlwqaypaTFSGGERQRVNLAQALAPKPDL 172
Cdd:TIGR01193 561 sgsILENL-LLGAKENVSQDEIWAACEiaeiKDDIENMPLGYQTELSEEGS-------SISGGQKQRIALARALLTDSKV 632
|
170 180
....*....|....*....|..
gi 493478021 173 LLLDEPTSALDPDTRRAAIDLL 194
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNL 654
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-187 |
1.79e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.20 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 20 DTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyhspdgDIDLASCPDRTVIDLRgDSIGYTSQ 99
Cdd:PRK13642 17 ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV-------KIDGELLTAENVWNLR-RKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 100 FLD-EIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPEsLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEP 178
Cdd:PRK13642 89 NPDnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLD-FKTREPARLSGGQKQRVAVAGIIALRPEIIILDES 167
|
....*....
gi 493478021 179 TSALDPDTR 187
Cdd:PRK13642 168 TSMLDPTGR 176
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
26-209 |
1.85e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 69.37 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGD--IDLASCPDRTVIDLRG-----------D 92
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL---DGVplVQYDHHYLHRQVALVGqepvlfsgsvrE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 93 SIGYTSQFL-DEIPRVPAVDVVARPLI---EQGVDREdarsvardllsalsVPESLWQaypatFSGGERQRVNLAQALAP 168
Cdd:TIGR00958 574 NIAYGLTDTpDEEIMAAAKAANAHDFImefPNGYDTE--------------VGEKGSQ-----LSGGQKQRIAIARALVR 634
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493478021 169 KPDLLLLDEPTSALDPDTRRAAIDLLSTYlgsETTVVGVFH 209
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQESRSRA---SRTVLLIAH 672
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-188 |
1.95e-13 |
|
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: 69.55 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPS------SGEVVYHSPDGDIDLASCPDRTVIDLRGDSIGYTS- 98
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSegkikhSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSv 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 99 ----QFLDEIPRVPAVDVVarPLIEQGVdredarsvardllsalsvpeslwqaypaTFSGGERQRVNLAQALAPKPDLLL 174
Cdd:TIGR01271 522 ikacQLEEDIALFPEKDKT--VLGEGGI----------------------------TLSGGQRARISLARAVYKDADLYL 571
|
170
....*....|....
gi 493478021 175 LDEPTSALDPDTRR 188
Cdd:TIGR01271 572 LDSPFTHLDVVTEK 585
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-200 |
2.00e-13 |
|
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: 69.19 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDMHVLgdtqvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGD-IDLASC 81
Cdd:TIGR03719 322 VIEAENLTKAFGDKLL-------IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI----GEtVKLAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 82 --------PDRTVIDLrgdsigyTSQFLDEIpRVPAVDVVARPLIEQ----GVDRedarsvardllsalsvpeslwQAYP 149
Cdd:TIGR03719 391 dqsrdaldPNKTVWEE-------ISGGLDII-KLGKREIPSRAYVGRfnfkGSDQ---------------------QKKV 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493478021 150 ATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGS 200
Cdd:TIGR03719 442 GQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGC 492
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-189 |
2.89e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.21 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 9 LSKTFdmhvlGDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspdgdIDLASCPDRTvID 88
Cdd:PRK11432 12 ITKRF-----GSNTVI--DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF-------IDGEDVTHRS-IQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 89 LRGDSIGYTSQFLdeIPRVPAVDVVARPLIEQGVDREDARSVARDLLsALSVPESLWQAYPATFSGGERQRVNLAQALAP 168
Cdd:PRK11432 77 QRDICMVFQSYAL--FPHMSLGENVGYGLKMLGVPKEERKQRVKEAL-ELVDLAGFEDRYVDQISGGQQQRVALARALIL 153
|
170 180
....*....|....*....|.
gi 493478021 169 KPDLLLLDEPTSALDPDTRRA 189
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRS 174
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-184 |
3.11e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.84 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFDmhvlgDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspDGDIDLAS 80
Cdd:PRK10895 1 MATLTAKNLAKAYK-----GRRVV--EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID--DEDISLLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 CPDRTvidLRGdsIGYTSQFLDEIPRVPAVD-VVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQR 159
Cdd:PRK10895 72 LHARA---RRG--IGYLPQEASIFRRLSVYDnLMAVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRR 145
|
170 180
....*....|....*....|....*
gi 493478021 160 VNLAQALAPKPDLLLLDEPTSALDP 184
Cdd:PRK10895 146 VEIARALAANPKFILLDEPFAGVDP 170
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-194 |
3.85e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.34 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 25 GLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVV---YHSPDGDIDLascpdRTVIDLRGDsIGYTSQF- 100
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIvgdYAIPANLKKI-----KEVKRLRKE-IGLVFQFp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 101 -----LDEIPRvpavDVVARPlIEQGVDREDARSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPKPDLLLL 175
Cdd:PRK13645 100 eyqlfQETIEK----DIAFGP-VNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVL 174
|
170
....*....|....*....
gi 493478021 176 DEPTSALDPDTRRAAIDLL 194
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINLF 193
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
26-210 |
4.28e-13 |
|
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: 66.40 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdGDIdlaSCPdrtvidlrgdsIGYTSQFLDEIp 105
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR---GRV---SSL-----------LGLGGGFNPEL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 rvPAVDVVARPLIEQGVDREDARSVARDLLS------ALSVPESlwqaypaTFSGGERQRVNLAQALAPKPDLLLLDEPT 179
Cdd:cd03220 100 --TGRENIYLNGRLLGLSRKEIDEKIDEIIEfselgdFIDLPVK-------TYSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190
....*....|....*....|....*....|.
gi 493478021 180 SALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:cd03220 171 AVGDAAFQEKCQRRLRELLKQGKTVILVSHD 201
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-209 |
4.58e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.84 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyHSPdgdidlascp 82
Cdd:PRK11819 6 IYTMNRVSKVVP----PKKQI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR-PAP---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 drtvidlrGDSIGYTSQ--FLDEIPRV---------PAVDVVAR----------------PLI-EQG-----VDREDARS 129
Cdd:PRK11819 69 --------GIKVGYLPQepQLDPEKTVrenveegvaEVKAALDRfneiyaayaepdadfdALAaEQGelqeiIDAADAWD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 130 VARDL---LSALSVPEslWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTrraaIDLLSTYLGS-ETTVV 205
Cdd:PRK11819 141 LDSQLeiaMDALRCPP--WDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLEQFLHDyPGTVV 214
|
....
gi 493478021 206 GVFH 209
Cdd:PRK11819 215 AVTH 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
28-183 |
4.92e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 28 DVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDG--DIDLA-------------------------- 79
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNlkDINLKwwrskigvvsqdpllfsnsiknniky 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 80 ---SCPDRTVIDLRGDSIGYTSQ----------------FLDEIPRVPAVDVVARPLIEQGVDREDARSVAR-----DLL 135
Cdd:PTZ00265 483 slySLKDLEALSNYYNEDGNDSQenknkrnscrakcagdLNDMSNTTDSNELIEMRKNYQTIKDSEVVDVSKkvlihDFV 562
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493478021 136 SALSVP-ESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALD 183
Cdd:PTZ00265 563 SALPDKyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-209 |
8.96e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 65.87 E-value: 8.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 5 SVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLASCPDR 84
Cdd:COG4604 3 EIKNVSKRY-----GGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLV---DG-LDVATTPSR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 85 tvidlrgdsigytsqfldEIPRVPAV-----DVVARPLIEQGV------------DREDARSVAR-----DLlsalsvpE 142
Cdd:COG4604 72 ------------------ELAKRLAIlrqenHINSRLTVRELVafgrfpyskgrlTAEDREIIDEaiaylDL-------E 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478021 143 SLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDP--------DTRRAAIDLlstylgsETTVVGVFH 209
Cdd:COG4604 127 DLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvqmmkLLRRLADEL-------GKTVVIVLH 194
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-184 |
1.33e-12 |
|
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: 64.73 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFdmhvlGDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDidlascpD 83
Cdd:TIGR03740 1 LETKNLSKRF-----GKQTAV--NNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIF---DGH-------P 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 84 RTVIDLRgdSIGYtsqfLDEIPrvpavdvvarPLIEQGVDREDARSVArdllSALSVPESLWQAYPAT------------ 151
Cdd:TIGR03740 64 WTRKDLH--KIGS----LIESP----------PLYENLTARENLKVHT----TLLGLPDSRIDEVLNIvdltntgkkkak 123
|
170 180 190
....*....|....*....|....*....|....
gi 493478021 152 -FSGGERQRVNLAQALAPKPDLLLLDEPTSALDP 184
Cdd:TIGR03740 124 qFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDP 157
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-232 |
1.73e-12 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 64.50 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 30 SFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDIDLASCPDRTVIdlrgdsigytSQFLDEIPRVPA 109
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKV---NDQSHTGLAPYQRPV----------SMLFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 110 VDV-------VARPLIEQGVDREDARSVAR-----DLLSALsvPESLwqaypatfSGGERQRVNLAQALAPKPDLLLLDE 177
Cdd:TIGR01277 85 LTVrqniglgLHPGLKLNAEQQEKVVDAAQqvgiaDYLDRL--PEQL--------SGGQRQRVALARCLVRPNPILLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493478021 178 PTSALDPDTRRAAIDLLSTyLGSET--TVVGVFHNTDVVDAVADRVVVLDDGRLQRV 232
Cdd:TIGR01277 155 PFSALDPLLREEMLALVKQ-LCSERqrTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-190 |
1.78e-12 |
|
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: 64.74 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 32 DVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVV-----------YHSPDGDIdlascpdrTVIDL---RGDSIGYT 97
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEieldtvsykpqYIKADYEG--------TVRDLlssITKDFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 98 SQFLDEIprvpavdvvARPL-IEQGVDREdarsvardllsalsVPEslwqaypatFSGGERQRVNLAQALAPKPDLLLLD 176
Cdd:cd03237 93 PYFKTEI---------AKPLqIEQILDRE--------------VPE---------LSGGELQRVAIAACLSKDADIYLLD 140
|
170
....*....|....
gi 493478021 177 EPTSALDPDTRRAA 190
Cdd:cd03237 141 EPSAYLDVEQRLMA 154
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
27-229 |
2.07e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.01 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 27 DDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDiDLASCPDRTVidlrGDSIGYTSQFLDEIPR 106
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL---DGE-HIQHYASKEV----ARRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 107 VPAVDVVAR------PLIEQGvDREDARSVARdLLSALSVPESLWQAYPaTFSGGERQRVNLAQALAPKPDLLLLDEPTS 180
Cdd:PRK10253 96 ITVQELVARgryphqPLFTRW-RKEDEEAVTK-AMQATGITHLADQSVD-TLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493478021 181 ALDPDTRRAAIDLLSTyLGSET--TVVGVFHNTDVVDAVADRVVVLDDGRL 229
Cdd:PRK10253 173 WLDISHQIDLLELLSE-LNREKgyTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-183 |
2.52e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.68 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDMHVLgdtqvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVY------------HS 71
Cdd:PRK15064 320 LEVENLTKGFDNGPL-------FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWsenanigyyaqdHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 72 PDGDIDLascpdrTVIDlrgdsigYTSQFldeipRVPAVDvvarpliEQGVdredaRSV-ARDLLSALSVPESlwqayPA 150
Cdd:PRK15064 393 YDFENDL------TLFD-------WMSQW-----RQEGDD-------EQAV-----RGTlGRLLFSQDDIKKS-----VK 437
|
170 180 190
....*....|....*....|....*....|...
gi 493478021 151 TFSGGERQRVNLAQALAPKPDLLLLDEPTSALD 183
Cdd:PRK15064 438 VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-182 |
2.76e-12 |
|
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: 65.62 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDmhvlgdtQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLyrtydpsSGEVVYHSPDGDIDLASCP 82
Cdd:TIGR02633 1 LLEMKGIVKTFG-------GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIL-------SGVYPHGTWDGEIYWSGSP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 --DRTVIDLRGDSIGYTSQFLDEIPRVPAVD--VVARPLIEQGVDREDARSVAR--DLLSALSVPESLWQAYPATFSGGE 156
Cdd:TIGR02633 67 lkASNIRDTERAGIVIIHQELTLVPELSVAEniFLGNEITLPGGRMAYNAMYLRakNLLRELQLDADNVTRPVGDYGGGQ 146
|
170 180
....*....|....*....|....*.
gi 493478021 157 RQRVNLAQALAPKPDLLLLDEPTSAL 182
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSL 172
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-209 |
2.79e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.24 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFdmhvlGDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEV-VYHSPdgdidla 79
Cdd:PRK13536 39 TVAIDLAGVSKSY-----GDKAVV--NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVP------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 80 sCPDRTVIDLRGdsIGYTSQF--LDeiprvPAVDVVARPLIEQGVDREDARSVARDLLSALSVP--ESLWQAYPATFSGG 155
Cdd:PRK13536 105 -VPARARLARAR--IGVVPQFdnLD-----LEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFArlESKADARVSDLSGG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493478021 156 ERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFH 209
Cdd:PRK13536 177 MKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-209 |
3.61e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 64.86 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFDmhvlGDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKC---LYRTydpSSGEVvyhspdgDID 77
Cdd:PRK11650 1 MAGLKLQAVRKSYD----GKTQVI--KGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEI-------WIG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 78 lascpDRTVIDL----RG-----------------DSIGY------TSQflDEIPRvpAVDVVARPL-IEQGVDREdars 129
Cdd:PRK11650 65 -----GRVVNELepadRDiamvfqnyalyphmsvrENMAYglkirgMPK--AEIEE--RVAEAARILeLEPLLDRK---- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 130 vardllsalsvpeslwqayPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTR---RAAIDLLSTYLGseTTVVG 206
Cdd:PRK11650 132 -------------------PRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRvqmRLEIQRLHRRLK--TTSLY 190
|
...
gi 493478021 207 VFH 209
Cdd:PRK11650 191 VTH 193
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-187 |
4.21e-12 |
|
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: 65.19 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 32 DVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyhspDGDIDLASCP-------DRTVIDL----RGDSIGyTSQF 100
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----DEDLKISYKPqyispdyDGTVEEFlrsaNTDDFG-SSYY 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 101 LDEIprvpavdvvARPL-IEQGVDREdarsvARDLlsalsvpeslwqaypatfSGGERQRVNLAQALAPKPDLLLLDEPT 179
Cdd:COG1245 436 KTEI---------IKPLgLEKLLDKN-----VKDL------------------SGGELQRVAIAACLSRDADLYLLDEPS 483
|
....*...
gi 493478021 180 SALDPDTR 187
Cdd:COG1245 484 AHLDVEQR 491
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-205 |
4.56e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 64.76 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 4 LSVDGLSKTFDmhvlgdtQVVGLDDVSFDVREGEFLAVVGESGSG--KSSLLKclyRTYDPSSGEVVYHSPDGDIDLASC 81
Cdd:NF000106 14 VEVRGLVKHFG-------EVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPA---HV*GPDAGRRPWRF*TWCANRRAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 82 pDRTVIDLRGDSIGYTSQFLDEiprvPAVDVVARPLieqGVDREDARSVARDLLSALSVPESLWQAyPATFSGGERQRVN 161
Cdd:NF000106 84 -RRTIG*HRPVR*GRRESFSGR----ENLYMIGR*L---DLSRKDARARADELLERFSLTEAAGRA-AAKYSGGMRRRLD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493478021 162 LAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:NF000106 155 LAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVL 198
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-182 |
5.00e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFDmhvlgdtQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLyrtydpsSGEVVYHSPDGDIDLAS 80
Cdd:PRK13549 3 EYLLEMKNITKTFG-------GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-------SGVYPHGTYEGEIIFEG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 CP--DRTVIDLRGDSIGYTSQfldEIPRVPAVDV-----VARPLIEQGV-DREDARSVARDLLSALSVPESlwqayPAT- 151
Cdd:PRK13549 69 EElqASNIRDTERAGIAIIHQ---ELALVKELSVlenifLGNEITPGGImDYDAMYLRAQKLLAQLKLDIN-----PATp 140
|
170 180 190
....*....|....*....|....*....|....
gi 493478021 152 ---FSGGERQRVNLAQALAPKPDLLLLDEPTSAL 182
Cdd:PRK13549 141 vgnLGLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-194 |
5.27e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.41 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 29 VSFDVREGEFLAVVGESGSGKSSLLKCLYRTYdPSSGEVVYhspdGDIDLASCPDRTVIDLRgdsiGYTSQfldEIPRVP 108
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQF----AGQPLEAWSAAELARHR----AYLSQ---QQTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 109 AVDV-----VARPlieQGVDREDARSVARDLLSALSVPESLwqAYPA-TFSGGERQRVNLAQA-------LAPKPDLLLL 175
Cdd:PRK03695 83 AMPVfqyltLHQP---DKTRTEAVASALNEVAEALGLDDKL--GRSVnQLSGGEWQRVRLAAVvlqvwpdINPAGQLLLL 157
|
170
....*....|....*....
gi 493478021 176 DEPTSALDPdTRRAAIDLL 194
Cdd:PRK03695 158 DEPMNSLDV-AQQAALDRL 175
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
31-210 |
5.40e-12 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 63.33 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 31 FDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGevvyhspdgDIDLASCPDRTvidlRGDSIGYTSQ---FLDEIP-- 105
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKG---------TVKVAGASPGK----GWRHIGYVPQrheFAWDFPis 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 --------RVPAVDVVARPlieqgvDREDARSVaRDLLSALSVPEsLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDE 177
Cdd:TIGR03771 68 vahtvmsgRTGHIGWLRRP------CVADFAAV-RDALRRVGLTE-LADRPVGELSGGQRQRVLVARALATRPSVLLLDE 139
|
170 180 190
....*....|....*....|....*....|...
gi 493478021 178 PTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:TIGR03771 140 PFTGLDMPTQELLTELFIELAGAGTAILMTTHD 172
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
29-198 |
6.22e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 62.76 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 29 VSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEvvyhspdgdIDLASCPDRTVIDLRGDSIGYtsqfLDEIPRVP 108
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGE---------VRWNGTPLAEQRDEPHENILY----LGHLPGLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 109 AVDVVARPL-----IEQGVDREDARSVARDLLSALSvpeslwQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALD 183
Cdd:TIGR01189 86 PELSALENLhfwaaIHGGAQRTIEDALAAVGLTGFE------DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170
....*....|....*
gi 493478021 184 PdtrrAAIDLLSTYL 198
Cdd:TIGR01189 160 K----AGVALLAGLL 170
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-193 |
7.17e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.76 E-value: 7.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 7 DGLSKTFdmhvlGD-TQVvglDDVSFDVREGE---FLavvGESGSGKSSLLKCLYRTYDPSSGEVVY--HSPD-GDIDla 79
Cdd:NF033858 270 RGLTMRF-----GDfTAV---DHVSFRIRRGEifgFL---GSNGCGKSTTMKMLTGLLPASEGEAWLfgQPVDaGDIA-- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 80 scpdrtvIDLRgdsIGYTSQ-F-----------LD---EIPRVPAVDVVARplIEQGVDREDARSVARDLLSALSVpesl 144
Cdd:NF033858 337 -------TRRR---VGYMSQaFslygeltvrqnLElhaRLFHLPAAEIAAR--VAEMLERFDLADVADALPDSLPL---- 400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493478021 145 wqaypatfsgGERQRVNLAQALAPKPDLLLLDEPTSALDPDTR----RAAIDL 193
Cdd:NF033858 401 ----------GIRQRLSLAVAVIHKPELLILDEPTSGVDPVARdmfwRLLIEL 443
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-209 |
9.70e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.29 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFdmhvlGDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEvvyhspdgdIDLASCP 82
Cdd:PRK13537 7 PIDFRNVEKRY-----GDKLVV--DGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGS---------ISLCGEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTVIDLRGDSIGYTSQF--LDeiprvPAVDVVARPLIEQ---GVDREDARSVARDLLSALSVpESLWQAYPATFSGGER 157
Cdd:PRK13537 71 VPSRARHARQRVGVVPQFdnLD-----PDFTVRENLLVFGryfGLSAAAARALVPPLLEFAKL-ENKADAKVGELSGGMK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493478021 158 QRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFH 209
Cdd:PRK13537 145 RRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
11-185 |
1.27e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.50 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 11 KTFDMHVLGDTQVVGLDdvsFDVREGEFLAVVGESGSGKSSLLKCL--YRTYDPSSGEVVYHSPDGdidLASCPDrtviD 88
Cdd:PRK09580 5 KDLHVSVEDKAILRGLN---LEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDL---LELSPE----D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 89 LRGDSIGYTSQFLDEIPRVP-------AVDVVARPLIEQGVDREDARSVARDLLSALSVPESLWQ-AYPATFSGGERQRV 160
Cdd:PRK09580 75 RAGEGIFMAFQYPVEIPGVSnqfflqtALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTrSVNVGFSGGEKKRN 154
|
170 180
....*....|....*....|....*
gi 493478021 161 NLAQALAPKPDLLLLDEPTSALDPD 185
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDID 179
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-196 |
1.34e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.29 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 30 SFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDIDLASCPDRtvidlRGDSIGYTSQFLdeiprvpa 109
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL---NGQDHTTTPPSR-----RPVSMLFQENNL-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 110 vdvVARPLIEQ----GVD---------REDARSVAR-----DLLSALsvpeslwqayPATFSGGERQRVNLAQALAPKPD 171
Cdd:PRK10771 83 ---FSHLTVAQniglGLNpglklnaaqREKLHAIARqmgieDLLARL----------PGQLSGGQRQRVALARCLVREQP 149
|
170 180
....*....|....*....|....*
gi 493478021 172 LLLLDEPTSALDPDTRRAAIDLLST 196
Cdd:PRK10771 150 ILLLDEPFSALDPALRQEMLTLVSQ 174
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
26-205 |
1.71e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.58 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHS-PDGDIDLASCPDRTVIdlrgdsigyTSQ----F 100
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDiPLTKLQLDSWRSRLAV---------VSQtpflF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 101 LDEIPRVPAVdvvARPLIEQGVDREDAR--SVARDLLSalsvpesLWQAYPA-------TFSGGERQRVNLAQALAPKPD 171
Cdd:PRK10789 402 SDTVANNIAL---GRPDATQQEIEHVARlaSVHDDILR-------LPQGYDTevgergvMLSGGQKQRISIARALLLNAE 471
|
170 180 190
....*....|....*....|....*....|....
gi 493478021 172 LLLLDEPTSALDPDTRRAAIDLLSTYlGSETTVV 205
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQW-GEGRTVI 504
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
36-200 |
2.04e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.36 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 36 GEFLAVVGESGSGKSSLLKCLyrtydpsSGEVVYHSPDGDIdLAScpDRTVIDLRGDSIGYTSQflDEIpRVPAVDV--- 112
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNAL-------AGRIQGNNFTGTI-LAN--NRKPTKQILKRTGFVTQ--DDI-LYPHLTVret 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 113 ---VARPLIEQGVDREDARSVARDLLSALSVPESLWQAYPATF----SGGERQRVNLAQALAPKPDLLLLDEPTSALDPD 185
Cdd:PLN03211 161 lvfCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170
....*....|....*
gi 493478021 186 trrAAIDLLSTyLGS 200
Cdd:PLN03211 241 ---AAYRLVLT-LGS 251
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-209 |
2.18e-11 |
|
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: 63.26 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 34 REGEFLAVVGESGSGKSSLLKCLyrtydpsSGEVVyhsPD-GDIDlaSCPD-RTVID-LRGDSIG--------------Y 96
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKIL-------SGELK---PNlGDYD--EEPSwDEVLKrFRGTELQdyfkklangeikvaH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 97 TSQFLDEIPRVpaVDVVARPLIEqgvdREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLD 176
Cdd:COG1245 165 KPQYVDLIPKV--FKGTVRELLE----KVDERGKLDELAEKLGL-ENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|...
gi 493478021 177 EPTSALDPDTRRAAIDLLSTYLGSETTVVGVFH 209
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
26-196 |
2.82e-11 |
|
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: 60.74 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCL---YRTYDPSSGEVVYHSPDGDIDLASCPdrtvidlrGDSIgYTSQfld 102
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEKYP--------GEII-YVSE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 103 eiprvpavDVVARPLIeqgvdredarSVARDLLSALSVPESlwqAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSAL 182
Cdd:cd03233 91 --------EDVHFPTL----------TVRETLDFALRCKGN---EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170
....*....|....
gi 493478021 183 DPDTrraAIDLLST 196
Cdd:cd03233 150 DSST---ALEILKC 160
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-183 |
2.99e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 33 VREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyhspDGDIDLASCPDRtvidLRGDSIGYTSQFLDEIPrvPAVDV 112
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-----DPELKISYKPQY----IKPDYDGTVEDLLRSIT--DDLGS 430
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493478021 113 ------VARPL-IEQGVDREdarsvARDLlsalsvpeslwqaypatfSGGERQRVNLAQALAPKPDLLLLDEPTSALD 183
Cdd:PRK13409 431 syykseIIKPLqLERLLDKN-----VKDL------------------SGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-189 |
3.57e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTFDMHVLgdtqvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspdGDidlasc 81
Cdd:PRK11819 323 KVIEAENLSKSFGDRLL-------IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI----GE------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 82 pdrTVidlrgdSIGYTSQFLDEIPRVPAV-DVVA--RPLIEQGvDREdarsvardllsalsVPEslwQAYPATF------ 152
Cdd:PRK11819 386 ---TV------KLAYVDQSRDALDPNKTVwEEISggLDIIKVG-NRE--------------IPS---RAYVGRFnfkggd 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493478021 153 --------SGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRA 189
Cdd:PRK11819 439 qqkkvgvlSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRA 483
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
26-183 |
3.79e-11 |
|
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: 61.41 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPS------SGEVVYHSPDGDIDLASCPDRTVIDLRGDSIGYTS- 98
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSegkikhSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSv 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 99 ----QFLDEIPRVPAVDVVarPLIEQGVdredarsvardllsalsvpeslwqaypaTFSGGERQRVNLAQALAPKPDLLL 174
Cdd:cd03291 133 vkacQLEEDITKFPEKDNT--VLGEGGI----------------------------TLSGGQRARISLARAVYKDADLYL 182
|
....*....
gi 493478021 175 LDEPTSALD 183
Cdd:cd03291 183 LDSPFGYLD 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-210 |
4.12e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.72 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDmhvlgDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLyrtydpsSGEVVYHSpdGDIDLASCP 82
Cdd:TIGR01257 1937 ILRLNELTKVYS-----GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKML-------TGDTTVTS--GDATVAGKS 2002
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTVIDLRGDSIGYTSQF--LDEI-PRVPAVDVVARpliEQGVDREDARSVARDLLSALSVpeSLWQAYPA-TFSGGERQ 158
Cdd:TIGR01257 2003 ILTNISDVHQNMGYCPQFdaIDDLlTGREHLYLYAR---LRGVPAEEIEKVANWSIQSLGL--SLYADRLAgTYSGGNKR 2077
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493478021 159 RVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:TIGR01257 2078 KLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHS 2129
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-205 |
5.61e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.95 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 18 LGDTQVVGLDdvSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspdgdidlasCPDRTVIDLrgdSIGYT 97
Cdd:PRK10938 13 LSDTKTLQLP--SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ------------SQFSHITRL---SFEQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 98 SQFLDEIPRVPAVDVVarplieqGVDRED-ARSVARDLLSALSVPEsLWQAYPATF-------------SGGERQRVNLA 163
Cdd:PRK10938 76 QKLVSDEWQRNNTDML-------SPGEDDtGRTTAEIIQDEVKDPA-RCEQLAQQFgitalldrrfkylSTGETRKTLLC 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493478021 164 QALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVV 205
Cdd:PRK10938 148 QALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLV 189
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-183 |
6.40e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 60.62 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYdPSSGEVVYhspdGDIDLASCPDRTVIDLRGdsigYTSQfldEIP 105
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILL----NGRPLSDWSAAELARHRA----YLSQ---QQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPAVDV-----VARPlieQGVDREDARSVARDLLSALSVPESLwqAYPAT-FSGGERQRVNLAQALA-------PKPDL 172
Cdd:COG4138 80 PPFAMPVfqylaLHQP---AGASSEAVEQLLAQLAEALGLEDKL--SRPLTqLSGGEWQRVRLAAVLLqvwptinPEGQL 154
|
170
....*....|.
gi 493478021 173 LLLDEPTSALD 183
Cdd:COG4138 155 LLLDEPMNSLD 165
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
142-183 |
7.03e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.04 E-value: 7.03e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 493478021 142 ESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALD 183
Cdd:PRK11144 119 EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
26-183 |
7.57e-11 |
|
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: 59.56 E-value: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCL-YRTydpSSGEVvyhspDGDIDLASCPdRTVIDLRgdSIGYtsqfldei 104
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRK---TAGVI-----TGEILINGRP-LDKNFQR--STGY-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 105 prVPAVDVvarplieqgvdredarsvardLLSALSVPESL-WQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALD 183
Cdd:cd03232 84 --VEQQDV---------------------HSPNLTVREALrFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-198 |
8.49e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 8.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFDMHVLgdtqvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDIDLAS 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPL-------LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY---EQDLIVAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 C---PDR----TVIDLRGDSIGYTSQFLDE---IPRVPAVDVVARPLIE----------QGVDREDARsvARDLLSALSV 140
Cdd:PRK11147 71 LqqdPPRnvegTVYDFVAEGIEEQAEYLKRyhdISHLVETDPSEKNLNElaklqeqldhHNLWQLENR--INEVLAQLGL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493478021 141 -PESLWqaypATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTrraaIDLLSTYL 198
Cdd:PRK11147 149 dPDAAL----SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFL 199
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-195 |
8.55e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 60.69 E-value: 8.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 23 VVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSsgevvYH-SPD----GDIDLASCPDRTVIDLRGDSIGYT 97
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN-----WHvTADrfrwNGIDLLKLSPRERRKIIGREIAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 98 SQ----FLDeiPRVPavdvVARPLIEQGVDRE----------DARSVARDLLSALSV--PESLWQAYPATFSGGERQRVN 161
Cdd:COG4170 95 FQepssCLD--PSAK----IGDQLIEAIPSWTfkgkwwqrfkWRKKRAIELLHRVGIkdHKDIMNSYPHELTEGECQKVM 168
|
170 180 190
....*....|....*....|....*....|....
gi 493478021 162 LAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLS 195
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQAQIFRLLA 202
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-185 |
1.03e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.95 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 24 VGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDIDLASCPDRT----------VIDlrGDS 93
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---PGNWQLAWVNQETpalpqpaleyVID--GDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 94 igYTSQFLDEIPRVPAV-DVVARPLIEQGVDREDA---RSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPK 169
Cdd:PRK10636 90 --EYRQLEAQLHDANERnDGHAIATIHGKLDAIDAwtiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICR 167
|
170
....*....|....*.
gi 493478021 170 PDLLLLDEPTSALDPD 185
Cdd:PRK10636 168 SDLLLLDEPTNHLDLD 183
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-204 |
1.05e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.95 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEvvyhspdgdIDLAscpdrtvidlRGDSIGYTSQ----FL 101
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE---------IGLA----------KGIKLGYFAQhqleFL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 102 --DEIPRVPAVDVVARPLIEQgvdredarsvARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPT 179
Cdd:PRK10636 389 raDESPLQHLARLAPQELEQK----------LRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
170 180
....*....|....*....|....*
gi 493478021 180 SALDPDTRRAAIDLLSTYLGSETTV 204
Cdd:PRK10636 459 NHLDLDMRQALTEALIDFEGALVVV 483
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
26-184 |
1.70e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.86 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGD-IDLAScpdRTVIDLRgDSIGYTSQ----- 99
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILF---DGKpIDYSR---KGLMKLR-ESVGMVFQdpdnq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 100 -FLDEIPRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLWqaypatFSGGERQRVNLAQALAPKPDLLLLDEP 178
Cdd:PRK13636 95 lFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHC------LSFGQKKRVAIAGVLVMEPKVLVLDEP 168
|
....*.
gi 493478021 179 TSALDP 184
Cdd:PRK13636 169 TAGLDP 174
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-210 |
2.04e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.42 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVR-------------EGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVV--------YHSPDGDIDLASCPDR 84
Cdd:PRK10575 14 LRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILldaqplesWSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 85 TvidlrGDSIGYTSQFLDEIPRVP------AVDVVARPLIEQGVDREDARSVARDLLSALSvpeslwqaypatfsGGERQ 158
Cdd:PRK10575 94 L-----PAAEGMTVRELVAIGRYPwhgalgRFGAADREKVEEAISLVGLKPLAHRLVDSLS--------------GGERQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493478021 159 RVNLAQALAPKPDLLLLDEPTSALDPDTR---RAAIDLLSTYLGseTTVVGVFHN 210
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQvdvLALVHRLSQERG--LTVIAVLHD 207
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-195 |
3.11e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.05 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFdmhVLGDTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIDLAS 80
Cdd:PRK15093 1 MPLLDIRNLTIEF---KTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 CPDRTVIDLRGDSIGYTSQ----FLDEIPRVpavdvvARPLIE------------QGVDREDARSVarDLLSALSV--PE 142
Cdd:PRK15093 78 LSPRERRKLVGHNVSMIFQepqsCLDPSERV------GRQLMQnipgwtykgrwwQRFGWRKRRAI--ELLHRVGIkdHK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493478021 143 SLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLS 195
Cdd:PRK15093 150 DAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLT 202
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-210 |
3.19e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.96 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspDGDIDLASCPDR--------------TVIdlrg 91
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLD--GGDIDDPDVAEAchylghrnamkpalTVA---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 92 DSIGYTSQFLDEIPR--VPAVDVVARPLIEqgvDREdarsvARDLlsalsvpeslwqaypatfSGGERQRVNLAQALAPK 169
Cdd:PRK13539 92 ENLEFWAAFLGGEELdiAAALEAVGLAPLA---HLP-----FGYL------------------SAGQKRRVALARLLVSN 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493478021 170 PDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:PRK13539 146 RPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-209 |
4.28e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 18 LGDTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSG--------EVVY---HSPDGDidlascPDRTV 86
Cdd:PRK11147 329 IDGKQLV--KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGrihcgtklEVAYfdqHRAELD------PEKTV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 87 IDLRGDS-------------IGYTSQFLDEIPRvpavdvvarplieqgvdredarsvARDLLSALSvpeslwqaypatfs 153
Cdd:PRK11147 401 MDNLAEGkqevmvngrprhvLGYLQDFLFHPKR------------------------AMTPVKALS-------------- 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493478021 154 GGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGsetTVVGVFH 209
Cdd:PRK11147 443 GGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQG---TVLLVSH 495
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-184 |
5.32e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.08 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTFDmhvlgdtqvvGL---DDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspdgdidl 78
Cdd:PRK11300 4 PLLSVSGLMMRFG----------GLlavNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIL---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 79 ascpdrtvidLRGDSI-GYTSQfldEIPRVPAV------------DVVARPLIEQgvdredARSVARDLLSAL------- 138
Cdd:PRK11300 64 ----------LRGQHIeGLPGH---QIARMGVVrtfqhvrlfremTVIENLLVAQ------HQQLKTGLFSGLlktpafr 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493478021 139 -SVPESLWQAY--------------PA-TFSGGERQRVNLAQALAPKPDLLLLDEPTSALDP 184
Cdd:PRK11300 125 rAESEALDRAAtwlervgllehanrQAgNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNP 186
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-183 |
7.86e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 7.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 25 GLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyhSPDGDIDLASCPDrtviDLRGDSIGYTSQ----- 99
Cdd:PRK10762 267 GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYV---TLDGHEVVTRSPQ----DGLANGIVYISEdrkrd 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 100 ------FLDEIPRVPAVDVVARPLIeqGVDREDARSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPKPDLL 173
Cdd:PRK10762 340 glvlgmSVKENMSLTALRYFSRAGG--SLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVL 417
|
170
....*....|
gi 493478021 174 LLDEPTSALD 183
Cdd:PRK10762 418 ILDEPTRGVD 427
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-204 |
9.87e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.32 E-value: 9.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGlsktfdmHVLgdtqvvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCL-----YRtydpssgevvyhspdGDI 76
Cdd:PRK11174 356 EILSPDG-------KTL-------AGPLNFTLPAGQRIALVGPSGAGKTSLLNALlgflpYQ---------------GSL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 77 DLASCPDRTvIDLrgdsigytSQFLDEI------PRVPAVDV-----VARPLI-EQGVDREDARSVARDLLSALsvPESL 144
Cdd:PRK11174 407 KINGIELRE-LDP--------ESWRKHLswvgqnPQLPHGTLrdnvlLGNPDAsDEQLQQALENAWVSEFLPLL--PQGL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478021 145 wqAYP-----ATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTV 204
Cdd:PRK11174 476 --DTPigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTL 538
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
27-183 |
9.91e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.02 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 27 DDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYdP--SSGEVVYhspDG-DIDLASCPD--RTVI-----DLRGDSIgy 96
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PgrWEGEIFI---DGkPVKIRNPQQaiAQGIamvpeDRKRDGI-- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 97 tsqfldeiprVPAVDV-----------VARPLIeqgVDREDARSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQA 165
Cdd:PRK13549 353 ----------VPVMGVgknitlaaldrFTGGSR---IDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKC 419
|
170
....*....|....*...
gi 493478021 166 LAPKPDLLLLDEPTSALD 183
Cdd:PRK13549 420 LLLNPKILILDEPTRGID 437
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
26-210 |
1.01e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.44 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyhspdgDIDLASCPDRTVIDLRGdSIGYTSQFLD-EI 104
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV-------KVMGREVNAENEKWVRS-KVGLVFQDPDdQV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 105 PRVPAVDVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDP 184
Cdd:PRK13647 93 FSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180
....*....|....*....|....*.
gi 493478021 185 DTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:PRK13647 172 RGQETLMEILDRLHNQGKTVIVATHD 197
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-197 |
1.25e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.40 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFDMHV-----LGD---------TQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCL----YrtydPSS 64
Cdd:COG4586 1 IIEVENLSKTYRVYEkepglKGAlkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtgilV----PTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 65 GEVvyhspdgdidlascpdrTVIdlrgdsiGYT-----SQFLDEIprvpAV----------DVvarPLIEQ--------G 121
Cdd:COG4586 77 GEV-----------------RVL-------GYVpfkrrKEFARRI----GVvfgqrsqlwwDL---PAIDSfrllkaiyR 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478021 122 VDREDARSVARDLLSALSVPESLWQayPA-TFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTY 197
Cdd:COG4586 126 IPDAEYKKRLDELVELLDLGELLDT--PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEY 200
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
28-195 |
1.95e-09 |
|
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: 57.45 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 28 DVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYdPSSGEVVYHSPDGDI-DLASCPDRTVIDLRG-----DSI------G 95
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAKGKLfYVPQRPYMTLGTLRDqiiypDSSedmkrrG 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 96 YTSQFLDEIprvpaVDVVArplIEQGVDREDARSVARDLLSALsvpeslwqaypatfSGGERQRVNLAQALAPKPDLLLL 175
Cdd:TIGR00954 549 LSDKDLEQI-----LDNVQ---LTHILEREGGWSAVQDWMDVL--------------SGGEKQRIAMARLFYHKPQFAIL 606
|
170 180
....*....|....*....|....*...
gi 493478021 176 DEPTSALDPDT--------RRAAIDLLS 195
Cdd:TIGR00954 607 DECTSAVSVDVegymyrlcREFGITLFS 634
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
122-198 |
2.41e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.18 E-value: 2.41e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478021 122 VDREDARSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDpdtrRAAIDLLSTYL 198
Cdd:PLN03073 315 IDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD----LHAVLWLETYL 387
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
36-199 |
3.41e-09 |
|
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: 53.92 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 36 GEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPdgdidlascpdrtvidlrgdsigytsqfldeiprvpavdvvar 115
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 116 plieqgvdrEDARSVARDLLSALSVPESlwqayPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLS 195
Cdd:smart00382 39 ---------EDILEEVLDQLLLIIVGGK-----KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104
|
....
gi 493478021 196 TYLG 199
Cdd:smart00382 105 LRLL 108
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-183 |
3.42e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.81 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 27 DDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSpdgdIDLASCPDrtvidlrgdsigytsQFLDE--- 103
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG----EPIRRQRD---------------EYHQDlly 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 104 IPRVPAVDVVARPLieqgvdrEDARSVARdlLSALSVPESLWQAY-----------PA-TFSGGERQRVNLAQALAPKPD 171
Cdd:PRK13538 79 LGHQPGIKTELTAL-------ENLRFYQR--LHGPGDDEALWEALaqvglagfedvPVrQLSAGQQRRVALARLWLTRAP 149
|
170
....*....|..
gi 493478021 172 LLLLDEPTSALD 183
Cdd:PRK13538 150 LWILDEPFTAID 161
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-183 |
4.46e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 33 VREGEFLAVVGESGSGKSSLLKCLyrtydpsSGEVVyhsPD-GDIDLASCPDRtVID-LRGDSIG--------------Y 96
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL-------SGELI---PNlGDYEEEPSWDE-VLKrFRGTELQnyfkklyngeikvvH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 97 TSQFLDEIPRVpaVDVVARPLIEqgvdREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLD 176
Cdd:PRK13409 165 KPQYVDLIPKV--FKGKVRELLK----KVDERGKLDEVVERLGL-ENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
....*..
gi 493478021 177 EPTSALD 183
Cdd:PRK13409 238 EPTSYLD 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
28-183 |
4.50e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 28 DVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIdlascpdRTVIDLRGDSIGYTSQFLDEIPRV 107
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP-------RSPLDAVKKGMAYITESRRDNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 108 PAVDV-----VARPLIEQG-------VDREDARSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPKPDLLLL 175
Cdd:PRK09700 354 PNFSIaqnmaISRSLKDGGykgamglFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIF 433
|
....*...
gi 493478021 176 DEPTSALD 183
Cdd:PRK09700 434 DEPTRGID 441
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-210 |
4.82e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.07 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 33 VREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEvvYHSPdgdidlascPD-RTVID-------------LRGDSIGYT- 97
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDP---------PDwDEILDefrgselqnyftkLLEGDVKVIv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 98 -SQFLDEIPRvpAVDVVARPLIEqgvdREDARSVARDLLSALSVPESLWQAYPAtFSGGERQRVNLAQALAPKPDLLLLD 176
Cdd:cd03236 92 kPQYVDLIPK--AVKGKVGELLK----KKDERGKLDELVDQLELRHVLDRNIDQ-LSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190
....*....|....*....|....*....|....
gi 493478021 177 EPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHD 198
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
39-199 |
5.40e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.02 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 39 LAVVGESGSGKSSLLKCLYRTYDPSSGeVVYHSPDGDIDLASCPDRTVIDLRGDSIGYTSQFLdeiPRVPavdvvarpli 118
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSG-TVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCF---PGVP---------- 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 119 EQGVdredarsvaRDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYL 198
Cdd:PLN03073 604 EQKL---------RAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQ 674
|
.
gi 493478021 199 G 199
Cdd:PLN03073 675 G 675
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
42-188 |
5.65e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 42 VGESGSGKSSLLKCLYRTYDPSSGEVVyhspdgdIDlascPDRTVIDLRGDsigytsQFLDEIPRVpaVDVVA---RPL- 117
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVS-------LD----PNERLGKLRQD------QFAFEEFTV--LDTVImghTELw 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 118 -IEQGVDR---------ED------------------ARSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPK 169
Cdd:PRK15064 94 eVKQERDRiyalpemseEDgmkvadlevkfaemdgytAEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSN 173
|
170
....*....|....*....
gi 493478021 170 PDLLLLDEPTSALDPDTRR 188
Cdd:PRK15064 174 PDILLLDEPTNNLDINTIR 192
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-194 |
5.91e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.09 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 20 DTQVVGLDDVSFDVREGEFLAVVGESGSGKS----SLLKCLYRTYDPSSGEVVYhspDGdIDLASCpdrtviDLRGDSIG 95
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLL---DG-KPVAPC------ALRGRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 96 YTSQFldeiPRVP--AVDVVARPLIE--QGVDREDARSVARDLLSA--LSVPESLWQAYPATFSGGERQRVNLAQALAPK 169
Cdd:PRK10418 83 TIMQN----PRSAfnPLHTMHTHAREtcLALGKPADDATLTAALEAvgLENAARVLKLYPFEMSGGMLQRMMIALALLCE 158
|
170 180
....*....|....*....|....*
gi 493478021 170 PDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLL 183
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-183 |
6.46e-09 |
|
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: 55.60 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYdPSSGEVVYHSPDGDIDLASC------------PDRT---VIDLR 90
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKFEGNVFINGKPVDIRNPaqairagiamvpEDRKrhgIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 91 GDSIGYTSQFLDEIPRVPAVDVVAR-PLIEQGVDREDARSVARDLlsalsvpeslwqayP-ATFSGGERQRVNLAQALAP 168
Cdd:TIGR02633 355 GVGKNITLSVLKSFCFKMRIDAAAElQIIGSAIQRLKVKTASPFL--------------PiGRLSGGNQQKAVLAKMLLT 420
|
170
....*....|....*
gi 493478021 169 KPDLLLLDEPTSALD 183
Cdd:TIGR02633 421 NPRVLILDEPTRGVD 435
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-183 |
1.02e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspdGDIDLASCPDRTVI---DLRGDSIgytsqFLD 102
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----AERSIAYVPQQAWImnaTVRGNIL-----FFD 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 103 EiprvpavdvvarpliEQGVDREDARSVAR---DLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPT 179
Cdd:PTZ00243 746 E---------------EDAARLADAVRVSQleaDLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
....
gi 493478021 180 SALD 183
Cdd:PTZ00243 811 SALD 814
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-191 |
1.15e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.01 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSKTFdmhvlgdTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDgdidlasc 81
Cdd:PRK10762 3 ALLQLKGIDKAF-------PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 82 pdrtvIDLRG--DS----IGYTSQFLDEIPRVPAVD--VVARPLIEQ--GVDREDARSVARDLLSALSVPESLWQAYpAT 151
Cdd:PRK10762 68 -----VTFNGpkSSqeagIGIIHQELNLIPQLTIAEniFLGREFVNRfgRIDWKKMYAEADKLLARLNLRFSSDKLV-GE 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493478021 152 FSGGERQRVNLAQALAPKPDLLLLDEPTSALDpDTRRAAI 191
Cdd:PRK10762 142 LSIGEQQMVEIAKVLSFESKVIIMDEPTDALT-DTETESL 180
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-186 |
1.33e-08 |
|
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: 54.95 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspdgdIDLASCPDRTVIDLRGDsigytsqfLDEIP 105
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEII-------IDGLNIAKIGLHDLRFK--------ITIIP 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPavdVVARPLIEQGVDREDARSvARDLLSALSVP--ESLWQAYPA-----------TFSGGERQRVNLAQALAPKPDL 172
Cdd:TIGR00957 1367 QDP---VLFSGSLRMNLDPFSQYS-DEEVWWALELAhlKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKI 1442
|
170
....*....|....
gi 493478021 173 LLLDEPTSALDPDT 186
Cdd:TIGR00957 1443 LVLDEATAAVDLET 1456
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
27-205 |
1.45e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.00 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 27 DDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDIDLASCPDRTVIDLRGDSIGYTSQ--FLDei 104
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILF---DGENIPAMSRSRLYTVRKRMSMLFQSGalFTD-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 105 prVPAVDVVARPLIEQG-VDREDARSVARDLLSALSVpESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTSALD 183
Cdd:PRK11831 99 --MNVFDNVAYPLREHTqLPAPLLHSTVMMKLEAVGL-RGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180
....*....|....*....|....*
gi 493478021 184 PDTRRA---AIDLLSTYLGSETTVV 205
Cdd:PRK11831 176 PITMGVlvkLISELNSALGVTCVVV 200
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
26-210 |
1.70e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 53.77 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLL-KCLYRT-YDPSSGEVVYHSPDGDIDLASCPDRtVIDLRGDSIG-------- 95
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLInDTLYPAlARRLHLKKEQPGNHDRIEGLEHIDK-VIVIDQSPIGrtprsnpa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 96 -YTSQFlDEI--------------PRVPAV--------DVVARPlIEQGVDR-EDARSVARDLLSALSVPES---LWQAY 148
Cdd:cd03271 90 tYTGVF-DEIrelfcevckgkrynRETLEVrykgksiaDVLDMT-VEEALEFfENIPKIARKLQTLCDVGLGyikLGQPA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478021 149 PaTFSGGERQRVNLAQAL---APKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:cd03271 168 T-TLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-192 |
1.89e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYrtydpssGEVvyhspdgdidlaSCPDRTVIDLRGdSIGYtsqfldeIP 105
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAML-------GEL------------SHAETSSVVIRG-SVAY-------VP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPAV-DVVARPLIEQGVDREDARSVARDLLSALSVPESLWQAYPAT--------FSGGERQRVNLAQALAPKPDLLLLD 176
Cdd:PLN03232 686 QVSWIfNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTeigergvnISGGQKQRVSMARAVYSNSDIYIFD 765
|
170
....*....|....*.
gi 493478021 177 EPTSALDPDTRRAAID 192
Cdd:PLN03232 766 DPLSALDAHVAHQVFD 781
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-210 |
1.93e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.47 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 20 DTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIDlascpDRTVIDLRGDsigYTSQ 99
Cdd:PRK13638 13 DEPV--LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYS-----KRGLLALRQQ---VATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 100 FLDEIPRVPAVDV---VARPLIEQGVDREDarsVARDLLSALSV--PESLWQAYPATFSGGERQRVNLAQALAPKPDLLL 174
Cdd:PRK13638 83 FQDPEQQIFYTDIdsdIAFSLRNLGVPEAE---ITRRVDEALTLvdAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 493478021 175 LDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHD 195
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-210 |
1.99e-08 |
|
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: 52.33 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLK-CLYrtydpSSGEVVYHSpdgdiDLASCPDRTVIdlrgdsigytsqFLDEI 104
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNeGLY-----ASGKARLIS-----FLPKFSRNKLI------------FIDQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 105 prvpavdvvaRPLIEQGvdredarsvardlLSALSVPESLwqaypATFSGGERQRVNLAQALA--PKPDLLLLDEPTSAL 182
Cdd:cd03238 69 ----------QFLIDVG-------------LGYLTLGQKL-----STLSGGELQRVKLASELFsePPGTLFILDEPSTGL 120
|
170 180
....*....|....*....|....*...
gi 493478021 183 DPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:cd03238 121 HQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
28-188 |
2.48e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.26 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 28 DVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIDL----------------------------A 79
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMtneqdyqgdeeqnvgmknvnefsltkegG 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 80 SCPDRTVIDLRG----DSIGYTSQFLDEIPRVPAVdVVARPLI------------EQGVDREDARSVARdlLSAL-SVPE 142
Cdd:PTZ00265 1266 SGEDSTVFKNSGkillDGVDICDYNLKDLRNLFSI-VSQEPMLfnmsiyenikfgKEDATREDVKRACK--FAAIdEFIE 1342
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493478021 143 SLWQAYPA-------TFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRR 188
Cdd:PTZ00265 1343 SLPNKYDTnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1395
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-183 |
3.08e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspdgdIDLASCPDRTVIDLRgdsigytsQFLDEIP 105
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIM-------IDDCDVAKFGLTDLR--------RVLSIIP 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPAV-DVVARPLIEQGVDREDA-------RSVARDLL--SALSVPESLWQAyPATFSGGERQRVNLAQALAPKPDLLLL 175
Cdd:PLN03232 1317 QSPVLfSGTVRFNIDPFSEHNDAdlwealeRAHIKDVIdrNPFGLDAEVSEG-GENFSVGQRQLLSLARALLRRSKILVL 1395
|
....*...
gi 493478021 176 DEPTSALD 183
Cdd:PLN03232 1396 DEATASVD 1403
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-184 |
3.56e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.57 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 1 MTVLSVDGLSKTFdmhvlGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDiDLAS 80
Cdd:PRK11614 3 KVMLSFDKVSAHY-----GKIQA--LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVF---DGK-DITD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 CPdrtvidlrgdsigyTSQFLDE-IPRVP-AVDVVARPLIEQG-------VDREDARS-VAR--DLLSALSvpESLWQAy 148
Cdd:PRK11614 72 WQ--------------TAKIMREaVAIVPeGRRVFSRMTVEENlamggffAERDQFQErIKWvyELFPRLH--ERRIQR- 134
|
170 180 190
....*....|....*....|....*....|....*.
gi 493478021 149 PATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDP 184
Cdd:PRK11614 135 AGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-186 |
4.28e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdgDIDLASCpdrTVIDLRgdsigytsQFLDEIP 105
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILID----GCDISKF---GLMDLR--------KVLGIIP 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVP-----AVDVVARPLIE-------QGVDREDARSVARDllSALSVPESLWQAyPATFSGGERQRVNLAQALAPKPDLL 173
Cdd:PLN03130 1320 QAPvlfsgTVRFNLDPFNEhndadlwESLERAHLKDVIRR--NSLGLDAEVSEA-GENFSVGQRQLLSLARALLRRSKIL 1396
|
170
....*....|...
gi 493478021 174 LLDEPTSALDPDT 186
Cdd:PLN03130 1397 VLDEATAAVDVRT 1409
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
26-210 |
4.76e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.58 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYrtydpssGEVvyHSPDGDIDLASCPDRTVidLRGDSIGYtsqfldeIP 105
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALM-------GFV--RLASGKISILGQPTRQA--LQKNLVAY-------VP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPAVDVVARPLIEQGV-------------DREDARSVARDLLSALSVPESLWQAYpATFSGGERQRVNLAQALAPKPDL 172
Cdd:PRK15056 85 QSEEVDWSFPVLVEDVVmmgryghmgwlrrAKKRDRQIVTAALARVDMVEFRHRQI-GELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 493478021 173 LLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
29-202 |
5.18e-08 |
|
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: 51.72 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 29 VSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVyhspdgdidLASCPDRTVIDLRGDSIGYtsqfldeIPRVP 108
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVL---------LNGGPLDFQRDSIARGLLY-------LGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 109 AVDVVARPlieqgvdREDARsvardLLSALSVPESLWQAYP------------ATFSGGERQRVNLAQALAPKPDLLLLD 176
Cdd:cd03231 83 GIKTTLSV-------LENLR-----FWHADHSDEQVEEALArvglngfedrpvAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180
....*....|....*....|....*.
gi 493478021 177 EPTSALDpdtrRAAIDLLSTYLGSET 202
Cdd:cd03231 151 EPTTALD----KAGVARFAEAMAGHC 172
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-182 |
6.45e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 23 VVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDI----------------DLASCPDRTV 86
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFksskealengismvhqELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 87 IDlrgdsigytSQFLDEIPRvpavdvvARPLIEQGVDREDARSVARDLLSALSVPESLwqaypATFSGGERQRVNLAQAL 166
Cdd:PRK10982 91 MD---------NMWLGRYPT-------KGMFVDQDKMYRDTKAIFDELDIDIDPRAKV-----ATLSVSQMQMIEIAKAF 149
|
170
....*....|....*.
gi 493478021 167 APKPDLLLLDEPTSAL 182
Cdd:PRK10982 150 SYNAKIVIMDEPTSSL 165
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-183 |
6.56e-08 |
|
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: 53.03 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSpdgdiDLASCPDRTVIdlRGDSIGYTSQFldeip 105
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-----SVAYVPQQAWI--QNDSLRENILF----- 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 rvpavdvvARPLIEQgvdREDARSVARDLLSALSVPESLWQA----YPATFSGGERQRVNLAQALAPKPDLLLLDEPTSA 181
Cdd:TIGR00957 722 --------GKALNEK---YYQQVLEACALLPDLEILPSGDRTeigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
..
gi 493478021 182 LD 183
Cdd:TIGR00957 791 VD 792
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-186 |
1.33e-07 |
|
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: 51.83 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDpSSGEVvyhSPDG----DIDLAS-------CPDRTVI---DLRG 91
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEI---QIDGvswnSVTLQTwrkafgvIPQKVFIfsgTFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 92 DSIGYTSQFLDEIPRVpAVDVVARPLIEQGVDREDARSVARDLLsalsvpeslwqaypatFSGGERQRVNLAQALAPKPD 171
Cdd:TIGR01271 1311 NLDPYEQWSDEEIWKV-AEEVGLKSVIEQFPDKLDFVLVDGGYV----------------LSNGHKQLMCLARSILSKAK 1373
|
170
....*....|....*
gi 493478021 172 LLLLDEPTSALDPDT 186
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVT 1388
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-209 |
1.62e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.94 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 25 GLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIDLAS-------CPDRTVIDLR---GDSI 94
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAvrqslgmCPQHNILFHHltvAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 95 GYTSQFLDEIPRVPAVDVVArpLIEQGVDREDARSVARDLlsalsvpeslwqaypatfSGGERQRVNLAQALAPKPDLLL 174
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEA--MLEDTGLHHKRNEEAQDL------------------SGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190
....*....|....*....|....*....|....*
gi 493478021 175 LDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFH 209
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHH 1119
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-187 |
2.04e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.21 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 2 TVLSVDGLSktfdmhvlGDtqvvGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPD-GDIDLAS 80
Cdd:PRK15439 267 PVLTVEDLT--------GE----GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEiNALSTAQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 CPDRTVIDLRGDSIGYtSQFLDEIPR--VPAVDVVARPLIEQGvdREDARSVARdLLSALSVPESLWQAYPATFSGGERQ 158
Cdd:PRK15439 335 RLARGLVYLPEDRQSS-GLYLDAPLAwnVCALTHNRRGFWIKP--ARENAVLER-YRRALNIKFNHAEQAARTLSGGNQQ 410
|
170 180
....*....|....*....|....*....
gi 493478021 159 RVNLAQALAPKPDLLLLDEPTSALDPDTR 187
Cdd:PRK15439 411 KVLIAKCLEASPQLLIVDEPTRGVDVSAR 439
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
14-209 |
2.37e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.41 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 14 DMHV-LGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCL--YRTYDPSSGEVVYHspdgdidlascpDRTVIDLR 90
Cdd:CHL00131 12 NLHAsVNENEI--LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFK------------GESILDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 91 GDSIGYTSQFLD-----EIPRVPAVDVV-----ARpLIEQGVDREDARSVARDLLSALSV----PESLWQAYPATFSGGE 156
Cdd:CHL00131 78 PEERAHLGIFLAfqypiEIPGVSNADFLrlaynSK-RKFQGLPELDPLEFLEIINEKLKLvgmdPSFLSRNVNEGFSGGE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493478021 157 RQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFH 209
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
12-194 |
2.66e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 12 TFDMHVLGDTQVVgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLyrtydpsSGEVVYHSPDGDIDLASCPDRTVIDLRg 91
Cdd:TIGR00956 766 TYEVKIKKEKRVI-LNNVDGWVKPGTLTALMGASGAGKTTLLNVL-------AERVTTGVITGGDRLVNGRPLDSSFQR- 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 92 dSIGYTSQFLDEIPRVP---AVDVVARPLIEQGVDREDARSVARDLLSALSVpESLWQAYPATFSGG----ERQRVNLAQ 164
Cdd:TIGR00956 837 -SIGYVQQQDLHLPTSTvreSLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEM-ESYADAVVGVPGEGlnveQRKRLTIGV 914
|
170 180 190
....*....|....*....|....*....|.
gi 493478021 165 ALAPKPDLLL-LDEPTSALDPDTRRAAIDLL 194
Cdd:TIGR00956 915 ELVAKPKLLLfLDEPTSGLDSQTAWSICKLM 945
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-183 |
3.26e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.83 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 15 MHVLGDTQVVgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYdPSSGEVVYHSPDGDIDLASCPDRTVIDLRgdsI 94
Cdd:PRK13547 7 LHVARRHRAI-LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL-TGGGAPRGARVTGDVTLNGEPLAAIDAPR---L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 95 GYTSQFLDEIPRvPAVDVVARPLIEQG----VDREDARSVA-RDLLS---ALSVPESLWQAYPATFSGGERQRVNLAQAL 166
Cdd:PRK13547 82 ARLRAVLPQAAQ-PAFAFSAREIVLLGryphARRAGALTHRdGEIAWqalALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180
....*....|....*....|....*.
gi 493478021 167 A---------PKPDLLLLDEPTSALD 183
Cdd:PRK13547 161 AqlwpphdaaQPPRYLLLDEPTAALD 186
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-183 |
3.66e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.43 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCL-YRtydpSSGEVVYhspDGDIDLASCP-DRTVIDLRGdsiGYTSQFLDE 103
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFR----SPKGVKG---SGSVLLNGMPiDAKEMRAIS---AYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 104 IPRVPAVD---VVARPLIEQGVDREDARSVARDLLSALS----------VPESLwqaypATFSGGERQRVNLAQALAPKP 170
Cdd:TIGR00955 111 IPTLTVREhlmFQAHLRMPRRVTKKEKRERVDEVLQALGlrkcantrigVPGRV-----KGLSGGERKRLAFASELLTDP 185
|
170
....*....|...
gi 493478021 171 DLLLLDEPTSALD 183
Cdd:TIGR00955 186 PLLFCDEPTSGLD 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-183 |
1.03e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.14 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 29 VSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEV-------VYHSPDGDID--LASCPDrtviDLRGDSIGYTSQ 99
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVyldgkpiDIRSPRDAIRagIMLCPE----DRKAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 100 FLDEIprvpavDVVARP-------LIEQGVDREDARSVARDLlsALSVPeSLWQAYpATFSGGERQRVNLAQALAPKPDL 172
Cdd:PRK11288 348 VADNI------NISARRhhlragcLINNRWEAENADRFIRSL--NIKTP-SREQLI-MNLSGGNQQKAILGRWLSEDMKV 417
|
170
....*....|.
gi 493478021 173 LLLDEPTSALD 183
Cdd:PRK11288 418 ILLDEPTRGID 428
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-183 |
1.39e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 20 DTQVVglDDVSFDVREGEFLAVVGESGSGKSSLLKCLY-RTYDPS-SGEVVYHspdG-DIDLascpdRTVIDLRGDSIGY 96
Cdd:NF040905 272 ERKVV--DDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgRSYGRNiSGTVFKD---GkEVDV-----STVSDAIDAGLAY 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 97 TSQ--------FLDEIPR---VPAVDVVARPLIeqgVDREDARSVARDLLSALSV--PeSLWQAYpATFSGGERQRVNLA 163
Cdd:NF040905 342 VTEdrkgyglnLIDDIKRnitLANLGKVSRRGV---IDENEEIKVAEEYRKKMNIktP-SVFQKV-GNLSGGNQQKVVLS 416
|
170 180
....*....|....*....|
gi 493478021 164 QALAPKPDLLLLDEPTSALD 183
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGID 436
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-186 |
1.55e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPS----SGEVVYHSPDgdidlascPDRTVIDLRGDSIgYTSQFL 101
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGIT--------PEEIKKHYRGDVV-YNAETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 102 DEIPRVP---AVDVVARPLIEQ----GVDREDARSVARDLlsalsvpeslwqaYPATF------------------SGGE 156
Cdd:TIGR00956 148 VHFPHLTvgeTLDFAARCKTPQnrpdGVSREEYAKHIADV-------------YMATYglshtrntkvgndfvrgvSGGE 214
|
170 180 190
....*....|....*....|....*....|
gi 493478021 157 RQRVNLAQALAPKPDLLLLDEPTSALDPDT 186
Cdd:TIGR00956 215 RKRVSIAEASLGGAKIQCWDNATRGLDSAT 244
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
26-210 |
1.91e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.50 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHspdGDIdlascpdrTVIDLrgdSIGYTSQfldeip 105
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN---GEV--------SVIAI---SAGLSGQ------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 rVPAVDVVARPLIEQGVDREDARSVARDLLSALSVPESLWQAYpATFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPD 185
Cdd:PRK13546 100 -LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPV-KKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180
....*....|....*....|....*
gi 493478021 186 TRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTIFFVSHN 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-209 |
2.02e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLyrTYD-PS--------------SGEVV--------YHSPDGDIDL-ASC 81
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI--TGDhPQgysndltlfgrrrgSGETIwdikkhigYVSSSLHLDYrVST 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 82 PDRTVIdLRG--DSIGytsqfldeiprvpavdvvarplIEQGV-DREdaRSVARDLLSALSVPESLWQAYPATFSGGERQ 158
Cdd:PRK10938 354 SVRNVI-LSGffDSIG----------------------IYQAVsDRQ--QKLAQQWLDILGIDKRTADAPFHSLSWGQQR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493478021 159 RVNLAQALAPKPDLLLLDEPTSALDPDTR---RAAIDLLSTYlgSETTVVGVFH 209
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRqlvRRFVDVLISE--GETQLLFVSH 460
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
146-210 |
2.80e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.80e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493478021 146 QAYPATF-SGGERQRVNLAQALA------PKPDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:PRK03918 782 KERPLTFlSGGERIALGLAFRLAlslylaGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHD 853
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-192 |
3.66e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.81 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYrtydpssGEvvyhspdgdidLASCPDRTVIdLRGdSIGYtsqfldeIP 105
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAML-------GE-----------LPPRSDASVV-IRG-TVAY-------VP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPAV-DVVARPLIEQGVDREDARSVARDLLSALSVPESLWQAYPAT--------FSGGERQRVNLAQALAPKPDLLLLD 176
Cdd:PLN03130 686 QVSWIfNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTeigergvnISGGQKQRVSMARAVYSNSDVYIFD 765
|
170
....*....|....*.
gi 493478021 177 EPTSALDPDTRRAAID 192
Cdd:PLN03130 766 DPLSALDAHVGRQVFD 781
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
26-209 |
4.83e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 47.02 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDiDLASCPDRT----VIDLRGDSIGYTSQFL 101
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL---DGR-PLSSLSHSVlrqgVAMVQQDPVVLADTFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 102 DEIprvpavdVVARPLIEQGVDREDARSVARDLLSALsvPESLW-----QAypATFSGGERQRVNLAQALAPKPDLLLLD 176
Cdd:PRK10790 433 ANV-------TLGRDISEEQVWQALETVQLAELARSL--PDGLYtplgeQG--NNLSVGQKQLLALARVLVQTPQILILD 501
|
170 180 190
....*....|....*....|....*....|...
gi 493478021 177 EPTSALDPDTRRAAIDLLSTyLGSETTVVGVFH 209
Cdd:PRK10790 502 EATANIDSGTEQAIQQALAA-VREHTTLVVIAH 533
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
26-183 |
7.08e-06 |
|
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: 45.78 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIDLASCPDRTVidlRGdSIGYTSQfldeIP 105
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRN---RY-SVAYAAQ----KP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPAVDVVARPLIEQGVDRE------DARSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPT 179
Cdd:cd03290 89 WLLNATVEENITFGSPFNKQrykavtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
....
gi 493478021 180 SALD 183
Cdd:cd03290 169 SALD 172
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
27-191 |
7.75e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 45.29 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 27 DDVSFDVREGEFLaVVGESGSGKSSLLKC----LYRTYDPSSGEVVyHSPDgdiDLASCPDRTVIDLRgdsigytsqFLD 102
Cdd:cd03240 14 ERSEIEFFSPLTL-IVGQNGAGKTTIIEAlkyaLTGELPPNSKGGA-HDPK---LIREGEVRAQVKLA---------FEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 103 EiprvpavdvvarplieQGVDREDARSVARdLLSALSVP--ESLWQAY--PATFSGGERQ------RVNLAQALAPKPDL 172
Cdd:cd03240 80 A----------------NGKKYTITRSLAI-LENVIFCHqgESNWPLLdmRGRCSGGEKVlasliiRLALAETFGSNCGI 142
|
170
....*....|....*....
gi 493478021 173 LLLDEPTSALDPDTRRAAI 191
Cdd:cd03240 143 LALDEPTTNLDEENIEESL 161
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
40-194 |
9.82e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.00 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 40 AVVGESGSGKSSLLK----CLY-------------RTYDPSSGEVVYH-SPDGDIDLASCPDRTVIDLRGDSIGYTSQFL 101
Cdd:COG0419 27 LIVGPNGAGKSTILEairyALYgkarsrsklrsdlINVGSEEASVELEfEHGGKRYRIERRQGEFAEFLEAKPSERKEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 102 DEIPRVPAVDVVAR-------PLIEQGVDREDARSVARDLLSALSVPESlwqayPATFSGGERQRVNLAQALApkpdlLL 174
Cdd:COG0419 107 KRLLGLEIYEELKErlkeleeALESALEELAELQKLKQEILAQLSGLDP-----IETLSGGERLRLALADLLS-----LI 176
|
170 180
....*....|....*....|
gi 493478021 175 LDepTSALDPDTRRAAIDLL 194
Cdd:COG0419 177 LD--FGSLDEERLERLLDAL 194
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
28-210 |
1.02e-05 |
|
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: 44.27 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 28 DVSFDvrEGEFLAVVGESGSGKSSLLKCLyrtydpssgevvyhspdgdidLASCPDRTVIDLRGDSIGYTSQfldeiprV 107
Cdd:cd03227 15 DVTFG--EGSLTIITGPNGSGKSTILDAI---------------------GLALGGAQSATRRRSGVKAGCI-------V 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 108 PAVDVVARPLIEQgvdredarsvardllsalsvpeslwqaypatFSGGERQRVNLAQALA---PKPD-LLLLDEPTSALD 183
Cdd:cd03227 65 AAVSAELIFTRLQ-------------------------------LSGGEKELSALALILAlasLKPRpLYILDEIDRGLD 113
|
170 180
....*....|....*....|....*..
gi 493478021 184 PDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:cd03227 114 PRDGQALAEAILEHLVKGAQVIVITHL 140
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
151-210 |
1.76e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.59 E-value: 1.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478021 151 TFSGGERQRVNLAQAL---APKPDLLLLDEPTSALDPDTRRAAIDLLS--TYLGSetTVVGVFHN 210
Cdd:PRK00635 809 SLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQslTHQGH--TVVIIEHN 871
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
26-183 |
2.85e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIDLASCPDRTV-----IDLRGDSIGYTSQF 100
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLtgienIELKGLMMGLTKEK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 101 LDEI-PRVPAVDVVARpLIEQGVDredarsvardllsalsvpeslwqaypaTFSGGERQRVNLAQALAPKPDLLLLDEPT 179
Cdd:PRK13545 120 IKEIiPEIIEFADIGK-FIYQPVK---------------------------TYSSGMKSRLGFAISVHINPDILVIDEAL 171
|
....
gi 493478021 180 SALD 183
Cdd:PRK13545 172 SVGD 175
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
26-183 |
3.18e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.40 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYHSPDGDIDLAS-----C---------PDRTV----- 86
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTyqkqlCfvghrsginPYLTLrencl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 87 IDLRGDSigyTSQFLDEIPRVPAvdvvarplIEQGVDredarsvardllsalsvpeslwqaYP-ATFSGGERQRVNLAQA 165
Cdd:PRK13540 97 YDIHFSP---GAVGITELCRLFS--------LEHLID------------------------YPcGLLSSGQKRQVALLRL 141
|
170
....*....|....*...
gi 493478021 166 LAPKPDLLLLDEPTSALD 183
Cdd:PRK13540 142 WMSKAKLWLLDEPLVALD 159
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
149-210 |
3.37e-05 |
|
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: 44.62 E-value: 3.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493478021 149 PATF-SGGERQRVNLAQALAPK---PDLLLLDEPTSALDPDTRRAAIDLLSTYLGSETTVVGVFHN 210
Cdd:TIGR00630 826 PATTlSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHN 891
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-188 |
3.88e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.35 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSktfdmHVLGDTQVvgLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyHSPDGDIDLAS-- 80
Cdd:NF033858 1 VARLEGVS-----HRYGKTVA--LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV--EVLGGDMADARhr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 81 ---CPDrtvidlrgdsIGYTSQFL----------DEiprvpAVDVVARpLIEQGVDREDARsvARDLLSA---LSVPESl 144
Cdd:NF033858 72 ravCPR----------IAYMPQGLgknlyptlsvFE-----NLDFFGR-LFGQDAAERRRR--IDELLRAtglAPFADR- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493478021 145 wqayPA-TFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRR 188
Cdd:NF033858 133 ----PAgKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRR 173
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
29-188 |
5.01e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.81 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 29 VSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGDIDLASCPDRtvidlrgdsigYTSQFldeiprvP 108
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL---DGKPVTAEQPED-----------YRKLF-------S 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 109 AV--DV--VARPLIEQGVDREDARsvARDLLSALSVPESL----WQAYPATFSGGERQRVNLAQALAPKPDLLLLDEPTS 180
Cdd:PRK10522 401 AVftDFhlFDQLLGPEGKPANPAL--VEKWLERLKMAHKLeledGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAA 478
|
....*...
gi 493478021 181 ALDPDTRR 188
Cdd:PRK10522 479 DQDPHFRR 486
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
150-194 |
6.12e-05 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 40.68 E-value: 6.12e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 493478021 150 ATFSGGERQR---VNLAQALA----------PKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELL 88
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-183 |
1.89e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYH-------SPDGDID----LASCPDRTVIDLRGDSI 94
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHgkkinnhNANEAINhgfaLVTEERRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 95 GYTSqfldeiprvpAVDVVARPLIEQGV-DREDARSVARDLLSALSVPESLWQAYPATFSGGERQRVNLAQALAPKPDLL 173
Cdd:PRK10982 344 GFNS----------LISNIRNYKNKVGLlDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEIL 413
|
170
....*....|
gi 493478021 174 LLDEPTSALD 183
Cdd:PRK10982 414 MLDEPTRGID 423
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-188 |
2.50e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.58 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 3 VLSVDGLSKTFdmhvlgdTQVVGLDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVvyhspdgDIDLASCP 82
Cdd:PRK15439 11 LLCARSISKQY-------SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL-------EIGGNPCA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 83 DRTVIDLRGDSIGYTSQfldEIPRVPAVDVVARPLIEQGVDREDARSVArDLLSALSVPESLwQAYPATFSGGERQRVNL 162
Cdd:PRK15439 77 RLTPAKAHQLGIYLVPQ---EPLLFPNLSVKENILFGLPKRQASMQKMK-QLLAALGCQLDL-DSSAGSLEVADRQIVEI 151
|
170 180
....*....|....*....|....*..
gi 493478021 163 AQALAPKPDLLLLDEPTSALDP-DTRR 188
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASLTPaETER 178
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
26-209 |
3.64e-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: 40.66 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEVVYhspDGdIDLASCPDRTvidLRGDsigytsqfLDEIP 105
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI---DG-IDISKLPLHT---LRSR--------LSIIL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPavdVVARPLIEQGVDREDARSVARdLLSALSVPE--SLWQAYPA-----------TFSGGERQRVNLAQALAPKPDL 172
Cdd:cd03288 102 QDP---ILFSGSIRFNLDPECKCTDDR-LWEALEIAQlkNMVKSLPGgldavvteggeNFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 493478021 173 LLLDEPTSALDPDTRRAAIDLLSTYLgSETTVVGVFH 209
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAF-ADRTVVTIAH 213
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-190 |
3.69e-04 |
|
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: 40.25 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 32 DVREGEFLAVVGESGSGKSSLLKCLYRTYDPSSGEvvyhspdgdidlascpdrtvIDLRGDSIGYTSQFLDeiprvpavd 111
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN--------------------DEWDGITPVYKPQYID--------- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493478021 112 vvarplieqgvdredarsvardllsalsvpeslwqaypatFSGGERQRVNLAQALAPKPDLLLLDEPTSALDPDTRRAA 190
Cdd:cd03222 72 ----------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA 110
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
149-182 |
6.97e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 6.97e-04
10 20 30
....*....|....*....|....*....|....*....
gi 493478021 149 PA-TFSGGERQRVNLAQALApKPD----LLLLDEPTSAL 182
Cdd:COG0178 823 PAtTLSGGEAQRVKLASELS-KRStgktLYILDEPTTGL 860
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-185 |
7.85e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.45 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 31 FDVREGEFLAVVGESGSGKSSLLKCLyrtydpsSGevVYHSPDGDIDLASCPDRtvidlRGDSIGYTSqFLDEIPRV-PA 109
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVL-------AG--LLHVESGQIQIDGKTAT-----RGDRSRFMA-YLGHLPGLkAD 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478021 110 VDVVARPLIEQGVDREDARSVARDLLSALSVPESLwQAYPATFSGGERQRVNLAQA-LAPKPdLLLLDEPTSALDPD 185
Cdd:PRK13543 97 LSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYE-DTLVRQLSAGQKKRLALARLwLSPAP-LWLLDEPYANLDLE 171
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
149-182 |
1.78e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.29 E-value: 1.78e-03
10 20 30
....*....|....*....|....*....|....*...
gi 493478021 149 PA-TFSGGERQRVNLAQALAPKPD---LLLLDEPTSAL 182
Cdd:PRK00349 827 PAtTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGL 864
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
28-207 |
1.98e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.40 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 28 DVSF-DVREGEFLAVVGESGSGKSSLLKCL-YRTYDPSSGEVVYHSPDGDIDLASCPDRTVIDLRGDSIGYtsqfldEIP 105
Cdd:cd03279 19 VIDFtGLDNNGLFLICGPTGAGKSTILDAItYALYGKTPRYGRQENLRSVFAPGEDTAEVSFTFQLGGKKY------RVE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 106 RVPAVD------VVarpLIEQG-VDREDARSVArdllsalsvpeslwqaypaTFSGGERQRVNLAQALA----------P 168
Cdd:cd03279 93 RSRGLDydqftrIV---LLPQGeFDRFLARPVS-------------------TLSGGETFLASLSLALAlsevlqnrggA 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 493478021 169 KPDLLLLDEPTSALDPDTRRAAIDLLSTyLGSETTVVGV 207
Cdd:cd03279 151 RLEALFIDEGFGTLDPEALEAVATALEL-IRTENRMVGV 188
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
26-69 |
2.56e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 38.23 E-value: 2.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 493478021 26 LDDVSFDVREGE-FLAVVGESGSGKSSLLKCLYRTYDPsSGEVVY 69
Cdd:COG3267 32 LARLEYALAQGGgFVVLTGEVGTGKTTLLRRLLERLPD-DVKVAY 75
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
38-69 |
2.73e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 36.94 E-value: 2.73e-03
10 20 30
....*....|....*....|....*....|..
gi 493478021 38 FLAVVGESGSGKSSLLKCLYRTYDPSSGEVVY 69
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLLEQLPEVRDSVVF 38
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
26-188 |
4.88e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 37.24 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 26 LDDVSFDVREGEFLAVVGESGSGKSSL-LKCLYrtydpssgevvyhspdgdidlASCPDRTVidlrgDSIG-YTSQFLDE 103
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLaFDTIY---------------------AEGQRRYV-----ESLSaYARQFLGQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 104 IPRvPAVDVVA--RPL--IEQGVDREDARSV---------------ARD-LLSALSVPESLWQAY------PATFSGGER 157
Cdd:cd03270 65 MDK-PDVDSIEglSPAiaIDQKTTSRNPRSTvgtvteiydylrllfARVgIRERLGFLVDVGLGYltlsrsAPTLSGGEA 143
|
170 180 190
....*....|....*....|....*....|....
gi 493478021 158 QRVNLAQALAPKPD--LLLLDEPTSALDP-DTRR 188
Cdd:cd03270 144 QRIRLATQIGSGLTgvLYVLDEPSIGLHPrDNDR 177
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
87-194 |
5.01e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 38.03 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478021 87 IDLRGDSIgytSQFLDEIPRVPAVDVVARPLIEQGVDREDARSVARD--LLSALSVPESLWQAYP-ATFSGGERQRVNLA 163
Cdd:TIGR00618 886 IQFDGDAL---IKFLHEITLYANVRLANQSEGRFHGRYADSHVNARKyqGLALLVADAYTGSVRPsATLSGGETFLASLS 962
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 493478021 164 QALA----------PKPDLLLLDEPTSALDPDTRRAAIDLL 194
Cdd:TIGR00618 963 LALAladllstsggTVLDSLFIDEGFGSLDEDSLDRAIGIL 1003
|
|
| |
