|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-245 |
8.17e-129 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 364.41 E-value: 8.17e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 1 MYLSLQRVSKTFHGER-PVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVGYM 79
Cdd:COG1116 6 PALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 80 PQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEP 159
Cdd:COG1116 86 FQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 160 FGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSARPGRLIADVPIHLARPRRE---SDEAFLRLQ 236
Cdd:COG1116 166 FGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDRelrTSPEFAALR 245
|
....*....
gi 1279381529 237 AQLLGSLAA 245
Cdd:COG1116 246 AEILDLLRE 254
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-221 |
7.38e-114 |
|
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: 325.20 E-value: 7.38e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTF-HGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVGYMPQ 81
Cdd:cd03293 1 LEVRNVSKTYgGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 82 RDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 162 ALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSARPGRLIADVPIHL 221
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-245 |
4.54e-77 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 233.60 E-value: 4.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGER-PVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVGYMPQ 81
Cdd:COG4525 4 LTVRHVSVRYPGGGqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 82 RDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:COG4525 84 KDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 162 ALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSARPGRLIADVPIHLAR------PRRE--SDEAFL 233
Cdd:COG4525 164 ALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELDFSRrflageDARAikSDPAFI 243
|
250
....*....|..
gi 1279381529 234 RLQAQLLGSLAA 245
Cdd:COG4525 244 ALREELLDIIFA 255
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-214 |
7.26e-72 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 223.05 E-value: 7.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 2 YLSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH---VGY 78
Cdd:COG3842 5 ALELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEkrnVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 79 MPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDE 158
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1279381529 159 PFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLI 214
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND--GRIE 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-215 |
5.20e-70 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 218.48 E-value: 5.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 1 MYLSLQRVSKTFHGErpvQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG--ALINGQTG--HV 76
Cdd:COG1118 1 MSIEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdLFTNLPPRerRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRtILMDRP-LLL 155
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALAR-ALAVEPeVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 156 LDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIA 215
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ--GRIEQ 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-215 |
4.09e-69 |
|
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: 211.61 E-value: 4.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING---QTGHVGYM 79
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvppERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 80 PQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEP 159
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1279381529 160 FGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIA 215
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNE--GRIVQ 211
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
3-230 |
2.81e-67 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 208.06 E-value: 2.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPV-QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVGYMPQ 81
Cdd:NF040729 2 LKIQNISKTFINNKKEnEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGPDRGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 82 RDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:NF040729 82 NYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEPLG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 162 ALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSARPGRLIADVPIHLARPR-RESDE 230
Cdd:NF040729 162 AVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRDKGKILEDLKIDLPRPRnRESEK 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-218 |
5.54e-67 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 206.43 E-value: 5.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFH-GERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG------- 74
Cdd:COG1136 5 LELRNLTKSYGtGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErelarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 --HVGYMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRP 152
Cdd:COG1136 85 rrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279381529 153 LLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDvREAALLSDRVLVLsaRPGRLIADVP 218
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRL--RDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-213 |
2.41e-66 |
|
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: 204.65 E-value: 2.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFH-GERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG------- 74
Cdd:cd03255 1 IELKNLSKTYGgGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 --HVGYMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRP 152
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279381529 153 LLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDvREAALLSDRVLVLsaRPGRL 213
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIEL--RDGKI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-233 |
6.92e-63 |
|
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: 196.75 E-value: 6.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPvqALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG-----HVG 77
Cdd:cd03295 1 IEFENVTKRYGGGKK--AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPvelrrKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLE--GFADAYPRQLSGGMRQRAALLRTILMDRPLLL 155
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 156 LDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIA-DVPIH-LARPRRESDEAFL 233
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN--GEIVQvGTPDEiLRSPANDFVAEFV 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-235 |
9.50e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 193.36 E-value: 9.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhgeRPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT----GHVGY 78
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPaevrRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 79 MPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDE 158
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 159 PFGALDALTRREMQNwLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIADVPIHLARpRRESDEAFLRL 235
Cdd:COG1131 158 PTSGLDPEARRELWE-LLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDK--GRIVADGTPDELK-ARLLEDVFLEL 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-242 |
7.12e-59 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 186.83 E-value: 7.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERpvqALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVGYMPQR 82
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 83 DLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGA 162
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 163 LDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSARPGRLIADVPIHLAR------PRR--ESDEAFLR 234
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLNFARrfvageSSRsiKSDPQFIA 238
|
....*...
gi 1279381529 235 LQAQLLGS 242
Cdd:PRK11248 239 MREYVLSR 246
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-224 |
1.07e-58 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 187.99 E-value: 1.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 5 LQRVSKTFHGERPvqALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG-----HVGYM 79
Cdd:COG1125 4 FENVTKRYPDGTV--AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPvelrrRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 80 PQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGL--EGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLD 157
Cdd:COG1125 82 IQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 158 EPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLI-ADVPIH-LARP 224
Cdd:COG1125 162 EPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM--REGRIVqYDTPEEiLANP 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-216 |
2.01e-57 |
|
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: 182.15 E-value: 2.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPvqALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG-----HVG 77
Cdd:COG1122 1 IELENLSFSYPGGTP--ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLrelrrKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YM---PQRDLLMPwrTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLL 154
Cdd:COG1122 79 LVfqnPDDQLFAP--TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 155 LLDEPFGALDALTRREMQNWLMTvWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKR-LNKEGKTVIIVTHDLDLVAELADRVIVLDD--GRIVAD 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-225 |
7.24e-57 |
|
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: 181.12 E-value: 7.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVGYMPQRDLLMPWRTVLQNVILGAE 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 101 IARKPLEQARQRA--RSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTV 178
Cdd:TIGR01184 81 RVLPDLSKSERRAivEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1279381529 179 WAQLQPTVLFVTHDVREAALLSDRVLVLSARPGRLIADV-PIHLARPR 225
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQIlEVPFPRPR 208
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-214 |
1.28e-56 |
|
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: 181.69 E-value: 1.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 17 PVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGqtghvgyMPQRDL------------ 84
Cdd:cd03294 36 QTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAA-------MSRKELrelrrkkismvf 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 85 ----LMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPF 160
Cdd:cd03294 109 qsfaLLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 161 GALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLI 214
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIM--KDGRLV 240
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
19-207 |
1.63e-56 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 180.38 E-value: 1.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 19 QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG---ALINGQTGHVGYMPQRDLLMPWRTVLQNV 95
Cdd:TIGR00968 14 QALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGqdaTRVHARDRKIGFVFQHYALFKHLTVRDNI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 96 ILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWL 175
Cdd:TIGR00968 94 AFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRKELRSWL 173
|
170 180 190
....*....|....*....|....*....|..
gi 1279381529 176 MTVWAQLQPTVLFVTHDVREAALLSDRVLVLS 207
Cdd:TIGR00968 174 RKLHDEVHVTTVFVTHDQEEAMEVADRIVVMS 205
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-208 |
2.08e-56 |
|
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: 179.74 E-value: 2.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGErpvQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH---VGYM 79
Cdd:cd03300 1 IELENVSKFYGGF---VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHkrpVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 80 PQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEP 159
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1279381529 160 FGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSA 208
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNK 206
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-207 |
9.76e-56 |
|
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: 178.30 E-value: 9.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 1 MYLSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG---ALINGQTGHVG 77
Cdd:cd03296 1 MSIEVRNVSKRFGD---FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedaTDVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQRDLLMPWRTVLQNVILGAEI----ARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPL 153
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 154 LLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLS 207
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMN 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-225 |
1.22e-55 |
|
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: 185.49 E-value: 1.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERP--VQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG------ 74
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 --HVGYMPQ--RDLLMPWRTVLQNVILGAEIARK-PLEQARQRARSLLPLFGL-EGFADAYPRQLSGGMRQRAALLRTIL 148
Cdd:COG1123 341 rrRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 149 MDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIADVPIH--LARPR 225
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD--GRIVEDGPTEevFANPQ 497
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
3-214 |
2.36e-55 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 181.84 E-value: 2.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhGERPVQALA----------------------EVSFVIEQGE-FVsLIGQSGSGKSTLCNLIAGLLTPDS 59
Cdd:COG4175 4 IEVRNLYKIF-GKRPERALKlldqgkskdeilektgqtvgvnDASFDVEEGEiFV-IMGLSGSGKSTLVRCLNRLIEPTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 60 GEIRLNGALINGqtghvgyMPQRDL----------------LMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLE 123
Cdd:COG4175 82 GEVLIDGEDITK-------LSKKELrelrrkkmsmvfqhfaLLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 124 GFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRV 203
Cdd:COG4175 155 GWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRI 234
|
250
....*....|.
gi 1279381529 204 LVLsaRPGRLI 214
Cdd:COG4175 235 AIM--KDGRIV 243
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-208 |
3.73e-55 |
|
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: 174.68 E-value: 3.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG-------H 75
Cdd:cd03229 1 LELKNVSKRYGQ---KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelpplrrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 76 VGYMPQRDLLMPWRTVLQNVILGaeiarkpleqarqrarsllplfglegfadayprqLSGGMRQRAALLRTILMDRPLLL 155
Cdd:cd03229 78 IGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1279381529 156 LDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSA 208
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-233 |
7.20e-55 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 175.71 E-value: 7.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERpvqalAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH---VGYM 79
Cdd:COG3840 2 LRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAerpVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 80 PQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEP 159
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279381529 160 FGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIADVPIH--LARPRRESDEAFL 233
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVAD--GRIAADGPTAalLDGEPPPALAAYL 230
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-235 |
1.07e-54 |
|
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: 175.82 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT----GHVGY 78
Cdd:COG4555 2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPrearRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 79 MPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDE 158
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 159 PFGALDALTRREMQNWLMTvWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIADVPIH--LARPRRES-DEAFLRL 235
Cdd:COG4555 159 PTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHK--GKVVAQGSLDelREEIGEENlEDAFVAL 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-207 |
2.02e-53 |
|
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: 171.50 E-value: 2.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 4 SLQRVSKTFhGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVGY 78
Cdd:cd03225 1 ELKNLSFSY-PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlkelrRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 79 M---PQRDLLMPwrTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLL 155
Cdd:cd03225 80 VfqnPDDQFFGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 156 LDEPFGALDALTRREMQNWLMTVWAQLQpTVLFVTHDVREAALLSDRVLVLS 207
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLE 208
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-213 |
2.61e-53 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 175.65 E-value: 2.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING-QTGH--VGYM 79
Cdd:COG3839 4 LELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDlPPKDrnIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 80 PQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEP 159
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 160 FGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRL 213
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND--GRI 212
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-240 |
3.15e-52 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 169.86 E-value: 3.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVGYMPQR 82
Cdd:PRK11247 13 LLLNAVSKRY-GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 83 DLLMPWRTVLQNVILGAEiarkplEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTiLMDRP-LLLLDEPFG 161
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARA-LIHRPgLLLLDEPLG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 162 ALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLIADVPIHLARPRRESDEAFLRLQAQLL 240
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLI--EEGKIGLDLTVDLPRPRRRGSARLAELEAEVL 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-214 |
1.36e-51 |
|
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: 167.30 E-value: 1.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTF-HGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-------- 73
Cdd:cd03257 2 LEVKNLSVSFpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 74 GHVGYMPQRDL--LMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGL---EGFADAYPRQLSGGMRQRAALLRTIL 148
Cdd:cd03257 82 KEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279381529 149 MDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLI 214
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYA--GKIV 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-218 |
2.20e-51 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 166.38 E-value: 2.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPvqALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG-------- 74
Cdd:COG2884 2 IRFENVSKRYPGGRE--ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreipylrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 HVGYMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLL 154
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 155 LLDEPFGALDALTRREmqnwLMTVWAQLQ---PTVLFVTHDVREAALLSDRVLVLSArpGRLIADVP 218
Cdd:COG2884 160 LADEPTGNLDPETSWE----IMELLEEINrrgTTVLIATHDLELVDRMPKRVLELED--GRLVRDEA 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-218 |
6.32e-51 |
|
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: 165.68 E-value: 6.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFH-GERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-------- 73
Cdd:COG4181 9 IELRGLTKTVGtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedararlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 74 -GHVGYMPQRDLLMPWRTVLQNVILGAEIARKPleQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRP 152
Cdd:COG4181 89 aRHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279381529 153 LLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAAlLSDRVLVLSArpGRLIADVP 218
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRA--GRLVEDTA 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-214 |
4.80e-50 |
|
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: 163.52 E-value: 4.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTF-HGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG------- 74
Cdd:cd03258 2 IELKNVSKVFgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 -HVGYMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPL 153
Cdd:cd03258 82 rRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 154 LLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHD---VREAAllsDRVLVLSArpGRLI 214
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmevVKRIC---DRVAVMEK--GEVV 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-216 |
2.03e-49 |
|
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: 162.07 E-value: 2.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG-------- 74
Cdd:COG1127 6 IEVRNLTKSF-GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelyelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 HVGYMPQRDLL---MpwrTVLQNVILG-AEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMD 150
Cdd:COG1127 83 RIGMLFQGGALfdsL---TVFENVAFPlREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279381529 151 RPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLAD--GKIIAE 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-219 |
2.12e-49 |
|
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: 162.28 E-value: 2.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTF-HGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQ-----TGHV 76
Cdd:COG1124 2 LEVRNLSVSYgQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRrrkafRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQ--RDLLMPWRTVLQNVILGAEIARKPleQARQRARSLLPLFGL-EGFADAYPRQLSGGMRQRAALLRTILMDRPL 153
Cdd:COG1124 82 QMVFQdpYASLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279381529 154 LLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIADVPI 219
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN--GRIVEELTV 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-204 |
8.75e-48 |
|
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: 156.92 E-value: 8.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGErpvQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-------GH 75
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKkninelrQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 76 VGYMPQRDLLMPWRTVLQNVILGAEIARK-PLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLL 154
Cdd:cd03262 78 VGMVFQQFNLFPHLTVLENITLAPIKVKGmSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1279381529 155 LLDEPFGALDALTRREMQNwLMTVWAQLQPTVLFVTHDVREAALLSDRVL 204
Cdd:cd03262 158 LFDEPTSALDPELVGEVLD-VMKDLAEEGMTMVVVTHEMGFAREVADRVI 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-220 |
2.07e-47 |
|
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: 156.89 E-value: 2.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG-------- 74
Cdd:cd03261 1 IELRGLTKSF-GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelyrlrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 HVGYMPQRDLLMPWRTVLQNVILG-AEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPL 153
Cdd:cd03261 78 RMGMLFQSGALFDSLTVFENVAFPlREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 154 LLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSarPGRLIADVPIH 220
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLY--DGKIVAEGTPE 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-212 |
4.21e-47 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 160.11 E-value: 4.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGErpvQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING---QTGHVGYM 79
Cdd:PRK09452 15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 80 PQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILmDRP-LLLLDE 158
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV-NKPkVLLLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 159 PFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGR 212
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGR 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-215 |
5.58e-47 |
|
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: 155.36 E-value: 5.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT----GHVGY 78
Cdd:cd03263 1 LQIRNLTKTY-KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRkaarQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 79 MPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDE 158
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 159 PFGALDALTRREMqnWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIA 215
Cdd:cd03263 160 PTSGLDPASRRAI--WDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSD--GKLRC 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-206 |
1.28e-46 |
|
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: 153.95 E-value: 1.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINgqtghvgYMP-- 80
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-------DLPpk 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 81 QRDLLM--------PWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRP 152
Cdd:cd03301 71 DRDIAMvfqnyalyPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 153 LLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-215 |
1.50e-46 |
|
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: 154.80 E-value: 1.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING---QTGHVGYMPQRDLLMPWRTVLQNVIL 97
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNlppEKRDISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 98 GAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMT 177
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1279381529 178 VWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLIA 215
Cdd:cd03299 175 IRKEFGVTVLHVTHDFEEAWALADKVAIM--LNGKLIQ 210
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-206 |
3.83e-46 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 157.12 E-value: 3.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 2 YLSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING---QTGHVGY 78
Cdd:TIGR03265 4 YLSIDNIRKRFGA---FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRlppQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 79 MPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDE 158
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1279381529 159 PFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVM 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-216 |
6.12e-46 |
|
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: 152.45 E-value: 6.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 23 EVSFVIEqGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING---------QTGHVGYMPQRDLLMPWRTVLQ 93
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinlppQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 94 NVILGAEiaRKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQN 173
Cdd:cd03297 95 NLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1279381529 174 WLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLIAD 216
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM--EDGRLQYI 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-245 |
6.75e-46 |
|
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: 159.68 E-value: 6.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPD---SGEIRLNGALINGQT-----G 74
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSealrgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 HVGYMPQ--RDLLMPWrTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRP 152
Cdd:COG1123 84 RIGMVFQdpMTQLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 153 LLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLIADVPIH--LARPRRESDE 230
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM--DDGRIVEDGPPEeiLAAPQALAAV 240
|
250
....*....|....*
gi 1279381529 231 AFLRLQAQLLGSLAA 245
Cdd:COG1123 241 PRLGAARGRAAPAAA 255
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-213 |
1.35e-45 |
|
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: 150.24 E-value: 1.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhGERPvqALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT----GHVGY 78
Cdd:cd03230 1 IEVRNLSKRY-GKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPeevkRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 79 MPQRDLLMPWRTVLQNVilgaeiarkpleqarqrarsllplfglegfadayprQLSGGMRQRAALLRTILMDRPLLLLDE 158
Cdd:cd03230 78 LPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 159 PFGALDALTRREMQNWLMTvWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRL 213
Cdd:cd03230 122 PTSGLDPESRREFWELLRE-LKKEGKTILLSSHILEEAERLCDRVAILNN--GRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-218 |
2.08e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.78 E-value: 2.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERpvqALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVGYMPQR 82
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 83 ---DLLMP---WRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLL 156
Cdd:COG1121 84 aevDWDFPitvRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 157 DEPFGALDALTRREMQNwLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSarpGRLIADVP 218
Cdd:COG1121 164 DEPFAGVDAATEEALYE-LLRELRREGKTILVVTHDLGAVREYFDRVLLLN---RGLVAHGP 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-216 |
2.55e-45 |
|
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: 150.72 E-value: 2.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 28 IEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIrlngaLINGQTghVGYMP----------QRDLLMPWRTVLQNVIL 97
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV-----LINGVD--VTAAPpadrpvsmlfQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 98 GAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMT 177
Cdd:cd03298 94 GLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1279381529 178 VWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDN--GRIAAQ 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-234 |
4.56e-45 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 150.91 E-value: 4.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGAL-------INGQTGH 75
Cdd:COG1126 2 IEIENLHKSFGD---LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDltdskkdINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 76 VGYMPQRDLLMPWRTVLQNVILGAEIARK-PLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLL 154
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLAPIKVKKmSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 155 LLDEPFGALD------------ALTRREMqnwlmtvwaqlqpTVLFVTHDVREAALLSDRVLVLSArpGRLIADVPIH-- 220
Cdd:COG1126 159 LFDEPTSALDpelvgevldvmrDLAKEGM-------------TMVVVTHEMGFAREVADRVVFMDG--GRIVEEGPPEef 223
|
250
....*....|....
gi 1279381529 221 LARPRRESDEAFLR 234
Cdd:COG1126 224 FENPQHERTRAFLS 237
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
21-233 |
5.29e-45 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 153.69 E-value: 5.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING---QTGHVGYMPQRDLLMPWRTVLQNVIL 97
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNlppEKRGIAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 98 GAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMT 177
Cdd:NF040840 96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 178 VWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRL--IADVPIHLARPRRESDEAFL 233
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIM--LNGRLsqVGDVREVFRRPKNEFVARFV 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-234 |
7.33e-45 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 153.31 E-value: 7.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFH-GERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG------- 74
Cdd:COG1135 2 IELENLSKTFPtKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 -HVGYMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPL 153
Cdd:COG1135 82 rKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 154 LLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHD---VREAAllsDRVLVLSArpGRLIADVPIH--LARPRRES 228
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEmdvVRRIC---DRVAVLEN--GRIVEQGPVLdvFANPQSEL 236
|
....*.
gi 1279381529 229 DEAFLR 234
Cdd:COG1135 237 TRRFLP 242
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-207 |
1.15e-44 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 153.32 E-value: 1.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 1 MYLSLQRVSKTFhGERpvQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG---ALINGQTGHVG 77
Cdd:PRK10851 1 MSIEIANIKKSF-GRT--QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvSRLHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQRDLLMPWRTVLQNVILGAEI----ARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPL 153
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 154 LLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLS 207
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMS 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-209 |
1.29e-43 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 146.47 E-value: 1.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTfHGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPD---SGEIRLNGALING---QTGHV 76
Cdd:COG4136 2 LSLENLTIT-LGGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAlpaEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPWRTVLQNVILG--AEIARkplEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLL 154
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFAlpPTIGR---AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 155 LLDEPFGALDALTRREMQNWlmtVWAQLQ----PTVLfVTHDVrEAALLSDRVLVLSAR 209
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREF---VFEQIRqrgiPALL-VTHDE-EDAPAAGRVLDLGNW 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-209 |
4.09e-43 |
|
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: 144.93 E-value: 4.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT----GHVGY 78
Cdd:COG4133 3 LEAENLSCRR-GERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARedyrRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 79 MPQRDLLMPWRTVLQNVILGAEIarKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDE 158
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAAL--YGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1279381529 159 PFGALDALTRREMQNWLMTvWAQLQPTVLFVTHDvrEAALLSDRVLVLSAR 209
Cdd:COG4133 158 PFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ--PLELAAARVLDLGDF 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-213 |
1.24e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.80 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH-----VG 77
Cdd:COG4619 1 LELEGLSFRV-GGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPewrrqVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQRDLLmpWR-TVLQNVILGAEIARKPLEqaRQRARSLLPLFGL-EGFADAYPRQLSGGMRQRAALLRTILMDRPLLL 155
Cdd:COG4619 78 YVPQEPAL--WGgTVRDNLPFPFQLRERKFD--RERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 156 LDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRL 213
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTL--EAGRL 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-215 |
1.68e-42 |
|
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: 143.44 E-value: 1.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 20 ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVGYMPQR---DLLMPWrTVLQNVI 96
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRrsiDRDFPI-SVRDVVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 97 LG----AEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREmq 172
Cdd:cd03235 93 MGlyghKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQED-- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1279381529 173 nwLMTVWAQLQP---TVLFVTHDVREAALLSDRVLVLSarpGRLIA 215
Cdd:cd03235 171 --IYELLRELRRegmTILVVTHDLGLVLEYFDRVLLLN---RTVVA 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-213 |
2.15e-42 |
|
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: 143.32 E-value: 2.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 5 LQRVSKTFHGErpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG--------HV 76
Cdd:cd03292 3 FINVTKTYPNG--TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraipylrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLL 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 157 DEPFGALDALTRREMQNwLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRL 213
Cdd:cd03292 161 DEPTGNLDPDTTWEIMN-LLKKINKAGTTVVVATHAKELVDTTRHRVIAL--ERGKL 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-216 |
3.56e-42 |
|
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: 144.03 E-value: 3.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH------V 76
Cdd:COG0411 5 LEVRGLTKRFGG---LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHriarlgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPWRTVLQNVILGAEI---------------ARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRA 141
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVLVAAHArlgrgllaallrlprARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 142 ALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF--GRVIAE 234
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-216 |
5.91e-42 |
|
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: 145.33 E-value: 5.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 36 LIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG---ALINGQTGHVGYMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQR 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGedvTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 113 ARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHD 192
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180
....*....|....*....|....
gi 1279381529 193 VREAALLSDRVLVLsaRPGRLIAD 216
Cdd:TIGR01187 161 QEEAMTMSDRIAIM--RKGKIAQI 182
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-216 |
4.68e-41 |
|
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: 140.65 E-value: 4.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH------V 76
Cdd:cd03219 1 LEVRGLTKRFGG---LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHeiarlgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPWRTVLQNVILGAEI----------ARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRT 146
Cdd:cd03219 78 GRTFQIPRLFPELTVLENVMVAAQArtgsglllarARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 147 ILMDRPLLLLDEPFGALDALTRREMQNWLMTVwAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQ--GRVIAE 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-224 |
7.72e-40 |
|
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: 140.62 E-value: 7.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 23 EVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGA-LINGQTG--------HVGYMPQRDLLMPWRTVLQ 93
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvLQDSARGiflpphrrRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 94 NVILGAeiARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQN 173
Cdd:COG4148 97 NLLYGR--KRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1279381529 174 WLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIADVPIH--LARP 224
Cdd:COG4148 175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQ--GRVVASGPLAevLSRP 225
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-205 |
1.10e-39 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 137.02 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 25 SFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGAlingqtGHVGYMP---------QRDLLMPWRTVLQNV 95
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ------DHTTTPPsrrpvsmlfQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 96 ILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWL 175
Cdd:PRK10771 93 GLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190
....*....|....*....|....*....|
gi 1279381529 176 MTVWAQLQPTVLFVTHDVREAALLSDRVLV 205
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLV 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-160 |
1.69e-39 |
|
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: 133.93 E-value: 1.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 24 VSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVGYMPQRDLLMPWRTVLQNVILG 98
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDErkslrKEIGYVFQDPQLFPRLTVRENLRLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279381529 99 AEIARKPLEQARQRARSLLPLFGLEGFAD----AYPRQLSGGMRQRAALLRTILMDRPLLLLDEPF 160
Cdd:pfam00005 84 LLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-216 |
2.22e-39 |
|
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: 136.71 E-value: 2.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTfHGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG-----HVG 77
Cdd:COG1120 2 LEAENLSVG-YGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrelarRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQrDLLMPWR-TVLQNVILGAEIARKPLEQA----RQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRP 152
Cdd:COG1120 79 YVPQ-EPPAPFGlTVRELVALGRYPHLGLFGRPsaedREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 153 LLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLIAD 216
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLL--KDGRIVAQ 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-206 |
3.17e-39 |
|
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: 133.14 E-value: 3.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 4 SLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGAlingqtghvgympqrd 83
Cdd:cd00267 1 EIENLSFRYGG---RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 84 llmpwrtvlqnvilgaEIARKPLEQARQRArSLLPlfglegfadayprQLSGGMRQRAALLRTILMDRPLLLLDEPFGAL 163
Cdd:cd00267 62 ----------------DIAKLPLEELRRRI-GYVP-------------QLSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1279381529 164 DALTRREMQNWLMTvWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:cd00267 112 DPASRERLLELLRE-LAEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-218 |
3.35e-39 |
|
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: 135.77 E-value: 3.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERpvQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG-------- 74
Cdd:cd03256 1 IEVENLSKTYPNGK--KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqlrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 HVGYMPQRDLLMPWRTVLQNVILGAeIARKPL---------EQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLR 145
Cdd:cd03256 79 QIGMIFQQFNLIERLSVLENVLSGR-LGRRSTwrslfglfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 146 TiLMDRP-LLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIADVP 218
Cdd:cd03256 158 A-LMQQPkLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD--GRIVFDGP 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-206 |
5.31e-39 |
|
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: 134.33 E-value: 5.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhgeRPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH-VGYMPQ 81
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNrIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 82 RDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1279381529 162 ALDALTRREMQNWLMTVWAQlQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:cd03269 158 GLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLL 201
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-206 |
8.13e-39 |
|
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: 137.11 E-value: 8.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFH-GERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTP---DSGEIRLNGALINGQTG---- 74
Cdd:COG0444 2 LEVRNLKVYFPtRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 -----HVGYMPQRDL--LMPWRTVLQNVILGAEIARK-PLEQARQRARSLLPLFGL---EGFADAYPRQLSGGMRQRAAL 143
Cdd:COG0444 82 kirgrEIQMIFQDPMtsLNPVMTVGDQIAEPLRIHGGlSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279381529 144 LRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-206 |
3.08e-38 |
|
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: 130.97 E-value: 3.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTfHGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVG 77
Cdd:cd03228 1 IEFKNVSFS-YPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDleslrKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQRDLLMPwRTVLQNVilgaeiarkpleqarqrarsllplfglegfadayprqLSGGMRQRAALLRTILMDRPLLLLD 157
Cdd:cd03228 80 YVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1279381529 158 EPFGALDALTRREMQNwLMTVWAQlQPTVLFVTHDVrEAALLSDRVLVL 206
Cdd:cd03228 122 EATSALDPETEALILE-ALRALAK-GKTVIVIAHRL-STIRDADRIIVL 167
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-213 |
6.43e-38 |
|
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: 132.09 E-value: 6.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFH-GERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG------- 74
Cdd:TIGR02211 2 LKCENLGKRYQeGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSneraklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 --HVGYMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRP 152
Cdd:TIGR02211 82 nkKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279381529 153 LLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLsDRVLVLsaRPGRL 213
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEM--KDGQL 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-234 |
9.75e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 132.57 E-value: 9.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 5 LQRVSKTFHGErpvQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING------QTG---- 74
Cdd:PRK11264 6 VKNLVKKFHGQ---TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarslsqQKGlirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 ---HVGYMPQRDLLMPWRTVLQNVILGAEIARK-PLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMD 150
Cdd:PRK11264 83 lrqHVGFVFQNFNLFPHRTVLENIIEGPVIVKGePKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 151 RPLLLLDEPFGALDALTRREMQNWLMTVwAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIADVPIH--LARPRRES 228
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQ--GRIVEQGPAKalFADPQQPR 239
|
....*.
gi 1279381529 229 DEAFLR 234
Cdd:PRK11264 240 TRQFLE 245
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-207 |
1.39e-37 |
|
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: 130.75 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 23 EVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH---VGYMPQRDLLMPWRTVLQNVILGA 99
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYqrpVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 100 EIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVW 179
Cdd:TIGR01277 96 HPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLC 175
|
170 180
....*....|....*....|....*...
gi 1279381529 180 AQLQPTVLFVTHDVREAALLSDRVLVLS 207
Cdd:TIGR01277 176 SERQRTLLMVTHHLSDARAIASQIAVVS 203
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-206 |
2.27e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 134.08 E-value: 2.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 2 YLSLQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIrlngaLINGQTGHVGYMPQ 81
Cdd:PRK11432 6 FVVLKNITKRF-GSNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI-----FIDGEDVTHRSIQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 82 RDLLM--------PWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPL 153
Cdd:PRK11432 78 RDICMvfqsyalfPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1279381529 154 LLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVM 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-219 |
1.25e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 134.77 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 1 MYLSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG----------ALIN 70
Cdd:COG3845 4 PALELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvrirsprdAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 71 GqtghVGYMPQRDLLMPWRTVLQNVILGAEIARKP---LEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTI 147
Cdd:COG3845 81 G----IGMVHQHFMLVPNLTVAENIVLGLEPTKGGrldRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 148 LMDRPLLLLDEP------------FGALDALTRREMqnwlmtvwaqlqpTVLFVTHDVREAALLSDRVLVLsaRPGRLIA 215
Cdd:COG3845 157 YRGARILILDEPtavltpqeadelFEILRRLAAEGK-------------SIIFITHKLREVMAIADRVTVL--RRGKVVG 221
|
....
gi 1279381529 216 DVPI 219
Cdd:COG3845 222 TVDT 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-207 |
2.71e-36 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 131.88 E-value: 2.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGErpvQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG---ALINGQTGHVGYM 79
Cdd:PRK11607 20 LEIRNLTKSFDGQ---HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlSHVPPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 80 PQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTiLMDRP-LLLLDE 158
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARS-LAKRPkLLLLDE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1279381529 159 PFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLS 207
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-216 |
3.80e-36 |
|
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: 127.83 E-value: 3.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 12 FHGE-RPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQtgHVGYMPQRDLLMPWRT 90
Cdd:cd03267 27 FKRKyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKR--RKKFLRRIGVVFGQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 91 -------VLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGAL 163
Cdd:cd03267 105 qlwwdlpVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1279381529 164 DALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:cd03267 185 DVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK--GRLLYD 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-216 |
5.23e-36 |
|
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: 134.58 E-value: 5.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPvQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVG 77
Cdd:COG2274 474 IELENVSFRYPGDSP-PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDpaslrRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQRDLLMPwRTVLQNVILGAEIArkPLEQARQRARsllpLFGLEGFADAYP-----------RQLSGGMRQRAALLRT 146
Cdd:COG2274 553 VVLQDVFLFS-GTIRENITLGDPDA--TDEEIIEAAR----LAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279381529 147 ILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLqpTVLFVTHdvREAAL-LSDRVLVLSArpGRLIAD 216
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAH--RLSTIrLADRIIVLDK--GRIVED 690
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-206 |
6.18e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 131.31 E-value: 6.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 20 ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGA---------LINGQTGHVGYMPQRDLLMPWRT 90
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiakisdaeLREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 91 VLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRRE 170
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190
....*....|....*....|....*....|....*.
gi 1279381529 171 MQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-216 |
1.18e-35 |
|
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: 127.55 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGErPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG-ALINGQTG-----HV 76
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLweirkKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYmpqrdllmpwrtVLQN-------------VILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAAL 143
Cdd:TIGR04520 80 GM------------VFQNpdnqfvgatveddVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 144 LRTILMDRPLLLLDEPFGALDALTRREmqnwLMTVWAQLQP----TVLFVTHDVREAAlLSDRVLVLSArpGRLIAD 216
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKE----VLETIRKLNKeegiTVISITHDMEEAV-LADRVIVMNK--GKIVAE 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-219 |
1.25e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.06 E-value: 1.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH------V 76
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaqaagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPWRTVLQNVILGAEIARKPL---EQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPL 153
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPRRGGLidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 154 LLLDEPfgaLDALTRREMQNwLMTVWAQLQP---TVLFVTHDVREAALLSDRVLVLsaRPGRLIADVPI 219
Cdd:COG1129 162 LILDEP---TASLTEREVER-LFRIIRRLKAqgvAIIYISHRLDEVFEIADRVTVL--RDGRLVGTGPV 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-215 |
1.38e-35 |
|
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: 132.57 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPvqALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVG 77
Cdd:COG4988 337 IELEDVSFSYPGGRP--ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDpaswrRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQRDLLMPWrTVLQNVILGA-EIARKPLEQARQRArsllplfGLEGFADAYP-----------RQLSGGMRQRAALLR 145
Cdd:COG4988 415 WVPQNPYLFAG-TIRENLRLGRpDASDEELEAALEAA-------GLDEFVAALPdgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 146 TILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLqpTVLFVTHDVrEAALLSDRVLVLSArpGRLIA 215
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRL-ALLAQADRILVLDD--GRIVE 551
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-216 |
5.72e-35 |
|
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: 124.58 E-value: 5.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH------V 76
Cdd:cd03218 1 LRAENLSKRY-GKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHkrarlgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQ-----RDLlmpwrTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDR 151
Cdd:cd03218 78 GYLPQeasifRKL-----TVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 152 PLLLLDEPFGALDALTRREMQNwLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQK-IIKILKDRGIGVLITDHNVRETLSITDRAYIIYE--GKVLAE 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
13-216 |
1.60e-34 |
|
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: 121.77 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 13 HGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINgqtghvgympqrdllmpwrtvl 92
Cdd:cd03214 9 YGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA---------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 93 qnvilgaeiARKPLEQARQRArsLLP----LFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTR 168
Cdd:cd03214 65 ---------SLSPKELARKIA--YVPqaleLLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1279381529 169 REMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKD--GRIVAQ 179
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-234 |
2.05e-34 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 126.07 E-value: 2.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 5 LQRVSKTFH-GERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG----ALINGQTGH---- 75
Cdd:PRK11153 4 LKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltALSEKELRKarrq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 76 VGYMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLL 155
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 156 LDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHD---VREAAllsDRVLVLSArpGRLI-----ADVpihLARPRRE 227
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEmdvVKRIC---DRVAVIDA--GRLVeqgtvSEV---FSHPKHP 235
|
....*..
gi 1279381529 228 SDEAFLR 234
Cdd:PRK11153 236 LTREFIQ 242
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-219 |
2.05e-34 |
|
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: 126.38 E-value: 2.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 23 EVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQ------TGH---VGYMPQRDLLMPWRTVLQ 93
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSrkgiflPPEkrrIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 94 NVILGAEIARKPLEQARQRArsLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQN 173
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFER--VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1279381529 174 WLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLIADVPI 219
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVL--EDGRVAAAGPI 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-206 |
5.73e-34 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 124.96 E-value: 5.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTghvgymP-Q 81
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE------PaD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 82 RDLLM--------PWRTVLQNVILGAEIARKPLEQARQR----ARSLlplfGLEGFADAYPRQLSGGMRQRAALLRTILM 149
Cdd:PRK11650 76 RDIAMvfqnyalyPHMSVRENMAYGLKIRGMPKAEIEERvaeaARIL----ELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 150 DRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVM 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-231 |
7.57e-34 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 128.30 E-value: 7.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTF-HGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG---------ALINGQ 72
Cdd:PRK10535 5 LELKDIRRSYpSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdvatldadALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 73 TGHVGYMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRP 152
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 153 LLLLDEPFGALDALTRREmqnwLMTVWAQLQP---TVLFVTHDVREAAlLSDRVLVLsaRPGRLIADVPIHLARPRRESD 229
Cdd:PRK10535 165 VILADEPTGALDSHSGEE----VMAILHQLRDrghTVIIVTHDPQVAA-QAERVIEI--RDGEIVRNPPAQEKVNVAGGT 237
|
..
gi 1279381529 230 EA 231
Cdd:PRK10535 238 EP 239
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-216 |
2.18e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 122.14 E-value: 2.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH-VGYMPQ 81
Cdd:COG4152 2 LELKGLTKRFGD---KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 82 RDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:COG4152 79 ERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 162 ALDALTrremQNWLMTVWAQLQP---TVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:COG4152 159 GLDPVN----VELLKDVIRELAAkgtTVIFSSHQMELVEELCDRIVIINK--GRKVLS 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
18-215 |
2.26e-33 |
|
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: 120.17 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 18 VQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHV----GYMPQRDLLMPWRTVLQ 93
Cdd:cd03265 13 FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVrrriGIVFQDLSVDDELTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 94 NVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQN 173
Cdd:cd03265 93 NLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1279381529 174 WLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIA 215
Cdd:cd03265 173 YIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDH--GRIIA 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-216 |
2.68e-33 |
|
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: 119.63 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALIN---GQTGHVGYM 79
Cdd:cd03268 1 LKTNDLTKTYGK---KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQkniEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 80 PQRDLLMPWRTVLQNVILGAEIARKPleqaRQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEP 159
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 160 FGALDALTRREMQNWLMtVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLIAD 216
Cdd:cd03268 154 TNGLDPDGIKELRELIL-SLRDQGITVLISSHLLSEIQKVADRIGII--NKGKLIEE 207
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-215 |
9.91e-33 |
|
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: 124.88 E-value: 9.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPvQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG-----HVG 77
Cdd:COG4987 334 LELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEddlrrRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQRDLLMPwRTVLQNVILGAEIA-RKPLEQARQRArsllplfGLEGFADAYP-----------RQLSGGMRQRAALLR 145
Cdd:COG4987 413 VVPQRPHLFD-TTLRENLRLARPDAtDEELWAALERV-------GLGDWLAALPdgldtwlgeggRRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279381529 146 TILMDRPLLLLDEPFGALDALTRREMqnwLMTVWAQLQP-TVLFVTHDVREAALLsDRVLVLSArpGRLIA 215
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQAL---LADLLEALAGrTVLLITHRLAGLERM-DRILVLED--GRIVE 549
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-216 |
1.68e-32 |
|
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: 115.99 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNgalingqtghvgympqr 82
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD----------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 83 dllmpwrtvlqnvilGAEIARKPLEQARQRarsllplfgleGFADAYprQLSGGMRQRAALLRTILMDRPLLLLDEPFGa 162
Cdd:cd03216 61 ---------------GKEVSFASPRDARRA-----------GIAMVY--QLSVGERQMVEIARALARNARLLILDEPTA- 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 163 ldALTRREMQNwLMTVWAQLQP---TVLFVTHDVREAALLSDRVLVLsaRPGRLIAD 216
Cdd:cd03216 112 --ALTPAEVER-LFKVIRRLRAqgvAVIFISHRLDEVFEIADRVTVL--RDGRVVGT 163
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-215 |
1.81e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 118.21 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 1 MYLSLQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH----- 75
Cdd:COG1137 2 MTLEAENLVKSY-GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHkrarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 76 -VGYMPQ-----RDLlmpwrTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILM 149
Cdd:COG1137 79 gIGYLPQeasifRKL-----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 150 DRPLLLLDEPFGALDALTRREMQNWLmtvwAQLQPT---VLFVTHDVREAALLSDRVLVLSArpGRLIA 215
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKII----RHLKERgigVLITDHNVRETLGICDRAYIISE--GKVLA 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-215 |
2.42e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.96 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 19 QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVGYMPQR-DLLMPWRTVL 92
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdvrRQVGMVFQNpDNQFVGATVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 93 QNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAAlLRTILMDRP-LLLLDEPFGALDALTRREM 171
Cdd:PRK13635 101 DDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVA-IAGVLALQPdIIILDEATSMLDPRGRREV 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1279381529 172 QNWLMTVWAQLQPTVLFVTHDVREAAlLSDRVLVLsaRPGRLIA 215
Cdd:PRK13635 180 LETVRQLKEQKGITVLSITHDLDEAA-QADRVIVM--NKGEILE 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-206 |
2.88e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 119.07 E-value: 2.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGAL--------INGQTGHVGYMPQRDLLMPwrTVL 92
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdIRHKIGMVFQNPDNQFVGA--TVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 93 QNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQ 172
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190
....*....|....*....|....*....|....
gi 1279381529 173 NWLMTVWAQLQPTVLFVTHDVREAAlLSDRVLVL 206
Cdd:PRK13650 181 KTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVM 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-206 |
1.94e-31 |
|
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: 114.66 E-value: 1.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 11 TFHGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT--GHVGYMPQ---RDLL 85
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKErrKSIGYVMQdvdYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 86 MpwRTVLQNVILGAEIARKPLEQARQrarsLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDA 165
Cdd:cd03226 86 T--DSVREELLLGLKELDAGNEQAET----VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1279381529 166 LTRREMQNWLMTVWAQlQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:cd03226 160 KNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-221 |
2.98e-31 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 118.21 E-value: 2.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 4 SLQRVSKTFhGERPVQAlaEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALIN----GQTGhVGYM 79
Cdd:PRK11000 5 TLRNVTKAY-GDVVISK--DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNdvppAERG-VGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 80 PQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEP 159
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 160 FGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRlIADV--PIHL 221
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA--GR-VAQVgkPLEL 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-216 |
5.61e-31 |
|
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: 113.83 E-value: 5.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERpvqALAEVSFVIEQGEFVsLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG--ALINGQT--GHVGY 78
Cdd:cd03264 1 LQLENLTKRYGKKR---ALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdVLKQPQKlrRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 79 MPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDE 158
Cdd:cd03264 77 LPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 159 PFGALDALTRREMQNWLMTVWAqlQPTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNK--GKLVFE 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-218 |
8.33e-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: 113.81 E-value: 8.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKtFHGERpvQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLL-----TPDSGEIRLNGALINGQTGH-- 75
Cdd:cd03260 1 IELRDLNV-YYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 76 -----VGYMPQRDLLMPwRTVLQNVILGAEIAR-KPLEQARQRARSLLPLFGL--EGFADAYPRQLSGGMRQRAALLRTI 147
Cdd:cd03260 78 elrrrVGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279381529 148 LMDRPLLLLDEPFGALDALTRREMQNwLMTVWAQlQPTVLFVTHDVREAALLSDRVLVLSArpGRLIADVP 218
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEE-LIAELKK-EYTIVIVTHNMQQAARVADRTAFLLN--GRLVEFGP 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-218 |
8.41e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.03 E-value: 8.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 5 LQRVSKTFHgerPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHV-------G 77
Cdd:PRK09493 4 FKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQRDLLMPWRTVLQNVILGAEIARK-PLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLL 156
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGaSKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 157 DEPFGALDALTRREMQNwLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIADVP 218
Cdd:PRK09493 161 DEPTSALDPELRHEVLK-VMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDK--GRIAEDGD 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-217 |
1.03e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 114.41 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERP--VQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQ-----TGH 75
Cdd:COG1101 2 LELKNLSKTFNPGTVneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpeykrAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 76 VGYMPQrDLLM---PWRTVLQNVIL----GaeiARKPLEQARQRAR--------SLLPLfGLEGFADAYPRQLSGGMRQR 140
Cdd:COG1101 82 IGRVFQ-DPMMgtaPSMTIEENLALayrrG---KRRGLRRGLTKKRrelfrellATLGL-GLENRLDTKVGLLSGGQRQA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 141 AALLRTIlMDRP-LLLLDEPFGALD--------ALTRRemqnwlmtVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpG 211
Cdd:COG1101 157 LSLLMAT-LTKPkLLLLDEHTAALDpktaalvlELTEK--------IVEENNLTTLMVTHNMEQALDYGNRLIMMHE--G 225
|
....*.
gi 1279381529 212 RLIADV 217
Cdd:COG1101 226 RIILDV 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-214 |
1.21e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 114.84 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 1 MYLSLQRVSKTFHGERPVQ--ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT----- 73
Cdd:PRK13649 1 MGINLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 74 -------GHVGYMPQRDLLMpwRTVLQNVILGAEIARKPLEQARQRARSLLPLFGL-EGFADAYPRQLSGGMRQRAALLR 145
Cdd:PRK13649 81 kqirkkvGLVFQFPESQLFE--ETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 146 TILMDRPLLLLDEPFGALDALTRREmqnwLMTVWAQLQP---TVLFVTHDVREAALLSDRVLVLSArpGRLI 214
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKE----LMTLFKKLHQsgmTIVLVTHLMDDVANYADFVYVLEK--GKLV 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-217 |
1.77e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 112.99 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFH-GERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG------- 74
Cdd:PRK11629 6 LQCDNLCKRYQeGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 --HVGYMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRP 152
Cdd:PRK11629 86 nqKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 153 LLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRvlvLSARPGRLIADV 217
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ---LEMRDGRLTAEL 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
15-216 |
1.89e-30 |
|
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: 112.68 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 15 ERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGA---LINGQT--GHVGYMPQrDLLMPWR 89
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirQLDPADlrRNIGYVPQ-DVTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 90 TVLQNVILGAEIA--RKPLEQARqrarsllpLFGLEGFADAYP-----------RQLSGGMRQRAALLRTILMDRPLLLL 156
Cdd:cd03245 93 TLRDNITLGAPLAddERILRAAE--------LAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 157 DEPFGALDALTRRE----MQNWLMtvwaqlQPTVLFVTHdvREAAL-LSDRVLVLSArpGRLIAD 216
Cdd:cd03245 165 DEPTSAMDMNSEERlkerLRQLLG------DKTLIIITH--RPSLLdLVDRIIVMDS--GRIVAD 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-215 |
2.52e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 117.96 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVG 77
Cdd:COG1132 340 IEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTleslrRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQRDLLMPwRTVLQNVILGA-EIARKPLEQARQRArsllplfGLEGFADAYP-----------RQLSGGMRQRAALLR 145
Cdd:COG1132 418 VVPQDTFLFS-GTIRENIRYGRpDATDEEVEEAAKAA-------QAHEFIEALPdgydtvvgergVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279381529 146 TILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAqlQPTVLFVTHD---VREAallsDRVLVLSArpGRLIA 215
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRlstIRNA----DRILVLDD--GRIVE 554
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-214 |
2.64e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.47 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLngalinGQTGHVGYMPQ- 81
Cdd:COG0488 316 LELEGLSKSY-GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL------GETVKIGYFDQh 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 82 RDLLMPWRTVLQNVILGAEiarkplEQARQRARSLLPLFGLEG-FADAYPRQLSGGMRQRAALLRtILMDRP-LLLLDEP 159
Cdd:COG0488 387 QEELDPDKTVLDELRDGAP------GGTEQEVRGYLGRFLFSGdDAFKPVGVLSGGEKARLALAK-LLLSPPnVLLLDEP 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1279381529 160 FGALDALTRREMQNWLmtvwAQLQPTVLFVTHDvREA-ALLSDRVLVLsaRPGRLI 214
Cdd:COG0488 460 TNHLDIETLEALEEAL----DDFPGTVLLVSHD-RYFlDRVATRILEF--EDGGVR 508
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-192 |
2.77e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.47 E-value: 2.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 5 LQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALingqtgHVGYMPQRDL 84
Cdd:COG0488 1 LENLSKSF-GGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL------RIGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 85 LMPWRTVLQNVILG-----------AEIARKPLE---------------------QARQRARSLlpLFGLeGFADAYPRQ 132
Cdd:COG0488 72 LDDDLTVLDTVLDGdaelraleaelEELEAKLAEpdedlerlaelqeefealggwEAEARAEEI--LSGL-GFPEEDLDR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 133 ----LSGGMRQRAALLRtILMDRP-LLLLDEPFGALDAltrrEMQNWLMTVWAQLQPTVLFVTHD 192
Cdd:COG0488 149 pvseLSGGWRRRVALAR-ALLSEPdLLLLDEPTNHLDL----ESIEWLEEFLKNYPGTVLVVSHD 208
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-215 |
2.81e-30 |
|
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: 114.02 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 20 ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG-------ALINGQTGHVGYMPQRDLLMPWRtvl 92
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvvrepRKVRRSIGIVPQYASVDEDLTGR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 93 QNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQ 172
Cdd:TIGR01188 85 ENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIW 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1279381529 173 NWLMTVwAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLIA 215
Cdd:TIGR01188 165 DYIRAL-KEEGVTILLTTHYMEEADKLCDRIAII--DHGRIIA 204
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-205 |
3.31e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 114.44 E-value: 3.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTF--------HGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG 74
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 HVGYMPQRDLLM----------PWRTVLQnvILGA--EIAR-KPLEQARQRARSLLPLFGL-EGFADAYPRQLSGGMRQR 140
Cdd:COG4608 88 RELRPLRRRMQMvfqdpyaslnPRMTVGD--IIAEplRIHGlASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 141 AALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHD---VREaalLSDRVLV 205
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDlsvVRH---ISDRVAV 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-214 |
4.66e-30 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 112.03 E-value: 4.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 1 MYLSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG------ 74
Cdd:COG4161 1 MSIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKpsekai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 -----HVGYMPQRDLLMPWRTVLQNVILG-AEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTIL 148
Cdd:COG4161 78 rllrqKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 149 MDRPLLLLDEPFGALDAltrrEMQNWLMTVWAQLQP---TVLFVTHDVREAALLSDRVLVLSArpGRLI 214
Cdd:COG4161 158 MEPQVLLFDEPTAALDP----EITAQVVEIIRELSQtgiTQVIVTHEVEFARKVASQVVYMEK--GRII 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-206 |
6.41e-30 |
|
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: 110.99 E-value: 6.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSkTFHGErpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH------V 76
Cdd:cd03224 1 LEVENLN-AGYGK--SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHeraragI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPWRTVLQNVILGAEIARKPLEQAR-QRARSLLPLfgLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLL 155
Cdd:cd03224 78 GYVPEGRRIFPELTVEENLLLGAYARRRAKRKARlERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1279381529 156 LDEPFGALDALTRREMQNWLMTVwAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVL 205
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-206 |
7.07e-30 |
|
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: 116.62 E-value: 7.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPvqALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVG 77
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP--ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADadswrDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQRDLLMPwRTVLQNVILG-AEIARKPLEQARQRA-----RSLLPLfGLEGFADAYPRQLSGGMRQRAALLRTILMDR 151
Cdd:TIGR02857 400 WVPQHPFLFA-GTIAENIRLArPDASDAEIREALERAgldefVAALPQ-GLDTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 152 PLLLLDEPFGALDALTRREMQNWLMTVwAQLQpTVLFVTHDvREAALLSDRVLVL 206
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRAL-AQGR-TVLLVTHR-LALAALADRIVVL 529
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-206 |
1.27e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 110.87 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 1 MYLSLQRVSKtFHGERpvQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG------ 74
Cdd:PRK11124 1 MSIQLNGINC-FYGAH--QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTpsdkai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 -----HVGYMPQRDLLMPWRTVLQNVIlgaEIARKPL----EQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLR 145
Cdd:PRK11124 78 relrrNVGMVFQQYNLWPHLTVQQNLI---EAPCRVLglskDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 146 TILMDRPLLLLDEPFGALDAltrrEMQNWLMTVWAQLQP---TVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDP----EITAQIVSIIRELAEtgiTQVIVTHEVEVARKTASRVVYM 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-219 |
2.17e-28 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 107.86 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSkTFHGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSG-EIRLNGAlingQTG------- 74
Cdd:COG1119 4 LELRNVT-VRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGE----RRGgedvwel 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 --HVGY----MPQRdlLMPWRTVLQNVILGA----EIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALL 144
Cdd:COG1119 77 rkRIGLvspaLQLR--FPRDETVLDVVLSGFfdsiGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 145 RTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLIADVPI 219
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL--KDGRVVAAGPK 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-216 |
2.39e-28 |
|
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: 107.07 E-value: 2.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGER-PVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHV----G 77
Cdd:cd03266 2 ITADALTKRFRDVKkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEArrrlG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLD 157
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 158 EPFGALDALTRREMQNWLMTVWAQlQPTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHR--GRVVYE 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-197 |
2.96e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 107.17 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTF-HGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG-----------ALIN 70
Cdd:PRK10584 7 VEVHHLKKSVgQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeearAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 71 GQtgHVGYMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMD 150
Cdd:PRK10584 87 AK--HVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1279381529 151 RPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAA 197
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAA 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-206 |
3.38e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 108.21 E-value: 3.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 20 ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING----------QTGHVGYMPQRDLLMpwR 89
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvklsdirkKVGLVFQYPEYQLFE--E 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 90 TVLQNVILGAEIARKPLEQARQRARSLLPLFGL--EGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALT 167
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1279381529 168 RREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVM 218
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
24-220 |
3.55e-28 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 107.07 E-value: 3.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 24 VSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPD----SGEIRLNGALING---QTGHVGYMPQ--RDLLMPWRTVLQN 94
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPlsiRGRHIATIMQnpRTAFNPLFTMGNH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 95 VILGAEIARKPLEQARQRARSLLPLFGLEGFA---DAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREM 171
Cdd:TIGR02770 85 AIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQARV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1279381529 172 QNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIADVPIH 220
Cdd:TIGR02770 165 LKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDD--GRIVERGTVK 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-215 |
4.94e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.38 E-value: 4.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 19 QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVGYMPQR-DLLMPWRTVL 92
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlkeirKKIGIIFQNpDNQFIGATVE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 93 QNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQ 172
Cdd:PRK13632 103 DDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1279381529 173 NWLMTVWAQLQPTVLFVTHDVREaALLSDRVLVLSArpGRLIA 215
Cdd:PRK13632 183 KIMVDLRKTRKKTLISITHDMDE-AILADKVIVFSE--GKLIA 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-216 |
6.37e-28 |
|
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: 106.08 E-value: 6.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 16 RPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG---ALINGQTGhvgympqrdlLMPWRTVL 92
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvsSLLGLGGG----------FNPELTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 93 QNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQ 172
Cdd:cd03220 103 ENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1279381529 173 NWLMTVWAQlQPTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:cd03220 183 RRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEK--GKIRFD 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-216 |
6.43e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 107.97 E-value: 6.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH----VGY 78
Cdd:PRK13537 8 IDFRNVEKRY-GDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHarqrVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 79 MPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDE 158
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 159 PFGALDALTRREMQNWLMTVWAQLQpTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEE--GRKIAE 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-234 |
9.18e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 107.48 E-value: 9.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 1 MYLSLQRVSKTFHGERP--VQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIR--LNGALINGQTGHV 76
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLPteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPWR----------------------------TVLQNVILGAEIARKPLEQARQRARSLLPLFGL-EGFAD 127
Cdd:PRK13651 81 EKVLEKLVIQKTRfkkikkikeirrrvgvvfqfaeyqlfeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 128 AYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQpTVLFVTHDVREAALLSDRVLVLs 207
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFF- 238
|
250 260
....*....|....*....|....*..
gi 1279381529 208 aRPGRLIADVPIHLARprreSDEAFLR 234
Cdd:PRK13651 239 -KDGKIIKDGDTYDIL----SDNKFLI 260
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-206 |
1.17e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.62 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 20 ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALingqtgHVGYMPQRDLLmPWR---TVLQNVI 96
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA------RVAYVPQRSEV-PDSlplTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 97 LGAEIARKPLEQARQRARSL----LPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQ 172
Cdd:NF040873 80 MGRWARRGLWRRLTRDDRAAvddaLERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180 190
....*....|....*....|....*....|....
gi 1279381529 173 NwLMTVWAQLQPTVLFVTHDvREAALLSDRVLVL 206
Cdd:NF040873 160 A-LLAEEHARGATVVVVTHD-LELVRRADPCVLL 191
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-214 |
1.36e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.84 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 1 MYLSLQRVSKTFHGERPVQA--LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH--- 75
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 76 ---------VGYMPQRDLLMpwRTVLQNVILGAEIARKPLEQARQRARSLLPLFGL-EGFADAYPRQLSGGMRQRAALLR 145
Cdd:PRK13641 81 kklrkkvslVFQFPEAQLFE--NTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 146 TILMDRPLLLLDEPFGALDALTRREMqnwlMTVWAQLQP---TVLFVTHDVREAALLSDRVLVLSArpGRLI 214
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEM----MQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEH--GKLI 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-206 |
3.04e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.87 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 1 MYLSLQRVSKTFHGERPVQ--ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT----- 73
Cdd:PRK13634 1 MDITFQKVEHRYQYKTPFErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKknkkl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 74 -------GHVGYMPQRDLLMpwRTVLQNVILGAEIARKPLEQARQRARSLLPLFGL-EGFADAYPRQLSGGMRQRAALLR 145
Cdd:PRK13634 81 kplrkkvGIVFQFPEHQLFE--ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 146 TILMDRPLLLLDEPFGALDALTRREMqnwlMTVWAQL----QPTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEM----MEMFYKLhkekGLTTVLVTHSMEDAARYADQIVVM 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-216 |
3.08e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.78 E-value: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFH-------------------GERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIR 63
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 64 LNG---ALINgqTGhVGYMPqrDLlmpwrTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAyP-RQLSGGMRQ 139
Cdd:COG1134 85 VNGrvsALLE--LG-AGFHP--EL-----TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQ-PvKTYSSGMRA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 140 RAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQpTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:COG1134 154 RLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWLEK--GRLVMD 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-230 |
3.14e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 106.84 E-value: 3.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 1 MYLSLQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT----GHV 76
Cdd:PRK13536 40 VAIDLAGVSKSY-GDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARArlarARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLL 156
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 157 DEPFGALDALTRREMQNWLMTVWAQLQpTVLFVTHDVREAALLSDRVLVLSArpGRLIADvpihlARPRRESDE 230
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEA--GRKIAE-----GRPHALIDE 262
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
38-206 |
5.74e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 106.11 E-value: 5.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 38 GQSGSGKSTLCNLIAGLLTPDSGEIRLNG-ALINGQTG--------HVGYMPQRDLLMPWRTVLQNVILGaeIARKPLEQ 108
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAEKGiclppekrRIGYVFQDARLFPHYKVRGNLRYG--MAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 109 ARQrarsLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLF 188
Cdd:PRK11144 109 FDK----IVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILY 184
|
170
....*....|....*...
gi 1279381529 189 VTHDVREAALLSDRVLVL 206
Cdd:PRK11144 185 VSHSLDEILRLADRVVVL 202
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-206 |
6.06e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.86 E-value: 6.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 1 MYLSLQRVSKTFHGERPVQ--ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT----- 73
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTPYEhqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 74 -------GHVGYMPQRDLLMPwrTVLQNVILGAEIARKPLEQARQRARSLLPLFGLE-GFADAYPRQLSGGMRQRAALLR 145
Cdd:PRK13646 81 rpvrkriGMVFQFPESQLFED--TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 146 TILMDRPLLLLDEPFGALDALTRREmqnwLMTVWAQLQ----PTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQ----VMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVM 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-214 |
6.19e-27 |
|
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: 108.35 E-value: 6.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHG-ERPV-QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGE--IRLN---------GALI 69
Cdd:TIGR03269 280 IKVRNVSKRYISvDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGdewvdmtkpGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 70 NGQ-TGHVGYMPQRDLLMPWRTVLQNVI--LGAEIarkPLEQARQRARSLLPLFGL-----EGFADAYPRQLSGGMRQRA 141
Cdd:TIGR03269 360 RGRaKRYIGILHQEYDLYPHRTVLDNLTeaIGLEL---PDELARMKAVITLKMVGFdeekaEEILDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279381529 142 ALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLI 214
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM--RDGKIV 507
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-216 |
1.00e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.17 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 12 FHGE-RPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGalingqtghvgYMPQRD------- 83
Cdd:COG4586 28 FRREyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----------YVPFKRrkefarr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 84 --LLMPWRT-------VLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLL 154
Cdd:COG4586 97 igVVFGQRSqlwwdlpAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 155 LLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH--GRIIYD 236
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
14-216 |
1.51e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.31 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 14 GERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG-----HVGYMPQR-DLLMP 87
Cdd:PRK13548 13 GGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPaelarRRAVLPQHsSLSFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 88 WrTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTIL------MDRPLLLLDEPFG 161
Cdd:PRK13548 91 F-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 162 ALDALtrreMQNWLMTVWAQL----QPTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:PRK13548 170 ALDLA----HQHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQ--GRLVAD 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-207 |
1.55e-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: 102.69 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 8 VSKTFHGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVGYMPQr 82
Cdd:cd03253 6 VTFAYDPGRPV--LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTldslrRAIGVVPQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 83 DLLMPWRTVLQNVILGAEIARKplEQARQRARSLLPLFGLEGFADAYPRQ-------LSGGMRQRAALLRTILMDRPLLL 155
Cdd:cd03253 83 DTVLFNDTIGYNIRYGRPDATD--EEVIEAAKAAQIHDKIMRFPDGYDTIvgerglkLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 156 LDEPFGALDALTRREMQNWLMTVWAqlQPTVLFVTHDVREAAlLSDRVLVLS 207
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIV-NADKIIVLK 209
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-206 |
2.08e-26 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 100.75 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPVQaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVG 77
Cdd:cd03246 1 LEVENVSFRYPGAEPPV-LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDpnelgDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQRDLLMPwRTVLQNVilgaeiarkpleqarqrarsllplfglegfadayprqLSGGMRQRAALLRTILMDRPLLLLD 157
Cdd:cd03246 80 YLPQDDELFS-GSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1279381529 158 EPFGALDALTRRemqnWLMTVWAQLQ---PTVLFVTHdvREAALLS-DRVLVL 206
Cdd:cd03246 122 EPNSHLDVEGER----ALNQAIAALKaagATRIVIAH--RPETLASaDRILVL 168
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-206 |
1.99e-25 |
|
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: 99.61 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 11 TFH-GERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVGYMPQrDL 84
Cdd:cd03251 7 TFRyPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlaslrRQIGLVSQ-DV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 85 LMPWRTVLQNVILGAEIArkPLEQARQRARSLLPLFGLEGFADAYPR-------QLSGGMRQRAALLRTILMDRPLLLLD 157
Cdd:cd03251 86 FLFNDTVAENIAYGRPGA--TREEVEEAARAANAHEFIMELPEGYDTvigergvKLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 158 EPFGALDALTRREMQNWLmtvwAQLQP--TVLFVTH---DVREAallsDRVLVL 206
Cdd:cd03251 164 EATSALDTESERLVQAAL----ERLMKnrTTFVIAHrlsTIENA----DRIVVL 209
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-208 |
3.17e-25 |
|
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: 99.05 E-value: 3.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFH----GERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLN--GALINgqtghV 76
Cdd:COG4778 5 LEVENLSKTFTlhlqGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVD-----L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPWRTVL----Q--NVI--LGA-EIARKPL-------EQARQRARSLLPLFGL-EGFADAYPRQLSGGMRQ 139
Cdd:COG4778 80 AQASPREILALRRRTIgyvsQflRVIprVSAlDVVAEPLlergvdrEEARARARELLARLNLpERLWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 140 RAALLRTILMDRPLLLLDEPFGALDALTRRemqnwlmTVWAQLQP------TVLFVTHD--VREAalLSDRVLVLSA 208
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRA-------VVVELIEEakargtAIIGIFHDeeVREA--VADRVVDVTP 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-214 |
5.97e-25 |
|
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: 97.24 E-value: 5.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTP--DSGEIRLNGALINGQT--GHVGY 78
Cdd:cd03213 9 LTVTVKSSPSKSGKQL--LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSfrKIIGY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 79 MPQRDLLMPWRTVLQNVILGAEIarkpleqarqrarsllplfglegfadaypRQLSGGMRQRAALLRTILMDRPLLLLDE 158
Cdd:cd03213 87 VPQDDILHPTLTVRETLMFAAKL-----------------------------RGLSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 159 PFGALDALTRREMQNWLMTVwAQLQPTVLFVTHDVR-EAALLSDRVLVLSarPGRLI 214
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPSsEIFELFDKLLLLS--QGRVI 191
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-219 |
6.17e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.49 E-value: 6.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHgERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGE---IRLNGALINGQT-----G 74
Cdd:PRK13640 6 VEFKHVSFTYP-DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTvwdirE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 HVGYMPQR-DLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPL 153
Cdd:PRK13640 85 KVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 154 LLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAAlLSDRVLVLSarPGRLIA-DVPI 219
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLD--DGKLLAqGSPV 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-206 |
7.40e-25 |
|
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: 96.61 E-value: 7.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALI----NGQTGHVGY 78
Cdd:cd03247 1 LSINNVSFSY-PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVsdleKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 79 MPQRDLLMPwRTVLQNviLGaeiarkpleqarqrarsllplfglegfadaypRQLSGGMRQRAALLRTILMDRPLLLLDE 158
Cdd:cd03247 80 LNQRPYLFD-TTLRNN--LG--------------------------------RRFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1279381529 159 PFGALDALTRREMqnwLMTVWAQLQ-PTVLFVTHDVREAALLsDRVLVL 206
Cdd:cd03247 125 PTVGLDPITERQL---LSLIFEVLKdKTLIWITHHLTGIEHM-DKILFL 169
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
17-206 |
1.18e-24 |
|
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: 97.75 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 17 PVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH------VGYMPQRDLLMPWRT 90
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriarlgIGYVPEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 91 VLQNVILGAEIARKPLEQARQRAR--SLLPLfgLEGFADAYPRQLSGGMRQRAALLRTiLMDRP-LLLLDEP-------- 159
Cdd:COG0410 95 VEENLLLGAYARRDRAEVRADLERvyELFPR--LKERRRQRAGTLSGGEQQMLAIGRA-LMSRPkLLLLDEPslglapli 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1279381529 160 ----FGALDALTRREMqnwlmtvwaqlqpTVLFVTHDVREAALLSDRVLVL 206
Cdd:COG0410 172 veeiFEIIRRLNREGV-------------TILLVEQNARFALEIADRAYVL 209
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-216 |
1.25e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 98.63 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT--------G 74
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrrkiG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 HVGYMPQRDLLMPwrTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLL 154
Cdd:PRK13642 85 MVFQNPDNQFVGA--TVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 155 LLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAAlLSDRVLVLsaRPGRLIAD 216
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVM--KAGEIIKE 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-213 |
1.30e-24 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 97.25 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERpvQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEI--------RLNGALINGQTG 74
Cdd:PRK10908 2 IRFEHVSKAYLGGR--QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditRLKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 HVGYMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLL 154
Cdd:PRK10908 80 QIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 155 LLDEPFGALD-ALTRREMQnwLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRL 213
Cdd:PRK10908 160 LADEPTGNLDdALSEGILR--LFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSD--GHL 215
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-191 |
1.93e-24 |
|
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: 96.27 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 14 GERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVG----YMPQRDLLMPWR 89
Cdd:TIGR01189 11 GERML--FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHenilYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 90 TVLQNVILGAEIarkpLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDAlTRR 169
Cdd:TIGR01189 89 SALENLHFWAAI----HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK-AGV 163
|
170 180
....*....|....*....|..
gi 1279381529 170 EMQNWLMTVWAQLQPTVLFVTH 191
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-214 |
1.96e-24 |
|
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: 96.91 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 8 VSKTFHGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVGYMPQR 82
Cdd:cd03254 8 VNFSYDEKKPV--LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkslrSMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 83 DLLMPwRTVLQNVILGAEIARKPLEQ-ARQRARSLLPLFGLEGFADAYPRQ----LSGGMRQRAALLRTILMDRPLLLLD 157
Cdd:cd03254 86 TFLFS-GTIMENIRLGRPNATDEEVIeAAKEAGAHDFIMKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 158 EPFGALDALTRREMQNWLMTVwaQLQPTVLFVTH---DVREAallsDRVLVLsaRPGRLI 214
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKL--MKGRTSIIIAHrlsTIKNA----DKILVL--DDGKII 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-216 |
2.08e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.78 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGErpvQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSG----------EIRLNGAL---I 69
Cdd:PRK09984 5 IRVEKLAKTFNQH---QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREGRLardI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 70 NGQTGHVGYMPQRDLLMPWRTVLQNVILGAeIARKPL---------EQARQRARSLLPLFGLEGFADAYPRQLSGGMRQR 140
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIGA-LGSTPFwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279381529 141 AALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLIAD 216
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL--RQGHVFYD 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-216 |
3.77e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 96.69 E-value: 3.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 4 SLQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGqtghvgyMPQRD 83
Cdd:COG4604 3 EIKNVSKRY-GGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT-------TPSRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 84 L------------LMPWRTVLQNVILGaeiaRKPLEQAR---------QRArslLPLFGLEGFADAYPRQLSGGMRQRAA 142
Cdd:COG4604 73 LakrlailrqenhINSRLTVRELVAFG----RFPYSKGRltaedreiiDEA---IAYLDLEDLADRYLDELSGGQRQRAF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 143 LLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLIAD 216
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAM--KDGRVVAQ 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-206 |
4.36e-24 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 95.23 E-value: 4.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 20 ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNgalingqtGHVGYMPQRdllmPW---RTVLQNVI 96
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP--------GSIAYVSQE----PWiqnGTIRENIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 97 LGaeiarKPLEQARQ----RARSLLPLF-----------GLEGFAdayprqLSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:cd03250 88 FG-----KPFDEERYekviKACALEPDLeilpdgdlteiGEKGIN------LSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1279381529 162 ALDALTRRE-MQNWLMTVWAqLQPTVLFVTHDVrEAALLSDRVLVL 206
Cdd:cd03250 157 AVDAHVGRHiFENCILGLLL-NNKTRILVTHQL-QLLPHADQIVVL 200
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-175 |
4.51e-24 |
|
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: 96.07 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 15 ERP-VQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVGYMPQRDLLMPw 88
Cdd:cd03249 12 SRPdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNlrwlrSQIGLVSQEPVLFD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 89 RTVLQNVILGAEIArkPLEQARQRARSLLPLFGLEGFADAY-----PR--QLSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:cd03249 91 GTIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPDGYdtlvgERgsQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170
....*....|....
gi 1279381529 162 ALDALTRREMQNWL 175
Cdd:cd03249 169 ALDAESEKLVQEAL 182
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-219 |
5.33e-24 |
|
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: 96.80 E-value: 5.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 19 QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVGYMPQRDLLMpwrtVLQNVIlG 98
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQL----VFQDSP-S 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 99 A--------EIARKPLE------QARQRAR--SLLPLFGLEG-FADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:TIGR02769 100 AvnprmtvrQIIGEPLRhltsldESEQKARiaELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 162 ALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIADVPI 219
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK--GQIVEECDV 235
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-207 |
6.92e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 96.69 E-value: 6.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 19 QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG--------ALINGQ--TGHVGYMPQRDLLMPw 88
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkSLLEVRktVGIVFQNPDDQLFAP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 89 rTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTR 168
Cdd:PRK13639 95 -TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1279381529 169 REMQNWLMTVWAQlQPTVLFVTHDVREAALLSDRVLVLS 207
Cdd:PRK13639 174 SQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMS 211
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-219 |
1.10e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 95.91 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 19 QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVGYMPQRDLLMpwrtVLQNVIlG 98
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQM----VFQDSI-S 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 99 A--------EIARKPL-------EQARQ-RARSLLPLFGL-EGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:PRK10419 101 AvnprktvrEIIREPLrhllsldKAERLaRASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 162 ALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIADVPI 219
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN--GQIVETQPV 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-214 |
1.29e-23 |
|
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: 99.02 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGeRPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTghvgympQR 82
Cdd:TIGR02203 331 VEFRNVTFRYPG-RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT-------LA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 83 DLLMPWRTVLQNVIL-----GAEIARKPLEQA-RQRARSLLPLFGLEGFADAYPR-----------QLSGGMRQRAALLR 145
Cdd:TIGR02203 403 SLRRQVALVSQDVVLfndtiANNIAYGRTEQAdRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIAR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279381529 146 TILMDRPLLLLDEPFGALDALTRREMQNWLmtvwAQLQP--TVLFVTHDVR--EAAllsDRVLVLSArpGRLI 214
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAAL----ERLMQgrTTLVIAHRLStiEKA---DRIVVMDD--GRIV 546
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-207 |
1.53e-23 |
|
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: 98.66 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 20 ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVGYMPQrDLLMPWRTVLQN 94
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDrhtlrQFINYLPQ-EPYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 95 VILGAEiaRKPLEQARQRARSL---------LPLfGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDA 165
Cdd:TIGR01193 568 LLLGAK--ENVSQDEIWAACEIaeikddienMPL-GYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1279381529 166 LTRREMQNWLMTVWAQlqpTVLFVTHDVrEAALLSDRVLVLS 207
Cdd:TIGR01193 645 ITEKKIVNNLLNLQDK---TIIFVAHRL-SVAKQSDKIIVLD 682
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-214 |
4.46e-23 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 94.13 E-value: 4.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 5 LQRVSKTFHGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLngALINGQTGHVGYMPQ--R 82
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATY--IMRSGAELELYQLSEaeR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 83 DLLM--PWRTVLQN--------VILGAEIARKPLE-------QARQRARSLLPLFGLE-GFADAYPRQLSGGMRQRAALL 144
Cdd:TIGR02323 81 RRLMrtEWGFVHQNprdglrmrVSAGANIGERLMAigarhygNIRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 145 RTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLI 214
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM--QQGRVV 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
12-206 |
7.12e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 94.65 E-value: 7.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 12 FHGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG--ALINGQTGhvgympQRDLLMPWR 89
Cdd:PRK11308 22 FKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdLLKADPEA------QKLLRQKIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 90 TVLQN------------VILGAeiarkPLE--------QARQRARSLLPLFGLEG-FADAYPRQLSGGMRQRAALLRTIL 148
Cdd:PRK11308 96 IVFQNpygslnprkkvgQILEE-----PLLintslsaaERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279381529 149 MDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHD---VREAAllsDRVLVL 206
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDlsvVEHIA---DEVMVM 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-192 |
7.56e-23 |
|
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: 90.59 E-value: 7.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGeRPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLngalinGQTGHVGYMPqr 82
Cdd:cd03221 1 IELENLSKTYGG-KLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW------GSTVKIGYFE-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 83 dllmpwrtvlqnvilgaeiarkpleqarqrarsllplfglegfadayprQLSGGMRQRAALLRTILMDRPLLLLDEPFGA 162
Cdd:cd03221 70 -------------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190
....*....|....*....|....*....|
gi 1279381529 163 LDALTRREMQNWLmtvwAQLQPTVLFVTHD 192
Cdd:cd03221 101 LDLESIEALEEAL----KEYPGTVILVSHD 126
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-206 |
7.65e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.03 E-value: 7.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPV--QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING--------- 71
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStskqkeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 72 ---QTGHVGYMPQRDLLMpwRTVLQNVILGAEIARKPLEQARQRARSLLPLFGL-EGFADAYPRQLSGGMRQRAALLRTI 147
Cdd:PRK13643 82 vrkKVGVVFQFPESQLFE--ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 148 LMDRPLLLLDEPFGALDALTRREMQNWLMTVwAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLL 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-236 |
7.73e-23 |
|
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: 96.68 E-value: 7.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFH-GERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPD----SGEIRLNGALINGqtghvg 77
Cdd:COG4172 7 LSVEDLSVAFGqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLG------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 yMPQRDL------------------LMPWRTVLQNVilgAEIAR--KPL--EQARQRARSLLPLFGL---EGFADAYPRQ 132
Cdd:COG4172 81 -LSERELrrirgnriamifqepmtsLNPLHTIGKQI---AEVLRlhRGLsgAAARARALELLERVGIpdpERRLDAYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 133 LSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHD---VREAAllsDRVLV---- 205
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvVRRFA---DRVAVmrqg 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1279381529 206 ----------LSARPG-----RLIADVPIHLARPRRESDEAFLRLQ 236
Cdd:COG4172 234 eiveqgptaeLFAAPQhpytrKLLAAEPRGDPRPVPPDAPPLLEAR 279
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-165 |
2.31e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 91.02 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 14 GERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHvgymPQRDLLM------- 86
Cdd:PRK13538 12 DERIL--FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE----YHQDLLYlghqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 87 -PWRTVLQNVILGAEIARKPLEQARQRArslLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDA 165
Cdd:PRK13538 86 kTELTALENLRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-192 |
3.12e-22 |
|
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: 94.73 E-value: 3.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 2 YLSLQRVSKTFHGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH-----V 76
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevrrrV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPwRTVLQNVILGA-EIARKPLEQARQRARSLLPLFGLEGFAD----AYPRQLSGGMRQRAALLRTILMDR 151
Cdd:TIGR02868 412 SVCAQDAHLFD-TTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDtvlgEGGARLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1279381529 152 PLLLLDEPFGALDALTRREMqnwLMTVWAQLQ-PTVLFVTHD 192
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADEL---LEDLLAALSgRTVVLITHH 529
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
17-214 |
3.38e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.53 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 17 PVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGAliNGQTGHVGYMPQRDLLMPWRT----VL 92
Cdd:PRK11701 18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR--DGQLRDLYALSEAERRRLLRTewgfVH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 93 QN--------VILGAEIARKPLEQ-----ARQRARSLLPLFGLE---GFADAYPRQLSGGMRQRAALLRTILMDRPLLLL 156
Cdd:PRK11701 96 QHprdglrmqVSAGGNIGERLMAVgarhyGDIRATAGDWLERVEidaARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 157 DEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLI 214
Cdd:PRK11701 176 DEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM--KQGRVV 231
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
26-224 |
5.87e-22 |
|
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: 90.30 E-value: 5.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 26 FVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVGYMPQRDLLMpWR---TVLQNVILGAE-- 100
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQRHEFA-WDfpiSVAHTVMSGRTgh 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 101 --IARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTrREMQNWLMTV 178
Cdd:TIGR03771 80 igWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPT-QELLTELFIE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1279381529 179 WAQLQPTVLFVTHDVREAALLSDRVLVLSarpGRLIAD-VPIHLARP 224
Cdd:TIGR03771 159 LAGAGTAILMTTHDLAQAMATCDRVVLLN---GRVIADgTPQQLQDP 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-206 |
7.65e-22 |
|
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: 93.60 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 16 RPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLtPDSGEIRLNGALINGqtghvgyMPQRDLLmPWR------ 89
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDG-------LSRRALR-PLRrrmqvv 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 90 ------------TVLQNVILGAEIARKPL--EQARQRARSLLPLFGL-EGFADAYPRQLSGGMRQRAALLRTILMDRPLL 154
Cdd:COG4172 368 fqdpfgslsprmTVGQIIAEGLRVHGPGLsaAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 155 LLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:COG4172 448 VLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVM 499
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-213 |
7.94e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.16 E-value: 7.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 14 GERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVGYMPQRDLLMPw 88
Cdd:PRK10247 18 GDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeiyrQQVSYCAQTPTLFG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 89 RTVLQNVILGAEIARKPLEqaRQRARSLLPLFGL-EGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALT 167
Cdd:PRK10247 95 DTVYDNLIFPWQIRNQQPD--PAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1279381529 168 RREMQNWLMTVWAQLQPTVLFVTHDVREAAlLSDRVLVLSARPGRL 213
Cdd:PRK10247 173 KHNVNEIIHRYVREQNIAVLWVTHDKDEIN-HADKVITLQPHAGEM 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-206 |
8.69e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.97 E-value: 8.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPVqALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVG 77
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfeklrKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQR-DLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLL 156
Cdd:PRK13648 87 IVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1279381529 157 DEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREaALLSDRVLVL 206
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSE-AMEADHVIVM 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-218 |
1.17e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.05 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 2 YLSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG----------ALING 71
Cdd:PRK11288 4 YLSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrfasttaALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 72 qtghVGYMPQRDLLMPWRTVLQNVILGAEIARKPL---EQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTIL 148
Cdd:PRK11288 81 ----VAIIYQELHLVPEMTVAENLYLGQLPHKGGIvnrRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279381529 149 MDRPLLLLDEPFGALDAltrREMQNwLMTVWAQLQP---TVLFVTHDVREAALLSDRVLVLsaRPGRLIADVP 218
Cdd:PRK11288 157 RNARVIAFDEPTSSLSA---REIEQ-LFRVIRELRAegrVILYVSHRMEEIFALCDAITVF--KDGRYVATFD 223
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-208 |
1.29e-21 |
|
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: 93.18 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVS-KTFHGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING----QTG-HV 76
Cdd:TIGR01842 317 LSVENVTiVPPGGKKPT--LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwdreTFGkHI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPwRTVLQNVILGAEIA--RKPLEQARQRARSLLPLfgleGFADAYPRQ-------LSGGMRQRAALLRTI 147
Cdd:TIGR01842 395 GYLPQDVELFP-GTVAENIARFGENAdpEKIIEAAKLAGVHELIL----RLPDGYDTVigpggatLSGGQRQRIALARAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 148 LMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQlQPTVLFVTHdvREAAL-LSDRVLVLSA 208
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH--RPSLLgCVDKILVLQD 528
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-216 |
2.95e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.30 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 1 MYLSLQRVSKTFHGERPVQALaevSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG-----H 75
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDL---SLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrqlarR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 76 VGYMPQRDLLMPWRTVLQNVILGaeiaRKPL--------EQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTI 147
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVAYG----RSPWlslwgrlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 148 LMDRPLLLLDEPFGALDALTRREMQNwLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMR-LMRELNTQGKTVVTVLHDLNQASRYCDHLVVLAN--GHVMAQ 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-214 |
4.80e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.14 E-value: 4.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 19 QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALIN----------GQTGHVGYMPQRDLLMPw 88
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkglmklrESVGMVFQDPDNQLFSA- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 89 rTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTR 168
Cdd:PRK13636 99 -SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1279381529 169 REMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLI 214
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKE--GRVI 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-201 |
5.26e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 88.67 E-value: 5.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 14 GERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVGYMPQRDLLMPWR---- 89
Cdd:PRK11831 18 GNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQsgal 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 90 ----TVLQNVILG-AEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALD 164
Cdd:PRK11831 96 ftdmNVFDNVAYPlREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 1279381529 165 ALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSD 201
Cdd:PRK11831 176 PITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIAD 212
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-165 |
6.06e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.24 E-value: 6.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 13 HGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG--ALINGQTGHVGYMPQRDLLMPWRT 90
Cdd:PRK13539 12 RGGRVL--FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdIDDPDVAEACHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 91 VLQNVILGAEIarkpLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDA 165
Cdd:PRK13539 90 VAENLEFWAAF----LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-235 |
8.77e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 88.25 E-value: 8.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 19 QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVGYMPQR-DLLMPWRTVL 92
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENekwvrSKVGLVFQDpDDQVFSSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 93 QNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREmq 172
Cdd:PRK13647 99 DDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET-- 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279381529 173 nwLMTVWAQLQ---PTVLFVTHDVREAALLSDRVLVLSArpGRLIADVPIHLARPRRESDEAFLRL 235
Cdd:PRK13647 177 --LMEILDRLHnqgKTVIVATHDVDLAAEWADQVIVLKE--GRVLAEGDKSLLTDEDIVEQAGLRL 238
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-214 |
9.09e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 90.79 E-value: 9.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 8 VSKTFHGERpvQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVGYMPQR 82
Cdd:PRK13657 340 VSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTraslrRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 83 DLLMPwRTVLQNVILGAEIA-----RKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLD 157
Cdd:PRK13657 418 AGLFN-RSIEDNIRVGRPDAtdeemRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 158 EPFGALDALTRREMQNWLMTVwaQLQPTVLFVTH---DVREAallsDRVLVLSArpGRLI 214
Cdd:PRK13657 497 EATSALDVETEAKVKAALDEL--MKGRTTFIIAHrlsTVRNA----DRILVFDN--GRVV 548
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-206 |
1.41e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.84 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 20 ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGA---------LINGQTGHVGYMPQRDLLMPwrT 90
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdtsdeenlwDIRNKAGMVFQNPDNQIVAT--I 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 91 VLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRRE 170
Cdd:PRK13633 103 VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRE 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 1279381529 171 MQNWLMTVWAQLQPTVLFVTHDVREAAlLSDRVLVL 206
Cdd:PRK13633 183 VVNTIKELNKKYGITIILITHYMEEAV-EADRIIVM 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-215 |
1.87e-20 |
|
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: 89.81 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHG-ERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALIN-------GQtg 74
Cdd:COG4618 331 LSVENLTVVPPGsKRPI--LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwdreelGR-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 HVGYMPQRDLLMPwRTVLQNvilgaeIARKP------LEQARQRAR-----SLLPLfGLEGFADAYPRQLSGGMRQRAAL 143
Cdd:COG4618 407 HIGYLPQDVELFD-GTIAEN------IARFGdadpekVVAAAKLAGvhemiLRLPD-GYDTRIGEGGARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 144 LRTILMDRPLLLLDEPFGALD-----ALTRremqnwLMTVWAQLQPTVLFVTHdvREAAL-LSDRVLVLsaRPGRLIA 215
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDdegeaALAA------AIRALKARGATVVVITH--RPSLLaAVDKLLVL--RDGRVQA 546
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3-215 |
2.88e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.10 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPVQalaEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH------V 76
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVE---DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHararrgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPWRTVLQNVILGAEIaRKPL--EQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLL 154
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQI-RDDLsaEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 155 LLDEPFGALDALTRREMQNwlmtVWAQLQPT---VLFVTHDVREAALLSDRVLVLSArpGRLIA 215
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKR----IIEHLRDSglgVLITDHNVRETLAVCERAYIVSQ--GHLIA 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-211 |
2.93e-20 |
|
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: 86.31 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 28 IEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIrlngaLINGQTghVGYMPQ----------RDLLMpwrtvlqnvil 97
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-----EIELDT--VSYKPQyikadyegtvRDLLS----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 98 gaEIARKPLEQARQRARSLLPLfGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMT 177
Cdd:cd03237 84 --SITKDFYTHPYFKTEIAKPL-QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180 190
....*....|....*....|....*....|....
gi 1279381529 178 VWAQLQPTVLFVTHDVREAALLSDRVLVLSARPG 211
Cdd:cd03237 161 FAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-191 |
3.92e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.73 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHgERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVG 77
Cdd:PRK11160 339 LTLNNVSFTYP-DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSeaalrQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQR-DLLMpwRTVLQNVILGAEIAR-KPLEQARQRArsllplfGLEGFADAYP----------RQLSGGMRQRAALLR 145
Cdd:PRK11160 418 VVSQRvHLFS--ATLRDNLLLAAPNASdEALIEVLQQV-------GLEKLLEDDKglnawlgeggRQLSGGEQRRLGIAR 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1279381529 146 TILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAqlQPTVLFVTH 191
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH 532
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
15-207 |
5.73e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.83 E-value: 5.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 15 ERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALIN---GQTGHVGYMPQRDLLMPWR-- 89
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGdkkNNHELITNPYSKKIKNFKElr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 90 -----------------TVLQNVILGAEIARKPLEQARQRARSLLPLFGL-EGFADAYPRQLSGGMRQRAALLRTILMDR 151
Cdd:PRK13631 116 rrvsmvfqfpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1279381529 152 PLLLLDEPFGALDALTRREMQNWLMTVWAQlQPTVLFVTHDVREAALLSDRVLVLS 207
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMD 250
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-171 |
6.28e-20 |
|
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: 86.06 E-value: 6.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 17 PVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRlngalingQTGHVGYMPQRDLLMPwRTVLQNVI 96
Cdd:cd03291 51 PV--LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--------HSGRISFSSQFSWIMP-GTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 97 LGaeiarkpLEQARQRARSLLPLFGLEGFADAYPRQ-----------LSGGMRQRAALLRTILMDRPLLLLDEPFGALDA 165
Cdd:cd03291 120 FG-------VSYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
....*.
gi 1279381529 166 LTRREM 171
Cdd:cd03291 193 FTEKEI 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-213 |
7.92e-20 |
|
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: 88.15 E-value: 7.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 16 RPvqALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHV----GYMPQRDLLMPWRTV 91
Cdd:TIGR01257 943 RP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVrqslGMCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 92 LQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREM 171
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1279381529 172 qnWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRL 213
Cdd:TIGR01257 1101 --WDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQ--GRL 1138
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-213 |
8.11e-20 |
|
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: 83.64 E-value: 8.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 20 ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH------VGYMP---QRDLLMPWRT 90
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdairagIAYVPedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 91 VLQNVILgaeiarkpleqarqrarsllplfglegfadayPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRRE 170
Cdd:cd03215 95 VAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1279381529 171 MQNWLMTVwAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRL 213
Cdd:cd03215 143 IYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYE--GRI 182
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-215 |
9.97e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.62 E-value: 9.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 18 VQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH-----VGYM---PQRDLLMPwr 89
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRevrkfVGLVfqnPDDQIFSP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 90 TVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRR 169
Cdd:PRK13652 95 TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVK 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1279381529 170 EMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIA 215
Cdd:PRK13652 175 ELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDK--GRIVA 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-206 |
1.11e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.41 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT---GH---V 76
Cdd:PRK15439 12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHqlgI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPWRTVLQNVILGaeIARKPLEQARQRArsLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLL 156
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENILFG--LPKRQASMQKMKQ--LLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 157 DEPFGaldALTRREMQNWLMTVWAQLQPTV--LFVTHDVREAALLSDRVLVL 206
Cdd:PRK15439 165 DEPTA---SLTPAETERLFSRIRELLAQGVgiVFISHKLPEIRQLADRISVM 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-207 |
2.17e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.05 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 1 MYLSLQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG-----H 75
Cdd:PRK09536 2 PMIDVSDLSVEF-GDTTV--LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAraasrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 76 VGYMPQRDLLMPWRTVLQNVILG-----------AEIARKPLEQARQRArsllplfGLEGFADAYPRQLSGGMRQRAALL 144
Cdd:PRK09536 79 VASVPQDTSLSFEFDVRQVVEMGrtphrsrfdtwTETDRAAVERAMERT-------GVAQFADRPVTSLSGGERQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279381529 145 RTILMDRPLLLLDEPFGALD--------ALTRRemqnwlmtvWAQLQPTVLFVTHDVREAALLSDRVLVLS 207
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDinhqvrtlELVRR---------LVDDGKTAVAAIHDLDLAARYCDELVLLA 213
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-224 |
3.32e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.68 E-value: 3.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG-----HVGYMPQRDLLMPWRTVLQNV 95
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSkafarKVAYLPQQLPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 96 ILGaeiaRKPLEQA--------RQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALT 167
Cdd:PRK10575 107 AIG----RYPWHGAlgrfgaadREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 168 RREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLIAD-VPIHLARP 224
Cdd:PRK10575 183 QVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVAL--RGGEMIAQgTPAELMRG 238
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-206 |
6.24e-19 |
|
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: 82.53 E-value: 6.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPVqALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG---ALINGQT--GHVG 77
Cdd:cd03252 1 ITFEHVRFRYKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlALADPAWlrRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQRDLLMPwRTVLQNVILGAEIArkPLEQARQRAR--------SLLPLfGLEGFADAYPRQLSGGMRQRAALLRTILM 149
Cdd:cd03252 80 VVLQENVLFN-RSIRDNIALADPGM--SMERVIEAAKlagahdfiSELPE-GYDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 150 DRPLLLLDEPFGALDALTRREMQNWLMTVWAqlQPTVLFVTHDVrEAALLSDRVLVL 206
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRL-STVKNADRIIVM 209
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-210 |
6.44e-19 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 81.82 E-value: 6.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG--ALINGQTGHVGYMPQRDLLMPWRTVLQNV-IL 97
Cdd:PRK13543 27 FGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktATRGDRSRFMAYLGHLPGLKADLSTLENLhFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 98 GAEIARKPleqaRQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDaLTRREMQNWLMT 177
Cdd:PRK13543 107 CGLHGRRA----KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD-LEGITLVNRMIS 181
|
170 180 190
....*....|....*....|....*....|...
gi 1279381529 178 VWAQLQPTVLFVTHDVREAALLSDRVLVLSARP 210
Cdd:PRK13543 182 AHLRGGGAALVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-165 |
6.59e-19 |
|
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: 81.77 E-value: 6.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 14 GERPVQALAE-VSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVG----YMPQRDLLMPW 88
Cdd:cd03231 8 CERDGRALFSgLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIArgllYLGHAPGIKTT 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 89 RTVLQNV-ILGAEIARKPLEQARQRArsllplfGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDA 165
Cdd:cd03231 88 LSVLENLrFWHADHSDEQVEEALARV-------GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-214 |
8.45e-19 |
|
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: 84.87 E-value: 8.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVG 77
Cdd:COG5265 358 VRFENVSFGYDPERPI--LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTqaslrAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQrDllmpwrTVLQNVILGAEIA-------RKPLEQARQRARsllplfgLEGFADAYPRQ-----------LSGGMRQ 139
Cdd:COG5265 436 IVPQ-D------TVLFNDTIAYNIAygrpdasEEEVEAAARAAQ-------IHDFIESLPDGydtrvgerglkLSGGEKQ 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 140 RAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVwAQLQpTVLFVTH---DVREAallsDRVLVLSArpGRLI 214
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGR-TTLVIAHrlsTIVDA----DEILVLEA--GRIV 571
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
3-165 |
8.63e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.10 E-value: 8.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPV-QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPD---SGEIRLNGALINGQTGHV-- 76
Cdd:TIGR00955 22 QLVSRLRGCFCRERPRkHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAis 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPWRTVLQNVILGAEI---ARKPLEQARQRARSLLPLFGLEGFAD------AYPRQLSGGMRQRAALLRTI 147
Cdd:TIGR00955 102 AYVQQDDLFIPTLTVREHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASEL 181
|
170
....*....|....*...
gi 1279381529 148 LMDRPLLLLDEPFGALDA 165
Cdd:TIGR00955 182 LTDPPLLFCDEPTSGLDS 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-175 |
1.11e-18 |
|
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: 84.60 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 8 VSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLngalinGQTGHVGYMPQ-RDLLM 86
Cdd:TIGR03719 328 LTKAF-GDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------GETVKLAYVDQsRDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 87 PWRTVLQNVILGAEIARkpLEQARQRARSLLPLFGLEGfADAYPR--QLSGGMRQRAALLRTILMDRPLLLLDEPFGALD 164
Cdd:TIGR03719 399 PNKTVWEEISGGLDIIK--LGKREIPSRAYVGRFNFKG-SDQQKKvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
170
....*....|.
gi 1279381529 165 ALTRREMQNWL 175
Cdd:TIGR03719 476 VETLRALEEAL 486
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-167 |
1.16e-18 |
|
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: 81.55 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 18 VQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPD---SGEIRLNGALINGQT--GHVGYMPQRDLLMPWRTVL 92
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQfqKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 93 QNVILGAEIA-RKPLEQARQRAR---SLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALT 167
Cdd:cd03234 100 ETLTYTAILRlPRKSSDAIRKKRvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-242 |
1.20e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.05 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 24 VSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPdsGEIRLNGA-LINGQTGHVGYMPQRDLlmpwRTVLQN-------V 95
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRvLLDGKPVAPCALRGRKI----ATIMQNprsafnpL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 96 ILGAEIARKPLEQ-----ARQRARSLLPLFGLEG---FADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALT 167
Cdd:PRK10418 96 HTMHTHARETCLAlgkpaDDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 168 RREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIADVPIH--LARPRRESDEAFLRLQAQLLGS 242
Cdd:PRK10418 176 QARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSH--GRIVEQGDVEtlFNAPKHAVTRSLVSAHLALYGM 250
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-206 |
1.29e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 82.75 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 5 LQRVSKTFHGERPVQ--ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING----------- 71
Cdd:PRK13645 9 LDNVSYTYAKKTPFEfkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikevkrl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 72 --QTGHVGYMPQRDLLMpwRTVLQNVILGAEIARKPLEQARQRARSLLPLFGL-EGFADAYPRQLSGGMRQRAALLRTIL 148
Cdd:PRK13645 89 rkEIGLVFQFPEYQLFQ--ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 149 MDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-192 |
1.68e-18 |
|
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: 83.83 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 4 SLQRVSKTFHGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLngalingQTG-HVGYMPQR 82
Cdd:TIGR03719 6 TMNRVSKVVPPKKEI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-------QPGiKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 83 DLLMPWRTVLQNVILGAEIARKPL----------------------EQA---------------RQRARSLLPLFGLEGf 125
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGVAEIKDALdrfneisakyaepdadfdklaaEQAelqeiidaadawdldSQLEIAMDALRCPPW- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 126 aDAYPRQLSGGMRQRAALLRtILMDRP-LLLLDEPFGALDAltrrEMQNWLMTVWAQLQPTVLFVTHD 192
Cdd:TIGR03719 156 -DADVTKLSGGERRRVALCR-LLLSKPdMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHD 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-171 |
2.16e-18 |
|
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: 84.19 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 17 PVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRlngalingQTGHVGYMPQRDLLMPwRTVLQNVI 96
Cdd:TIGR01271 440 PV--LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--------HSGRISFSPQTSWIMP-GTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 97 LGaeiarkpLEQARQRARSLLPLFGLEGFADAYPRQ-----------LSGGMRQRAALLRTILMDRPLLLLDEPFGALDA 165
Cdd:TIGR01271 509 FG-------LSYDEYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
....*.
gi 1279381529 166 LTRREM 171
Cdd:TIGR01271 582 VTEKEI 587
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-217 |
3.01e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.30 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 2 YLSLQRVSKTFHgerPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALIN-------GQTG 74
Cdd:PRK09700 5 YISMAGIGKSFG---PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNkldhklaAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 hVGYMPQRDLLMPWRTVLQNVILGAEIARKPL-------EQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTI 147
Cdd:PRK09700 82 -IGIIYQELSVIDELTVLENLYIGRHLTKKVCgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279381529 148 LMDRPLLLLDEPfgaLDALTRREMqNWLMTVWAQLQ---PTVLFVTHDVREAALLSDRVLVL---SARPGRLIADV 217
Cdd:PRK09700 161 MLDAKVIIMDEP---TSSLTNKEV-DYLFLIMNQLRkegTAIVYISHKLAEIRRICDRYTVMkdgSSVCSGMVSDV 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-206 |
8.77e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.01 E-value: 8.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 13 HGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG---ALINGQTGHVGYMPQRDL----- 84
Cdd:PRK10619 15 YGEHEV--LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtiNLVRDKDGQLKVADKNQLrllrt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 85 ----------LMPWRTVLQNV------ILGAEIArkpleQARQRARSLLPLFGLEGFA-DAYPRQLSGGMRQRAALLRTI 147
Cdd:PRK10619 93 rltmvfqhfnLWSHMTVLENVmeapiqVLGLSKQ-----EARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 148 LMDRPLLLLDEPFGALDALTRREMQNwLMTVWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLR-IMQQLAEEGKTMVVVTHEMGFARHVSSHVIFL 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-220 |
9.67e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.61 E-value: 9.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSktFHGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH------V 76
Cdd:COG3845 258 LEVENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRerrrlgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMP---QRDLLMPWRTVLQNVILG----AEIARKPL---EQARQRARSLlplfgLEGF------ADAYPRQLSGGMRQR 140
Cdd:COG3845 336 AYIPedrLGRGLVPDMSVAENLILGryrrPPFSRGGFldrKAIRAFAEEL-----IEEFdvrtpgPDTPARSLSGGNQQK 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 141 AALLRTILMDRPLLLLDEP-----FGALDAltrremqnwlmtVWAQLQP------TVLFVTHDVREAALLSDRVLVLSAr 209
Cdd:COG3845 411 VILARELSRDPKLLIAAQPtrgldVGAIEF------------IHQRLLElrdagaAVLLISEDLDEILALSDRIAVMYE- 477
|
250
....*....|.
gi 1279381529 210 pGRLIADVPIH 220
Cdd:COG3845 478 -GRIVGEVPAA 487
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
8-191 |
1.22e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.60 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 8 VSKTFHG-ERPvqALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----GHVGYMPQ 81
Cdd:PRK11176 347 VTFTYPGkEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTlaslrNQVALVSQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 82 RDLLMPwRTVLQNVILGAE--IARKPLEQARQRARSLLPLFGLEGFADAYPRQ----LSGGMRQRAALLRTILMDRPLLL 155
Cdd:PRK11176 425 NVHLFN-DTIANNIAYARTeqYSREQIEEAARMAYAMDFINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILI 503
|
170 180 190
....*....|....*....|....*....|....*...
gi 1279381529 156 LDEPFGALDALTRREMQNWLmtvwAQLQP--TVLFVTH 191
Cdd:PRK11176 504 LDEATSALDTESERAIQAAL----DELQKnrTSLVIAH 537
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-206 |
1.75e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.04 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 24 VSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLtPDSGEIRLNGALIN--------GQTGHVGYMPQrdllMPWRTVLQNV 95
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELReldpeswrKHLSWVGQNPQ----LPHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 96 ILG-AEIARKPLEQARQRAR-----SLLPLfGLEgfadaYPRQ-----LSGGMRQRAALLRTILMDRPLLLLDEPFGALD 164
Cdd:PRK11174 444 LLGnPDASDEQLQQALENAWvseflPLLPQ-GLD-----TPIGdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1279381529 165 ALTRREMQNWLMTVWAQLqpTVLFVTHdvREAALLS-DRVLVL 206
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQ--TTLMVTH--QLEDLAQwDQIWVM 556
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-219 |
2.15e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.88 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPvqALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG------ALINGQTGHV 76
Cdd:PRK13644 2 IRLENVSYSYPDGTP--ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQR-DLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLL 155
Cdd:PRK13644 80 GIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279381529 156 LDEPFGALDALTRREMQNWLMTVWAQLQpTVLFVTHDVREAAlLSDRVLV-------LSARPGRLIADVPI 219
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEELH-DADRIIVmdrgkivLEGEPENVLSDVSL 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-159 |
2.50e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.94 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 24 VSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING---QT-GHVGYMPQRDLLMPWRTVLQNVILGA 99
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAgdiATrRRVGYMSQAFSLYGELTVRQNLELHA 364
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 100 EIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEP 159
Cdd:NF033858 365 RLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-206 |
3.96e-17 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 77.51 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 6 QRVSKTFHGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALIN--------GQTGHVG 77
Cdd:cd03248 15 QNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqyehkylhSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQrdllMPWRTVLQNVILGaeIARKPLE-----QARQRARSLLPLFGLEGFADAYPR--QLSGGMRQRAALLRTILMD 150
Cdd:cd03248 95 QEPV----LFARSLQDNIAYG--LQSCSFEcvkeaAQKAHAHSFISELASGYDTEVGEKgsQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 151 RPLLLLDEPFGALDALTRREMQNwLMTVWAQLQpTVLFVTHDVR--EAAllsDRVLVL 206
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQ-ALYDWPERR-TVLVIAHRLStvERA---DQILVL 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-192 |
4.70e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 79.78 E-value: 4.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 4 SLQRVSKTFHGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLngalingQTGH-VGYMPQR 82
Cdd:PRK11819 8 TMNRVSKVVPPKKQI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP-------APGIkVGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 83 DLLMPWRTVLQNVILG-AEIARK-------------PL--------EQAR------------------QRARSL-LPLfg 121
Cdd:PRK11819 79 PQLDPEKTVRENVEEGvAEVKAAldrfneiyaayaePDadfdalaaEQGElqeiidaadawdldsqleIAMDALrCPP-- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 122 legfADAYPRQLSGGMRQRAALLRtILMDRP-LLLLDEPFGALDAltrrEMQNWLMTVWAQLQPTVLFVTHD 192
Cdd:PRK11819 157 ----WDAKVTKLSGGERRRVALCR-LLLEKPdMLLLDEPTNHLDA----ESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-206 |
1.20e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALingqtgHVGYMPQR 82
Cdd:PRK09544 5 VSLENVSVSF-GQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL------RIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 83 ---DLLMPWrTVLQNVILGAEIARKPLEQARQRARSllplfglEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEP 159
Cdd:PRK09544 76 lylDTTLPL-TVNRFLRLRPGTKKEDILPALKRVQA-------GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1279381529 160 FGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK09544 148 TQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-206 |
1.52e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.44 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 19 QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVGYMPQRDLLM----------PW 88
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMifqdplaslnPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 89 RTVlqnvilgAEIARKPL---------EQARQRARSLLPLFGL-EGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDE 158
Cdd:PRK15079 115 MTI-------GEIIAEPLrtyhpklsrQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1279381529 159 PFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-219 |
1.79e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.05 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLtPD---SGEIRLNGALINGQ----TGH 75
Cdd:PRK13549 6 LEMKNITKTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASnirdTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 76 VG--YMPQRDLLMPWRTVLQNVILGAEIARKPL---EQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMD 150
Cdd:PRK13549 82 AGiaIIHQELALVKELSVLENIFLGNEITPGGImdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 151 RPLLLLDEPFGaldALTRREMQNwLMTVWAQLQP---TVLFVTHDVREAALLSDRVLVLsaRPGRLIADVPI 219
Cdd:PRK13549 162 ARLLILDEPTA---SLTESETAV-LLDIIRDLKAhgiACIYISHKLNEVKAISDTICVI--RDGRHIGTRPA 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-216 |
2.40e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.80 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 20 ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH-VGYMP-----QRDLLMPWRTVLQ 93
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHqIARMGvvrtfQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 94 NV-----------ILGAEIA----RKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDE 158
Cdd:PRK11300 100 NLlvaqhqqlktgLFSGLLKtpafRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 159 PFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQ--GTPLAN 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-167 |
2.42e-16 |
|
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: 77.54 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGL--LTPDSGEIRLNGALIN---------- 70
Cdd:TIGR03269 1 IEVKNLTKKFDG---KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEkcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 71 -GQ---------------------------TGHVGYMPQRDL-LMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFG 121
Cdd:TIGR03269 78 vGEpcpvcggtlepeevdfwnlsdklrrriRKRIAIMLQRTFaLYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1279381529 122 LEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALT 167
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQT 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-218 |
6.03e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.60 E-value: 6.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 24 VSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-------GhVGYMP---QRDLLMPWRTVLQ 93
Cdd:COG1129 271 VSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSprdairaG-IAYVPedrKGEGLVLDLSIRE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 94 NVILGA--EIARKPL---EQARQRARSLLPLFGLE-GFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPF-----GA 162
Cdd:COG1129 350 NITLASldRLSRGGLldrRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTrgidvGA 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279381529 163 -------LDALTRREMqnwlmtvwaqlqpTVLFVTHDVREAALLSDRVLVLSArpGRLIADVP 218
Cdd:COG1129 430 kaeiyrlIRELAAEGK-------------AVIVISSELPELLGLSDRILVMRE--GRIVGELD 477
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-214 |
7.33e-16 |
|
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: 73.68 E-value: 7.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 20 ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINgQTG------HVGYMPQRDLLMPwRTVLQ 93
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS-KIGlhdlrsRISIIPQDPVLFS-GTIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 94 NV-ILG----AEIARKpLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTR 168
Cdd:cd03244 97 NLdPFGeysdEELWQA-LERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1279381529 169 REMQNWLMTVWAqlQPTVLFVTHDVrEAALLSDRVLVLSArpGRLI 214
Cdd:cd03244 176 ALIQKTIREAFK--DCTVLTIAHRL-DTIIDSDRILVLDK--GRVV 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-175 |
7.71e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 76.31 E-value: 7.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 8 VSKTFhGERpvqALAE-VSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLngalinGQTGHVGYMPQ-RDLL 85
Cdd:PRK11819 330 LSKSF-GDR---LLIDdLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------GETVKLAYVDQsRDAL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 86 MPWRTVLQNVILGAEIARkpLEQARQRARSLLPLFGLEGfADAYPR--QLSGGMRQRAALLRTILMDRPLLLLDEPFGAL 163
Cdd:PRK11819 400 DPNKTVWEEISGGLDIIK--VGNREIPSRAYVGRFNFKG-GDQQKKvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDL 476
|
170
....*....|..
gi 1279381529 164 DALTRREMQNWL 175
Cdd:PRK11819 477 DVETLRALEEAL 488
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
3-225 |
1.16e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 75.60 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGE--RPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTghvgYMP 80
Cdd:COG4615 328 LELRGVTYRYPGEdgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN----REA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 81 QRDLLmpwRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEG--------FADaypRQLSGGMRQRAALLRTILMDRP 152
Cdd:COG4615 404 YRQLF---SAVFSDFHLFDRLLGLDGEADPARARELLERLELDHkvsvedgrFST---TDLSQGQRKRLALLVALLEDRP 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 153 LLLLDEpfgaldaltrremqnwlmtvWA-------------QLQP-------TVLFVTHDVR--EAAllsDRVLVLSArp 210
Cdd:COG4615 478 ILVFDE--------------------WAadqdpefrrvfytELLPelkargkTVIAISHDDRyfDLA---DRVLKMDY-- 532
|
250
....*....|....*
gi 1279381529 211 GRLIADVPIHLARPR 225
Cdd:COG4615 533 GKLVELTGPAALAAS 547
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-167 |
2.69e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.90 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG----HVGYMPQRDLLMPWRTVLQNVI 96
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCtyqkQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279381529 97 LGAEIARKPLEqarqrARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALT 167
Cdd:PRK13540 97 YDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-208 |
2.77e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.90 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFH------GERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALIngQTGHV 76
Cdd:PRK15112 5 LEVRNLSKTFRyrtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL--HFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQR---------DLLMPWRTVLQ--------NVILGAEIARKPLEQArQRARSLLPlfgleGFADAYPRQLSGGMRQ 139
Cdd:PRK15112 83 SYRSQRirmifqdpsTSLNPRQRISQildfplrlNTDLEPEQREKQIIET-LRQVGLLP-----DHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 140 RAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSA 208
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-206 |
4.13e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.37 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 16 RP-VQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINgQTGH------VGYMPQRDLLMPw 88
Cdd:TIGR00958 491 RPdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV-QYDHhylhrqVALVGQEPVLFS- 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 89 RTVLQNVILGaeIARKPLEQARQRARSLLPLFGLEGFADAYP-------RQLSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:TIGR00958 569 GSVRENIAYG--LTDTPDEEIMAAAKAANAHDFIMEFPNGYDtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1279381529 162 ALDALTRREMQNWLmtvwAQLQPTVLFVTHD---VREAallsDRVLVL 206
Cdd:TIGR00958 647 ALDAECEQLLQESR----SRASRTVLLIAHRlstVERA----DQILVL 686
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-206 |
4.39e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.12 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 16 RPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVGYMPQRDLLM----PWRTV 91
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFifqdPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 92 LQNVILGAEIArKPL--------EQARQRARSLLPLFGLE-GFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGA 162
Cdd:PRK10261 415 DPRQTVGDSIM-EPLrvhgllpgKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1279381529 163 LDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVM 537
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-208 |
4.91e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 73.24 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGER-PVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLT-PdsGEIRLNGALINGqtghvgymp 80
Cdd:PRK11022 4 LNVDKLSVHFGDESaPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVMAEKLEFNG--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 81 qRDLLMPWRTVLQNVIlGAEIA---RKPL-------------------------EQARQRARSLLPLFGL---EGFADAY 129
Cdd:PRK11022 73 -QDLQRISEKERRNLV-GAEVAmifQDPMtslnpcytvgfqimeaikvhqggnkKTRRQRAIDLLNQVGIpdpASRLDVY 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 130 PRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSA 208
Cdd:PRK11022 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYA 229
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-207 |
5.17e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.76 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDS--GEIRLNGALINGQT-GHVGYMPQRDLLMPWRTVLQNVIL 97
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQIlKRTGFVTQDDILYPHLTVRETLVF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 98 GAeIARKPLEQARQR----ARSLLPLFGLEG-----FADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTR 168
Cdd:PLN03211 164 CS-LLRLPKSLTKQEkilvAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1279381529 169 REMQNWLMTVwAQLQPTVLFVTHDVREAAL-LSDRVLVLS 207
Cdd:PLN03211 243 YRLVLTLGSL-AQKGKTIVTSMHQPSSRVYqMFDSVLVLS 281
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-218 |
6.91e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.05 E-value: 6.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT-----------GHVGYMPQRDLLMPwR 89
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSifnyrdvlefrRRVGMLFQRPNPFP-M 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 90 TVLQNVILGAEIAR-KPLEQARQRARSLLPLFGL-----EGFADAyPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGAL 163
Cdd:PRK14271 116 SIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwdavkDRLSDS-PFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 164 DALTRREMQNWLMTVWAQLqpTVLFVTHDVREAALLSDRVLVLSarPGRLIADVP 218
Cdd:PRK14271 195 DPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFF--DGRLVEEGP 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-206 |
7.94e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 7.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERP-VQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALI---NGQTGHVGY 78
Cdd:PRK10261 13 LAVENLNIAFMQEQQkIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrSRQVIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 79 MPQR--------DLLMPWR---TVLQNVI-LGAEIARK-------PLEQARQRARSLLPLFGL---EGFADAYPRQLSGG 136
Cdd:PRK10261 93 QSAAqmrhvrgaDMAMIFQepmTSLNPVFtVGEQIAESirlhqgaSREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGG 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 137 MRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-218 |
9.87e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.94 E-value: 9.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDS--GEIRLNGALINGQT------G 74
Cdd:TIGR02633 2 LEMKGIVKTFGG---VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNirdterA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 75 HVGYMPQRDLLMPWRTVLQNVILGAEI----ARKPLEQARQRARSLLPLFGLEGFADAYP-RQLSGGMRQRAALLRTILM 149
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 150 DRPLLLLDEPFGaldALTRREMQNwLMTVWAQLQP---TVLFVTHDVREAALLSDRVLVLsaRPGRLIADVP 218
Cdd:TIGR02633 159 QARLLILDEPSS---SLTEKETEI-LLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVI--RDGQHVATKD 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-214 |
2.28e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 70.45 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 12 FHGERpvQALAEVSFVIEQGEFVSLIGQSGSGKSTL--C-N----LIAGLLTpdSGEIRLNGALINGQTG-------HVG 77
Cdd:COG1117 20 YYGDK--QALKDINLDIPENKVTALIGPSGCGKSTLlrClNrmndLIPGARV--EGEILLDGEDIYDPDVdvvelrrRVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 78 YMPQRDLLMPWrTVLQNVILG------------AEIARKPLEQA----------RQRARSllplfglegfadayprqLSG 135
Cdd:COG1117 96 MVFQKPNPFPK-SIYDNVAYGlrlhgikskselDEIVEESLRKAalwdevkdrlKKSALG-----------------LSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 136 GMRQRAALLRTILMDRPLLLLDEPFGALDAL-TRR--EmqnwLMtvwAQL--QPTVLFVTHDVREAALLSDRVLVLSArp 210
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPIsTAKieE----LI---LELkkDYTIVIVTHNMQQAARVSDYTAFFYL-- 228
|
....
gi 1279381529 211 GRLI 214
Cdd:COG1117 229 GELV 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-212 |
3.13e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.38 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 28 IEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIrlngalinGQTGHVGYMPQ----------RDLLMPWRTVLQNVIL 97
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPELKISYKPQyikpdydgtvEDLLRSITDDLGSSYY 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 98 GAEIArKPLeqarqrarsllplfGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDA--------LTRR 169
Cdd:PRK13409 434 KSEII-KPL--------------QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlavakAIRR 498
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1279381529 170 EMQNwlmtvwaqLQPTVLFVTHDVREAALLSDRVLVLSARPGR 212
Cdd:PRK13409 499 IAEE--------REATALVVDHDIYMIDYISDRLMVFEGEPGK 533
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-212 |
4.68e-14 |
|
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: 70.97 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 28 IEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIrlNGALIngqtghVGYMPQR---DLLMPWRTVLQNVI-------- 96
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLK------ISYKPQYispDYDGTVEEFLRSANtddfgssy 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 97 LGAEIARKpleqarqrarsllplFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLM 176
Cdd:COG1245 435 YKTEIIKP---------------LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170 180 190
....*....|....*....|....*....|....*.
gi 1279381529 177 TVWAQLQPTVLFVTHDVREAALLSDRVLVLSARPGR 212
Cdd:COG1245 500 RFAENRGKTAMVVDHDIYLIDYISDRLMVFEGEPGV 535
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-202 |
4.81e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.42 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 19 QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLI--AGLLTPD---SGEIRLNGALINGQTG-------HVGYMPQRDLLM 86
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTdtvdlrkEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 87 PWrTVLQNVILGAEIA----RKPLEQARQRArsllpLFGLEGFADAYPR------QLSGGMRQRAALLRTILMDRPLLLL 156
Cdd:PRK14239 99 PM-SIYENVVYGLRLKgikdKQVLDEAVEKS-----LKGASIWDEVKDRlhdsalGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1279381529 157 DEPFGALDALTRREMQNWLMTVwaQLQPTVLFVTHDVREAALLSDR 202
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDR 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-206 |
6.97e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 6.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 19 QALAEVSFVIEQGEFVSLIGQSGSGKSTlcnliAGL----LTPDSGEIRLNGALINgQTGHVGYMPQR-----------D 83
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKST-----TGLallrLINSQGEIWFDGQPLH-NLNRRQLLPVRhriqvvfqdpnS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 84 LLMPWRTVLQNVILGAEIARKPL--EQARQRARSLLPLFGLEGFA-DAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPF 160
Cdd:PRK15134 374 SLNPRLNVLQIIEEGLRVHQPTLsaAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1279381529 161 GALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVL 499
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-212 |
8.94e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.37 E-value: 8.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 18 VQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPD---SGEIRLNGALINGqtghvgyMPQRDL---------- 84
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILN-------LPEKELnklraeqism 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 85 --------LMPWRTV---LQNVIL---------GAEIARKPLE-----QARQRARsllplfglegfadAYPRQLSGGMRQ 139
Cdd:PRK09473 102 ifqdpmtsLNPYMRVgeqLMEVLMlhkgmskaeAFEESVRMLDavkmpEARKRMK-------------MYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 140 RaALLRTILMDRP-LLLLDEPFGALDAltrrEMQNWLMTVWAQLQ----PTVLFVTHDVREAALLSDRVLVLSArpGR 212
Cdd:PRK09473 169 R-VMIAMALLCRPkLLIADEPTTALDV----TVQAQIMTLLNELKrefnTAIIMITHDLGVVAGICDKVLVMYA--GR 239
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-215 |
1.04e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLtPDSGEIRLNGALI-----NGQTGHVGYMPQRD---LLMPwrtVL 92
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLeawsaAELARHRAYLSQQQtppFAMP---VF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 93 QNVILgAEIARKPLEQARQRARSLLPLFGLEgfaDAYPR---QLSGGMRQRAALLRTILMDRP-------LLLLDEPFGA 162
Cdd:PRK03695 88 QYLTL-HQPDKTRTEAVASALNEVAEALGLD---DKLGRsvnQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1279381529 163 LD-----ALTRremqnwLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIA 215
Cdd:PRK03695 164 LDvaqqaALDR------LLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQ--GKLLA 213
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-192 |
1.26e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.62 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVskTFHGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT--------- 73
Cdd:PRK10522 323 LELRNV--TFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQpedyrklfs 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 74 -------------GHVGYMPQRDLLMPWRTVLQnvilgaeIARKpLEQARQRARSLlplfglegfadayprQLSGGMRQR 140
Cdd:PRK10522 401 avftdfhlfdqllGPEGKPANPALVEKWLERLK-------MAHK-LELEDGRISNL---------------KLSKGQKKR 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 141 AALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHD 192
Cdd:PRK10522 458 LALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-206 |
1.98e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 69.66 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPvQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHV----GY 78
Cdd:TIGR01257 1938 LRLNELTKVYSGTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVhqnmGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 79 MPQRDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDE 158
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1279381529 159 PFGALDALTRREMQNWLMTVWAQLQPTVLfVTHDVREAALLSDRVLVL 206
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIREGRAVVL-TSHSMEECEALCTRLAIM 2143
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-206 |
2.38e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.21 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSkTFHGErpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING-QTGH-----V 76
Cdd:PRK11614 6 LSFDKVS-AHYGK--IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKimreaV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPWRTVLQNVILGAEIARKplEQARQRARSLLPLFglegfadayPR----------QLSGGMRQRAALLRT 146
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAER--DQFQERIKWVYELF---------PRlherriqragTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279381529 147 iLMDRP-LLLLDEPFGALDALTRREMQNWLMTVWAQLQpTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK11614 152 -LMSQPrLLLLDEPSLGLAPIIIQQIFDTIEQLREQGM-TIFLVEQNANQALKLADRGYVL 210
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-194 |
2.62e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 66.97 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQT---------GHVGYMPQRdllmPW--- 88
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSfeatrsrnrYSVAYAAQK----PWlln 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 89 RTVLQNVILGAeiarkPLEQARQRAR----SLLPLFGLEGFADAYPR-----QLSGGMRQRAALLRTILMDRPLLLLDEP 159
Cdd:cd03290 93 ATVEENITFGS-----PFNKQRYKAVtdacSLQPDIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 1279381529 160 FGALDA-LTRREMQNWLMTVWAQLQPTVLFVTHDVR 194
Cdd:cd03290 168 FSALDIhLSDHLMQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-174 |
3.01e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.61 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 18 VQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIR-LNGALinGQTGH-------VGYMPQ---RDlLM 86
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGDM--ADARHrravcprIAYMPQglgKN-LY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 87 PWRTVLQNVI-------LGAeiarkplEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEP 159
Cdd:NF033858 91 PTLSVFENLDffgrlfgQDA-------AERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
170
....*....|....*
gi 1279381529 160 FGALDALTRRemQNW 174
Cdd:NF033858 164 TTGVDPLSRR--QFW 176
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-219 |
4.90e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALIN------GQTGHV 76
Cdd:PRK10762 5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpksSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 77 GYMPQRDLLMPWRTVLQNVILGAEI----ARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRP 152
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGREFvnrfGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 153 LLLLDEPfgaLDALTRREMQNwLMTVWAQLQPT---VLFVTHDVREAALLSDRVLVLsaRPGRLIADVPI 219
Cdd:PRK10762 162 VIIMDEP---TDALTDTETES-LFRVIRELKSQgrgIVYISHRLKEIFEICDDVTVF--RDGQFIAEREV 225
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-206 |
5.19e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.82 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG---------ALINGQT 73
Cdd:PRK10790 341 IDIDNVSFAYRDDNLV--LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsVLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 74 ghvgyMPQRDLLMPWRTVLQNVILGAEIARKPLEQARQR------ARSLLPlfGLEGFADAYPRQLSGGMRQRAALLRTI 147
Cdd:PRK10790 419 -----MVQQDPVVLADTFLANVTLGRDISEEQVWQALETvqlaelARSLPD--GLYTPLGEQGNNLSVGQKQLLALARVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 148 LMDRPLLLLDEPFGALDALTRREMQNWLMTVwaQLQPTVLFVTH---DVREAallsDRVLVL 206
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAHrlsTIVEA----DTILVL 547
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-192 |
1.51e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 25 SFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALingqtgHVGYMPQ-RDLLMPWRTVLQNVilgAEIAR 103
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKL------EVAYFDQhRAELDPEKTVMDNL---AEGKQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 104 KPLEQARQR-------------ARSLLPLfglegfadaypRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRRE 170
Cdd:PRK11147 410 EVMVNGRPRhvlgylqdflfhpKRAMTPV-----------KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLEL 478
|
170 180
....*....|....*....|..
gi 1279381529 171 MQNWLmtvwAQLQPTVLFVTHD 192
Cdd:PRK11147 479 LEELL----DSYQGTVLLVSHD 496
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-195 |
2.82e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.68 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNgalingQTGHVGYMPQ- 81
Cdd:PRK15064 320 LEVENLTKGF-DNGPL--FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS------ENANIGYYAQd 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 82 ------RDL-LMPW--------------RTVLQNVILGAEIARKPleqarqrarsllplfglegfadayPRQLSGGMRQR 140
Cdd:PRK15064 391 haydfeNDLtLFDWmsqwrqegddeqavRGTLGRLLFSQDDIKKS------------------------VKVLSGGEKGR 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 141 AALLRTILMDRPLLLLDEPFGALDALTRREMQNWLmtvwAQLQPTVLFVTHDvRE 195
Cdd:PRK15064 447 MLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMAL----EKYEGTLIFVSHD-RE 496
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-206 |
5.84e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 63.71 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 24 VSFVIEQGEFVSLIGQSGSGKSTLCNLIAGL--LTPDS---GEIRLNGALINGQT-------GHVGYMPQRDLLMPWRTV 91
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEArveGEVRLFGRNIYSPDvdpievrREVGMVFQYPNPFPHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 92 LQNVILGAEIAR--KPLEQARQRARSLLPLFGL----EGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDA 165
Cdd:PRK14267 103 YDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDP 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1279381529 166 LTRREMQNWLMTVWAQLqpTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK14267 183 VGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFL 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-193 |
8.00e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.36 E-value: 8.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 20 ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING--QTGHVGYMPQR---DLLMPwrTVLQN 94
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQalQKNLVAYVPQSeevDWSFP--VLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 95 VILGAEIA-----RKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRR 169
Cdd:PRK15056 100 VVMMGRYGhmgwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180
....*....|....*....|....
gi 1279381529 170 EMQNWLMTVWAQLQpTVLFVTHDV 193
Cdd:PRK15056 180 RIISLLRELRDEGK-TMLVSTHNL 202
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-233 |
9.89e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.01 E-value: 9.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 18 VQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGL--LTPD---SGEIRLNG--------ALINGQTGHVGYMPQRdl 84
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGqdifkmdvIELRRRVQMVFQIPNP-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 85 lMPWRTVLQNVILGAEIAR--KPLEQARQRARSLLPLFGL----EGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDE 158
Cdd:PRK14247 94 -IPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 159 PFGALDALTRREMQNWLMTVWAQLqpTVLFVTHDVREAALLSDRVLVLSArpGRLIADVPIH--LARPRRESDEAFL 233
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYK--GQIVEWGPTRevFTNPRHELTEKYV 245
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
28-216 |
1.34e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.70 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 28 IEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTG-----HVGYMPQrDLLMPWRTVLQNVILGAEIA 102
Cdd:PRK10253 30 IPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASkevarRIGLLAQ-NATTPGDITVQELVARGRYP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 103 RKPL--------EQARQRArslLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNW 174
Cdd:PRK10253 109 HQPLftrwrkedEEAVTKA---MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1279381529 175 LMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLIAD 216
Cdd:PRK10253 186 LSELNREKGYTLAAVLHDLNQACRYASHLIAL--REGKIVAQ 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-211 |
1.52e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.67 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNgalingQTGHVGYMPQRdLLMPWRTVLQNVILGAE 100
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP------AGARVLFLPQR-PYLPLGTLREALLYPAT 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 101 IARKPLEQARQrarsLLPLFGLEGFAD------AYPRQLSGGMRQRAALLRtILMDRP-LLLLDEPFGALDAltrrEMQN 173
Cdd:COG4178 452 AEAFSDAELRE----ALEAVGLGHLAErldeeaDWDQVLSLGEQQRLAFAR-LLLHKPdWLFLDEATSALDE----ENEA 522
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1279381529 174 WLMTVWAQLQP--TVLFVTHdvREA-ALLSDRVLVLSARPG 211
Cdd:COG4178 523 ALYQLLREELPgtTVISVGH--RSTlAAFHDRVLELTGDGS 561
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-196 |
2.66e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.72 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 13 HGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLlTPDS--------GEIRLNGALINGQTGHVGYMPQRdL 84
Cdd:PRK10938 270 YNDRPI--LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQGysndltlfGRRRGSGETIWDIKKHIGYVSSS-L 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 85 LMPWR--TVLQNVILGAEIARKPLEQA-----RQRARSLLPLFGLEG-FADAYPRQLSGGmRQRAALL-RTILMDRPLLL 155
Cdd:PRK10938 346 HLDYRvsTSVRNVILSGFFDSIGIYQAvsdrqQKLAQQWLDILGIDKrTADAPFHSLSWG-QQRLALIvRALVKHPTLLI 424
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1279381529 156 LDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREA 196
Cdd:PRK10938 425 LDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-206 |
2.80e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.01 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDsGEIRLNGALINGQTghvgympqrdlLMPWR----TVLQNVI 96
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVT-----------LQTWRkafgVIPQKVF 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 97 LGAEIARK---PLEQ-ARQRARSLLPLFGLEGFADAYPRQ-----------LSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:TIGR01271 1303 IFSGTFRKnldPYEQwSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1279381529 162 ALDALTRREMQNWLMTVWAQLqpTVLFVTHDVrEAALLSDRVLVL 206
Cdd:TIGR01271 1383 HLDPVTLQIIRKTLKQSFSNC--TVILSEHRV-EALLECQQFLVI 1424
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-245 |
5.81e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.85 E-value: 5.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 24 VSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALIN----GQTGHVGYM--PQ---RDLLMPWRTVLQN 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirspRDAIRAGIMlcPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 95 VILGAEI----------ARKPLEQARQRARSL---LPlfglegFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:PRK11288 352 INISARRhhlragclinNRWEAENADRFIRSLnikTP------SREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 162 ALDALTRREMQNWLMTVwAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLIADVpihlarPRRESDEAFLrLQAQLLG 241
Cdd:PRK11288 426 GIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVM--REGRIAGEL------AREQATERQA-LSLALPR 495
|
....
gi 1279381529 242 SLAA 245
Cdd:PRK11288 496 TSAA 499
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-195 |
7.40e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.44 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 20 ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG--ALINGQTGHVGYMpqrdllmpwrTVLQNVIL 97
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGsaALIAISSGLNGQL----------TGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 98 GAEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALD-ALTRREMQNwlM 176
Cdd:PRK13545 109 KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqTFTKKCLDK--M 186
|
170
....*....|....*....
gi 1279381529 177 TVWAQLQPTVLFVTHDVRE 195
Cdd:PRK13545 187 NEFKEQGKTIFFISHSLSQ 205
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-211 |
8.06e-11 |
|
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: 59.12 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 27 VIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALIngqtghvGYMPQRdllmpwrtvlqnvilgaeiarkpl 106
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-------VYKPQY------------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 107 eqarqrarsllplfglegfadaypRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTV 186
Cdd:cd03222 70 ------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTA 125
|
170 180
....*....|....*....|....*
gi 1279381529 187 LFVTHDVREAALLSDRVLVLSARPG 211
Cdd:cd03222 126 LVVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-163 |
8.35e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.34 E-value: 8.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDS--GEIRLNGAL-----INgQTGH 75
Cdd:NF040905 2 LEMRGITKTFPG---VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVcrfkdIR-DSEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 76 VG--YMPQRDLLMPWRTVLQNVILGAEIARKPL---EQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMD 150
Cdd:NF040905 78 LGivIIHQELALIPYLSIAENIFLGNERAKRGVidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKD 157
|
170
....*....|...
gi 1279381529 151 RPLLLLDEPFGAL 163
Cdd:NF040905 158 VKLLILDEPTAAL 170
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-192 |
9.86e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 9.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 26 FVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALI---------NGQTGHV------GYMPQRDLLMPWRT 90
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvarlqqdppRNVEGTVydfvaeGIEEQAEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 91 VLQNVilGAEIARKPLEQARQ---------------RARSLLPLFGLEgfADAYPRQLSGGMRQRAALLRTILMDRPLLL 155
Cdd:PRK11147 104 ISHLV--ETDPSEKNLNELAKlqeqldhhnlwqlenRINEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLL 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 1279381529 156 LDEPFGALDAltrrEMQNWLMTVWAQLQPTVLFVTHD 192
Cdd:PRK11147 180 LDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHD 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-212 |
1.06e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.87 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTF-HGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLL-TPD----SGEIRLNG--------AL 68
Cdd:PRK15134 6 LAIENLSVAFrQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpSPPvvypSGDIRFHGesllhaseQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 69 INGQTGH-VGYMPQRDL--LMPWRTV---LQNVILGAEIARKplEQARQRARSLLPLFGLEGFA---DAYPRQLSGGMRQ 139
Cdd:PRK15134 86 LRGVRGNkIAMIFQEPMvsLNPLHTLekqLYEVLSLHRGMRR--EAARGEILNCLDRVGIRQAAkrlTDYPHQLSGGERQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279381529 140 RAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGR 212
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM--QNGR 234
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-192 |
1.26e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.95 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 3 LSLQRVSKTFhGERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALingqtgHVGYMPQR 82
Cdd:PRK10636 313 LKMEKVSAGY-GDRII--LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGI------KLGYFAQH 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 83 DL--LMPWRTVLQNVilgAEIARKPLEqarQRARSLLPLFGLEGFADAYP-RQLSGGMRQRaALLRTILMDRP-LLLLDE 158
Cdd:PRK10636 384 QLefLRADESPLQHL---ARLAPQELE---QKLRDYLGGFGFQGDKVTEEtRRFSGGEKAR-LVLALIVWQRPnLLLLDE 456
|
170 180 190
....*....|....*....|....*....|....
gi 1279381529 159 PFGALDAltrrEMQNWLMTVWAQLQPTVLFVTHD 192
Cdd:PRK10636 457 PTNHLDL----DMRQALTEALIDFEGALVVVSHD 486
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-206 |
1.74e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 59.48 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDsGEIRLNGALINGQTghvgympqrdlLMPWR----TVLQNVI 96
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVP-----------LQKWRkafgVIPQKVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 97 LGAEIARKPLEQARQRARSLL----PLFGLEGFADAYPRQ-----------LSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:cd03289 88 IFSGTFRKNLDPYGKWSDEEIwkvaEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1279381529 162 ALDALTRREMQNWLMTVWAQLqpTVLFVTHDVrEAALLSDRVLVL 206
Cdd:cd03289 168 HLDPITYQVIRKTLKQAFADC--TVILSEHRI-EAMLECQRFLVI 209
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-165 |
1.89e-10 |
|
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: 60.73 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGAlingqtghVGYMPQRDLLMPwRTVLQNVILGae 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------VAYVPQQAWIQN-DSLRENILFG-- 722
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 101 iarKPLEQARQR----ARSLLPLFGLEGFADAYP-----RQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDA 165
Cdd:TIGR00957 723 ---KALNEKYYQqvleACALLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-210 |
4.09e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 58.25 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 20 ALAEVSFVIEQGEFVSLIGQSGSGKSTL--C-----NLIAGLLTpdSGEIRLNGALINGQT-------GHVGYMPQRDLL 85
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTIlrCfnrlnDLIPGFRV--EGKVTFHGKNLYAPDvdpvevrRRIGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 86 MPwRTVLQNVILGA----------EIARKPLEQAR--QRARSLLPLFGLegfadayprQLSGGMRQRAALLRTILMDRPL 153
Cdd:PRK14243 103 FP-KSIYDNIAYGAringykgdmdELVERSLRQAAlwDEVKDKLKQSGL---------SLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 154 LLLDEPFGALDALTRREMQNWLMTVWAQLqpTVLFVTHDVREAALLSDRVLVLSARP 210
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNVEL 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-206 |
4.11e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 22 AEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING-------QTGHVgYMPQR--------DLLM 86
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAlstaqrlARGLV-YLPEDrqssglylDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 87 PWRTVlqnvilGAEIARKPLEQARQRARSLLplfglEGF----------ADAYPRQLSGGMRQRAALLRTILMDRPLLLL 156
Cdd:PRK15439 359 AWNVC------ALTHNRRGFWIKPARENAVL-----ERYrralnikfnhAEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1279381529 157 DEPFGALDALTRREMQNWLMTVWAQlQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVM 476
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
12-195 |
6.70e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.90 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 12 FHGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG--------ALINGQTGHVGYMPQRD 83
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGevsviaisAGLSGQLTGIENIEFKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 84 LLMPWRtvlqnvilgaeiaRKpleQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGAL 163
Cdd:PRK13546 111 LCMGFK-------------RK---EIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190
....*....|....*....|....*....|...
gi 1279381529 164 D-ALTRREMQNwlMTVWAQLQPTVLFVTHDVRE 195
Cdd:PRK13546 175 DqTFAQKCLDK--IYEFKEQNKTIFFVSHNLGQ 205
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
5-207 |
9.66e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 9.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 5 LQRVSKTFHGERPVQ---ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLL--TPDSGEIRLngalingqtghvgym 79
Cdd:COG2401 27 VAIVLEAFGVELRVVeryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV--------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 80 pqrdllmPWRTVLQNVILGAEIARK-PLEQArqrarslLPLFGLEGFADAY-----PRQLSGGMRQRAALLRTILMDRPL 153
Cdd:COG2401 92 -------PDNQFGREASLIDAIGRKgDFKDA-------VELLNAVGLSDAVlwlrrFKELSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1279381529 154 LLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTH--DVrEAALLSDRVLVLS 207
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHhyDV-IDDLQPDLLIFVG 212
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-223 |
1.40e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 56.00 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 24 VSFVIEQGEFVSLIGQSGSGKSTLCNLIAGL--LTPDSGEIRLNGALINgqtghvgympqrDLLMpwrtvlqnvilgAEI 101
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDIT------------DLPP------------EER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 102 ARKPLEQARQRA------------RSLlplfgLEGFadayprqlSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRR 169
Cdd:cd03217 75 ARLGIFLAFQYPpeipgvknadflRYV-----NEGF--------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 170 EMQNWLMTvWAQLQPTVLFVTHDVREAALL-SDRVLVLSArpGRLIADVPIHLAR 223
Cdd:cd03217 142 LVAEVINK-LREEGKSVLIITHYQRLLDYIkPDRVHVLYD--GRIVKSGDKELAL 193
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-214 |
1.81e-09 |
|
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: 55.73 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 9 SKTFHGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPD---SGEIRLNG--ALINGQT--GHVGYMPQ 81
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGipYKEFAEKypGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 82 RDLLMPWRTVlqnvilgaeiaRKPLEqarqrarsllplFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:cd03233 91 EDVHFPTLTV-----------RETLD------------FALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 162 ALDALTRREMQNWLMTVwAQLQPTVLFVThdVREAAL----LSDRVLVLSArpGRLI 214
Cdd:cd03233 148 GLDSSTALEILKCIRTM-ADVLKTTTFVS--LYQASDeiydLFDKVLVLYE--GRQI 199
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-170 |
3.63e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.67 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 14 GERPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGeirlNGALINGQtghVGYMPQrdllMPW---RT 90
Cdd:PLN03130 628 AERPT--LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD----ASVVIRGT---VAYVPQ----VSWifnAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 91 VLQNVILGAEIARKPLEQA-----RQRARSLLP-----LFGLEGFadayprQLSGGMRQRAALLRTILMDRPLLLLDEPF 160
Cdd:PLN03130 695 VRDNILFGSPFDPERYERAidvtaLQHDLDLLPggdltEIGERGV------NISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170
....*....|
gi 1279381529 161 GALDALTRRE 170
Cdd:PLN03130 769 SALDAHVGRQ 778
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-219 |
5.11e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 23 EVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGHVG------YMPQ---RDLLMPWRTVLQ 93
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlangivYISEdrkRDGLVLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 94 NVILGA--EIARKPL----EQARQRARSLLPLFGLEG-FADAYPRQLSGGMRQRAALLRTiLMDRP-LLLLDEPFGALDA 165
Cdd:PRK10762 350 NMSLTAlrYFSRAGGslkhADEQQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARG-LMTRPkVLILDEPTRGVDV 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 166 LTRREMQNwLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRLIADVPI 219
Cdd:PRK10762 429 GAKKEIYQ-LINQFKAEGLSIILVSSEMPEVLGMSDRILVM--HEGRISGEFTR 479
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-219 |
6.48e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 8 VSKTFHGerpVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH------VGYMPQ 81
Cdd:PRK10982 4 ISKSFPG---VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealengISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 82 RDLLMPWRTVLQNVILGAEIARKPLEQARQRARSLLPLFGlEGFADAYPRQ----LSGGMRQRAALLRTILMDRPLLLLD 157
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFD-ELDIDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 158 EPfgaLDALTRREMqNWLMTVWAQLQPT---VLFVTHDVREAALLSDRVLVLsaRPGRLIADVPI 219
Cdd:PRK10982 160 EP---TSSLTEKEV-NHLFTIIRKLKERgcgIVYISHKMEEIFQLCDEITIL--RDGQWIATQPL 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-206 |
6.51e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.87 E-value: 6.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 20 ALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGalingqtghvgyMPQRDL-LMPWR--------- 89
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD------------IPLTKLqLDSWRsrlavvsqt 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 90 ------TVLQNVILGAEIARKplEQARQRAR------SLLPL-FGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLL 156
Cdd:PRK10789 398 pflfsdTVANNIALGRPDATQ--QEIEHVARlasvhdDILRLpQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 157 DEPFGALDALTRRE-MQNwlMTVWAQlQPTVLFVTHdvREAALL-SDRVLVL 206
Cdd:PRK10789 476 DDALSAVDGRTEHQiLHN--LRQWGE-GRTVIISAH--RLSALTeASEILVM 522
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-208 |
7.10e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 54.34 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 19 QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGqtghvgyMPQRDLLMPWRTVLQNVILG 98
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIST-------IPLEDLRSSLTIIPQDPTLF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 99 AEIARKPL----EQARQRARSLLPLfgLEGFADayprqLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNW 174
Cdd:cd03369 95 SGTIRSNLdpfdEYSDEEIYGALRV--SEGGLN-----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKT 167
|
170 180 190
....*....|....*....|....*....|....
gi 1279381529 175 LMTVWAqlQPTVLFVTHDVREAALLsDRVLVLSA 208
Cdd:cd03369 168 IREEFT--NSTILTIAHRLRTIIDY-DKILVMDA 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-216 |
7.70e-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: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 23 EVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPD-SGEIRLNGALINGQT------GHVGYMPQ---RDLLMPWRTVL 92
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpaqairAGIAMVPEdrkRHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 93 QNVILG-----AEIARKPLEQARQRARSLLPLFGLEGFADAYP-RQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDAL 166
Cdd:TIGR02633 358 KNITLSvlksfCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1279381529 167 TRREMQNwLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:TIGR02633 438 AKYEIYK-LINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGE--GKLKGD 484
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
36-215 |
1.02e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 54.24 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 36 LIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALIN----------GQTGHVGYMPQR-----DLLMPWRTVLQNV-ILGA 99
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrgllalrQQVATVFQDPEQqifytDIDSDIAFSLRNLgVPEA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 100 EIARkpleqarqRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVW 179
Cdd:PRK13638 112 EITR--------RVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIV 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1279381529 180 AQLQpTVLFVTHDVREAALLSDRVLVLsaRPGRLIA 215
Cdd:PRK13638 184 AQGN-HVIISSHDIDLIYEISDAVYVL--RQGQILT 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-191 |
1.11e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 52.93 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGAlingqtGHVGYMPQRdllmpwrtvlqnvilgae 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG------EDLLFLPQR------------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 101 iarkpleqarqrarsllPLFGLEGFADA--YP--RQLSGGMRQRAALLRtILMDRP-LLLLDEPFGALDAltrrEMQNWL 175
Cdd:cd03223 73 -----------------PYLPLGTLREQliYPwdDVLSGGEQQRLAFAR-LLLHKPkFVFLDEATSALDE----ESEDRL 130
|
170
....*....|....*.
gi 1279381529 176 MTVWAQLQPTVLFVTH 191
Cdd:cd03223 131 YQLLKELGITVISVGH 146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-207 |
1.45e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.98 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTP---DSGEIRlngalingqtGHVGYMPQrdllMPW---RTVLQN 94
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaetSSVVIR----------GSVAYVPQ----VSWifnATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 95 VILGAEIA-----RKPLEQARQRARSLLPLFGLEGFADAyPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRR 169
Cdd:PLN03232 699 ILFGSDFEserywRAIDVTALQHDLDLLPGRDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190
....*....|....*....|....*....|....*...
gi 1279381529 170 EMQNWLMTVWAQLQPTVLfVTHDVREAALLsDRVLVLS 207
Cdd:PLN03232 778 QVFDSCMKDELKGKTRVL-VTNQLHFLPLM-DRIILVS 813
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-165 |
1.60e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.02 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 19 QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPD--SGEIRLNGALINGQ-TGHVGYMPQRDLLMPWRTVlqnv 95
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNfQRSTGYVEQQDVHSPNLTV---- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279381529 96 ilgaeiaRKPLEqarqrarsllplfglegFAdAYPRQLSGGMRQRAallrTI---LMDRPLLL-LDEPFGALDA 165
Cdd:cd03232 97 -------REALR-----------------FS-ALLRGLSVEQRKRL----TIgveLAAKPSILfLDEPTSGLDS 141
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
100-216 |
1.81e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.97 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 100 EIARKpleQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREmqnwlmtVW 179
Cdd:NF000106 115 DLSRK---DARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNE-------VW 184
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1279381529 180 AQLQ------PTVLFVTHDVREAALLSDRVLVLSArpGRLIAD 216
Cdd:NF000106 185 DEVRsmvrdgATVLLTTQYMEEAEQLAHELTVIDR--GRVIAD 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-167 |
2.07e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 19 QALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTpdSGEIRLNGALINGQ------TGHVGYMPQRDLLMPWRTVL 92
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT--TGVITGGDRLVNGRpldssfQRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 93 QNVILGAEIaRKP----LEQARQRARSLLPLFGLEGFADAYPRQLSGGM--RQRAALlrTI---LMDRP--LLLLDEPFG 161
Cdd:TIGR00956 855 ESLRFSAYL-RQPksvsKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnvEQRKRL--TIgveLVAKPklLLFLDEPTS 931
|
....*.
gi 1279381529 162 ALDALT 167
Cdd:TIGR00956 932 GLDSQT 937
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-191 |
3.10e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.18 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 38 GQSGSGKSTLCNLIAGLLTPDSGEIRLNGALING-QTGHVGYMPQRDLLMPWRTVLQNVILGAEIArkpleQARQRARSL 116
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKPYCTYIGHNLGLKLEMTVFENLKFWSEIY-----NSAETLYAA 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 117 LPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNwLMTVWAQLQPTVLFVTH 191
Cdd:PRK13541 108 IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN-LIVMKANSGGIVLLSSH 181
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
10-206 |
3.13e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 53.37 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 10 KTFHGerPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGlLTPDSGEIRLNGALINGQtghvgympqrDLL-MPW 88
Cdd:COG4170 14 DTPQG--RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICG-ITKDNWHVTADRFRWNGI----------DLLkLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 89 RTvlQNVILGAEIAR----------------KPLEQA-----------------RQRARSLLPLFGL---EGFADAYPRQ 132
Cdd:COG4170 81 RE--RRKIIGREIAMifqepsscldpsakigDQLIEAipswtfkgkwwqrfkwrKKRAIELLHRVGIkdhKDIMNSYPHE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 133 LSGGMRQRAallrTILM---DRP-LLLLDEPFGALDALTRREMQNwLMTVWAQLQPT-VLFVTHDVREAALLSDRVLVL 206
Cdd:COG4170 159 LTEGECQKV----MIAMaiaNQPrLLIADEPTNAMESTTQAQIFR-LLARLNQLQGTsILLISHDLESISQWADTITVL 232
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-216 |
3.21e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 25 SFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGE--------IRLNgalINGQTGHVGYMPQR---DLLMPW----- 88
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLS---FEQLQKLVSDEWQRnntDMLSPGeddtg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 89 RTVLQNVILGAEiarkpleqARQRARSLLPLFGLEGFADAYPRQLSGGmRQRAALLRTILMDRP-LLLLDEPFGALDALT 167
Cdd:PRK10938 100 RTTAEIIQDEVK--------DPARCEQLAQQFGITALLDRRFKYLSTG-ETRKTLLCQALMSEPdLLILDEPFDGLDVAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 168 RREMQNWLMTVWAQLQPTVLFVT--HD----VREAALLSDRVLVLSARPGRLIAD 216
Cdd:PRK10938 171 RQQLAELLASLHQSGITLVLVLNrfDEipdfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
7-224 |
3.57e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 7 RVSKTFHGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIA----GLLTPDSGEIRLNG----ALINGQTGHVGY 78
Cdd:TIGR00956 63 RKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGitpeEIKKHYRGDVVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 79 MPQRDLLMPWRTVLQNVILGAEIaRKP---------LEQARQRARSLLPLFGLE-----GFADAYPRQLSGGMRQRAALL 144
Cdd:TIGR00956 143 NAETDVHFPHLTVGETLDFAARC-KTPqnrpdgvsrEEYAKHIADVYMATYGLShtrntKVGNDFVRGVSGGERKRVSIA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 145 RTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAAL-LSDRVLVLSArpGRLIADVPIHLAR 223
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYeLFDKVIVLYE--GYQIYFGPADKAK 299
|
.
gi 1279381529 224 P 224
Cdd:TIGR00956 300 Q 300
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-206 |
6.27e-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: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGalINgqtghVGYMPQRDLLMPWRTVLQNVILGAE 100
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--LN-----IAKIGLHDLRFKITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 101 IARKPLEQARQRARS----LLPLFGLEGFADAYP-----------RQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDA 165
Cdd:TIGR00957 1375 SLRMNLDPFSQYSDEevwwALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1279381529 166 LTRREMQNwlmTVWAQLQP-TVLFVTHDVrEAALLSDRVLVL 206
Cdd:TIGR00957 1455 ETDNLIQS---TIRTQFEDcTVLTIAHRL-NTIMDYTRVIVL 1492
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-201 |
6.70e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 51.96 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 24 VSFVIEQGEFVSLIGQSGSGKSTLCNLIaGLLTPDSGEIRLNGAL-------------INGQTGHVGYMPQRDLLMPwRT 90
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVeffnqniyerrvnLNRLRRQVSMVHPKPNLFP-MS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 91 VLQNVILGAEIA--RKPLE-----QARQRARSLLPLFGLEGFADAYprQLSGGMRQRAALLRTILMDRPLLLLDEPFGAL 163
Cdd:PRK14258 104 VYDNVAYGVKIVgwRPKLEiddivESALKDADLWDEIKHKIHKSAL--DLSGGQQQRLCIARALAVKPKVLLMDEPCFGL 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1279381529 164 DALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSD 201
Cdd:PRK14258 182 DPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-220 |
7.22e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 7.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 23 EVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDS-GEIRLNG----------ALINGqtghVGYMPQ---RDLLMPW 88
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGkpvkirnpqqAIAQG----IAMVPEdrkRDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 89 RTVLQNVIL-------GAEIARKPLEQ-------ARQRARSLLPLFGLEgfadayprQLSGGMRQRAALLRTILMDRPLL 154
Cdd:PRK13549 356 MGVGKNITLaaldrftGGSRIDDAAELktilesiQRLKVKTASPELAIA--------RLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279381529 155 LLDEPFGALDALTRREMQNwLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSArpGRLIADVPIH 220
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYK-LINQLVQQGVAIIVISSELPEVLGLSDRVLVMHE--GKLKGDLINH 490
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-211 |
8.71e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.60 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 27 VIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALingqtghvgympqRDLLMPWR-TVLQNV---ILGAEI- 101
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDW-------------DEILDEFRgSELQNYftkLLEGDVk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 102 -ARKP-----------------LEQARQRAR--SLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:cd03236 89 vIVKPqyvdlipkavkgkvgelLKKKDERGKldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1279381529 162 ALDALTRREMQNwLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSARPG 211
Cdd:cd03236 169 YLDIKQRLNAAR-LIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYGEPG 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-206 |
1.05e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.20 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALIN-GQT----------GHVGYMPQRDLLMPWR 89
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfGKDifqidaiklrKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 90 TVLQNVILGAEI-ARKPLEQARQRARSLLPLFGLegFADAYPR------QLSGGMRQRAALLRTILMDRPLLLLDEPFGA 162
Cdd:PRK14246 106 SIYDNIAYPLKShGIKEKREIKKIVEECLRKVGL--WKEVYDRlnspasQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1279381529 163 LDALTRREMQNWLMTVWAQLqpTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFL 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6-165 |
1.06e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 6 QRVSKTFHGERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGAlingqtghVGYMPQRDLL 85
Cdd:PTZ00243 661 KMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS--------IAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 86 MPwRTVLQNVILGAEIARKPLEQA---RQRARSLLPL-FGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:PTZ00243 733 MN-ATVRGNILFFDEEDAARLADAvrvSQLEADLAQLgGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
....
gi 1279381529 162 ALDA 165
Cdd:PTZ00243 812 ALDA 815
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-165 |
2.41e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 14 GERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPD--SGEIRLNGALINGQTGH--VGYMPQRDLLMPWR 89
Cdd:PLN03140 889 TEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETFAriSGYCEQNDIHSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 90 TVLQNVILGAeIARKPLEQARQRARS----LLPLFGLEGFADA---YP--RQLSGGMRQRAALLRTILMDRPLLLLDEPF 160
Cdd:PLN03140 969 TVRESLIYSA-FLRLPKEVSKEEKMMfvdeVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
....*
gi 1279381529 161 GALDA 165
Cdd:PLN03140 1048 SGLDA 1052
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-211 |
3.00e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 27 VIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEI-----------RLNG--------ALINGQTgHVGYMPQRDLLMP 87
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGtelqdyfkKLANGEI-KVAHKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 88 wRTVLQNVilgaeiaRKPLEQARQR--ARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDA 165
Cdd:COG1245 174 -KVFKGTV-------RELLEKVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 166 LTR-------REMqnwlmtvwAQLQPTVLFVTHDVreAAL--LSDRVLVLSARPG 211
Cdd:COG1245 246 YQRlnvarliREL--------AEEGKYVLVVEHDL--AILdyLADYVHILYGEPG 290
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-206 |
5.12e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.75 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 30 QGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIrlngalingqtghvgympqrdllmpwrtvlqnVILGAEIARKPLEQA 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------IYIDGEDILEEVLDQ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 110 RqrarsllplfgLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQ-----NWLMTVWAQLQP 184
Cdd:smart00382 49 L-----------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLLKSEKNL 117
|
170 180
....*....|....*....|....*..
gi 1279381529 185 TVLFVTHDV-----REAALLSDRVLVL 206
Cdd:smart00382 118 TVILTTNDEkdlgpALLRRRFDRRIVL 144
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-206 |
1.28e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.26 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 14 GERPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGlLTPDSGEI-------------RLNGALINGQTGHVGYM- 79
Cdd:PRK15093 16 SDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVtadrmrfddidllRLSPRERRKLVGHNVSMi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 80 ---PQrDLLMPWRTV---LQNVILGAEIARKPLEQARQRARSLLPLFGLEGFAD------AYPRQLSGGMRQRaALLRTI 147
Cdd:PRK15093 95 fqePQ-SCLDPSERVgrqLMQNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIKDhkdamrSFPYELTEGECQK-VMIAIA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 148 LMDRP-LLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVL 206
Cdd:PRK15093 173 LANQPrLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-220 |
3.56e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.74 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLT--PDSGEIRLNGAL-INGQTGHVGYMPQrdlLMPWRTVLQN--- 94
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTggGAPRGARVTGDVtLNGEPLAAIDAPR---LARLRAVLPQaaq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 95 ----------VILG----AEIARKPLEQARQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRP-------- 152
Cdd:PRK13547 94 pafafsareiVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQLWPphdaaqpp 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279381529 153 -LLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLSarPGRLIADVPIH 220
Cdd:PRK13547 174 rYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLA--DGAIVAHGAPA 240
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-213 |
5.47e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 23 EVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGQTGH------VGYMPQ--RDL-LMPWRTVLQ 93
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdavkkgMAYITEsrRDNgFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 94 NVIL----------GAEIARKPLEQAR--QRARSLLPLFGLEgfADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFG 161
Cdd:PRK09700 361 NMAIsrslkdggykGAMGLFHEVDEQRtaENQRELLALKCHS--VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1279381529 162 ALDALTRREMQNwLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLsaRPGRL 213
Cdd:PRK09700 439 GIDVGAKAEIYK-VMRQLADDGKVILMVSSELPEIITVCDRIAVF--CEGRL 487
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-208 |
8.67e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.51 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALIN--GQTG---HVGYMPQRDLLMPwRTVLQNV 95
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfGLTDlrrVLSIIPQSPVLFS-GTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 96 ILGAEIARKPLEQARQRAR-----SLLPlFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRRE 170
Cdd:PLN03232 1331 DPFSEHNDADLWEALERAHikdviDRNP-FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
170 180 190
....*....|....*....|....*....|....*....
gi 1279381529 171 MQNwlmTVWAQLQP-TVLFVTHDVrEAALLSDRVLVLSA 208
Cdd:PLN03232 1410 IQR---TIREEFKScTMLVIAHRL-NTIIDCDKILVLSS 1444
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-192 |
1.22e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 24 VSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEI----RLNGALINgqtghvgympqrdllmpwrtvlQNVILGA 99
Cdd:PLN03073 528 LNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsaKVRMAVFS----------------------QHHVDGL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 100 EIARKPL--------EQARQRARSLLPLFGLEGFADAYPR-QLSGGMRQRAALLRtILMDRP-LLLLDEPFGALDaLTRR 169
Cdd:PLN03073 586 DLSSNPLlymmrcfpGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAK-ITFKKPhILLLDEPSNHLD-LDAV 663
|
170 180
....*....|....*....|...
gi 1279381529 170 EMqnwLMTVWAQLQPTVLFVTHD 192
Cdd:PLN03073 664 EA---LIQGLVLFQGGVLMVSHD 683
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-211 |
1.25e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 27 VIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGA-------------------LINGQTgHVGYMPQRDLLMP 87
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSwdevlkrfrgtelqnyfkkLYNGEI-KVVHKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 88 wRTVLQNVIlgaEIARKPLEqaRQRARSLLPLFGLEGFADAYPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALD--- 164
Cdd:PRK13409 174 -KVFKGKVR---ELLKKVDE--RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirq 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1279381529 165 ----ALTRREMQNwlmtvwaqlQPTVLFVTHDVreAAL--LSDRVLVLSARPG 211
Cdd:PRK13409 248 rlnvARLIRELAE---------GKYVLVVEHDL--AVLdyLADNVHIAYGEPG 289
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
129-212 |
2.04e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 129 YPRQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWAQLQPTVLFVTHdvREAAL-LSDRVLVLS 207
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH--RIASIkRSDKIVVFN 1432
|
....*
gi 1279381529 208 aRPGR 212
Cdd:PTZ00265 1433 -NPDR 1436
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
132-192 |
3.27e-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: 43.12 E-value: 3.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 132 QLSGGMRQRAAL-LRTILM---DRPLLLLDEPFGALDaLTRREMQNWLMTVWAQLQPTVLFVTHD 192
Cdd:cd03227 77 QLSGGEKELSALaLILALAslkPRPLYILDEIDRGLD-PRDGQALAEAILEHLVKGAQVIVITHL 140
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-192 |
3.41e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 28 IEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNG----ALINGQTghvgymPQRDllmpwRTVLQNVILGAEIAR 103
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlAWVNQET------PALP-----QPALEYVIDGDREYR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 104 KpLEQA----------------------------RQRARSLLPLFGLEGFADAYP-RQLSGGMRQRAALLRTILMDRPLL 154
Cdd:PRK10636 93 Q-LEAQlhdanerndghaiatihgkldaidawtiRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 1279381529 155 LLDEPFGALDALTRREMQNWLMTvwaqLQPTVLFVTHD 192
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKS----YQGTLILISHD 205
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
16-207 |
3.85e-05 |
|
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: 43.74 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 16 RPVqaLAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALINGqtghvgyMPQRDLLMPWRTVLQNV 95
Cdd:cd03288 34 KPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISK-------LPLHTLRSRLSIILQDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 96 ILGAEIARKPLEQARQ----RARSLLPLFGLEGFADAYPRQL-----------SGGMRQRAALLRTILMDRPLLLLDEPF 160
Cdd:cd03288 105 ILFSGSIRFNLDPECKctddRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1279381529 161 GALDALTRREMQNWLMTVWAqlQPTVLFVTHDVrEAALLSDRVLVLS 207
Cdd:cd03288 185 ASIDMATENILQKVVMTAFA--DRTVVTIAHRV-STILDADLVLVLS 228
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
12-230 |
1.50e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 12 FHGE--RPVQALAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGAL----INGQ--TGHVGYMPQRD 83
Cdd:PTZ00265 390 FHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnlkdINLKwwRSKIGVVSQDP 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 84 LLmpWRTVLQNVILGAEIARKPLE---------------------QARQRARSLLPLFG--------------------- 121
Cdd:PTZ00265 470 LL--FSNSIKNNIKYSLYSLKDLEalsnyynedgndsqenknkrnSCRAKCAGDLNDMSnttdsneliemrknyqtikds 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 122 ----------LEGFADAYP-----------RQLSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNWLMTVWA 180
Cdd:PTZ00265 548 evvdvskkvlIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKG 627
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1279381529 181 QLQPTVLFVTHDVrEAALLSDRVLVLSARPGRLIADVPIHLARPRRESDE 230
Cdd:PTZ00265 628 NENRITIIIAHRL-STIRYANTIFVLSNRERGSTVDVDIIGEDPTKDNKE 676
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
11-67 |
1.69e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 38.74 E-value: 1.69e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1279381529 11 TFHGErpvqalaevSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPdSGEIRLNGA 67
Cdd:pfam13555 11 TFDGH---------TIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVP-AKRARFNKA 57
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-206 |
1.91e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.46 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIRLNGALInGQTG------HVGYMPQRDLLMPwRTVLQN 94
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI-GAYGlrelrrQFSMIPQDPVLFD-GTVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 95 VilgaeiarKP-LEQARQRARSLLPLFGL--------EGFaDAypRQLSG------GMRQRAALLRTIL-MDRPLLLLDE 158
Cdd:PTZ00243 1404 V--------DPfLEASSAEVWAALELVGLrervasesEGI-DS--RVLEGgsnysvGQRQLMCMARALLkKGSGFILMDE 1472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1279381529 159 PFGALDALTRREMQNWLMTVWAQLqpTVLFVTHDVREAALLsDRVLVL 206
Cdd:PTZ00243 1473 ATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVM 1517
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-191 |
7.39e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 39.63 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 21 LAEVSFVIEQGEFVSLIGQSGSGKSTLCNLIAGllTPD----SGEIRLNGALINGQT----GHVGYMP--QRDLLMPWRT 90
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEpeerAHLGIFLafQYPIEIPGVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 91 VLQNVILGAEIARK--------PLEqARQRARSLLPLFGL----------EGFadayprqlSGGMRQRAALLRTILMDRP 152
Cdd:CHL00131 101 NADFLRLAYNSKRKfqglpeldPLE-FLEIINEKLKLVGMdpsflsrnvnEGF--------SGGEKKRNEILQMALLDSE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1279381529 153 LLLLDEPFGAL--DAL-TRREMQNWLMTvwaqLQPTVLFVTH 191
Cdd:CHL00131 172 LAILDETDSGLdiDALkIIAEGINKLMT----SENSIILITH 209
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
109-191 |
9.39e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279381529 109 ARQRARSLLPlfGLEGFADAYPR---QLSGGMRQRAALLRTILMDRPLLLLDEPFGALDAltrrEMQNWLMTVWAQLQPT 185
Cdd:PLN03073 320 AEARAASILA--GLSFTPEMQVKatkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL----HAVLWLETYLLKWPKT 393
|
....*.
gi 1279381529 186 VLFVTH 191
Cdd:PLN03073 394 FIVVSH 399
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
36-62 |
3.99e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 37.88 E-value: 3.99e-03
10 20
....*....|....*....|....*..
gi 1279381529 36 LIGQSGSGKSTLCNLIAGLLTPDSGEI 62
Cdd:PRK00098 169 LAGQSGVGKSTLLNALAPDLELKTGEI 195
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
38-65 |
8.34e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 35.54 E-value: 8.34e-03
10 20 30
....*....|....*....|....*....|.
gi 1279381529 38 GQSGSGKSTLCNLIA---GLLTPDSGEIRLN 65
Cdd:cd02020 6 GPAGSGKSTVAKLLAkklGLPYLDTGGIRTE 36
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
133-207 |
8.83e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 37.02 E-value: 8.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279381529 133 LSGGMRQRAALLRTILMDRPLLLLDEPFGALDALTRREMQNwLMTVWAQLQPTVLFVTHDVREAALLSDRVLVLS 207
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQ-LIAELAKKDKGIIIISSEMPELLGITDRILVMS 465
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
30-63 |
9.76e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 35.98 E-value: 9.76e-03
10 20 30
....*....|....*....|....*....|....
gi 1279381529 30 QGEFVSLIGQSGSGKSTLCNLIAGLLTPDSGEIR 63
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEIS 138
|
|
| |
