|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
27-278 |
1.71e-142 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 401.39 E-value: 1.71e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRGY 106
Cdd:COG1116 6 PALELRGVSKRFPTGGGGV-TALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 107 VFQQGSLFPWLTVEENIAFGLKAQGIYK-EHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDE 185
Cdd:COG1116 85 VFQEPALLPWLTVLDNVALGLELRGVPKaERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 186 PMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMTPRPGRIKEIVPINL----DARDRVSDEFAAY 261
Cdd:COG1116 165 PFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLprprDRELRTSPEFAAL 244
|
250
....*....|....*..
gi 505262942 262 RKQLLTKLHfDAHEEHA 278
Cdd:COG1116 245 RAEILDLLR-EEAERAA 260
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
29-248 |
8.74e-128 |
|
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: 362.94 E-value: 8.74e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRGYVF 108
Cdd:cd03293 1 LEVRNVSKTY-GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 109 QQGSLFPWLTVEENIAFGLKAQGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPM 187
Cdd:cd03293 80 QQDALLPWLTVLDNVALGLELQGVpKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505262942 188 GALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMTPRPGRIKEIVPINL 248
Cdd:cd03293 160 SALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
27-278 |
2.14e-104 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 305.25 E-value: 2.14e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFtAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRGY 106
Cdd:COG4525 2 SMLTVRHVSVRY-PGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 107 VFQQGSLFPWLTVEENIAFGLKAQGIYK-EHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDE 185
Cdd:COG4525 81 VFQKDALLPWLNVLDNVAFGLRLRGVPKaERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 186 PMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMTPRPGRIKEIVPINL--------DARDRVSD- 256
Cdd:COG4525 161 PFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELDFsrrflageDARAIKSDp 240
|
250 260
....*....|....*....|..
gi 505262942 257 EFAAYRKQLLTKLHFDAHEEHA 278
Cdd:COG4525 241 AFIALREELLDIIFAQEEAEAA 262
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
27-240 |
7.74e-90 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 271.20 E-value: 7.74e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFTApdgsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEG--PNpKR 104
Cdd:COG3842 4 PALELENVSKRYGD-----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlpPE-KR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 --GYVFQQGSLFPWLTVEENIAFGLKAQGIYK-EHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVL 181
Cdd:COG3842 78 nvGMVFQDYALFPHLTVAENVAFGLRMRGVPKaEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 182 LLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVM--NDGRI 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
29-240 |
1.71e-86 |
|
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: 257.83 E-value: 1.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapdGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---G 105
Cdd:cd03259 1 LELKGLSKTY----GSV-RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrniG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 106 YVFQQGSLFPWLTVEENIAFGLKAQGIYKEHEADAAR-YIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLD 184
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVReLLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505262942 185 EPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVM--NEGRI 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
28-243 |
1.13e-79 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 245.06 E-value: 1.13e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 28 ELSIEHVSREFTApdgsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGE--PIEGPNPKR- 104
Cdd:COG1118 2 SIEVRNISKRFGS-----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlFTNLPPRERr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -GYVFQQGSLFPWLTVEENIAFGLKAQGIYKEH-EADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLL 182
Cdd:COG1118 77 vGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEiRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505262942 183 LDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEI 243
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVM--NQGRIEQV 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
29-268 |
4.03e-78 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 238.06 E-value: 4.03e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFT-APdgsvvhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRGYV 107
Cdd:PRK11248 2 LQISHLYADYGgKP------ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 108 FQQGSLFPWLTVEENIAFGLKAQGIYK-EHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEP 186
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKmQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 187 MGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMTPRPGRIKEIVPINL--------DARDRVSD-E 257
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLNFarrfvageSSRSIKSDpQ 235
|
250
....*....|.
gi 505262942 258 FAAYRKQLLTK 268
Cdd:PRK11248 236 FIAMREYVLSR 246
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
49-253 |
2.46e-76 |
|
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: 232.74 E-value: 2.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRGYVFQQGSLFPWLTVEENIAFGLK 128
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 129 A---QGIYKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDI 205
Cdd:TIGR01184 81 RvlpDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505262942 206 WEQYHMTMILVTHDVDEAIYLGSRVVIMTPRPG-RIKEIVPINLD-ARDR 253
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAaNIGQILEVPFPrPRDR 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
26-242 |
6.00e-76 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 231.47 E-value: 6.00e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 26 NPELSIEHVSREFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR- 104
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEV-TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 --------GYVFQQGSLFPWLTVEENIAFGLKAQGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALI 175
Cdd:COG1136 81 arlrrrhiGFVFQFFNLLPELTALENVALPLLLAGVsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505262942 176 DHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDvDEAIYLGSRVVIMtpRPGRIKE 242
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRL--RDGRIVS 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
29-243 |
4.52e-75 |
|
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: 229.43 E-value: 4.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapDGSVvhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEG-PNPKR--G 105
Cdd:cd03300 1 IELENVSKFY---GGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPHKRpvN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 106 YVFQQGSLFPWLTVEENIAFGLKAQGIYK-EHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLD 184
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLRLKKLPKaEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 185 EPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEI 243
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVM--NKGKIQQI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-266 |
9.20e-74 |
|
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: 235.18 E-value: 9.20e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 11 VASGRQTLADVPAGVNPELSIEHVSREFTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTL 90
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 91 SLAGEPIEGPNPKR--------GYVFQ--QGSLFPWLTVEENIAFGLKAQGIY--KEHEADAARYIEMVGLH-GFEQAYP 157
Cdd:COG1123 323 LFDGKDLTKLSRRSlrelrrrvQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLsrAERRERVAELLERVGLPpDLADRYP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 158 HQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRP 237
Cdd:COG1123 403 HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVM--YD 480
|
250 260 270
....*....|....*....|....*....|
gi 505262942 238 GRIKEIVPinldaRDRV-SDEFAAYRKQLL 266
Cdd:COG1123 481 GRIVEDGP-----TEEVfANPQHPYTRALL 505
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
29-240 |
1.01e-73 |
|
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: 225.45 E-value: 1.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTApDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:cd03255 1 IELKNLSKTYGG-GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -----GYVFQQGSLFPWLTVEENIAFGLKAQGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHP 178
Cdd:cd03255 80 rrrhiGFVFQSFNLLPDLTALENVELPLLLAGVpKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505262942 179 DVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYlGSRVVIMtpRPGRI 240
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIEL--RDGKI 218
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
27-243 |
2.94e-72 |
|
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: 226.46 E-value: 2.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFTApdgsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEG-PNPKRG 105
Cdd:TIGR03265 3 PYLSIDNIRKRFGA-----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRlPPQKRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 106 Y--VFQQGSLFPWLTVEENIAFGLKAQGIYKEHEADAARYI-EMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLL 182
Cdd:TIGR03265 78 YgiVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELlDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505262942 183 LDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMTprPGRIKEI 243
Cdd:TIGR03265 158 LDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMN--HGVIEQV 216
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
31-240 |
1.48e-69 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 218.04 E-value: 1.48e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 31 IEHVSREFtaPDGSVvhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR-----G 105
Cdd:COG1125 4 FENVTKRY--PDGTV--AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrrriG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 106 YVFQQGSLFPWLTVEENIAFGLKAQGIYKEHEADAARY-IEMVGLH--GFEQAYPHQISGGMAQRVAIARALIDHPDVLL 182
Cdd:COG1125 80 YVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDElLELVGLDpeEYRDRYPHELSGGQQQRVGVARALAADPPILL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 183 LDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:COG1125 160 MDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM--REGRI 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
26-233 |
5.62e-69 |
|
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: 214.07 E-value: 5.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 26 NPELSIEHVSREFtapDGSVVHalSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR- 104
Cdd:COG1127 3 EPMIEVRNLTKSF---GDRVVL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -------GYVFQQGSLFPWLTVEENIAFGLKAQGIYKEHEAD--AARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALI 175
Cdd:COG1127 78 yelrrriGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRelVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 176 DHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVL 215
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
43-240 |
1.12e-68 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 218.43 E-value: 1.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 43 GSVVhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---------GYVFQQGSL 113
Cdd:COG4175 38 GQTV-GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrkkmSMVFQHFAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 114 FPWLTVEENIAFGLKAQGIYK-EHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDS 192
Cdd:COG4175 117 LPHRTVLENVAFGLEIQGVPKaERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDP 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505262942 193 FTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:COG4175 197 LIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIM--KDGRI 242
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
28-240 |
3.74e-68 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 215.71 E-value: 3.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 28 ELSIEHVSREFtapdGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR--- 104
Cdd:COG3839 3 SLELENVSKSY----GGV-EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDrni 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 GYVFQQGSLFPWLTVEENIAFGLKAQGIYKEhEAD-----AAryiEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPD 179
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKLRKVPKA-EIDrrvreAA---ELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505262942 180 VLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVM--NDGRI 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
27-243 |
6.70e-68 |
|
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: 212.50 E-value: 6.70e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFTAPDGSVVhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR-- 104
Cdd:cd03294 19 KLLAKGKSKEEILKKTGQTV-GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -------GYVFQQGSLFPWLTVEENIAFGLKAQGIYK-EHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALID 176
Cdd:cd03294 98 elrrkkiSMVFQSFALLPHRTVLENVAFGLEVQGVPRaEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505262942 177 HPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEI 243
Cdd:cd03294 178 DPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIM--KDGRLVQV 242
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
29-234 |
8.69e-68 |
|
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: 211.39 E-value: 8.69e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapdGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:cd03295 1 IEFENVTKRY----GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -GYVFQQGSLFPWLTVEENIAFGLKAQGIYKEH-EADAARYIEMVGL--HGFEQAYPHQISGGMAQRVAIARALIDHPDV 180
Cdd:cd03295 77 iGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKiRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505262942 181 LLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMT 234
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMK 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
29-243 |
1.91e-67 |
|
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: 209.67 E-value: 1.91e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTApDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:cd03257 2 LEVKNLSVSFPT-GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ----GYVFQ--QGSLFPWLTVEENIAFGLKAQGIYKEHEADAARYIEM---VGLH-GFEQAYPHQISGGMAQRVAIARAL 174
Cdd:cd03257 81 rkeiQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLlvgVGLPeEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 175 IDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEI 243
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVM--YAGKIVEE 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
29-233 |
6.02e-67 |
|
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: 208.90 E-value: 6.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:cd03261 1 IELRGLTKSF---GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ----GYVFQQGSLFPWLTVEENIAFGLKAQGIYKEHE-ADAARY-IEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHP 178
Cdd:cd03261 76 rrrmGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEiREIVLEkLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505262942 179 DVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVL 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
28-243 |
1.35e-66 |
|
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: 207.96 E-value: 1.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 28 ELSIEHVSREFtapdGSVVhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR--- 104
Cdd:cd03296 2 SIEVRNVSKRF----GDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 GYVFQQGSLFPWLTVEENIAFGLKAQGIYKEHEADAAR-----YIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPD 179
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRakvheLLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505262942 180 VLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEI 243
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVM--NKGRIEQV 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
29-233 |
4.81e-65 |
|
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: 202.03 E-value: 4.81e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapdgSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:cd03229 1 LELKNVSKRY-----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ---GYVFQQGSLFPWLTVEENIAFGLkaqgiykeheadaaryiemvglhgfeqayphqiSGGMAQRVAIARALIDHPDVL 181
Cdd:cd03229 76 rriGMVFQDFALFPHLTVLENIALGL---------------------------------SGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505262942 182 LLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVL 174
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
29-266 |
9.39e-65 |
|
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: 203.50 E-value: 9.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:COG1124 2 LEVRNLSVSYGQGGRRV-PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -GYVFQQ--GSLFPWLTVEENIAFGLKAQGIyKEHEADAARYIEMVGLH-GFEQAYPHQISGGMAQRVAIARALIDHPDV 180
Cdd:COG1124 81 vQMVFQDpyASLHPRHTVDRILAEPLRIHGL-PDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 181 LLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEIVPINlDARDRVSDEfaa 260
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVM--QNGRIVEELTVA-DLLAGPKHP--- 233
|
....*.
gi 505262942 261 YRKQLL 266
Cdd:COG1124 234 YTRELL 239
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
29-233 |
3.71e-62 |
|
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: 196.40 E-value: 3.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSreFTAPDGsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:COG1122 1 IELENLS--FSYPGG--TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -GYVFQ----QgsLF-PwlTVEENIAFGLKAQGIYKEhEAD--AARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALID 176
Cdd:COG1122 77 vGLVFQnpddQ--LFaP--TVEEDVAFGPENLGLPRE-EIRerVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505262942 177 HPDVLLLDEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVL 207
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
29-233 |
8.79e-62 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 195.60 E-value: 8.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapdGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:COG1126 2 IEIENLHKSF----GDL-EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInklr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ---GYVFQQGSLFPWLTVEENIAFGL-KAQGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPD 179
Cdd:COG1126 77 rkvGMVFQQFNLFPHLTVLENVTLAPiKVKKMsKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505262942 180 VLLLDEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:COG1126 157 VMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFM 209
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
31-259 |
9.22e-62 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 195.79 E-value: 9.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 31 IEHVSREFtapdGSVVhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---GYV 107
Cdd:TIGR00968 3 IANISKRF----GSFQ-ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDrkiGFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 108 FQQGSLFPWLTVEENIAFGLKAQGIYKEH-EADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEP 186
Cdd:TIGR00968 78 FQHYALFKHLTVRDNIAFGLEIRKHPKAKiKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505262942 187 MGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMTprPGRIKEIvpinlDARDRVSDEFA 259
Cdd:TIGR00968 158 FGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMS--NGKIEQI-----GSPDEVYDHPA 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
16-243 |
4.24e-61 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 198.25 E-value: 4.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 16 QTLADVPAGVNPELSIEHVSREFtapDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGE 95
Cdd:PRK09452 2 KKLNKQPSSLSPLVELRGISKSF---DGKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 96 PIEG-PNPKR--GYVFQQGSLFPWLTVEENIAFGLKAQGIYKEHEA----DAARyieMVGLHGFEQAYPHQISGGMAQRV 168
Cdd:PRK09452 77 DITHvPAENRhvNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITprvmEALR---MVQLEEFAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505262942 169 AIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEI 243
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRIEQD 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
30-233 |
5.76e-60 |
|
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: 189.99 E-value: 5.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 30 SIEHVSreFTAPDGSVVhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR----- 104
Cdd:cd03225 1 ELKNLS--FSYPDGARP-ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrrkv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 GYVFQ--QGSLFPwLTVEENIAFGLKAQGIYKEH-EADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVL 181
Cdd:cd03225 78 GLVFQnpDDQFFG-PTVEEEVAFGLENLGLPEEEiEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505262942 182 LLDEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVL 207
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
29-240 |
7.27e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 190.66 E-value: 7.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapdGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI--EGPNPKR-- 104
Cdd:COG1131 1 IEVRGLTKRY----GDK-TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVarDPAEVRRri 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 GYVFQQGSLFPWLTVEENIAFGLKAQGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLL 183
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLpRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505262942 184 DEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAII--DKGRI 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
29-233 |
2.38e-58 |
|
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: 186.20 E-value: 2.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapdGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNP------ 102
Cdd:cd03262 1 IEIKNLHKSF----GDF-HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKninelr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 103 -KRGYVFQQGSLFPWLTVEENIAFGL-KAQGIYK-EHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPD 179
Cdd:cd03262 76 qKVGMVFQQFNLFPHLTVLENITLAPiKVKGMSKaEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505262942 180 VLLLDEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFM 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
29-242 |
5.68e-58 |
|
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: 185.86 E-value: 5.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:cd03258 2 IELKNVSKVFGDTGGKV-TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ----GYVFQQGSLFPWLTVEENIAFGLKAQGIYKEH-EADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPD 179
Cdd:cd03258 81 rrriGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEiEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505262942 180 VLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMTprPGRIKE 242
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVME--KGEVVE 221
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
64-243 |
6.43e-58 |
|
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: 188.86 E-value: 6.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 64 IIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI-EGPNPKR--GYVFQQGSLFPWLTVEENIAFGLKAQGIYKEHEADA 140
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVtNVPPHLRhiNMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 141 AR-YIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHD 219
Cdd:TIGR01187 81 VLeALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180
....*....|....*....|....
gi 505262942 220 VDEAIYLGSRVVIMtpRPGRIKEI 243
Cdd:TIGR01187 161 QEEAMTMSDRIAIM--RKGKIAQI 182
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
29-221 |
1.82e-57 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 187.98 E-value: 1.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:COG1135 2 IELENLSKTFPTKGGPV-TALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ----GYVFQQGSLFPWLTVEENIAFGLKAQGIYKEH-EADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPD 179
Cdd:COG1135 81 rrkiGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEiRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505262942 180 VLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVD 221
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMD 202
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
58-234 |
2.72e-57 |
|
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: 183.27 E-value: 2.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 58 PGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEP-------IEGPNPKR--GYVFQQGSLFPWLTVEENIAFGLK 128
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkINLPPQQRkiGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 129 AQGiYKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQ 208
Cdd:cd03297 102 RKR-NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKN 180
|
170 180
....*....|....*....|....*.
gi 505262942 209 YHMTMILVTHDVDEAIYLGSRVVIMT 234
Cdd:cd03297 181 LNIPVIFVTHDLSEAEYLADRIVVME 206
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
25-233 |
1.37e-56 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 186.96 E-value: 1.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 25 VNPELSIEHVSREFtapDGSvvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR 104
Cdd:PRK11607 16 LTPLLEIRNLTKSF---DGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ---GYVFQQGSLFPWLTVEENIAFGLKAQGIYK-EHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDV 180
Cdd:PRK11607 91 rpiNMMFQSYALFPHMTVEQNIAFGLKQDKLPKaEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505262942 181 LLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIM 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
29-221 |
6.68e-56 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 180.25 E-value: 6.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtaPDGsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:COG2884 2 IRFENVSKRY--PGG--REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ----GYVFQQGSLFPWLTVEENIAFGLKAQGIYKEHEADAARYI-EMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPD 179
Cdd:COG2884 78 rrriGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVlDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505262942 180 VLLLDEPMGALDsftrADLQDRLLDIWEQYH---MTMILVTHDVD 221
Cdd:COG2884 158 LLLADEPTGNLD----PETSWEIMELLEEINrrgTTVLIATHDLE 198
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
49-266 |
1.83e-55 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 180.26 E-value: 1.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLsLAGE-PIEGPNPKRGYVFQQGSLFPWLTVEENIAFGL 127
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTaPLAEAREDTRLMFQDARLLPWKKVIDNVGLGL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 128 KaqGIYKEheaDAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWE 207
Cdd:PRK11247 107 K--GQWRD---AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQ 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505262942 208 QYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEIVPINLdARDRV--SDEFAAYRKQLL 266
Cdd:PRK11247 182 QHGFTVLLVTHDVSEAVAMADRVLLI--EEGKIGLDLTVDL-PRPRRrgSARLAELEAEVL 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
53-261 |
1.84e-55 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 179.18 E-value: 1.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 53 SLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNP-KRGY--VFQQGSLFPWLTVEENIAFGLKA 129
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPaERPVsmLFQENNLFPHLTVAQNIGLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 130 QGiyKEHEADAARYIEM---VGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIW 206
Cdd:COG3840 99 GL--KLTAEQRAQVEQAlerVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELC 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505262942 207 EQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEIVPINLDARDRVSDEFAAY 261
Cdd:COG3840 177 RERGLTVLMVTHDPEDAARIADRVLLV--ADGRIAADGPTAALLDGEPPPALAAY 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
29-243 |
5.42e-55 |
|
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: 177.45 E-value: 5.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapdGSVVhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---G 105
Cdd:cd03301 1 VELENVTKRF----GNVT-ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdiA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 106 YVFQQGSLFPWLTVEENIAFGLKAQGIYK-EHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLD 184
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLRKVPKdEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 185 EPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEI 243
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM--NDGQIQQI 212
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
22-223 |
7.85e-55 |
|
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: 177.63 E-value: 7.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 22 PAGVNPELSIEHVSREFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPN 101
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGEL-TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 102 --------PKR-GYVFQQGSLFPWLTVEENIAFGLKAQGiYKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIAR 172
Cdd:COG4181 81 edararlrARHvGFVFQSFQLLPTLTALENVMLPLELAG-RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505262942 173 ALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEA 223
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
31-243 |
9.17e-55 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 181.44 E-value: 9.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 31 IEHVSREFTApdgsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---GYV 107
Cdd:PRK10851 5 IANIKKSFGR-----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDrkvGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 108 FQQGSLFPWLTVEENIAFGLKAQGIYKEHEADAARY-----IEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLL 182
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAkvtqlLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505262942 183 LDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEI 243
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVM--SQGNIEQA 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
51-233 |
1.30e-54 |
|
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: 181.07 E-value: 1.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 51 DVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEP-------IEGPNPKR--GYVFQQGSLFPWLTVEE 121
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargIFLPPHRRriGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 122 NIAFGLKAQGIyKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDR 201
Cdd:COG4148 97 NLLYGRKRAPR-AERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPY 175
|
170 180 190
....*....|....*....|....*....|..
gi 505262942 202 LLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:COG4148 176 LERLRDELDIPILYVSHSLDEVARLADHVVLL 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
26-242 |
6.05e-54 |
|
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: 183.18 E-value: 6.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 26 NPELSIEHVSreFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGL-DHP--QSGTLSLAGEPIEGPNP 102
Cdd:COG1123 2 TPLLEVRDLS--VRYPGGDV-PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlPHGgrISGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 103 KR-----GYVFQ--QGSLFPwLTVEENIAFGLKAQGIYK-EHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARAL 174
Cdd:COG1123 79 ALrgrriGMVFQdpMTQLNP-VTVGDQIAEALENLGLSRaEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 175 IDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKE 242
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM--DDGRIVE 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
29-233 |
5.01e-53 |
|
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: 175.63 E-value: 5.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTAPDGsVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQ---SGTLSLAGEPIEGPNPK-- 103
Cdd:COG0444 2 LEVRNLKVYFPTRRG-VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 104 ---RG----YVFQ--QGSLFPWLTVEENIAFGLKAQGIYKEHEAD--AARYIEMVGLHGFEQ---AYPHQISGGMAQRVA 169
Cdd:COG0444 81 rkiRGreiqMIFQdpMTSLNPVMTVGDQIAEPLRIHGGLSKAEARerAIELLERVGLPDPERrldRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505262942 170 IARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
29-243 |
1.27e-52 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 175.65 E-value: 1.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSR---EFTapdgsvvhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEG-PNPKR 104
Cdd:NF040840 2 IRIENLSKdwkEFK---------LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNlPPEKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 G--YVFQQGSLFPWLTVEENIAFGLKAQGIYKEHEADAARYI-EMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVL 181
Cdd:NF040840 73 GiaYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEImELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505262942 182 LLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEI 243
Cdd:NF040840 153 LLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIM--LNGRLSQV 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
29-245 |
6.19e-52 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 174.14 E-value: 6.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapdGSVVhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEgpnpKRG--- 105
Cdd:PRK11432 7 VVLKNITKRF----GSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT----HRSiqq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 106 ----YVFQQGSLFPWLTVEENIAFGLKAQGIYKEHEADAAR-YIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDV 180
Cdd:PRK11432 78 rdicMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKeALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505262942 181 LLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEIVP 245
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVM--NKGKIMQIGS 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
49-243 |
1.47e-51 |
|
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: 169.44 E-value: 1.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---GYVFQQGSLFPWLTVEENIAF 125
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKrdiSYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 126 GLKAQGIYKEHEADAARYI-EMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLD 204
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIaEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 505262942 205 IWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEI 243
Cdd:cd03299 175 IRKEFGVTVLHVTHDFEEAWALADKVAIM--LNGKLIQV 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
49-186 |
1.55e-51 |
|
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: 166.28 E-value: 1.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR-----GYVFQQGSLFPWLTVEENI 123
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrkeiGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 124 AFGLKAQGIYKEH-EADAARYIEMVGLHGFE----QAYPHQISGGMAQRVAIARALIDHPDVLLLDEP 186
Cdd:pfam00005 81 RLGLLLKGLSKREkDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
47-245 |
3.72e-51 |
|
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: 168.13 E-value: 3.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 47 HALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDH-----PQSGTLSLAGEPIEGPNP-------KRGYVFQQGSLF 114
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVdvlelrrRVGMVFQKPNPF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 115 PwLTVEENIAFGLKAQGIYKEHEADA--ARYIEMVGLHGFE--QAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGAL 190
Cdd:cd03260 94 P-GSIYDNVAYGLRLHGIKLKEELDErvEEALRKAALWDEVkdRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505262942 191 DSFTRADLQDRLLDIWEQYhmTMILVTHDVDEAIYLGSRVVIMTprPGRIKEIVP 245
Cdd:cd03260 173 DPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLL--NGRLVEFGP 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
26-233 |
5.65e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 168.34 E-value: 5.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 26 NPELSIEHVSREFtapDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRG 105
Cdd:COG1121 4 MPAIELENLTVSY---GGRPV--LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 106 YVFQQGSL---FPwLTVEENIAFGLKAQ-----GIYKEHEADAARYIEMVGLHGFEQaypHQI---SGGMAQRVAIARAL 174
Cdd:COG1121 79 YVPQRAEVdwdFP-ITVRDVVLMGRYGRrglfrRPSRADREAVDEALERVGLEDLAD---RPIgelSGGQQQRVLLARAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 175 IDHPDVLLLDEPMGALDSFTRADLQDrLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYE-LLRELRREGKTILVVTHDLGAVREYFDRVLLL 212
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
31-240 |
1.00e-50 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 171.33 E-value: 1.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 31 IEHVSrefTAPDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQ--SGTLSLAGEPI-EGPNPKR--G 105
Cdd:TIGR03258 8 IDHLR---VAYGANTV--LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDLtHAPPHKRglA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 106 YVFQQGSLFPWLTVEENIAFGLKAQgiyKEHEADAARYI----EMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVL 181
Cdd:TIGR03258 83 LLFQNYALFPHLKVEDNVAFGLRAQ---KMPKADIAERVadalKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 182 LLDEPMGALDSFTRADLQDRLLDIWEQY-HMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:TIGR03258 160 LLDEPLSALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIM--KDGRL 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
29-240 |
8.94e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 163.83 E-value: 8.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTAPDGsvvhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNP----KR 104
Cdd:COG4619 1 LELEGLSFRVGGKPI-----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpewrRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -GYVFQQGSLFPwLTVEENIAFGLKAQGiYKEHEADAARYIEMVGL-HGFEQAYPHQISGGMAQRVAIARALIDHPDVLL 182
Cdd:COG4619 76 vAYVPQEPALWG-GTVRDNLPFPFQLRE-RKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 183 LDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTL--EAGRL 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
47-233 |
1.85e-48 |
|
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: 160.78 E-value: 1.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 47 HALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRGYVFQQGSL---FPwLTVEENI 123
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRSIdrdFP-ISVRDVV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 124 AFGLKA-----QGIYKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADL 198
Cdd:cd03235 92 LMGLYGhkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDI 171
|
170 180 190
....*....|....*....|....*....|....*
gi 505262942 199 QdRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:cd03235 172 Y-ELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
29-233 |
3.57e-48 |
|
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: 158.71 E-value: 3.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapdGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIeGPNPKR---- 104
Cdd:cd03230 1 IEVRNLSKRY----GKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEvkrr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -GYVFQQGSLFPWLTVEENIAFglkaqgiykeheadaaryiemvglhgfeqayphqiSGGMAQRVAIARALIDHPDVLLL 183
Cdd:cd03230 75 iGYLPEEPSLYENLTVRENLKL-----------------------------------SGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505262942 184 DEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAIL 168
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
27-240 |
4.23e-48 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 160.99 E-value: 4.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFtaPDGsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR-- 104
Cdd:COG3638 1 PMLELRNLSKRY--PGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ------GYVFQQGSLFPWLTVEENIAFGLKAQ--------GIYKEHEADAA-RYIEMVGLHGFEQAYPHQISGGMAQRVA 169
Cdd:COG3638 77 rlrrriGMIFQQFNLVPRLSVLTNVLAGRLGRtstwrsllGLFPPEDRERAlEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505262942 170 IARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGL--RDGRV 225
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
29-249 |
1.07e-47 |
|
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: 160.29 E-value: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSreFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGepIEGPNPKR---- 104
Cdd:TIGR04520 1 IEVENVS--FSYPESEK-PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENlwei 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ----GYVFQ----Q--GSlfpwlTVEENIAFGLKAQGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARA 173
Cdd:TIGR04520 76 rkkvGMVFQnpdnQfvGA-----TVEDDVAFGLENLGVpREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 174 LIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIyLGSRVVIM---------TPRP--GRIKE 242
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMnkgkivaegTPREifSQVEL 229
|
....*..
gi 505262942 243 IVPINLD 249
Cdd:TIGR04520 230 LKEIGLD 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
29-240 |
2.33e-47 |
|
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: 159.05 E-value: 2.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSreFTAPDGSVVHalsDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPK----- 103
Cdd:COG1120 2 LEAENLS--VGYGGRPVLD---DVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRelarr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 104 RGYVFQQGSLFPWLTVEENIAFGLKA-QGIY----KEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHP 178
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALGRYPhLGLFgrpsAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505262942 179 DVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLL--KDGRI 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
29-221 |
6.52e-47 |
|
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: 157.89 E-value: 6.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapdGSVVhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNP----KR 104
Cdd:COG0411 5 LEVRGLTKRF----GGLV-AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPhriaRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 GYV--FQQGSLFPWLTVEENIAFGLKAQGIY----------------KEHEADAARYIEMVGLHGFEQAYPHQISGGMAQ 166
Cdd:COG0411 80 GIArtFQNPRLFPELTVLENVLVAAHARLGRgllaallrlprarreeREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505262942 167 RVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVD 221
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMD 214
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
47-233 |
8.70e-47 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 158.38 E-value: 8.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 47 HALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR--------GYVFQ----QgsLF 114
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrkkvGLVFQfpehQ--LF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 115 PwLTVEENIAFGLKAQGIYKEH-EADAARYIEMVGLHG--FEQAyPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALD 191
Cdd:TIGR04521 97 E-ETVYKDIAFGPKNLGLSEEEaEERVKEALELVGLDEeyLERS-PFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505262942 192 SFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:TIGR04521 175 PKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVM 216
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
31-226 |
1.28e-46 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 155.85 E-value: 1.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 31 IEHVSREFtapdGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR------ 104
Cdd:TIGR03608 1 LKNISKKF----GDK-VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ---GYVFQQGSLFPWLTVEENIAFGLKAQGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDV 180
Cdd:TIGR03608 76 eklGYLFQNFALIENETVEENLDLGLKYKKLsKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505262942 181 LLLDEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHD------VDEAIYL 226
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDpevakqADRVIEL 206
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
27-236 |
2.12e-46 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 158.74 E-value: 2.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFTAPDG------SVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGP 100
Cdd:COG4608 6 PLLEVRDLKKHFPVRGGlfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 101 NPK--RGY------VFQ--QGSLFPWLTVEENIAFGLKAQGIY--KEHEADAARYIEMVGLH-GFEQAYPHQISGGMAQR 167
Cdd:COG4608 86 SGRelRPLrrrmqmVFQdpYASLNPRMTVGDIIAEPLRIHGLAskAERRERVAELLELVGLRpEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 168 VAIARALIDHPDVLLLDEPMGALDSFTRA-------DLQDRLldiweqyHMTMILVTHD--VDEAI-------YLGsRVV 231
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSIQAqvlnlleDLQDEL-------GLTYLFISHDlsVVRHIsdrvavmYLG-KIV 237
|
....*
gi 505262942 232 IMTPR 236
Cdd:COG4608 238 EIAPR 242
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
49-242 |
5.40e-46 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 155.25 E-value: 5.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR-------GYVFQQGSLFPWLTVEE 121
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqeaGMVFQQFYLFPHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 122 NIAFG-LKAQGIYKEHEADAAR-YIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQ 199
Cdd:PRK09493 97 NVMFGpLRVRGASKEEAEKQAReLLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505262942 200 DRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIMTprPGRIKE 242
Cdd:PRK09493 177 KVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFID--KGRIAE 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
29-240 |
1.04e-45 |
|
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: 154.65 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapdGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:cd03256 1 IEVENLSKTY----PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrql 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ----GYVFQQGSLFPWLTVEENIAFGLKAQ---------GIYKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIA 171
Cdd:cd03256 77 rrqiGMIFQQFNLIERLSVLENVLSGRLGRrstwrslfgLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 172 RALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGL--KDGRI 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
22-242 |
1.35e-45 |
|
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: 163.47 E-value: 1.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 22 PAGVNPELSIEHVSreFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPN 101
Cdd:COG2274 467 LPRLKGDIELENVS--FRYPGDSP-PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 102 PK--R---GYVFQQGSLFPwLTVEENIAFGlkAQGIYKEHEADAARyieMVGLHGFEQAYPH-----------QISGGMA 165
Cdd:COG2274 544 PAslRrqiGVVLQDVFLFS-GTIRENITLG--DPDATDEEIIEAAR---LAGLHDFIEALPMgydtvvgeggsNLSGGQR 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505262942 166 QRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQyhMTMILVTHDvDEAIYLGSRVVIMtpRPGRIKE 242
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHR-LSTIRLADRIIVL--DKGRIVE 689
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
51-240 |
2.75e-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: 152.65 E-value: 2.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 51 DVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---GYVFQQGSLFPWLTVEENIAFG- 126
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADrpvSMLFQENNLFAHLTVEQNVGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 127 ---LKAQGIYKEHEADAARyieMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLL 203
Cdd:cd03298 96 spgLKLTAEDRQAIEVALA---RVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 505262942 204 DIWEQYHMTMILVTHDVDEAIYLGSRVVIMTprPGRI 240
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLD--NGRI 207
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
51-279 |
3.84e-45 |
|
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: 156.43 E-value: 3.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 51 DVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGE-------PIEGPNPKR--GYVFQQGSLFPWLTVEE 121
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkGIFLPPEKRriGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 122 NIAFGLK-AQGiyKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQD 200
Cdd:TIGR02142 95 NLRYGMKrARP--SERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 201 RLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEIVPINLDARDRVSDEFAAYRKQLLTKLHFDAHEEHAG 279
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVL--EDGRVAAAGPIAEVWASPDLPWLAREDQGSLIEGVVAEHDQHYG 249
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
29-233 |
2.05e-44 |
|
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: 151.05 E-value: 2.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTApdgsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:cd03219 1 LEVRGLTKRFGG-----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEiarl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 --GYVFQQGSLFPWLTVEENIAFGLKAQGIY-----------KEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIA 171
Cdd:cd03219 76 giGRTFQIPRLFPELTVLENVMVAAQARTGSglllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505262942 172 RALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVL 216
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
31-233 |
3.32e-44 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 149.71 E-value: 3.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 31 IEHVSREFTAPdgsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI------EGPNPKR 104
Cdd:TIGR02673 4 FHNVSKAYPGG----VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVnrlrgrQLPLLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 --GYVFQQGSLFPWLTVEENIAFGLKAQGIYK-EHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVL 181
Cdd:TIGR02673 80 riGVVFQDFRLLPDRTVYENVALPLEVRGKKErEIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505262942 182 LLDEPMGALDsftrADLQDRLLDIWEQYH---MTMILVTHDVDEAIYLGSRVVIM 233
Cdd:TIGR02673 160 LADEPTGNLD----PDLSERILDLLKRLNkrgTTVIVATHDLSLVDRVAHRVIIL 210
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
48-242 |
3.32e-44 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 150.55 E-value: 3.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI---EGPNPKR--------GYVFQQGSLFPW 116
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAirllrqkvGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 117 LTVEEN-IAFGLKAQGIYKEHEADAARYI-EMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFT 194
Cdd:COG4161 97 LTVMENlIEAPCKVLGLSKEQAREKAMKLlARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505262942 195 RADLQDRLLDIwEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKE 242
Cdd:COG4161 177 TAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYM--EKGRIIE 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-242 |
3.67e-44 |
|
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: 157.54 E-value: 3.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 8 HLAVASGRQTLADVPAGVNPELSIEHVSREFTAPDG------SVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAG 81
Cdd:COG4172 255 KLLAAEPRGDPRPVPPDAPPLLEARDLKVWFPIKRGlfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 82 LdHPQSGTLSLAGEPIEGPNPK--RGY------VFQQ--GSLFPWLTVEENIAFGLKAQGI---YKEHEADAARYIEMVG 148
Cdd:COG4172 335 L-IPSEGEIRFDGQDLDGLSRRalRPLrrrmqvVFQDpfGSLSPRMTVGQIIAEGLRVHGPglsAAERRARVAEALEEVG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 149 LH-GFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLG 227
Cdd:COG4172 414 LDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALA 493
|
250
....*....|....*
gi 505262942 228 SRVVIMtpRPGRIKE 242
Cdd:COG4172 494 HRVMVM--KDGKVVE 506
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
48-242 |
1.19e-43 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 149.39 E-value: 1.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI---EGPNPKR--------GYVFQQGSLFPW 116
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAirelrrnvGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 117 LTVEEN-IAFGLKAQGIYKEH-EADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFT 194
Cdd:PRK11124 97 LTVQQNlIEAPCRVLGLSKDQaLARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505262942 195 RADLQDRLLDIwEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKE 242
Cdd:PRK11124 177 TAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYM--ENGHIVE 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
29-233 |
2.00e-43 |
|
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: 148.47 E-value: 2.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapdGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:COG4555 2 IEVENLSKKY----GKV-PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREArrqi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 GYVFQQGSLFPWLTVEENIAFGLKAQGIY-KEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLL 183
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYFAELYGLFdEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505262942 184 DEPMGALDSFTRADLQDRLLDIWEQYHmTMILVTHDVDEAIYLGSRVVIM 233
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEALCDRVVIL 205
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
19-242 |
3.67e-43 |
|
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: 155.30 E-value: 3.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 19 ADVPAGVNPELSIEHVSreFTAPDGSVvhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIE 98
Cdd:COG4988 327 APLPAAGPPSIELEDVS--FSYPGGRP--ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 99 GPNPKR-----GYVFQQGSLFPWlTVEENIAFGlkaqgiykEHEADAA---RYIEMVGLHGFEQAYPHQI---------- 160
Cdd:COG4988 403 DLDPASwrrqiAWVPQNPYLFAG-TIRENLRLG--------RPDASDEeleAALEAAGLDEFVAALPDGLdtplgeggrg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 161 -SGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYhmTMILVTHDvDEAIYLGSRVVIMtpRPGR 239
Cdd:COG4988 474 lSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHR-LALLAQADRILVL--DDGR 548
|
...
gi 505262942 240 IKE 242
Cdd:COG4988 549 IVE 551
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
49-233 |
4.39e-43 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 146.86 E-value: 4.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQ---SGTLSLAGEPIEG--PNPKR-GYVFQQGSLFPWLTVEEN 122
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAlpAEQRRiGILFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 123 IAFGLKAQGIYKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRL 202
Cdd:COG4136 97 LAFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFV 176
|
170 180 190
....*....|....*....|....*....|.
gi 505262942 203 LDIWEQYHMTMILVTHDVDEAIyLGSRVVIM 233
Cdd:COG4136 177 FEQIRQRGIPALLVTHDEEDAP-AAGRVLDL 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
27-219 |
9.17e-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: 145.70 E-value: 9.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFtapDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI----EGPNP 102
Cdd:COG4133 1 MMLEAENLSCRR---GERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIrdarEDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 103 KRGYVFQQGSLFPWLTVEENIAFGLKAQGIyKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLL 182
Cdd:COG4133 76 RLAYLGHADGLKPELTVRENLRFWAALYGL-RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 505262942 183 LDEPMGALDSFTRADLQdRLLDIWEQYHMTMILVTHD 219
Cdd:COG4133 155 LDEPFTALDAAGVALLA-ELIAAHLARGGAVLLTTHQ 190
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
53-240 |
9.88e-43 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 146.65 E-value: 9.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 53 SLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRGYV---FQQGSLFPWLTVEENIAFG--- 126
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVsmlFQENNLFSHLTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 127 -LKAQGIYKEHEADAARyieMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDI 205
Cdd:PRK10771 99 gLKLNAAQREKLHAIAR---QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190
....*....|....*....|....*....|....*
gi 505262942 206 WEQYHMTMILVTHDVDEAIYLGSRVVIMTprPGRI 240
Cdd:PRK10771 176 CQERQLTLLMVSHSLEDAARIAPRSLVVA--DGRI 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
29-233 |
1.14e-42 |
|
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: 146.11 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTapdGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIeGPNPKR---- 104
Cdd:cd03263 1 LQIRNLTKTYK---KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAarqs 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -GYVFQQGSLFPWLTVEENIAFGLKAQGIYKEHE-ADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLL 182
Cdd:cd03263 77 lGYCPQFDALFDELTVREHLRFYARLKGLPKSEIkEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505262942 183 LDEPMGALDSFTRADLQDRLLDiwEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILE--VRKGRSIILTTHSMDEAEALCDRIAIM 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
46-233 |
2.58e-42 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 149.41 E-value: 2.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 46 VHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI-EGPNPKR--GYVFQQGSLFPWLTVEEN 122
Cdd:PRK11000 16 VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMnDVPPAERgvGMVFQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 123 IAFGLKAQGIYKeheADAARYIEMVG----LHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADL 198
Cdd:PRK11000 96 MSFGLKLAGAKK---EEINQRVNQVAevlqLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQM 172
|
170 180 190
....*....|....*....|....*....|....*
gi 505262942 199 QDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK11000 173 RIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVL 207
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
31-278 |
3.90e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 148.03 E-value: 3.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 31 IEHVSREFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR------ 104
Cdd:PRK11153 4 LKNISKVFPQGGRTI-HALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 --GYVFQQGSLFPWLTVEENIAFGLKAQGIYKEH-EADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVL 181
Cdd:PRK11153 83 qiGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEiKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 182 LLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMTprPGRIKEivpinldaRDRVSDEFAAy 261
Cdd:PRK11153 163 LCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVID--AGRLVE--------QGTVSEVFSH- 231
|
250 260
....*....|....*....|...
gi 505262942 262 RKQLLTK------LHFDAHEEHA 278
Cdd:PRK11153 232 PKHPLTRefiqstLHLDLPEDYL 254
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
29-218 |
5.72e-42 |
|
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: 142.52 E-value: 5.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSreFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:cd03228 1 IEFKNVS--FSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrkn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -GYVFQQGSLFPwLTVEENIafglkaqgiykeheadaaryiemvglhgfeqayphqISGGMAQRVAIARALIDHPDVLLL 183
Cdd:cd03228 78 iAYVPQDPFLFS-GTIRENI------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 505262942 184 DEPMGALDSFTRADLQDRLLDIweQYHMTMILVTH 218
Cdd:cd03228 121 DEATSALDPETEALILEALRAL--AKGKTVIVIAH 153
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
46-243 |
1.50e-40 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 144.22 E-value: 1.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 46 VHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPK-RG--YVFQQGSLFPWLTVEEN 122
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAdRDiaMVFQNYALYPHMSVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 123 IAFGLKAQGIYKEHE----ADAARyieMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRA-- 196
Cdd:PRK11650 97 MAYGLKIRGMPKAEIeervAEAAR---ILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVqm 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505262942 197 -----DLQDRLldiweqyHMTMILVTHDVDEAIYLGSRVVIMTprPGRIKEI 243
Cdd:PRK11650 174 rleiqRLHRRL-------KTTSLYVTHDQVEAMTLADRVVVMN--GGVAEQI 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
26-243 |
1.52e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 142.08 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 26 NPELSIEHVSreFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPN---- 101
Cdd:PRK13635 3 EEIIRVEHIS--FRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 102 -PKRGYVFQQ-GSLFPWLTVEENIAFGLKAQGIYKE------HEAdaaryIEMVGLHGFEQAYPHQISGGMAQRVAIARA 173
Cdd:PRK13635 80 rRQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREemvervDQA-----LRQVGMEDFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 174 LIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYlGSRVVIMtpRPGRIKEI 243
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVM--NKGEILEE 221
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
29-240 |
2.76e-40 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 140.51 E-value: 2.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtaPDGsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:TIGR02315 2 LEVENLSKVY--PNG--KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrkl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ----GYVFQQGSLFPWLTVEENIAFG-LKAQ-------GIYKEHEADAARYI-EMVGLHGFEQAYPHQISGGMAQRVAIA 171
Cdd:TIGR02315 78 rrriGMIFQHYNLIERLTVLENVLHGrLGYKptwrsllGRFSEEDKERALSAlERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 172 RALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGL--KAGEI 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
47-233 |
6.65e-40 |
|
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: 136.61 E-value: 6.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 47 HALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRgyvfqqgslfpwltveeniafg 126
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 127 lkaqgiykeheadAARYIEMVglhgfeqaypHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIW 206
Cdd:cd00267 71 -------------LRRRIGYV----------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA 127
|
170 180
....*....|....*....|....*..
gi 505262942 207 EQyHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:cd00267 128 EE-GRTVIIVTHDPELAELAADRVIVL 153
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
49-242 |
1.28e-39 |
|
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: 138.25 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEG---------PNPKRGYVFQQGSLFPWLTV 119
Cdd:TIGR02211 21 LKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKlssneraklRNKKLGFIYQFHHLLPDFTA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 120 EENIAFGLKAQGIYKEHEADAARYI-EMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADL 198
Cdd:TIGR02211 101 LENVAMPLLIGKKSVKEAKERAYEMlEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKII 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505262942 199 QDRLLDIWEQYHMTMILVTHDvDEAIYLGSRVVIMtpRPGRIKE 242
Cdd:TIGR02211 181 FDLMLELNRELNTSFLVVTHD-LELAKKLDRVLEM--KDGQLFN 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
48-233 |
3.65e-39 |
|
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: 136.73 E-value: 3.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI--EGPNPKR--GYVFQQGSLFPWLTVEENI 123
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrEPREVRRriGIVFQDLSVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 124 AFGLKAQGiYKEHEAD--AARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDR 201
Cdd:cd03265 95 YIHARLYG-VPGAERRerIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY 173
|
170 180 190
....*....|....*....|....*....|..
gi 505262942 202 LLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:cd03265 174 IEKLKEEFGMTILLTTHYMEEAEQLCDRVAII 205
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
47-230 |
3.66e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 137.86 E-value: 3.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 47 HALSDVSLSIYPGELVSIIGPSGCGKTTLLR-------LIAGLDHpqSGTLSLAGEPIEGP--NP----KR-GYVFQQGS 112
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGEDIYDPdvDVvelrRRvGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 113 LFPwLTVEENIAFGLKAQGIYKEHEADAA--RYIEMVG--------LHgfEQAYphQISGGMAQRVAIARALIDHPDVLL 182
Cdd:COG1117 103 PFP-KSIYDNVAYGLRLHGIKSKSELDEIveESLRKAAlwdevkdrLK--KSAL--GLSGGQQQRLCIARALAVEPEVLL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505262942 183 LDEPMGALDSFTRADLQDRLLDIWEQYhmTMILVTHDVDEAiylgSRV 230
Cdd:COG1117 178 MDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQA----ARV 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
49-242 |
7.97e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 136.80 E-value: 7.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNP-------------KRGYVFQQGSLFP 115
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkglirqlrqHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 116 WLTVEENIAFG-LKAQGIYKEH-EADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSF 193
Cdd:PRK11264 99 HRTVLENIIEGpVIVKGEPKEEaTARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505262942 194 TRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIMTprPGRIKE 242
Cdd:PRK11264 179 LVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMD--QGRIVE 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
53-241 |
9.53e-39 |
|
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: 135.76 E-value: 9.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 53 SLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---GYVFQQGSLFPWLTVEENIAFG--- 126
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQrpvSMLFQENNLFAHLTVRQNIGLGlhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 127 -LKAQGIYKEHEADAARyieMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDI 205
Cdd:TIGR01277 98 gLKLNAEQQEKVVDAAQ---QVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 505262942 206 WEQYHMTMILVTHDVDEAIYLGSRVVIMTprPGRIK 241
Cdd:TIGR01277 175 CSERQRTLLMVTHHLSDARAIASQIAVVS--QGKIK 208
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
19-233 |
1.89e-38 |
|
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: 142.04 E-value: 1.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 19 ADVPAGVNPELSIEHVSreFTAPDGSVvhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIE 98
Cdd:TIGR02857 312 APVTAAPASSLEFSGVS--VAYPGRRP--ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 99 GPNPKR-----GYVFQQGSLFPWlTVEENIAFGLKAQGiykehEADAARYIEMVGLHGFEQAYP-----------HQISG 162
Cdd:TIGR02857 388 DADADSwrdqiAWVPQHPFLFAG-TIAENIRLARPDAS-----DAEIREALERAGLDEFVAALPqgldtpigeggAGLSG 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505262942 163 GMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYhmTMILVTHDvDEAIYLGSRVVIM 233
Cdd:TIGR02857 462 GQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHR-LALAALADRIVVL 529
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
49-240 |
2.40e-38 |
|
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: 133.33 E-value: 2.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPK-----RGYVFQqgslfpwltveeni 123
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKelarkIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 124 afglkaqgiykeheadaarYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLL 203
Cdd:cd03214 81 -------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLR 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 505262942 204 DIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:cd03214 142 RLARERGKTVVMVLHDLNLAARYADRVILL--KDGRI 176
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
49-249 |
5.96e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 135.63 E-value: 5.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPN-----PKRGYVFQQ-GSLFPWLTVEEN 122
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwdirHKIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 123 IAFGLKAQGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDR 201
Cdd:PRK13650 103 VAFGLENKGIpHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 202 LLDIWEQYHMTMILVTHDVDEaIYLGSRVVIM---------TPRP--GRIKEIVPINLD 249
Cdd:PRK13650 183 IKGIRDDYQMTVISITHDLDE-VALSDRVLVMkngqvestsTPRElfSRGNDLLQLGLD 240
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
46-219 |
8.39e-38 |
|
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: 133.30 E-value: 8.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 46 VHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEG------PNPKR--GYVFQQGSLFPWL 117
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraiPYLRRkiGVVFQDFRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 118 TVEENIAFGLKAqgIYKEHEADAARY---IEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDsft 194
Cdd:cd03292 94 NVYENVAFALEV--TGVPPREIRKRVpaaLELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD--- 168
|
170 180
....*....|....*....|....*...
gi 505262942 195 rADLQDRLLDIWEQYHM---TMILVTHD 219
Cdd:cd03292 169 -PDTTWEIMNLLKKINKagtTVVVATHA 195
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-233 |
1.06e-37 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 137.86 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 24 GVNPELSIEHV----SREFTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI-- 97
Cdd:PRK10070 15 GEHPQRAFKYIeqglSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIak 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 98 -------EGPNPKRGYVFQQGSLFPWLTVEENIAFGLKAQGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVA 169
Cdd:PRK10070 95 isdaelrEVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGInAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505262942 170 IARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK10070 175 LARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-218 |
5.06e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 135.68 E-value: 5.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 19 ADVPAGVNPELSIEHVSreFTAPDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIE 98
Cdd:COG1132 330 AVPLPPVRGEIEFENVS--FSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 99 GPNPKR-----GYVFQQGSLFPwLTVEENIAFGLKaqgiykehEADAARYIE---MVGLHGFEQAYPH-----------Q 159
Cdd:COG1132 406 DLTLESlrrqiGVVPQDTFLFS-GTIRENIRYGRP--------DATDEEVEEaakAAQAHEFIEALPDgydtvvgergvN 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 160 ISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEqyHMTMILVTH 218
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAH 533
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
47-240 |
5.94e-36 |
|
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: 128.10 E-value: 5.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 47 HALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI---EGPNPKRGYVFQQGSLFPWLTVEENI 123
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqknIEALRRIGALIEAPGFYPNLTARENL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 124 AFGLKAQGI-YKEHEadaaRYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRL 202
Cdd:cd03268 94 RLLARLLGIrKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELI 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 505262942 203 LDiWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:cd03268 170 LS-LRDQGITVLISSHLLSEIQKVADRIGII--NKGKL 204
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
19-242 |
6.29e-36 |
|
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: 135.28 E-value: 6.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 19 ADVPAGVNPELSIEHVSreFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIE 98
Cdd:COG4987 324 EPAPAPGGPSLELEDVS--FRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 99 GPNPKR-----GYVFQQGSLFPwLTVEENIAFGLKAQGiykehEADAARYIEMVGLHGFEQAYPH-----------QISG 162
Cdd:COG4987 401 DLDEDDlrrriAVVPQRPHLFD-TTLRENLRLARPDAT-----DEELWAALERVGLGDWLAALPDgldtwlgeggrRLSG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 163 GMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEqyHMTMILVTHDvDEAIYLGSRVVIMtpRPGRIKE 242
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHR-LAGLERMDRILVL--EDGRIVE 549
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
26-244 |
6.79e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 129.73 E-value: 6.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 26 NPELSIEHVSREFTapdGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPN---- 101
Cdd:PRK13632 5 SVMIKVENVSFSYP---NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlkei 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 102 -PKRGYVFQQ-GSLFPWLTVEENIAFGLKAQGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHP 178
Cdd:PRK13632 82 rKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVpPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 179 DVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIyLGSRVVIMTP----RPGRIKEIV 244
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEgkliAQGKPKEIL 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-240 |
8.35e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 134.38 E-value: 8.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 26 NPELSIEHVSREFTApdgsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR- 104
Cdd:COG1129 2 EPLLEMRGISKSFGG-----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -----GYVFQQGSLFPWLTVEENIAFG--LKAQGI--YKEHEADAARYIEMVGLHgFEqayPHQISG--GMAQR--VAIA 171
Cdd:COG1129 77 qaagiAIIHQELNLVPNLSVAENIFLGrePRRGGLidWRAMRRRARELLARLGLD-ID---PDTPVGdlSVAQQqlVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505262942 172 RALIDHPDVLLLDEPMGALdsfTRADlQDRLLDIWEQYH---MTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:COG1129 153 RALSRDARVLILDEPTASL---TERE-VERLFRIIRRLKaqgVAIIYISHRLDEVFEIADRVTVL--RDGRL 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
49-240 |
8.62e-36 |
|
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: 129.05 E-value: 8.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSG-TLSLAGEPIEGPN-----PKRGYV--FQQGSLFPWLTVE 120
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDvwelrKRIGLVspALQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 121 ENIAFGLKAQ-GIYKEHEAD----AARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTR 195
Cdd:COG1119 99 DVVLSGFFDSiGLYREPTDEqrerARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGAR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505262942 196 ADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:COG1119 179 ELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL--KDGRV 221
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
48-269 |
3.97e-35 |
|
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: 128.66 E-value: 3.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAG-EPIEGPNPKR---GYVFQQGSLFPWLTVEENI 123
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGyDVVREPRKVRrsiGIVPQYASVDEDLTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 124 AFGLKAQGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRL 202
Cdd:TIGR01188 88 EMMGRLYGLpKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 203 LDIWEQyHMTMILVTHDVDEAIYLGSRVVIMtpRPGR-IKEIVPINLdaRDRVSDEFAAYRKQLLTKL 269
Cdd:TIGR01188 168 RALKEE-GVTILLTTHYMEEADKLCDRIAII--DHGRiIAEGTPEEL--KRRLGKDTLESRPRDIQSL 230
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
49-191 |
5.88e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 127.15 E-value: 5.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNP-----KRGYVFQQGSL-FPWlTVEEN 122
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPwelarRRAVLPQHSSLaFPF-TVEEV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 123 IAFGLKAQGIYKEHEADAAR-YIEMVGLHGF-EQAYPhQISGGMAQRVAIARALI-------DHPDVLLLDEPMGALD 191
Cdd:COG4559 96 VALGRAPHGSSAAQDRQIVReALALVGLAHLaGRSYQ-TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD 172
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
48-229 |
6.39e-35 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 126.81 E-value: 6.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLD--HPQ---SGTLSLAGEPIEGPNPKR-------GYVFQQGSLFP 115
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlNPEvtiTGSIVYNGHNIYSPRTDTvdlrkeiGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 116 wLTVEENIAFGLKAQGIYKEHEADAARYIEMVGLHGFEQAYPH------QISGGMAQRVAIARALIDHPDVLLLDEPMGA 189
Cdd:PRK14239 100 -MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRlhdsalGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505262942 190 LDSFTRADLQDRLLDIWEQYhmTMILVTHDVDEAIYLGSR 229
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDR 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
46-240 |
8.83e-35 |
|
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: 125.62 E-value: 8.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 46 VHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR------GYVFQQGSLFPWLTV 119
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHEraragiGYVPEGRRIFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 120 EENIAFGLkaqgiYKEHEADAARYIEMV-----GLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFT 194
Cdd:cd03224 93 EENLLLGA-----YARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505262942 195 RADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:cd03224 168 VEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVL--ERGRV 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
42-240 |
1.25e-34 |
|
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: 125.01 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 42 DGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR-----GYVFQQGSLFpW 116
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrrniGYVPQDVTLF-Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 117 LTVEENIAFGLKaqgiykehEADAARYI---EMVGLHGFEQAYPH-----------QISGGMAQRVAIARALIDHPDVLL 182
Cdd:cd03245 92 GTLRDNITLGAP--------LADDERILraaELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 183 LDEPMGALDSFTRADLQDRLldiwEQY--HMTMILVTHDVdEAIYLGSRVVIMtpRPGRI 240
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERL----RQLlgDKTLIIITHRP-SLLDLVDRIIVM--DSGRI 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
26-219 |
1.36e-34 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 132.54 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 26 NPELSIEHVSREFTAPDGSVVhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNP--- 102
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVE-VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 103 ---KR---GYVFQQGSLFPWLTVEENIafglKAQGIY--KEHEADAARYIEMVGLHGFEQA---YPHQISGGMAQRVAIA 171
Cdd:PRK10535 81 aqlRRehfGFIFQRYHLLSHLTAAQNV----EVPAVYagLERKQRLLRAQELLQRLGLEDRveyQPSQLSGGQQQRVSIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505262942 172 RALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHmTMILVTHD 219
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHD 203
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
48-233 |
2.01e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 126.32 E-value: 2.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR-------GYVFQ--QGSLFPWlT 118
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdirkkvGLVFQypEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 119 VEENIAFGLKAQGIYKEH-EADAARYIEMVGL--HGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTR 195
Cdd:PRK13637 101 IEKDIAFGPINLGLSEEEiENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 505262942 196 ADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVM 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
30-233 |
2.39e-34 |
|
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: 123.91 E-value: 2.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 30 SIEHVSREFtaPDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIegPNPKR----G 105
Cdd:cd03226 1 RIENISFSY--KKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI--KAKERrksiG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 106 YVFQQ-GSLFPWLTVEENIAFGLKAQGIYKEheaDAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLD 184
Cdd:cd03226 75 YVMQDvDYQLFTDSVREELLLGLKELDAGNE---QAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505262942 185 EPMGALDSFTRADLQDRLLDIWEQYHmTMILVTHDVDEAIYLGSRVVIM 233
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLL 199
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
29-242 |
4.27e-34 |
|
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: 129.80 E-value: 4.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTAPDGsVVHALSDVSLSIYPGELVSIIGPSGCGKT----TLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR 104
Cdd:COG4172 7 LSVEDLSVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ---------GYVFQQ--GSLFPWLTVEENIAFGLKA-QGIYKEH-EADAARYIEMVGLHGFEQ---AYPHQISGGMAQRV 168
Cdd:COG4172 86 lrrirgnriAMIFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAaRARALELLERVGIPDPERrldAYPHQLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 169 AIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDvdeaiyLG------SRVVIMtpRPGRIKE 242
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD------LGvvrrfaDRVAVM--RQGEIVE 237
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
29-233 |
8.12e-34 |
|
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: 122.86 E-value: 8.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTAPDGsVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAG-----EPIEGPNpK 103
Cdd:cd03266 2 ITADALTKRFRDVKK-TVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAEARR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 104 RGYVFQQGSLFPWLTVEENIAFGLKAQGIyKEHEADaARYIEMVGLHGFEQAYPHQISG---GMAQRVAIARALIDHPDV 180
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGL-KGDELT-ARLEELADRLGMEELLDRRVGGfstGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505262942 181 LLLDEPMGALDSFTRADLQDRLLDIWEQYHmTMILVTHDVDEAIYLGSRVVIM 233
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVL 209
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
29-240 |
1.11e-33 |
|
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: 120.61 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTApdgsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKrgyvf 108
Cdd:cd03216 1 LELRGITKRFGG-----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 109 qqgslfpwltveeniafglkaqgiykehEADAARyIEMVglhgfeqaypHQISGGMAQRVAIARALIDHPDVLLLDEPMG 188
Cdd:cd03216 71 ----------------------------DARRAG-IAMV----------YQLSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505262942 189 ALDsftrADLQDRLLDIWEQYH---MTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:cd03216 112 ALT----PAEVERLFKVIRRLRaqgVAVIFISHRLDEVFEIADRVTVL--RDGRV 160
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
29-234 |
1.49e-33 |
|
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: 121.92 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtaPDGsvvHALSDVSLSIYPGeLVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI-EGPNPKR--- 104
Cdd:cd03264 1 LQLENLTKRY--GKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlKQPQKLRrri 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 GYVFQQGSLFPWLTVEENIAFGLKAQGIY-KEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLL 183
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPsKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505262942 184 DEPMGALDSFTRADLQDRLLDIWEQyhMTMILVTHDVDEAIYLGSRVVIMT 234
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLN 203
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
34-231 |
3.23e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 124.31 E-value: 3.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 34 VSREFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNP--------KRG 105
Cdd:PRK11308 17 VKRGLFKPERLV-KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqkllrqKIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 106 YVFQQ--GSLFPWLTV----EE--NIAFGLKAQgiykEHEADAARYIEMVGLHG-FEQAYPHQISGGMAQRVAIARALID 176
Cdd:PRK11308 96 IVFQNpyGSLNPRKKVgqilEEplLINTSLSAA----ERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505262942 177 HPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHD--VDEAI-------YLGsRVV 231
Cdd:PRK11308 172 DPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDlsVVEHIadevmvmYLG-RCV 234
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
49-246 |
5.16e-33 |
|
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: 122.22 E-value: 5.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRGYVFQQ----------GSLFPWLT 118
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRdvqlvfqdspSAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 119 VEENIAFGLKAQGIYKEHE--ADAARYIEMVGLHG-FEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTR 195
Cdd:TIGR02769 107 VRQIIGEPLRHLTSLDESEqkARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505262942 196 ADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEIVPI 246
Cdd:TIGR02769 187 AVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVM--DKGQIVEECDV 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
51-233 |
1.23e-32 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 123.06 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 51 DVSLSIyPGELVS-IIGPSGCGKTTLLRLIAGLDHPQSGTLSLAG-------EPIEGPNPKR--GYVFQQGSLFPWLTVE 120
Cdd:PRK11144 16 TVNLTL-PAQGITaIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLPPEKRriGYVFQDARLFPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 121 ENIAFGLKAQgiykeheaDAARYIEMVGLHGFE---QAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRAD 197
Cdd:PRK11144 95 GNLRYGMAKS--------MVAQFDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 505262942 198 LQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHSLDEILRLADRVVVL 202
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-233 |
3.64e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 119.81 E-value: 3.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEG-PNPKR--- 104
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlPEYKRaky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -GYVFQ---QGSlFPWLTVEENIA--------FGLKaQGIYKEHEADAARYIEMVGLhGFEQAYPHQI---SGGmaQRVA 169
Cdd:COG1101 82 iGRVFQdpmMGT-APSMTIEENLAlayrrgkrRGLR-RGLTKKRRELFRELLATLGL-GLENRLDTKVgllSGG--QRQA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 170 IA--RALIDHPDVLLLDEPMGALDSFTRA---DLQDRLLdiwEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:COG1101 157 LSllMATLTKPKLLLLDEHTAALDPKTAAlvlELTEKIV---EENNLTTLMVTHNMEQALDYGNRLIMM 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
46-233 |
5.13e-32 |
|
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: 118.55 E-value: 5.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 46 VHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR------GYVFQQGSLFPWLTV 119
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRiarlgiGYVPEGRRIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 120 EENIAFGLKAQGIYKEHEADAARYIEMvglhgfeqaYP------HQI----SGGMAQRVAIARALIDHPDVLLLDEP-MG 188
Cdd:COG0410 96 EENLLLGAYARRDRAEVRADLERVYEL---------FPrlkerrRQRagtlSGGEQQMLAIGRALMSRPKLLLLDEPsLG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505262942 189 aLDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:COG0410 167 -LAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVL 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
49-235 |
9.57e-32 |
|
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: 116.88 E-value: 9.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQ--SGTLSLAGEPIEGPNPKR--GYVFQQGSLFPWLTVEENIA 124
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSFRKiiGYVPQDDILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 125 FGLKAQGiykeheadaaryiemvglhgfeqayphqISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQdRLLD 204
Cdd:cd03213 105 FAAKLRG----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM-SLLR 155
|
170 180 190
....*....|....*....|....*....|..
gi 505262942 205 IWEQYHMTMILVTHDV-DEAIYLGSRVVIMTP 235
Cdd:cd03213 156 RLADTGRTIICSIHQPsSEIFELFDKLLLLSQ 187
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
44-240 |
1.10e-31 |
|
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: 115.99 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 44 SVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR------GYV----FQQGsL 113
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDairagiAYVpedrKREG-L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 114 FPWLTVEENIAFglkaqgiykeheadaaryiemvglhgfeqayPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSF 193
Cdd:cd03215 90 VLDLSVAENIAL-------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505262942 194 TRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:cd03215 139 AKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVM--YEGRI 182
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
31-233 |
1.23e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 118.64 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 31 IEHVSREFTAPDGSVvhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNP-------K 103
Cdd:PRK13639 2 LETRDLKYSYPDGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllevrkT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 104 RGYVFQQ--GSLF-PwlTVEENIAFGLKAQGIYKEH-EADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPD 179
Cdd:PRK13639 80 VGIVFQNpdDQLFaP--TVEEDVAFGPLNLGLSKEEvEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505262942 180 VLLLDEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVM 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
29-246 |
1.34e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 118.64 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTAPDGSVVHA----LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPN--P 102
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSGKHQhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 103 KRGY------VFQQ--GSLFPWLTVEENIA------FGLKAqgiyKEHEADAARYIEMVGLH-GFEQAYPHQISGGMAQR 167
Cdd:PRK10419 84 RKAFrrdiqmVFQDsiSAVNPRKTVREIIReplrhlLSLDK----AERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 168 VAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEIVPI 246
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVM--DNGQIVETQPV 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
26-243 |
1.68e-31 |
|
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: 122.60 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 26 NPELSIEHVSREFTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLS-LAGE--------- 95
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDewvdmtkpg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 96 PIEGPNPKR--GYVFQQGSLFPWLTVEENIAfglKAQGIYKEHEADAARYIEMVGLHGFEQ--------AYPHQISGGMA 165
Cdd:TIGR03269 357 PDGRGRAKRyiGILHQEYDLYPHRTVLDNLT---EAIGLELPDELARMKAVITLKMVGFDEekaeeildKYPDELSEGER 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 166 QRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEI 243
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM--RDGKIVKI 509
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
49-219 |
2.30e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 122.10 E-value: 2.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAgepiegPNPKRGYVFQQGSLFPWLTVEENIAFGLK 128
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------KGLRIGYLPQEPPLDDDLTVLDTVLDGDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 129 -----------AQGIYKEHEADAARYIE--------------------MVGLhGFEQAYPHQ----ISGGMAQRVAIARA 173
Cdd:COG0488 88 elraleaeleeLEAKLAEPDEDLERLAElqeefealggweaearaeeiLSGL-GFPEEDLDRpvseLSGGWRRRVALARA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505262942 174 LIDHPDVLLLDEPMGALDSFTRADLQDRLLdiweQYHMTMILVTHD 219
Cdd:COG0488 167 LLSEPDLLLLDEPTNHLDLESIEWLEEFLK----NYPGTVLVVSHD 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
48-233 |
2.94e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 118.20 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIE-GPNPKR--------GYVFQ--QGSLFPw 116
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKlkplrkkvGIVFQfpEHQLFE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 117 LTVEENIAFGLKAQGIYKEH-EADAARYIEMVGL-HGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFT 194
Cdd:PRK13634 101 ETVEKDICFGPMNFGVSEEDaKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 505262942 195 RADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVM 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
49-242 |
2.96e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 116.84 E-value: 2.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI---------EGPNPKRGYVFQQGSLFPWLTV 119
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssaakaELRNQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 120 EENIAFGLKAQGIYKEHEADAARyiEM---VGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTrA 196
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRAL--EMlaaVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN-A 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505262942 197 DLQDRLLDIWEQYHMTMIL-VTHDVDEAIYLgSRVVIMtpRPGRIKE 242
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAFLvVTHDLQLAKRM-SRQLEM--RDGRLTA 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
48-223 |
3.95e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 115.02 E-value: 3.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGepiegpNPKRGYVFQQGSL---FPwLTVEENIA 124
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG------GARVAYVPQRSEVpdsLP-LTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 125 FGLKA-QGIYKEHEADAARYI----EMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQ 199
Cdd:NF040873 80 MGRWArRGLWRRLTRDDRAAVddalERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180
....*....|....*....|....
gi 505262942 200 DrLLDIWEQYHMTMILVTHDVDEA 223
Cdd:NF040873 160 A-LLAEEHARGATVVVVTHDLELV 182
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
25-250 |
4.38e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 117.50 E-value: 4.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 25 VNPELSIEHVSreFTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPN--- 101
Cdd:PRK13642 1 MNKILEVENLV--FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 102 --PKRGYVFQQ-GSLFPWLTVEENIAFGLKAQGIYKEH---EADAAryIEMVGLHGFEQAYPHQISGGMAQRVAIARALI 175
Cdd:PRK13642 79 lrRKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEmikRVDEA--LLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505262942 176 DHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYlGSRVVIMtpRPGR-IKEIVPINLDA 250
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVM--KAGEiIKEAAPSELFA 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
49-223 |
9.59e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 115.26 E-value: 9.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---------GYVFQQGSLFPWLTV 119
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraklrakhvGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 120 EENIAFGLKAQGIY-KEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADL 198
Cdd:PRK10584 106 LENVELPALLRGESsRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180
....*....|....*....|....*
gi 505262942 199 QDRLLDIWEQYHMTMILVTHDVDEA 223
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
49-233 |
1.45e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 115.25 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPK-----RGYVFQQGSL-FPWlTVEEN 122
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarrRAVLPQHSSLsFPF-TVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 123 IAFGLKA-QGIYKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARAL--IDHPD----VLLLDEPMGALdsftr 195
Cdd:PRK13548 97 VAMGRAPhGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqLWEPDgpprWLLLDEPTSAL----- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505262942 196 aDL--QDRLLDIWEQY----HMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK13548 172 -DLahQHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLL 214
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
34-232 |
2.19e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 116.34 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 34 VSREFTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLS------------------LAGE 95
Cdd:PRK13651 8 IVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekekvLEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 96 PIEGPNPKR-----------GYVFQ--QGSLFPwLTVEENIAFGLKAQGIYKEhEAD--AARYIEMVGL-HGFEQAYPHQ 159
Cdd:PRK13651 88 VIQKTRFKKikkikeirrrvGVVFQfaEYQLFE-QTIEKDIIFGPVSMGVSKE-EAKkrAAKYIELVGLdESYLQRSPFE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505262942 160 ISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADlqdrLLDIWEQYHM---TMILVTHDVDEAIYLGSRVVI 232
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKE----ILEIFDNLNKqgkTIILVTHDLDNVLEWTKRTIF 237
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
50-224 |
2.56e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 115.25 E-value: 2.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 50 SDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRGY--------VFQQGSLFPWLTVEE 121
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYtvrkrmsmLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 122 NIAFGLkaqgiyKEHEADAARYI--------EMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSF 193
Cdd:PRK11831 104 NVAYPL------REHTQLPAPLLhstvmmklEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPI 177
|
170 180 190
....*....|....*....|....*....|.
gi 505262942 194 TRADLQDRLLDIWEQYHMTMILVTHDVDEAI 224
Cdd:PRK11831 178 TMGVLVKLISELNSALGVTCVVVSHDVPEVL 208
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
50-218 |
3.11e-30 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 112.98 E-value: 3.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 50 SDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEgpnpKRGYVFQQGSLF--------PWLTVEE 121
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRDEYHQDLLYlghqpgikTELTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 122 NIAFGLKAQGIYkeHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDR 201
Cdd:PRK13538 94 NLRFYQRLHGPG--DDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEAL 171
|
170
....*....|....*..
gi 505262942 202 LLDIWEQYHMTmILVTH 218
Cdd:PRK13538 172 LAQHAEQGGMV-ILTTH 187
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-219 |
3.26e-30 |
|
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: 119.47 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 15 RQTLADVPAGVNP--------ELSIEHVSrefTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQ 86
Cdd:COG4618 309 NELLAAVPAEPERmplprpkgRLSVENLT---VVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 87 SGTLSLAGEPIEGPNPKR-----GYVFQQGSLFPWlTVEENIA-FGlkaqgiykehEADAARYIE---MVGLH----GFE 153
Cdd:COG4618 386 AGSVRLDGADLSQWDREElgrhiGYLPQDVELFDG-TIAENIArFG----------DADPEKVVAaakLAGVHemilRLP 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505262942 154 QAYPHQI-------SGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHD 219
Cdd:COG4618 455 DGYDTRIgeggarlSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHR 526
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
47-233 |
3.62e-30 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 113.77 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 47 HALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR------GYVFQQGSLFPWLTVE 120
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHEraragiAYVPQGREIFPRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 121 ENIAFGLKAQGiYKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQD 200
Cdd:TIGR03410 94 ENLLTGLAALP-RRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGR 172
|
170 180 190
....*....|....*....|....*....|...
gi 505262942 201 RLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:TIGR03410 173 VIRRLRAEGGMAILLVEQYLDFARELADRYYVM 205
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
29-233 |
4.38e-30 |
|
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: 111.92 E-value: 4.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSreFTAPDGSVVhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIE--GPNPKR-- 104
Cdd:cd03246 1 LEVENVS--FRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwDPNELGdh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -GYVFQQGSLFPWlTVEENIafglkaqgiykeheadaaryiemvglhgfeqayphqISGGMAQRVAIARALIDHPDVLLL 183
Cdd:cd03246 78 vGYLPQDDELFSG-SIAENI------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505262942 184 DEPMGALDSFTRADLQDRLLDIwEQYHMTMILVTHDVdEAIYLGSRVVIM 233
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRP-ETLASADRILVL 168
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
27-290 |
4.87e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 115.29 E-value: 4.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFTapDGSVVHALSdvsLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNP---- 102
Cdd:PRK13537 6 APIDFRNVEKRYG--DKLVVDGLS---FHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARharq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 103 KRGYVFQQGSLFPWLTVEENIA-----FGLKAQGIykehEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDH 177
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLLvfgryFGLSAAAA----RALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 178 PDVLLLDEPMGALDSftradlQDRLLdIWEQYH------MTMILVTHDVDEAIYLGSRV-VIMTPRpgRIKEIVP----- 245
Cdd:PRK13537 157 PDVLVLDEPTTGLDP------QARHL-MWERLRsllargKTILLTTHFMEEAERLCDRLcVIEEGR--KIAEGAPhalie 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 505262942 246 --INLDARDRVSDEFAAYRKQLLTklhFDAHEEHAGDA---FVGDAQELL 290
Cdd:PRK13537 228 seIGCDVIEIYGPDPVALRDELAP---LAERTEISGETlfcYVRDPEPLH 274
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
27-239 |
8.07e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.82 E-value: 8.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFtapdGSVVhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR-- 104
Cdd:COG3845 4 PALELRGITKRF----GGVV-ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDai 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ----GYVFQQGSLFPWLTVEENIAFGLKAQGIYKEHEADAARYI-EMVGLHGFE---QAYPHQISGGMAQRVAIARALID 176
Cdd:COG3845 79 algiGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIrELSERYGLDvdpDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505262942 177 HPDVLLLDEP------------MGALDSFTRADLqdrlldiweqyhmTMILVTHDVDEAIYLGSRVVIMtpRPGR 239
Cdd:COG3845 159 GARILILDEPtavltpqeadelFEILRRLAAEGK-------------SIIFITHKLREVMAIADRVTVL--RRGK 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
49-242 |
1.04e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 113.14 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRG------------------YVFQQ 110
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkvadknqlrllrtrltMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 111 GSLFPWLTVEENIAFG-LKAQGIYK-EHEADAARYIEMVGLHGFEQA-YPHQISGGMAQRVAIARALIDHPDVLLLDEPM 187
Cdd:PRK10619 101 FNLWSHMTVLENVMEApIQVLGLSKqEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 188 GALDsftrADLQDRLLDIWEQYH---MTMILVTHDVDEAIYLGSRVVIMtpRPGRIKE 242
Cdd:PRK10619 181 SALD----PELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFL--HQGKIEE 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-219 |
1.39e-29 |
|
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: 117.46 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 19 ADVPAGVnPELSIEHVSreFTAPDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI- 97
Cdd:TIGR02868 326 GAVGLGK-PTLELRDLS--AGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVs 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 98 ---EGPNPKR-GYVFQQGSLFPwLTVEENIAFGLKaqgiyKEHEADAARYIEMVGLHGFEQAYPH-----------QISG 162
Cdd:TIGR02868 401 sldQDEVRRRvSVCAQDAHLFD-TTVRENLRLARP-----DATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505262942 163 GMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYhmTMILVTHD 219
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHH 529
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
26-242 |
2.42e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 111.34 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 26 NPELSIEHVSreFTAPDGSVVHalsDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR- 104
Cdd:PRK10247 5 SPLLQLQNVG--YLAGDAKILN---NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ----GYVFQQGSLFPwLTVEENIAFGLKAQGIYKEHEADAAryiemvGLHGFE------QAYPHQISGGMAQRVAIARAL 174
Cdd:PRK10247 80 rqqvSYCAQTPTLFG-DTVYDNLIFPWQIRNQQPDPAIFLD------DLERFAlpdtilTKNIAELSGGEKQRISLIRNL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 175 IDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEaIYLGSRVVIMTPRPGRIKE 242
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQPHAGEMQE 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
22-233 |
2.55e-29 |
|
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: 111.09 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 22 PAGVNPELSIEHVSREFTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGE---PIE 98
Cdd:cd03220 11 PTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssLLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 99 GpnpkrGYVFQqgslfPWLTVEENIAFGLKAQGIYKEhEADaARYIEMVGLHGFEQAYPHQI---SGGMAQRVAIARALI 175
Cdd:cd03220 91 L-----GGGFN-----PELTGRENIYLNGRLLGLSRK-EID-EKIDEIIEFSELGDFIDLPVktySSGMKARLAFAIATA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 176 DHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:cd03220 159 LEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVL 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-233 |
3.54e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.15 E-value: 3.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 23 AGVNPELSIEHVSREFtapDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNP 102
Cdd:PRK13648 2 EDKNSIIVFKNVSFQY---QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 103 KR-----GYVFQQ-GSLFPWLTVEENIAFGLKAQGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALI 175
Cdd:PRK13648 79 EKlrkhiGIVFQNpDNQFVGSIVKYDVAFGLENHAVpYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 176 DHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYlGSRVVIM 233
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVM 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
28-234 |
1.08e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.98 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 28 ELSIEHVSREFTAPDGSvvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR--- 104
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGT--KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 --GYVFQ--QGSLFPwLTVEENIAFGLKAQGIYK-EHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPD 179
Cdd:PRK13647 80 kvGLVFQdpDDQVFS-STVWDDVAFGPVNMGLDKdEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505262942 180 VLLLDEPMGALDSFTRADLQDrLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMT 234
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLME-ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLK 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
29-233 |
1.35e-28 |
|
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: 108.91 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapdGSVVhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI-EGPNPKRGYV 107
Cdd:cd03269 1 LEVENVTKRF----GRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLdIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 108 FQQGSLFPWLTVEENIAFGLKAQGiYKEHEA--DAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDE 185
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKG-LKKEEArrRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505262942 186 PMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLL 201
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-218 |
1.49e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 115.20 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 22 PAGVNPELSIEHVSreFTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPN 101
Cdd:TIGR00958 472 PLNLEGLIEFQDVS--FSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 102 -----PKRGYVFQQGSLFPWlTVEENIAFGLKAqgiYKEHEADAAryIEMVGLHGFEQAYPH-----------QISGGMA 165
Cdd:TIGR00958 550 hhylhRQVALVGQEPVLFSG-SVRENIAYGLTD---TPDEEIMAA--AKAANAHDFIMEFPNgydtevgekgsQLSGGQK 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505262942 166 QRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDrlldiW-EQYHMTMILVTH 218
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDAECEQLLQE-----SrSRASRTVLLIAH 672
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
32-226 |
1.62e-28 |
|
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: 109.63 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 32 EHVSreFTAPDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPN-----PKRGY 106
Cdd:cd03253 4 ENVT--FAYDPGRPV--LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTldslrRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 107 VFQQGSLFPwLTVEENIAFG-LKAQGIYKEHEADAAR-----------YIEMVGLHGFeqayphQISGGMAQRVAIARAL 174
Cdd:cd03253 80 VPQDTVLFN-DTIGYNIRYGrPDATDEEVIEAAKAAQihdkimrfpdgYDTIVGERGL------KLSGGEKQRVAIARAI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 175 IDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEqyHMTMILVTH------DVDEAIYL 226
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHrlstivNADKIIVL 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
29-194 |
1.71e-28 |
|
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: 109.28 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTAPDGSVVhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQ---SGTLSLAGEPIEGPNPKR- 104
Cdd:cd03234 4 LPWWDVGLKAKNWNKYAR-ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -GYVFQQGSLFPWLTVEENIAFG-------LKAQGIYKEHEADAAryIEMVGLHGFEQAYPHQISGGMAQRVAIARALID 176
Cdd:cd03234 83 vAYVRQDDILLPGLTVRETLTYTailrlprKSSDAIRKKRVEDVL--LRDLALTRIGGNLVKGISGGERRRVSIAVQLLW 160
|
170
....*....|....*...
gi 505262942 177 HPDVLLLDEPMGALDSFT 194
Cdd:cd03234 161 DPKVLILDEPTSGLDSFT 178
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
29-223 |
3.33e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.89 E-value: 3.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSreFTAPDgSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGL----DHPQSGT----LSLAGEPIEGP 100
Cdd:PRK13640 6 VEFKHVS--FTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpdDNPNSKItvdgITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 101 NPKRGYVFQQ-GSLFPWLTVEENIAFGLKAQGIYK-EHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHP 178
Cdd:PRK13640 83 REKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRpEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505262942 179 DVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEA 223
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
29-218 |
4.44e-28 |
|
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: 107.56 E-value: 4.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGepiegpnpKRGYVF 108
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------SIAYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 109 QQgslfPWL---TVEENIAFGlkaqgiykeHEADAARYIEMVGLHGFE---QAYPHQI-----------SGGMAQRVAIA 171
Cdd:cd03250 73 QE----PWIqngTIRENILFG---------KPFDEERYEKVIKACALEpdlEILPDGDlteigekginlSGGQKQRISLA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505262942 172 RALIDHPDVLLLDEPMGALDSFTRADLQDR-LLDIWeQYHMTMILVTH 218
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIFENcILGLL-LNNKTRILVTH 186
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
25-219 |
4.52e-28 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 109.16 E-value: 4.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 25 VNPELSIEHVSREFTAPDG----SVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIE-G 99
Cdd:COG4167 1 MSALLEVRNLSKTFKYRTGlfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEyG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 100 PNPKRG----YVFQ--QGSLFPWLTVEENIAFGLKAQGIYKEhEADAARYIE---MVGLHGfEQA--YPHQISGGMAQRV 168
Cdd:COG4167 81 DYKYRCkhirMIFQdpNTSLNPRLNIGQILEEPLRLNTDLTA-EEREERIFAtlrLVGLLP-EHAnfYPHMLSSGQKQRV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505262942 169 AIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHD 219
Cdd:COG4167 159 ALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQH 209
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
46-233 |
8.13e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 108.74 E-value: 8.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 46 VHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR-----GYVFQQ--GSLFPwLT 118
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrkfvGLVFQNpdDQIFS-PT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 119 VEENIAFGLKAQGIYKE---HEADAAryIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTR 195
Cdd:PRK13652 96 VEQDIAFGPINLGLDEEtvaHRVSSA--LHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 505262942 196 ADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK13652 174 KELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVM 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
48-240 |
1.12e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 107.79 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLR----LIAGLDHPQS------GTLSLAGE---PIEGPNPKRGYVFQQGSLF 114
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGShiellgRTVQREGRlarDIRKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 115 PWLTVEENIAFG-LKAQGIYK--------EHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDE 185
Cdd:PRK09984 99 NRLSVLENVLIGaLGSTPFWRtcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505262942 186 PMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL--RQGHV 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
49-192 |
1.33e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 106.11 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRG--YVFQQGSLFPWLTVEENIAFG 126
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchYLGHRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505262942 127 lkaQGIYKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDS 192
Cdd:PRK13539 98 ---AAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
39-231 |
1.65e-27 |
|
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: 106.85 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 39 TAPDgsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR-----GYVFQQGSL 113
Cdd:cd03249 12 SRPD---VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrsqiGLVSQEPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 114 FPwLTVEENIAFGLKaqGIYKEHEADAAR--------------YIEMVGLHGFeqayphQISGGMAQRVAIARALIDHPD 179
Cdd:cd03249 89 FD-GTIAENIRYGKP--DATDEEVEEAAKkanihdfimslpdgYDTLVGERGS------QLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 180 VLLLDEPMGALDSFTRADLQDRLLDIWEQyhMTMILVTH------DVDEAIYLG-SRVV 231
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKG--RTTIVIAHrlstirNADLIAVLQnGQVV 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
36-233 |
2.78e-27 |
|
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: 106.26 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 36 REFTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEpIEGPNPKR-----GYVFQQ 110
Cdd:cd03267 24 KSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKflrriGVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 111 GSLFPW-LTVEENIAFgLKAqgIYKEHEADAARYI----EMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDE 185
Cdd:cd03267 103 KTQLWWdLPVIDSFYL-LAA--IYDLPPARFKKRLdelsELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505262942 186 PMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVI 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
48-191 |
3.25e-27 |
|
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: 105.13 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRG----YVFQQGSLFPWLTVEENI 123
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHenilYLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 124 AFglkAQGIYKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALD 191
Cdd:TIGR01189 95 HF---WAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
48-233 |
5.61e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 105.84 E-value: 5.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEG-PNPK---RGYV--FQQGSLFPWLTVEE 121
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGHQiarMGVVrtFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 122 NIafgLKAQ----------GIYK-------EHEA--DAARYIEMVGLHGFEQ------AYPHQisggmaQRVAIARALID 176
Cdd:PRK11300 100 NL---LVAQhqqlktglfsGLLKtpafrraESEAldRAATWLERVGLLEHANrqagnlAYGQQ------RRLEIARCMVT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505262942 177 HPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
49-200 |
6.46e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 105.11 E-value: 6.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEG-PNPKR-----GYVFQQGSLFPWLTVEEN 122
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlPMHKRarlgiGYLPQEASIFRKLTVEDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 123 IAFGLKAQGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQD 200
Cdd:COG1137 99 ILAVLELRKLsKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQK 177
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
32-220 |
6.65e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 104.96 E-value: 6.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 32 EHVSREFTAPDgsvvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI------EGPNPKR- 104
Cdd:PRK10908 5 EHVSKAYLGGR----QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlknrEVPFLRRq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -GYVFQQGSLFPWLTVEENIAFGLKAQGIYKE---HEADAAryIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDV 180
Cdd:PRK10908 81 iGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDdirRRVSAA--LDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505262942 181 LLLDEPMGALDSftraDLQDRLLDIWEQYH---MTMILVTHDV 220
Cdd:PRK10908 159 LLADEPTGNLDD----ALSEGILRLFEEFNrvgVTVLMATHDI 197
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-233 |
7.22e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 106.35 E-value: 7.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapdGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR-GYV 107
Cdd:COG4152 2 LELKGLTKRF----GDK-TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRiGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 108 FQQGSLFPWLTVEENIAF-----GLKAqgiyKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLL 182
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYlarlkGLSK----AEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505262942 183 LDEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVII 202
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-233 |
9.56e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.22 E-value: 9.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 2 SDTELDHLAVASGRQTLADV---PAGVNPELSIEHVSREFTAPDGSVVhalSDVSLSIYPGELVSIIGPSGCGKTTLLRL 78
Cdd:PRK13536 10 APRRLELSPIERKHQGISEAkasIPGSMSTVAIDLAGVSKSYGDKAVV---NGLSFTVASGECFGLLGPNGAGKSTIARM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 79 IAGLDHPQSGTLSLAGEPIegPNPKR------GYVFQQGSLFPWLTVEENIA-----FGLKAQGIykehEADAARYIEMV 147
Cdd:PRK13536 87 ILGMTSPDAGKITVLGVPV--PARARlarariGVVPQFDNLDLEFTVRENLLvfgryFGMSTREI----EAVIPSLLEFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 148 GLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLG 227
Cdd:PRK13536 161 RLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLC 239
|
....*.
gi 505262942 228 SRVVIM 233
Cdd:PRK13536 240 DRLCVL 245
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
48-249 |
1.03e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.94 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAG------EPIEGPNPKRGYVFQQ-GSLFPWLTVE 120
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENLWDIRNKAGMVFQNpDNQIVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 121 ENIAFGLKAQGIY-KEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQ 199
Cdd:PRK13633 105 EDVAFGPENLGIPpEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505262942 200 DRLLDIWEQYHMTMILVTHDVDEAIYlGSRVVIM---------TPRP--GRIKEIVPINLD 249
Cdd:PRK13633 185 NTIKELNKKYGITIILITHYMEEAVE-ADRIIVMdsgkvvmegTPKEifKEVEMMKKIGLD 244
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
47-242 |
1.07e-26 |
|
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: 104.61 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 47 HALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR-----GYVFQQGSLFPWlTVEE 121
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrsmiGVVLQDTFLFSG-TIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 122 NIAFGlkAQGIYKEHEADAARyieMVGLHGF----EQAYPHQI-------SGGMAQRVAIARALIDHPDVLLLDEPMGAL 190
Cdd:cd03254 96 NIRLG--RPNATDEEVIEAAK---EAGAHDFimklPNGYDTVLgenggnlSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 191 DSFTRADLQDRLLDIWEQyhMTMILVTH------DVDEAIYLgsrvvimtpRPGRIKE 242
Cdd:cd03254 171 DTETEKLIQEALEKLMKG--RTSIIIAHrlstikNADKILVL---------DDGKIIE 217
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
48-246 |
1.90e-26 |
|
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: 103.99 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQ----SGTLSLAGEPIeGPNPKRG----YVFQ--QGSLFPWL 117
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPL-LPLSIRGrhiaTIMQnpRTAFNPLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 118 TVEENIAFGLKAQG-IYKEHEADAARYIEMVGLHGFEQ---AYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSF 193
Cdd:TIGR02770 80 TMGNHAIETLRSLGkLSKQARALILEALEAVGLPDPEEvlkKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505262942 194 TRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEIVPI 246
Cdd:TIGR02770 160 NQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVM--DDGRIVERGTV 210
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
27-242 |
2.38e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 104.24 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFTApdgsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAG------EPIEGP 100
Cdd:PRK11701 5 PLLSVRGLTKLYGP-----RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlrDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 101 NPKR--------GYVFQ---QGsLFPWLTVEENIAFGLKAQGI--YKEHEADAARYIEMVglhgfEQA------YPHQIS 161
Cdd:PRK11701 80 EAERrrllrtewGFVHQhprDG-LRMQVSAGGNIGERLMAVGArhYGDIRATAGDWLERV-----EIDaariddLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 162 GGMAQRVAIARALIDHPDVLLLDEPMGALDsftrADLQDRLLDIW----EQYHMTMILVTHDVDEAIYLGSRVVIMtpRP 237
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLD----VSVQARLLDLLrglvRELGLAVVIVTHDLAVARLLAHRLLVM--KQ 227
|
....*
gi 505262942 238 GRIKE 242
Cdd:PRK11701 228 GRVVE 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
29-244 |
3.48e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 103.24 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREF-----------------TAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLS 91
Cdd:COG1134 5 IEVENVSKSYrlyhepsrslkelllrrRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 92 LAGE---PIE---GPNPKrgyvfqqgslfpwLTVEENIAFGLKAQGIYKEhEADaARY---IEMVGLHGFE----QAYph 158
Cdd:COG1134 85 VNGRvsaLLElgaGFHPE-------------LTGRENIYLNGRLLGLSRK-EID-EKFdeiVEFAELGDFIdqpvKTY-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 159 qiSGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDV-------DEAIYLGSRVV 231
Cdd:COG1134 148 --SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMgavrrlcDRAIWLEKGRL 224
|
250
....*....|...
gi 505262942 232 IMTprpGRIKEIV 244
Cdd:COG1134 225 VMD---GDPEEVI 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
34-232 |
3.65e-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: 3.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 34 VSREFTapdgsVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPiegPNPKR-------GY 106
Cdd:COG4586 28 FRREYR-----EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV---PFKRRkefarriGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 107 VFQQGS-LFPWLTVEENIAFgLKAqgIY----KEHEADAARYIEMVGLHGFEQAYPHQISGGmaQRV--AIARALIDHPD 179
Cdd:COG4586 100 VFGQRSqLWWDLPAIDSFRL-LKA--IYripdAEYKKRLDELVELLDLGELLDTPVRQLSLG--QRMrcELAAALLHRPK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505262942 180 VLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVI 232
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIV 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
46-245 |
3.88e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 108.02 E-value: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 46 VHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR--------GYVFQQ--GSLFP 115
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrrdiQFIFQDpyASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 116 WLTVEENIAFGLKAQGIYKEHEADA--ARYIEMVGLHGfEQA--YPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALD 191
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGLLPGKAAAArvAWLLERVGLLP-EHAwrYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505262942 192 SFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMTprPGRIKEIVP 245
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMY--LGQIVEIGP 547
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
29-257 |
5.57e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.03 E-value: 5.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREftapdgsvvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:COG1129 257 LEVEGLSVG---------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaira 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 --GYV----FQQGsLFPWLTVEENIA---------FGLKAQGiyKEHEAdAARYIEMVGLHGfeqAYPHQI----SGGMA 165
Cdd:COG1129 328 giAYVpedrKGEG-LVLDLSIRENITlasldrlsrGGLLDRR--RERAL-AEEYIKRLRIKT---PSPEQPvgnlSGGNQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 166 QRVAIARALIDHPDVLLLDEP-----MGAldsftRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPtrgidVGA-----KAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVM--REGRI 472
|
250
....*....|....*..
gi 505262942 241 KEIVPinldaRDRVSDE 257
Cdd:COG1129 473 VGELD-----REEATEE 484
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
48-222 |
6.40e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.67 E-value: 6.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPN---------PKRGYVFQ--QGSLFPW 116
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikqirKKVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 117 lTVEENIAFGLKAQGIYKEH-EADAARYIEMVGLHG--FEQAyPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSF 193
Cdd:PRK13649 102 -TVLKDVAFGPQNFGVSQEEaEALAREKLALVGISEslFEKN-PFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190
....*....|....*....|....*....|..
gi 505262942 194 TRADlqdrLLDIWEQYH---MTMILVTHDVDE 222
Cdd:PRK13649 180 GRKE----LMTLFKKLHqsgMTIVLVTHLMDD 207
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
29-242 |
9.24e-26 |
|
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: 102.18 E-value: 9.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtAPDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNP-----K 103
Cdd:cd03252 1 ITFEHVRFRY-KPDGPVI--LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPawlrrQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 104 RGYVFQQGSLFPwLTVEENIAfgLKAQGIYKEHEADAARyieMVGLHGFEQAYPH-----------QISGGMAQRVAIAR 172
Cdd:cd03252 78 VGVVLQENVLFN-RSIRDNIA--LADPGMSMERVIEAAK---LAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 173 ALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEqyHMTMILVTHDVdEAIYLGSRVVIMtpRPGRIKE 242
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRL-STVKNADRIIVM--EKGRIVE 216
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
48-233 |
9.42e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 104.02 E-value: 9.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR--------GYVFQQ--GSLFPWL 117
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwravrsdiQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 118 TVEENIAFGLKaqgIYKEHEADAA---RYIEM---VGL-HGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGAL 190
Cdd:PRK15079 116 TIGEIIAEPLR---TYHPKLSRQEvkdRVKAMmlkVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505262942 191 DSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
47-232 |
1.19e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 102.23 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 47 HALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGL-----DHPQSGTLSLAGEPIEGP--NP-----KRGYVFQQGSLF 114
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPdvDPievrrEVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 115 PWLTVEENIAFGLKAQGIYK-EHEAD---------AARYIEmvgLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLD 184
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLVKsKKELDervewalkkAALWDE---VKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505262942 185 EPMGALDSFTRADLQDRLLDIWEQYhmTMILVTHDVDEA---------IYLGSRVVI 232
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAarvsdyvafLYLGKLIEV 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
47-219 |
1.45e-25 |
|
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: 106.17 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 47 HALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSgtlslaGEPIEGPNPKRGYVFQQGSLFPWLTVEENIAFG 126
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFN------GEARPQPGIKVGYLPQEPQLDPTKTVRENVEEG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 127 L-KAQGIYKEHEADAARY--------------------IEMVGLHGFEQ---------------AYPHQISGGMAQRVAI 170
Cdd:TIGR03719 93 VaEIKDALDRFNEISAKYaepdadfdklaaeqaelqeiIDAADAWDLDSqleiamdalrcppwdADVTKLSGGERRRVAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505262942 171 ARALIDHPDVLLLDEPMGALDSFTRADLQDRLldiwEQYHMTMILVTHD 219
Cdd:TIGR03719 173 CRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
26-235 |
1.54e-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: 101.36 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 26 NPELSIEHVSREFT--APDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSL--AGEPIE--G 99
Cdd:COG4778 2 TTLLEVENLSKTFTlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDlaQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 100 PNPKR---------GYVFQQGSLFPWLTVEENIAFGLKAQGIYKEHEADAARyiEMvgLHGFE------QAYPHQISGGM 164
Cdd:COG4778 82 ASPREilalrrrtiGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARAR--EL--LARLNlperlwDLPPATFSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505262942 165 AQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDVD--EAiyLGSRVVIMTP 235
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEvrEA--VADRVVDVTP 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-218 |
3.48e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.89 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 5 ELDHLAVASGRQTLADvpagvNPELSIEHVSreFTAPDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDH 84
Cdd:COG4178 344 AADALPEAASRIETSE-----DGALALEDLT--LRTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWP 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 85 PQSGTLSLagePiEGPN----PKRGYvFQQGSLfpwltvEENIAFGLKAQGIykeHEADAARYIEMVGLHGF------EQ 154
Cdd:COG4178 415 YGSGRIAR---P-AGARvlflPQRPY-LPLGTL------REALLYPATAEAF---SDAELREALEAVGLGHLaerldeEA 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505262942 155 AYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDiwEQYHMTMILVTH 218
Cdd:COG4178 481 DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
29-242 |
3.78e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.76 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLagepieGPNPKRGYVF 108
Cdd:COG0488 316 LELEGLSKSY---GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL------GETVKIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 109 Q-QGSLFPWLTVEENIafglkAQGIYKEHEADAARYIEMVGLHGFEQAYP-HQISGGMAQRVAIARALIDHPDVLLLDEP 186
Cdd:COG0488 385 QhQEELDPDKTVLDEL-----RDGAPGGTEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 187 MGALDSFTRADLQDRLLDiweqYHMTMILVTHDVdeaiYLGSRVV--IMTPRPGRIKE 242
Cdd:COG0488 460 TNHLDIETLEALEEALDD----FPGTVLLVSHDR----YFLDRVAtrILEFEDGGVRE 509
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
47-233 |
3.89e-25 |
|
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: 100.31 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 47 HALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEG-PNPKR-----GYVFQQGSLFPWLTVE 120
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlPMHKRarlgiGYLPQEASIFRKLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 121 ENIAFGLKAQGIYKEHEADAARY-IEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQ 199
Cdd:cd03218 94 ENILAVLEIRGLSKKEREEKLEElLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQ 173
|
170 180 190
....*....|....*....|....*....|....*
gi 505262942 200 dRLLDIWEQYHMTmILVT-HDVDEAIYLGSRVVIM 233
Cdd:cd03218 174 -KIIKILKDRGIG-VLITdHNVRETLSITDRAYII 206
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
20-192 |
3.99e-25 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 104.78 E-value: 3.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 20 DVPAGVNPELSIEHVSreFTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEG 99
Cdd:TIGR02204 329 TLPVPLRGEIEFEQVN--FAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 100 PNPKR-----GYVFQQGSLFPwLTVEENIAFG-LKAQGIYKEHEADAARyiemvgLHGFEQAYPH-----------QISG 162
Cdd:TIGR02204 407 LDPAElrarmALVPQDPVLFA-ASVMENIRYGrPDATDEEVEAAARAAH------AHEFISALPEgydtylgergvTLSG 479
|
170 180 190
....*....|....*....|....*....|
gi 505262942 163 GMAQRVAIARALIDHPDVLLLDEPMGALDS 192
Cdd:TIGR02204 480 GQRQRIAIARAILKDAPILLLDEATSALDA 509
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
48-222 |
4.51e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 101.73 E-value: 4.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAG---------EPIEGPNPKRGYVFQ--QGSLFPW 116
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqKEIKPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 117 lTVEENIAFGLKAQGIYKEH-EADAARYIEMVGLHG-FEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFT 194
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKaEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180
....*....|....*....|....*...
gi 505262942 195 RADLQdRLLDIWEQYHMTMILVTHDVDE 222
Cdd:PRK13643 180 RIEMM-QLFESIHQSGQTVVLVTHLMDD 206
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
48-266 |
5.90e-25 |
|
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: 100.29 E-value: 5.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLA---GEPIE---GPNPKR--------GYVFQ--QG 111
Cdd:TIGR02323 18 GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYImrsGAELElyqLSEAERrrlmrtewGFVHQnpRD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 112 SLFPWLTVEENIAFGLKAQGI--YKEHEADAARYIEMVGL-HGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMG 188
Cdd:TIGR02323 98 GLRMRVSAGANIGERLMAIGArhYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTG 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 189 ALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEivpinLDARDRVSDEFAAYRKQLL 266
Cdd:TIGR02323 178 GLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM--QQGRVVE-----SGLTDQVLDDPQHPYTQLL 248
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
49-233 |
9.41e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.67 E-value: 9.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEgPNP----------KRGYVFQ--QGSLFPw 116
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHIT-PETgnknlkklrkKVSLVFQfpEAQLFE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 117 LTVEENIAFGLKAQGIY-KEHEADAARYIEMVGL-HGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFT 194
Cdd:PRK13641 101 NTVLKDVEFGPKNFGFSeDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 505262942 195 RADLQDRLLDIWEQYHmTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK13641 181 RKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVL 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
29-219 |
1.11e-24 |
|
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: 96.75 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLagepieGPNPKRGYVf 108
Cdd:cd03221 1 IELENLSKTY---GGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW------GSTVKIGYF- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 109 qqgslfpwltveeniafglkaqgiykeheadaaryiemvglhgfeqaypHQISGGMAQRVAIARALIDHPDVLLLDEPMG 188
Cdd:cd03221 69 -------------------------------------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190
....*....|....*....|....*....|.
gi 505262942 189 ALDSFTRADLQDRLLDiweqYHMTMILVTHD 219
Cdd:cd03221 100 HLDLESIEALEEALKE----YPGTVILVSHD 126
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
38-218 |
2.94e-24 |
|
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: 97.93 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 38 FTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIegPNPKRGYVFQQGSLF--- 114
Cdd:cd03248 19 FAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI--SQYEHKYLHSKVSLVgqe 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 115 PWL---TVEENIAFGLkaQGIYKEHEADAAryiEMVGLHGFEQAYPH-----------QISGGMAQRVAIARALIDHPDV 180
Cdd:cd03248 97 PVLfarSLQDNIAYGL--QSCSFECVKEAA---QKAHAHSFISELASgydtevgekgsQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 505262942 181 LLLDEPMGALDSFTRADLQDRLLDiWEQYHmTMILVTH 218
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYD-WPERR-TVLVIAH 207
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
47-242 |
3.69e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.09 E-value: 3.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 47 HALSDVSLSIYPGELVSIIGPSGCGKTT----LLRLIAgldhpQSGTLSLAGEPIEGPNPKR--------GYVFQ--QGS 112
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrhriQVVFQdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 113 LFPWLTVEENIAFGLKAQGIY---KEHEADAARYIEMVGLH-GFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMG 188
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVHQPTlsaAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505262942 189 ALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKE 242
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVL--RQGEVVE 506
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
48-258 |
6.85e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.93 E-value: 6.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLR-------LIAGLDhpQSGTLSLAGEPIEGP--NP-----KRGYVFQQGSL 113
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLYAPdvDPvevrrRIGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 114 FPwLTVEENIAFGLKAQGIYKEHEADAARYIEMVGLHGFEQAYPHQ----ISGGMAQRVAIARALIDHPDVLLLDEPMGA 189
Cdd:PRK14243 103 FP-KSIYDNIAYGARINGYKGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 190 LDSFTRADLQDRLLDIWEQYhmTMILVTHDVDEAiylgSRVVIMT--------PRPGRIKEIV-----------PINLDA 250
Cdd:PRK14243 182 LDPISTLRIEELMHELKEQY--TIIIVTHNMQQA----ARVSDMTaffnveltEGGGRYGYLVefdrtekifnsPQQQAT 255
|
....*...
gi 505262942 251 RDRVSDEF 258
Cdd:PRK14243 256 RDYVSGRF 263
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
42-218 |
8.38e-24 |
|
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: 96.02 E-value: 8.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 42 DGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRG----YVFQQGSLFPWL 117
Cdd:cd03231 11 DGRAL--FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIArgllYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 118 TVEENIAFglkaqgiYKEHEADAA--RYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTR 195
Cdd:cd03231 89 SVLENLRF-------WHADHSDEQveEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|...
gi 505262942 196 ADLQDRLLDIWEQYHMtMILVTH 218
Cdd:cd03231 162 ARFAEAMAGHCARGGM-VVLTTH 183
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
29-218 |
1.05e-23 |
|
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: 94.53 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSreFTAPDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAgepiEGPN----PKR 104
Cdd:cd03223 1 IELENLS--LATPDGRVL--LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP----EGEDllflPQR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 GYvFQQGSL-----FPWLTVeeniafglkaqgiykeheadaaryiemvglhgfeqayphqISGGMAQRVAIARALIDHPD 179
Cdd:cd03223 73 PY-LPLGTLreqliYPWDDV----------------------------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*....
gi 505262942 180 VLLLDEPMGALDsftrADLQDRLLDIWEQYHMTMILVTH 218
Cdd:cd03223 112 FVFLDEATSALD----EESEDRLYQLLKELGITVISVGH 146
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
29-243 |
2.02e-23 |
|
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: 95.76 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTAPDGSVvhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEG---PNPKR- 104
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV---LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytlASLRRq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -GYVFQQGSLFPWlTVEENIAFGlkAQGIYKEHEADAARyieMVGLHGF----EQAYPHQI-------SGGMAQRVAIAR 172
Cdd:cd03251 78 iGLVSQDVFLFND-TVAENIAYG--RPGATREEVEEAAR---AANAHEFimelPEGYDTVIgergvklSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505262942 173 ALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEqyHMTMILVTHDVdEAIYLGSRVVIMTprPGRIKEI 243
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRL-STIENADRIVVLE--DGKIVER 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
48-234 |
2.98e-23 |
|
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: 100.09 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIE----GPNPKRGYVFQQGSLFPWLTVEENI 123
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtnldAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 124 AFGLKAQG-IYKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRL 202
Cdd:TIGR01257 1025 LFYAQLKGrSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190
....*....|....*....|....*....|..
gi 505262942 203 LDIweQYHMTMILVTHDVDEAIYLGSRVVIMT 234
Cdd:TIGR01257 1105 LKY--RSGRTIIMSTHHMDEADLLGDRIAIIS 1134
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
30-240 |
6.97e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.76 E-value: 6.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 30 SIEHVSREFtapDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI-EGPNP---KRG 105
Cdd:COG4604 3 EIKNVSKRY---GGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVaTTPSRelaKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 106 YVFQQGSLFPW-LTVEENIAFGL--KAQG-IYKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVL 181
Cdd:COG4604 78 AILRQENHINSrLTVRELVAFGRfpYSKGrLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 182 LLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAM--KDGRV 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
29-233 |
8.47e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.07 E-value: 8.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSL----------AGEPIE 98
Cdd:PRK13631 22 LRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 99 GPNPKR-----------GYVFQqgslFPWL-----TVEENIAFGLKAQGIYKEHEAD-AARYIEMVGL-HGFEQAYPHQI 160
Cdd:PRK13631 102 NPYSKKiknfkelrrrvSMVFQ----FPEYqlfkdTIEKDIMFGPVALGVKKSEAKKlAKFYLNKMGLdDSYLERSPFGL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505262942 161 SGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVM 249
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-202 |
9.27e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.11 E-value: 9.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 22 PAGVNPELSIEHVSREFtapDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPN 101
Cdd:PRK13657 328 LGRVKGAVEFDDVSFSY---DNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 102 PKR-----GYVFQQGSLFPwLTVEENIAFG---------LKAQGIYKEH---EADAARYIEMVGLHGfeqaypHQISGGM 164
Cdd:PRK13657 404 RASlrrniAVVFQDAGLFN-RSIEDNIRVGrpdatdeemRAAAERAQAHdfiERKPDGYDTVVGERG------RQLSGGE 476
|
170 180 190
....*....|....*....|....*....|....*...
gi 505262942 165 AQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRL 202
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL 514
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
29-233 |
1.03e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.91 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtaPDGSvvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIE----GPNPKR 104
Cdd:PRK13636 6 LKVEELNYNY--SDGT--HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ---GYVFQQ--GSLFPwLTVEENIAFGLKAQGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHP 178
Cdd:PRK13636 82 esvGMVFQDpdNQLFS-ASVYQDVSFGAVNLKLpEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505262942 179 DVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVM 215
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-233 |
5.63e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 95.62 E-value: 5.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 25 VNPELSIEHVSREFtapdgSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR 104
Cdd:PRK09700 2 ATPYISMAGIGKSF-----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ------GYVFQQGSLFPWLTVEENIAFGL----KAQGI----YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAI 170
Cdd:PRK09700 77 aaqlgiGIIYQELSVIDELTVLENLYIGRhltkKVCGVniidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505262942 171 ARALIDHPDVLLLDEPMGALdsfTRADLqDRLLDIWEQYH---MTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSL---TNKEV-DYLFLIMNQLRkegTAIVYISHKLAEIRRICDRYTVM 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
48-233 |
7.08e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.92 E-value: 7.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEG--------PNPKR-GYVFQ--QGSLFPw 116
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyirPVRKRiGMVFQfpESQLFE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 117 LTVEENIAFGLKAQGI-YKEHEADAARYIEMVGL-HGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFT 194
Cdd:PRK13646 101 DTVEREIIFGPKNFKMnLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQS 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 505262942 195 RADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK13646 181 KRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVM 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
49-223 |
1.26e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 91.61 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRgyVFQQGSLFPW-------LTVEE 121
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ--LARRLALLPQhhltpegITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 122 NIAFG----LKAQG-IYKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRA 196
Cdd:PRK11231 96 LVAYGrspwLSLWGrLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQV 175
|
170 180
....*....|....*....|....*..
gi 505262942 197 DLQdRLLDIWEQYHMTMILVTHDVDEA 223
Cdd:PRK11231 176 ELM-RLMRELNTQGKTVVTVLHDLNQA 201
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
47-218 |
1.27e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.73 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 47 HALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHP---QSGTLSLAGEPIEGPNPKR--GYVFQQGSLFPWLTVEE 121
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAisAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 122 NIAFG----LKAQGIYKEHEADAARYIEMVGLHGFEQ---AYPHQ---ISGGMAQRVAIARALIDHPDVLLLDEPMGALD 191
Cdd:TIGR00955 119 HLMFQahlrMPRRVTKKEKRERVDEVLQALGLRKCANtriGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180
....*....|....*....|....*..
gi 505262942 192 SFTRADLQDRLLDIwEQYHMTMILVTH 218
Cdd:TIGR00955 199 SFMAYSVVQVLKGL-AQKGKTIICTIH 224
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
29-233 |
1.36e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 92.88 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGL-DHP---QSGTLSLAGEPIEGPNPKR 104
Cdd:PRK11022 4 LNVDKLSVHF-GDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPgrvMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ---------GYVFQQG--SLFPWLTVEENIAFGLKAQ--GIYKEHEADAARYIEMVGLHGFE---QAYPHQISGGMAQRV 168
Cdd:PRK11022 83 rrnlvgaevAMIFQDPmtSLNPCYTVGFQIMEAIKVHqgGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 169 AIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHD---VDEAIYlgsRVVIM 233
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlalVAEAAH---KIIVM 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
29-218 |
1.51e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 89.29 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSreFTAPDgSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIegpnpkrgyvf 108
Cdd:cd03247 1 LSINNVS--FSYPE-QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 109 qqgslfpwLTVEENI--AFGLKAQGIYkeheADAARYIEMVGLhgfeqayphQISGGMAQRVAIARALIDHPDVLLLDEP 186
Cdd:cd03247 67 --------SDLEKALssLISVLNQRPY----LFDTTLRNNLGR---------RFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190
....*....|....*....|....*....|..
gi 505262942 187 MGALDSFTRADLQDRLLDIWEQyhMTMILVTH 218
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKD--KTLIWITH 155
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-218 |
1.62e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.51 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 26 NPELSIEHVSreFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPN---- 101
Cdd:PRK11160 336 QVSLTLNNVS--FTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSeaal 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 102 -------PKRGYVFQQgslfpwlTVEENIAFGLkaqgiykeHEADAARYIEM---VGLHGFEQAYP----------HQIS 161
Cdd:PRK11160 413 rqaisvvSQRVHLFSA-------TLRDNLLLAA--------PNASDEALIEVlqqVGLEKLLEDDKglnawlgeggRQLS 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 162 GGMAQRVAIARALIDHPDVLLLDEPMGALDsftrADLQDRLLDIWEQY--HMTMILVTH 218
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLD----AETERQILELLAEHaqNKTVLMITH 532
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
49-219 |
2.08e-21 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 94.03 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAgepiegPNPKRGYVFQQGSLFPWLTVEENIAFGLK 128
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA------PGIKVGYLPQEPQLDPEKTVRENVEEGVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 129 -AQGIYKEHEADAARY--------------------IEMVGLHGF----EQAY-----PH------QISGGMAQRVAIAR 172
Cdd:PRK11819 97 eVKAALDRFNEIYAAYaepdadfdalaaeqgelqeiIDAADAWDLdsqlEIAMdalrcPPwdakvtKLSGGERRRVALCR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505262942 173 ALIDHPDVLLLDEPMGALDSFTRADLQDRLldiwEQYHMTMILVTHD 219
Cdd:PRK11819 177 LLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYPGTVVAVTHD 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
29-242 |
2.50e-21 |
|
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: 93.63 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSreFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEG---PNPKR- 104
Cdd:TIGR02203 331 VEFRNVT--FRYPGRDR-PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytlASLRRq 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -GYVFQQGSLFPwLTVEENIAFGLKAQGIykehEADAARYIEMVGLHGFEQAYP---HQ--------ISGGMAQRVAIAR 172
Cdd:TIGR02203 408 vALVSQDVVLFN-DTIANNIAYGRTEQAD----RAEIERALAAAYAQDFVDKLPlglDTpigengvlLSGGQRQRLAIAR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 173 ALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQyhMTMILVTHDVdEAIYLGSRVVIMTprPGRIKE 242
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLMQG--RTTLVIAHRL-STIEKADRIVVMD--DGRIVE 547
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
49-248 |
4.56e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.10 E-value: 4.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQS-----GTLSLAGEPI--EGPNPKR-----GYVFQQGSLFPw 116
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRlrrqvSMVHPKPNLFP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 117 LTVEENIAFGLKAQGIYKEHEAD--------AARYIEMVGLHGFEQAYphQISGGMAQRVAIARALIDHPDVLLLDEPMG 188
Cdd:PRK14258 102 MSVYDNVAYGVKIVGWRPKLEIDdivesalkDADLWDEIKHKIHKSAL--DLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 189 ALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMTPRPGRIKEIVPINL 248
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEFGL 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
27-290 |
6.76e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.46 E-value: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFTApDGSVVHALSDVSLSIYPGELVSIIGPSGCGKT----TLLRLIAG--LDHPQsGTLSLAGEPIEGP 100
Cdd:PRK15134 4 PLLAIENLSVAFRQ-QQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppVVYPS-GDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 101 NPK-----RG----YVFQQG--SLFPWLTVEENIAFGLKA-QGIYKEheadAARY-----IEMVGLHgfeQA------YP 157
Cdd:PRK15134 82 SEQtlrgvRGnkiaMIFQEPmvSLNPLHTLEKQLYEVLSLhRGMRRE----AARGeilncLDRVGIR---QAakrltdYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 158 HQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRP 237
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM--QN 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 505262942 238 GRIKEivpinldaRDRVSDEFAA----YRKQLLtklhfDAHEEHAGDAFVGDAQELL 290
Cdd:PRK15134 233 GRCVE--------QNRAATLFSApthpYTQKLL-----NSEPSGDPVPLPEPASPLL 276
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
26-229 |
7.03e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 89.17 E-value: 7.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 26 NPELSIEHVSREFTApdgsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR- 104
Cdd:PRK11614 3 KVMLSFDKVSAHYGK-----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 -----GYVFQQGSLFPWLTVEENIAFGlkaqGIYKEHEADAARYIEMVGLHGFEQAYPHQ----ISGGMAQRVAIARALI 175
Cdd:PRK11614 78 mreavAIVPEGRRVFSRMTVEENLAMG----GFFAERDQFQERIKWVYELFPRLHERRIQragtMSGGEQQMLAIGRALM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505262942 176 DHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSR 229
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADR 206
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
26-218 |
7.62e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 92.50 E-value: 7.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 26 NPELSIEHVSREFtapdGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEgpNPKRG 105
Cdd:TIGR01193 471 NGDIVINDVSYSY----GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK--DIDRH 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 106 -------YVFQQGSLFPWlTVEENIAFGLKaQGIYKEHEADAARYIEM--------VGLHGFEQAYPHQISGGMAQRVAI 170
Cdd:TIGR01193 545 tlrqfinYLPQEPYIFSG-SILENLLLGAK-ENVSQDEIWAACEIAEIkddienmpLGYQTELSEEGSSISGGQKQRIAL 622
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505262942 171 ARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQyhmTMILVTH 218
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAH 667
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
49-231 |
1.01e-20 |
|
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: 92.19 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPK--R---GYVFQQGSLFPwLTVEENI 123
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRaaiGIVPQDTVLFN-DTIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 124 AFGlkAQGIYKEHEADAARyieMVGLHGFEQAYPHQI-----------SGGMAQRVAIARALIDHPDVLLLDEPMGALDS 192
Cdd:COG5265 453 AYG--RPDASEEEVEAAAR---AAQIHDFIESLPDGYdtrvgerglklSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505262942 193 FTRADLQDRLLDIWEqyHMTMILVTH------DVDEAIYLGS-RVV 231
Cdd:COG5265 528 RTERAIQAALREVAR--GRTTLVIAHrlstivDADEILVLEAgRIV 571
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
51-251 |
1.47e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.89 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 51 DVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR-----GYVFQQGSLFPWLTVEENIAF 125
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvarriGLLAQNATTPGDITVQELVAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 126 G-LKAQGIY----KEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQD 200
Cdd:PRK10253 105 GrYPHQPLFtrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505262942 201 RLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI------KEIVPINLDAR 251
Cdd:PRK10253 185 LLSELNREKGYTLAAVLHDLNQACRYASHLIAL--REGKIvaqgapKEIVTAELIER 239
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
29-233 |
1.77e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.89 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSreFTAPDGSvvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSL----AGEPIEGPNPKR 104
Cdd:PRK13644 2 IRLENVS--YSYPDGT--PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidTGDFSKLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 --GYVFQQ-GSLFPWLTVEENIAFG-----LKAQGIYKEHEadaaRYIEMVGLHGFEQAYPHQISGGMAQRVAIARALID 176
Cdd:PRK13644 78 lvGIVFQNpETQFVGRTVEEDLAFGpenlcLPPIEIRKRVD----RALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505262942 177 HPDVLLLDEPMGALDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEaIYLGSRVVIM 233
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVM 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
49-233 |
1.87e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.18 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGE---------PIEGPNPKR--GYVFQQGSLFPWL 117
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifQIDAIKLRKevGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 118 TVEENIAFGLKAQGIYKEHEAD--AARYIEMVGL----HGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALD 191
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKkiVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505262942 192 SFTRADLQDRLLDIweQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK14246 186 IVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFL 225
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
44-219 |
2.36e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.97 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 44 SVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLdHPQSGTLSLAGEPIEGPNP-----KRGYVFQQGSLFPWLT 118
Cdd:COG4138 7 AVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAaelarHRAYLSQQQSPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 119 VEENIAFGLKAQGiykEHEADAARYIEMVGLHGFEQAYP---HQISGGMAQRVAIARALID-HPDV------LLLDEPMG 188
Cdd:COG4138 86 VFQYLALHQPAGA---SSEAVEQLLAQLAEALGLEDKLSrplTQLSGGEWQRVRLAAVLLQvWPTInpegqlLLLDEPMN 162
|
170 180 190
....*....|....*....|....*....|.
gi 505262942 189 ALDSFTRADLqDRLLDIWEQYHMTMILVTHD 219
Cdd:COG4138 163 SLDVAQQAAL-DRLLRELCQQGITVVMSSHD 192
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
46-223 |
2.54e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 90.95 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 46 VHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPN------PKRGYVfQQG---SLFPW 116
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARhrravcPRIAYM-PQGlgkNLYPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 117 LTVEENIAF-----GLKAQgiykEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALD 191
Cdd:NF033858 93 LSVFENLDFfgrlfGQDAA----ERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
170 180 190
....*....|....*....|....*....|....*
gi 505262942 192 SFTRA---DLQDRLLDiwEQYHMTMILVTHDVDEA 223
Cdd:NF033858 169 PLSRRqfwELIDRIRA--ERPGMSVLVATAYMEEA 201
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
46-246 |
3.55e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 87.28 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 46 VHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLD--HPQ---SGTLSLAGE-----PIEGPNPKRGYVFQQGSLFP 115
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelYPEarvSGEVYLDGQdifkmDVIELRRRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 116 WLTVEENIAFGLKAQGIYK---EHEADAARYIEMVGLhgFEQ------AYPHQISGGMAQRVAIARALIDHPDVLLLDEP 186
Cdd:PRK14247 96 NLSIFENVALGLKLNRLVKskkELQERVRWALEKAQL--WDEvkdrldAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 187 MGALDSFTRADLQDRLLDIweQYHMTMILVTHDVDEAIYLGSRVVIMTprPGRIKEIVPI 246
Cdd:PRK14247 174 TANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLY--KGQIVEWGPT 229
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-186 |
5.36e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 86.71 E-value: 5.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapDGsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:COG4674 11 LYVEDLTVSF---DG--FKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEiarl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 --GYVFQQGSLFPWLTVEENIAFGLKAQ-GIY--------KEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARA 173
Cdd:COG4674 86 giGRKFQKPTVFEELTVFENLELALKGDrGVFaslfarltAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGML 165
|
170
....*....|...
gi 505262942 174 LIDHPDVLLLDEP 186
Cdd:COG4674 166 LAQDPKLLLLDEP 178
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-222 |
6.83e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 89.52 E-value: 6.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 5 ELDHLAVASGRQTLADvpagvNPELSIEHVSREFTAPDGSVvhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLdH 84
Cdd:PRK11174 329 ETPLAHPQQGEKELAS-----NDPVTIEAEDLEILSPDGKT--LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-L 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 85 PQSGTLSLAGEPIEGPNPKR-----GYVFQQGSLFPWlTVEENIAFGlkaQGIYKEHEADAAryIEMVGLHGFEQAYPH- 158
Cdd:PRK11174 401 PYQGSLKINGIELRELDPESwrkhlSWVGQNPQLPHG-TLRDNVLLG---NPDASDEQLQQA--LENAWVSEFLPLLPQg 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505262942 159 ----------QISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEqyHMTMILVTHDVDE 222
Cdd:PRK11174 475 ldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLED 546
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
49-204 |
2.45e-19 |
|
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: 88.07 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLagepieGPNPKRGYVFQQ-GSLFPWLTVEENIAFGL 127
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------GETVKLAYVDQSrDALDPNKTVWEEISGGL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 128 KAQGIYKeHEADAARYiemVGLHGF----EQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLL 203
Cdd:TIGR03719 412 DIIKLGK-REIPSRAY---VGRFNFkgsdQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
.
gi 505262942 204 D 204
Cdd:TIGR03719 488 N 488
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
26-233 |
2.76e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 86.32 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 26 NPELSIEHVSREFTAPDGSVVhALSDVSLSIYPGELVSIIGPSGCGKT----TLLRLIAG---------------LDHPQ 86
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVT-AVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAAngriggsatfngreiLNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 87 SGTLSLAGEPIegpnpkrGYVFQQ--GSLFPWLTVEENIAFGLKAQGIYKEHEA--DAARYIEMVGL---HGFEQAYPHQ 159
Cdd:PRK09473 89 KELNKLRAEQI-------SMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAfeESVRMLDAVKMpeaRKRMKMYPHE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505262942 160 ISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 235
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
29-220 |
3.03e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.78 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTAPdgsvvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTlslagepIEGPNPKR-GYV 107
Cdd:PRK09544 5 VSLENVSVSFGQR-----RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV-------IKRNGKLRiGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 108 FQQGSLFPW--LTVEEniaFGLKAQGIYKEHEADAARYIEMVGLHgfeQAYPHQISGGMAQRVAIARALIDHPDVLLLDE 185
Cdd:PRK09544 73 PQKLYLDTTlpLTVNR---FLRLRPGTKKEDILPALKRVQAGHLI---DAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190
....*....|....*....|....*....|....*
gi 505262942 186 PMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDV 220
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-240 |
3.65e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.41 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFTApdgsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRGY 106
Cdd:PRK15439 10 PLLCARSISKQYSG-----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 107 ------VFQQGSLFPWLTVEENIAFGLKAqgiykeHEADAARYIEMVGLHGFeQAYPHQISGGM----AQRVAIARALID 176
Cdd:PRK15439 85 qlgiylVPQEPLLFPNLSVKENILFGLPK------RQASMQKMKQLLAALGC-QLDLDSSAGSLevadRQIVEILRGLMR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505262942 177 HPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHmTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIRELLAQGV-GIVFISHKLPEIRQLADRISVM--RDGTI 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
27-261 |
4.10e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.43 E-value: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFtapdGSVVhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR-- 104
Cdd:PRK09536 2 PMIDVSDLSVEF----GDTT-VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAas 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 ---GYVFQQGSLFPWLTVEENIAFGLKAQ-GIYKEH-EADAA---RYIEMVGLHGFEQAYPHQISGGMAQRVAIARALID 176
Cdd:PRK09536 77 rrvASVPQDTSLSFEFDVRQVVEMGRTPHrSRFDTWtETDRAaveRAMERTGVAQFADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 177 HPDVLLLDEPMGALD---SFTRADLQDRLLDIWEqyhmTMILVTHDVDEAIYLGSRVVIMTprPGRIKEI-VPINLDARD 252
Cdd:PRK09536 157 ATPVLLLDEPTASLDinhQVRTLELVRRLVDDGK----TAVAAIHDLDLAARYCDELVLLA--DGRVRAAgPPADVLTAD 230
|
....*....
gi 505262942 253 RVSDEFAAY 261
Cdd:PRK09536 231 TLRAAFDAR 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
29-245 |
4.39e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.00 E-value: 4.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSreftAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR---- 104
Cdd:COG3845 258 LEVENLS----VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErrrl 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 --GYV----FQQGsLFPWLTVEENIAFG------LKAQGI--YKEHEADAARYIEmvglhgfeqAY------PHQI---- 160
Cdd:COG3845 334 gvAYIpedrLGRG-LVPDMSVAENLILGryrrppFSRGGFldRKAIRAFAEELIE---------EFdvrtpgPDTParsl 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 161 SGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLD-------IweqyhmtmILVTHDVDEAIYLGSRVVIM 233
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLElrdagaaV--------LLISEDLDEILALSDRIAVM 475
|
250
....*....|..
gi 505262942 234 tpRPGRIKEIVP 245
Cdd:COG3845 476 --YEGRIVGEVP 485
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
49-270 |
8.02e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.29 E-value: 8.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEgpNPKRGY---------VFQ--QGSLFpWL 117
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD--YSKRGLlalrqqvatVFQdpEQQIF-YT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 118 TVEENIAFGLKAQGIykeHEADAARYIE----MVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSF 193
Cdd:PRK13638 94 DIDSDIAFSLRNLGV---PEAEITRRVDealtLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505262942 194 TRADLQDRLLDIWEQYHMTMIlVTHDVDeAIYLGSRVVIMTPRPGRIKEIVPINLDARDRVSDEfAAYRKQLLTKLH 270
Cdd:PRK13638 171 GRTQMIAIIRRIVAQGNHVII-SSHDID-LIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQ-AGLTQPWLVKLH 244
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
28-233 |
1.94e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.52 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 28 ELSIEHVSREFTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTlSLAGEPIEGPNPKR--- 104
Cdd:PRK13645 6 DIILDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDYAIPANLKKike 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 --------GYVFQqgslFPWL-----TVEENIAFGLKAQGIYKEheaDAARYI-EMVGLHGFEQAY----PHQISGGMAQ 166
Cdd:PRK13645 85 vkrlrkeiGLVFQ----FPEYqlfqeTIEKDIAFGPVNLGENKQ---EAYKKVpELLKLVQLPEDYvkrsPFELSGGQKR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505262942 167 RVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
43-218 |
2.38e-18 |
|
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: 81.61 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 43 GSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRGYVFQQGSLF-----PWL 117
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAyaaqkPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 118 ---TVEENIAFGlkaqgiykeHEADAARY---IEMVGLHGFEQAYPH-----------QISGGMAQRVAIARALIDHPDV 180
Cdd:cd03290 91 lnaTVEENITFG---------SPFNKQRYkavTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNI 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 505262942 181 LLLDEPMGALDSFTRADL-QDRLLDIWEQYHMTMILVTH 218
Cdd:cd03290 162 VFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTH 200
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
42-233 |
4.54e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.14 E-value: 4.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 42 DGSVVHALSDVSLSIYPGELVSIIGPSGCGKT----TLLRLI--AG---------LDHPQSGTLSLAGEPIEGPNPKRG- 105
Cdd:PRK10261 25 EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGglvqcdkmlLRRRSRQVIELSEQSAAQMRHVRGa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 106 ---YVFQQ--GSLFPWLTVEENIAFGLKA-QGIYKEHE-ADAARYIEMVGL---HGFEQAYPHQISGGMAQRVAIARALI 175
Cdd:PRK10261 105 dmaMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAmVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 176 DHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
46-233 |
6.67e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 81.37 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 46 VHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIE-GPNPKRG----YVFQ--QGSLFPWLT 118
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDYSYRSqrirMIFQdpSTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 119 VEENIAFGLKAQGIYKEHEADAARY--IEMVGL---HGFeqAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSF 193
Cdd:PRK15112 106 ISQILDFPLRLNTDLEPEQREKQIIetLRQVGLlpdHAS--YYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505262942 194 TRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK15112 184 MRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVM 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
49-234 |
8.12e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.71 E-value: 8.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIE-GPNPKR-----GYVFQQGSLFPWLTVEEN 122
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISlLPLHARarrgiGYLPQEASIFRRLSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 123 IAFGLKA-QGIYKEHEAD-AARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQd 200
Cdd:PRK10895 99 LMAVLQIrDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIK- 177
|
170 180 190
....*....|....*....|....*....|....
gi 505262942 201 RLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMT 234
Cdd:PRK10895 178 RIIEHLRDSGLGVLITDHNVRETLAVCERAYIVS 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
29-237 |
2.60e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.77 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLD--HPQSGTL---------------- 90
Cdd:TIGR03269 1 IEVKNLTKKF---DGKEV--LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 91 SLAGEP------------IEGPNPKRGY----------VFQQG-SLFPWLTVEENIAFGLKAQGiYKEHEA--DAARYIE 145
Cdd:TIGR03269 76 SKVGEPcpvcggtlepeeVDFWNLSDKLrrrirkriaiMLQRTfALYGDDTVLDNVLEALEEIG-YEGKEAvgRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 146 MVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTH------- 218
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpevied 234
|
250
....*....|....*....
gi 505262942 219 DVDEAIYLGSRVVIMTPRP 237
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTP 253
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
55-238 |
2.68e-17 |
|
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: 79.37 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 55 SIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTlslagepIEGPNPKRGYVFQQGSLFPWLTVEENIAFGLKAQGIYK 134
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGD-------IEIELDTVSYKPQYIKADYEGTVRDLLSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 135 EHEADAARYIEMVGLhgFEQAYPhQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMI 214
Cdd:cd03237 94 YFKTEIAKPLQIEQI--LDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAF 170
|
170 180
....*....|....*....|....
gi 505262942 215 LVTHDVDEAIYLGSRVVIMTPRPG 238
Cdd:cd03237 171 VVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
49-233 |
3.41e-17 |
|
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: 78.07 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQ---SGTLSLAGEPI-EGPNPKRG---YVFQQGSLFPWLTVEE 121
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYkEFAEKYPGeiiYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 122 NIAFGLKAQGiykeheadaaryiemvglhgfeQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDR 201
Cdd:cd03233 103 TLDFALRCKG----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC 160
|
170 180 190
....*....|....*....|....*....|...
gi 505262942 202 LLDIWEQYHMT-MILVTHDVDEAIYLGSRVVIM 233
Cdd:cd03233 161 IRTMADVLKTTtFVSLYQASDEIYDLFDKVLVL 193
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-245 |
4.50e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.37 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 14 GRQTLADVPAGVnPELSIEHVSREFTapdGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLD-----HPQSG 88
Cdd:PRK14271 8 GQSGAADVDAAA-PAMAAVNLTLGFA---GKTV--LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 89 TLSLAGEPIEGPNP------KRGYVFQQGSLFPwLTVEENIAFGLKAQGIY--KEHEADAARYIEMVGLHGFEQA----Y 156
Cdd:PRK14271 82 DVLLGGRSIFNYRDvlefrrRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVprKEFRGVAQARLTEVGLWDAVKDrlsdS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 157 PHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQyhMTMILVTHDVDEAIYLGSRVVIMTpr 236
Cdd:PRK14271 161 PFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFF-- 236
|
....*....
gi 505262942 237 PGRIKEIVP 245
Cdd:PRK14271 237 DGRLVEEGP 245
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
40-247 |
5.27e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.59 E-value: 5.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 40 APDGSVVHalsDVSLSIYPGELVSIIGPSGCGKT-----TLLRLIAGLDHpQSGTLSLAGEPIEgPNPKRG----YVFQQ 110
Cdd:PRK10418 13 QAAQPLVH---GVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPVA-PCALRGrkiaTIMQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 111 G-SLF-PWLTVEENIAFGLKAQGIYKEhEADAARYIEMVGLHGFE---QAYPHQISGGMAQRVAIARALIDHPDVLLLDE 185
Cdd:PRK10418 88 PrSAFnPLHTMHTHARETCLALGKPAD-DATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505262942 186 PMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMTprPGRIKEIVPIN 247
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMS--HGRIVEQGDVE 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
50-233 |
1.51e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.71 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 50 SDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPK----RGYVF-----QQGSLFPWLTVE 120
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqrlaRGLVYlpedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 121 ENI-AFGLKAQGIYKEHEADAA---RYIEMVG--LHGFEQAYpHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFT 194
Cdd:PRK15439 360 WNVcALTHNRRGFWIKPARENAvleRYRRALNikFNHAEQAA-RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190
....*....|....*....|....*....|....*....
gi 505262942 195 RADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK15439 439 RNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVM 476
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
49-192 |
2.06e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.54 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQS--GTLSLAGEPIEGPNPKR-GYVFQQGSLFPWLTVEENIAF 125
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRtGFVTQDDILYPHLTVRETLVF 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505262942 126 ----GLKAQGIYKEHEADAARYIEMVGLHGFE-----QAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDS 192
Cdd:PLN03211 164 csllRLPKSLTKQEKILVAESVISELGLTKCEntiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
38-223 |
2.17e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.14 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 38 FTAPDGSVVHALSdvsLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR-----GYVFQQGS 112
Cdd:PRK10575 19 FRVPGRTLLHPLS---LTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfarkvAYLPQQLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 113 LFPWLTVEENIAFG-------LKAQGIYKEHEADAAryIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDE 185
Cdd:PRK10575 96 AAEGMTVRELVAIGrypwhgaLGRFGAADREKVEEA--ISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 505262942 186 PMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEA 223
Cdd:PRK10575 174 PTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMA 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
38-223 |
2.58e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.01 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 38 FTAPDgsvvhalsDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEgPNP----KR-GYVFQQGS 112
Cdd:NF033858 279 FTAVD--------HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD-AGDiatrRRvGYMSQAFS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 113 LFPWLTVEENIA-----FGLKAQGIykeheadAARYIEMV---GLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLD 184
Cdd:NF033858 350 LYGELTVRQNLElharlFHLPAAEI-------AARVAEMLerfDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
170 180 190
....*....|....*....|....*....|....*....
gi 505262942 185 EPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEA 223
Cdd:NF033858 423 EPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEA 461
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
56-191 |
2.94e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 76.04 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 56 IYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR--GYVFQQGSLFPWLTVEENIAFGLKAQGIY 133
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRfmAYLGHLPGLKADLSTLENLHFLCGLHGRR 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 134 KEHEADAAryIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALD 191
Cdd:PRK13543 114 AKQMPGSA--LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
51-257 |
3.40e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.67 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 51 DVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNP----KRGYVF-----QQGSLFPWLTVEE 121
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavKKGMAYitesrRDNGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 122 NIAF-------GLK-AQGIYKEHE----ADAARYIEMVGLHGFEQAYpHQISGGMAQRVAIARALIDHPDVLLLDEPMGA 189
Cdd:PRK09700 361 NMAIsrslkdgGYKgAMGLFHEVDeqrtAENQRELLALKCHSVNQNI-TELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 190 LDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEIvpinLDARDRVSDE 257
Cdd:PRK09700 440 IDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVF--CEGRLTQI----LTNRDDMSEE 500
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
44-219 |
3.90e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.12 E-value: 3.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 44 SVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLdHPQSGTLSLAGEPIEG-PNPK----RGYVFQQGSLFPWLT 118
Cdd:PRK03695 7 AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAwSAAElarhRAYLSQQQTPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 119 VEENIAFGLKAQGIYKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALID-HPDV------LLLDEPMGALD 191
Cdd:PRK03695 86 VFQYLTLHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLD 165
|
170 180
....*....|....*....|....*...
gi 505262942 192 SFTRADLqDRLLDIWEQYHMTMILVTHD 219
Cdd:PRK03695 166 VAQQAAL-DRLLSELCQQGIAVVMSSHD 192
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
51-204 |
6.47e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.85 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 51 DVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLagepieGPNPKRGYVFQQ-GSLFPWLTVEENIAFGLKA 129
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------GETVKLAYVDQSrDALDPNKTVWEEISGGLDI 415
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505262942 130 QGIYKeHEADAARYIEMVGLHGFEQAYP-HQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLD 204
Cdd:PRK11819 416 IKVGN-REIPSRAYVGRFNFKGGDQQKKvGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLE 490
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-192 |
6.51e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.64 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFTApdgsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRGY 106
Cdd:PRK11288 3 PYLSFDGIGKTFPG-----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 107 ------VFQQGSLFPWLTVEENIAFG-LKAQ-GIYKEHE--ADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALID 176
Cdd:PRK11288 78 aagvaiIYQELHLVPEMTVAENLYLGqLPHKgGIVNRRLlnYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALAR 157
|
170
....*....|....*.
gi 505262942 177 HPDVLLLDEPMGALDS 192
Cdd:PRK11288 158 NARVIAFDEPTSSLSA 173
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
49-192 |
1.25e-15 |
|
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: 73.43 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQ--SGTLSLAGEPIEGPNPKR-GYVFQQGSLFPWLTVEENIAF 125
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNFQRStGYVEQQDVHSPNLTVREALRF 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505262942 126 GLKAQGIYKEHEadaaryiemvglhgfeqayphqisggmaQRVAIARALIDHPDVLLLDEPMGALDS 192
Cdd:cd03232 103 SALLRGLSVEQR----------------------------KRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
29-240 |
1.42e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSreftapdGSVVHalsDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRG--- 105
Cdd:PRK10762 258 LKVDNLS-------GPGVN---DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlan 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 106 ---YVFQQ---GSLFPWLTVEENI-----------AFGLKAQgiyKEHEAdAARYIEMvglhgFEQAYPHQ------ISG 162
Cdd:PRK10762 328 givYISEDrkrDGLVLGMSVKENMsltalryfsraGGSLKHA---DEQQA-VSDFIRL-----FNIKTPSMeqaiglLSG 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 163 GMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDrLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRI 240
Cdd:PRK10762 399 GNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ-LINQFKAEGLSIILVSSEMPEVLGMSDRILVM--HEGRI 473
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
8-231 |
2.45e-15 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 76.15 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 8 HLAVASGRQTLADVPAGVNPELSIEHVSREFTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQS 87
Cdd:TIGR01194 317 ELELSDADNVLLLAHDKSVDSIELKDVHMNPKAPEGSEGFALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 88 GTLSLAGEPIEGPNpkRGYVFQqgsLFPWLTVEENIaFGLKAQGIYKEHEA--DAARYIEMVGL------HGFEQAYPHQ 159
Cdd:TIGR01194 397 GEILLDGAAVSADS--RDDYRD---LFSAIFADFHL-FDDLIGPDEGEHASldNAQQYLQRLEIadkvkiEDGGFSTTTA 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505262942 160 ISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDvDEAIYLGSRVV 231
Cdd:TIGR01194 471 LSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHD-DQYFELADQII 541
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-192 |
4.23e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.44 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 25 VNPELSIEHVSreFTAPdGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIegpnpkR 104
Cdd:PRK11176 338 AKGDIEFRNVT--FTYP-GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL------R 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 105 GY-----------VFQQGSLFPwLTVEENIAFGlkAQGIYKEHE-------ADAARYIE--------MVGLHGFeqayph 158
Cdd:PRK11176 409 DYtlaslrnqvalVSQNVHLFN-DTIANNIAYA--RTEQYSREQieeaarmAYAMDFINkmdngldtVIGENGV------ 479
|
170 180 190
....*....|....*....|....*....|....
gi 505262942 159 QISGGMAQRVAIARALIDHPDVLLLDEPMGALDS 192
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
47-217 |
9.20e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 74.77 E-value: 9.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 47 HALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLagepIEGpnpKRGYVFQQGSLFPwLTVEENIAFG 126
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV----IRG---TVAYVPQVSWIFN-ATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 127 LkaqgiykehEADAARY---IEMVGLHGFEQAYPH-----------QISGGMAQRVAIARALIDHPDVLLLDEPMGALDS 192
Cdd:PLN03130 703 S---------PFDPERYeraIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180
....*....|....*....|....*
gi 505262942 193 FTRADLQDRLLDiWEQYHMTMILVT 217
Cdd:PLN03130 774 HVGRQVFDKCIK-DELRGKTRVLVT 797
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
49-258 |
1.18e-14 |
|
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: 74.21 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPiegpnpkrGYVFQQGslfpWL---TVEENIAF 125
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV--------AYVPQQA----WIqndSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 126 GLKAQGIYKEHEADA-ARYIEMVGLHGFEQAYPHQ----ISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQD 200
Cdd:TIGR00957 722 GKALNEKYYQQVLEAcALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 201 RLLDIWEQY-HMTMILVTHDVDeaiYLGSRVVIMTPRPGRIKEIVPIN-LDARDRVSDEF 258
Cdd:TIGR00957 802 HVIGPEGVLkNKTRILVTHGIS---YLPQVDVIIVMSGGKISEMGSYQeLLQRDGAFAEF 858
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
49-221 |
1.54e-14 |
|
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: 72.20 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEpiegpnpkrgyvFQQGSLFPWL---TVEENIAF 125
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR------------ISFSSQFSWImpgTIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 126 GLKaqgiYKEHeadaaRYIEMVGLHGFEQ---AYPHQ-----------ISGGMAQRVAIARALIDHPDVLLLDEPMGALD 191
Cdd:cd03291 121 GVS----YDEY-----RYKSVVKACQLEEditKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190
....*....|....*....|....*....|
gi 505262942 192 SFTRADLQDRLLdIWEQYHMTMILVTHDVD 221
Cdd:cd03291 192 VFTEKEIFESCV-CKLMANKTRILVTSKME 220
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
27-244 |
1.78e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 72.63 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQ----SGTLSLAG-EPIEGPN 101
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRV-KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGiDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 102 PKR--------GYVFQ--QGSLFPWLTV----EENIAFGLKAQGIYKEHEADAARYIEM---VGLHGFE---QAYPHQIS 161
Cdd:COG4170 81 RERrkiigreiAMIFQepSSCLDPSAKIgdqlIEAIPSWTFKGKWWQRFKWRKKRAIELlhrVGIKDHKdimNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 162 GGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQdRLLDIWEQYH-MTMILVTHDVDEAIYLGSRVVIM----TPR 236
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIF-RLLARLNQLQgTSILLISHDLESISQWADTITVLycgqTVE 239
|
....*...
gi 505262942 237 PGRIKEIV 244
Cdd:COG4170 240 SGPTEQIL 247
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-222 |
2.12e-14 |
|
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: 73.32 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTApdgsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLdHPQ---SGTLSLAGEPIEGPN---- 101
Cdd:TIGR02633 2 LEMKGIVKTFGG-----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASNirdt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 102 PKRGYVF--QQGSLFPWLTVEENIAFG----------------LKAQGIYKEHEADAARYIEMVGlhgfeqayphQISGG 163
Cdd:TIGR02633 76 ERAGIVIihQELTLVPELSVAENIFLGneitlpggrmaynamyLRAKNLLRELQLDADNVTRPVG----------DYGGG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505262942 164 MAQRVAIARALIDHPDVLLLDEPMGALdsfTRADLQDrLLDI---WEQYHMTMILVTHDVDE 222
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPSSSL---TEKETEI-LLDIirdLKAHGVACVYISHKLNE 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
50-245 |
2.39e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 50 SDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPK----RGYVF------QQGsLFPWLTV 119
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdairAGIMLcpedrkAEG-IIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 120 EENIA-----FGLKAQGIYKEH-EAD-AARYIEMVGLhgfEQAYPHQ----ISGGMAQRVAIARALIDHPDVLLLDEPMG 188
Cdd:PRK11288 349 ADNINisarrHHLRAGCLINNRwEAEnADRFIRSLNI---KTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505262942 189 ALDSFTRADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEIVP 245
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVM--REGRIAGELA 479
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
47-221 |
4.66e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 4.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 47 HALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAG--LDHPQSGTLSLagepiegpnpkrgyvfqqgslfPWLTVEENIA 124
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV----------------------PDNQFGREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 125 FglkAQGIYKEHE-ADAARYIEMVGLhgfEQAY-----PHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADL 198
Cdd:COG2401 102 L---IDAIGRKGDfKDAVELLNAVGL---SDAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180
....*....|....*....|...
gi 505262942 199 QDRLLDIWEQYHMTMILVTHDVD 221
Cdd:COG2401 176 ARNLQKLARRAGITLVVATHHYD 198
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
46-257 |
4.82e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.13 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 46 VHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLdHPQ---SGTLSLAGEPIEGPN----PKRGYVF--QQGSLFPW 116
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCRFKDirdsEALGIVIihQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 117 LTVEENIAFG--LKAQGI--YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGAL-- 190
Cdd:NF040905 93 LSIAENIFLGneRAKRGVidWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALne 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 191 -DSftrADLQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIKEivpiNLDARDRVSDE 257
Cdd:NF040905 173 eDS---AALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVL--RDGRTIE----TLDCRADEVTE 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
43-233 |
6.58e-14 |
|
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: 72.35 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 43 GSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEP----IEGPNPKRGYVFQQGSLFPWLT 118
Cdd:TIGR01257 1949 GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltnISDVHQNMGYCPQFDAIDDLLT 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 119 VEENIAFGLKAQGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRAD 197
Cdd:TIGR01257 2029 GREHLYLYARLRGVpAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180 190
....*....|....*....|....*....|....*.
gi 505262942 198 LQDRLLDIWEQyHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:TIGR01257 2109 LWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
49-233 |
7.46e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.24 E-value: 7.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGlDHPQS---------GTLSLAGEPIEGPNPK-----RGYVFQQGS-L 113
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPrlarlRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 114 FPWlTVEENIAFG----LKAQGIYKEHEAD-AARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALID-HPD-------- 179
Cdd:PRK13547 96 FAF-SAREIVLLGryphARRAGALTHRDGEiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlWPPhdaaqppr 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505262942 180 VLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAML 228
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
49-205 |
8.59e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.20 E-value: 8.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGlDHPQ--SGTLSL------AGEPIEGPNPKRGYVFQQGSLFPWL--T 118
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgySNDLTLfgrrrgSGETIWDIKKHIGYVSSSLHLDYRVstS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 119 VEENIAFG-LKAQGIYKE----HEADAARYIEMVGLHGFEQAYP-HQISGGMAQRVAIARALIDHPDVLLLDEPMGALDS 192
Cdd:PRK10938 355 VRNVILSGfFDSIGIYQAvsdrQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
170
....*....|...
gi 505262942 193 FTRaDLQDRLLDI 205
Cdd:PRK10938 435 LNR-QLVRRFVDV 446
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
28-255 |
9.68e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.16 E-value: 9.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 28 ELSIEHVSreFTAPDGSVvhALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPkRGY- 106
Cdd:PRK10522 322 TLELRNVT--FAYQDNGF--SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP-EDYr 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 107 -----VFQQGSLFPWLtveeniafgLKAQGIYKEhEADAARYIEMVGLHGFEQAYPHQI-----SGGMAQRVAIARALID 176
Cdd:PRK10522 397 klfsaVFTDFHLFDQL---------LGPEGKPAN-PALVEKWLERLKMAHKLELEDGRIsnlklSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 177 HPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDvDEAIYLGSRVVIMtpRPGRIKEIVPinlDARDRVS 255
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEM--RNGQLSELTG---EERDAAS 539
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
49-205 |
1.61e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 67.97 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEG-PNPKRGYVFQQGSLFPWLTVEENIAFGL 127
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKPYCTYIGHNLGLKLEMTVFENLKFWS 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 128 KaqgIYKEHEA-DAAryIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRaDLQDRLLDI 205
Cdd:PRK13541 96 E---IYNSAETlYAA--IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR-DLLNNLIVM 168
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
49-191 |
1.72e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.05 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEgpnpKRGYVFQQGSLF--------PWLTVE 120
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTYQKQLCFvghrsginPYLTLR 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505262942 121 ENIAFGLkaqgiykeHEADAARYI-EMVGLHGFEQA--YP-HQISGGMAQRVAIARALIDHPDVLLLDEPMGALD 191
Cdd:PRK13540 93 ENCLYDI--------HFSPGAVGItELCRLFSLEHLidYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
9-101 |
1.93e-13 |
|
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: 70.21 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 9 LAVASGRQTLADVPAGVNP----ELSIEHVSREFTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDH 84
Cdd:COG4615 304 LALAAAEPAAADAAAPPAPadfqTLELRGVTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYR 383
|
90
....*....|....*..
gi 505262942 85 PQSGTLSLAGEPIEGPN 101
Cdd:COG4615 384 PESGEILLDGQPVTADN 400
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
46-196 |
2.32e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.03 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 46 VHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR------GYVFQQGSLFPWLTV 119
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsqeagiGIIHQELNLIPQLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 120 EENI--------AFGlkaqGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGAL 190
Cdd:PRK10762 97 AENIflgrefvnRFG----RIdWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
....*..
gi 505262942 191 -DSFTRA 196
Cdd:PRK10762 173 tDTETES 179
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
49-192 |
3.11e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.00 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAG-LDHPQSGTLSLAGEPiegpnpkrGYVFQqgslFPWL---TVEENIA 124
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSV--------AYVPQ----VSWIfnaTVRENIL 700
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505262942 125 FGLKAQG---------IYKEHEAD--AARYIEMVGLHGFeqayphQISGGMAQRVAIARALIDHPDVLLLDEPMGALDS 192
Cdd:PLN03232 701 FGSDFESerywraidvTALQHDLDllPGRDLTEIGERGV------NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
38-203 |
3.41e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 69.94 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 38 FTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNpkrgyvfqqgslFPWL 117
Cdd:TIGR01271 431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQ------------TSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 118 ---TVEENIAFGLKaqgiYKEHeadaaRYIEMVGLHGFEQ---AYPHQ-----------ISGGMAQRVAIARALIDHPDV 180
Cdd:TIGR01271 499 mpgTIKDNIIFGLS----YDEY-----RYTSVIKACQLEEdiaLFPEKdktvlgeggitLSGGQRARISLARAVYKDADL 569
|
170 180
....*....|....*....|...
gi 505262942 181 LLLDEPMGALDSFTRADLQDRLL 203
Cdd:TIGR01271 570 YLLDSPFTHLDVVTEKEIFESCL 592
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
43-239 |
7.59e-13 |
|
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: 68.66 E-value: 7.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 43 GSVVHALSDVSLS-----IYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSG----TLSLAGEP--IEGPNPKrgyvfqqg 111
Cdd:COG1245 345 PDLTKSYGGFSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGevdeDLKISYKPqyISPDYDG-------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 112 slfpwlTVEENI--AFGLKAQGIYKEHEadaarYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGA 189
Cdd:COG1245 417 ------TVEEFLrsANTDDFGSSYYKTE-----IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505262942 190 LDSFTRADLQDRLLDIWEQYHMTMILVTHDV---DeaiYLGSRVVIMTPRPGR 239
Cdd:COG1245 486 LDVEQRLAVAKAIRRFAENRGKTAMVVDHDIyliD---YISDRLMVFEGEPGV 535
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-222 |
1.07e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFTApdgsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLdHPQ---SGTLSLAGEPIEGPNPK-- 103
Cdd:PRK13549 6 LEMKNITKTFGG-----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNIRdt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 104 --RGYV--FQQGSLFPWLTVEENIAFG--LKAQGI--YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALI 175
Cdd:PRK13549 80 erAGIAiiHQELALVKELSVLENIFLGneITPGGImdYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505262942 176 DHPDVLLLDEPMGALdsfTRADLqDRLLDIWE---QYHMTMILVTHDVDE 222
Cdd:PRK13549 160 KQARLLILDEPTASL---TESET-AVLLDIIRdlkAHGIACIYISHKLNE 205
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
29-218 |
1.70e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.44 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSreFTAPDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPK--RGY 106
Cdd:PRK10790 341 IDIDNVS--FAYRDDNLV--LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 107 V--FQQGSLFPWLTVEENIAFGlkaQGIYKEHEADAaryIEMVGLHGFEQAYPHQI-----------SGGMAQRVAIARA 173
Cdd:PRK10790 417 VamVQQDPVVLADTFLANVTLG---RDISEEQVWQA---LETVQLAELARSLPDGLytplgeqgnnlSVGQKQLLALARV 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505262942 174 LIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEqyHMTMILVTH 218
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAH 533
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-218 |
2.55e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.04 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 15 RQTLADVPAGVNPELSIEHVS-------REFTAPdGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQS 87
Cdd:PRK10789 291 RAMLAEAPVVKDGSEPVPEGRgeldvniRQFTYP-QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 88 GTLSLAGEPI-----EGPNPKRGYVFQQGSLFPwLTVEENIAFG---LKAQGIykEHEADAAR-----------YIEMVG 148
Cdd:PRK10789 370 GDIRFHDIPLtklqlDSWRSRLAVVSQTPFLFS-DTVANNIALGrpdATQQEI--EHVARLASvhddilrlpqgYDTEVG 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505262942 149 LHGFeqayphQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRAD-LQDrlLDIWEQyHMTMILVTH 218
Cdd:PRK10789 447 ERGV------MLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQiLHN--LRQWGE-GRTVIISAH 508
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
48-220 |
1.02e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKR--GYVFQQGSL---FPWLtVEEN 122
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNlvAYVPQSEEVdwsFPVL-VEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 123 IAFG-------LKAQGIYKEHEADAAryIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTR 195
Cdd:PRK15056 101 VMMGryghmgwLRRAKKRDRQIVTAA--LARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180
....*....|....*....|....*
gi 505262942 196 ADLQDRLLDIWEQyHMTMILVTHDV 220
Cdd:PRK15056 179 ARIISLLRELRDE-GKTMLVSTHNL 202
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
58-237 |
2.12e-11 |
|
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: 60.85 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 58 PGELVSIIGPSGCGKTTLLRLIAG-LDHPQSGTLSLAGEPIEGPNPKRGYVFQQGSlfpwltveeniafglkaqgiykeh 136
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLIIVGG------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 137 eadaaryiemvglhgfeqaYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQD-----RLLDIWEQYHM 211
Cdd:smart00382 57 -------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrLLLLLKSEKNL 117
|
170 180 190
....*....|....*....|....*....|
gi 505262942 212 TMILVTHDV----DEAIYLGSRVVIMTPRP 237
Cdd:smart00382 118 TVILTTNDEkdlgPALLRRRFDRRIVLLLI 147
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
38-222 |
2.40e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.14 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 38 FTAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPI-----EGPNPKrgyvfqqgs 112
Cdd:PRK13545 29 FRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAliaisSGLNGQ--------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 113 lfpwLTVEENIAFGLKAQGIYKEHEAD-AARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALD 191
Cdd:PRK13545 100 ----LTGIENIELKGLMMGLTKEKIKEiIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190
....*....|....*....|....*....|..
gi 505262942 192 -SFTRADLqDRLLDIWEQyHMTMILVTHDVDE 222
Cdd:PRK13545 176 qTFTKKCL-DKMNEFKEQ-GKTIFFISHSLSQ 205
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-219 |
2.57e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.04 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 26 NPELSIEHVSREFTapDGSVvhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAgepiegPNPKRG 105
Cdd:PRK10636 310 NPLLKMEKVSAGYG--DRII---LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA------KGIKLG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 106 YvFQQGSLfPWLTVEENIAFGLkAQGIYKEHEADAARYIEMVGLHGFEQAYP-HQISGGMAQRVAIARALIDHPDVLLLD 184
Cdd:PRK10636 379 Y-FAQHQL-EFLRADESPLQHL-ARLAPQELEQKLRDYLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190
....*....|....*....|....*....|....*
gi 505262942 185 EPMGALDSFTRADLQDRLLDiweqYHMTMILVTHD 219
Cdd:PRK10636 456 EPTNHLDLDMRQALTEALID----FEGALVVVSHD 486
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
27-233 |
2.93e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.28 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 27 PELSIEHVSREFTAPDGSVvHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGL--DHPQSGTLSLAGEPIE----GP 100
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWV-KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkDNWRVTADRMRFDDIDllrlSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 101 NPKRGYV-------FQ--QGSLFPwltvEENIAFGLkAQGI----YKEH-----EADAARYIEMVGLHGFE------QAY 156
Cdd:PRK15093 81 RERRKLVghnvsmiFQepQSCLDP----SERVGRQL-MQNIpgwtYKGRwwqrfGWRKRRAIELLHRVGIKdhkdamRSF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505262942 157 PHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:PRK15093 156 PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
56-239 |
3.53e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 56 IYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSlagepiegPNPKRGYVFQQGSLFPWLTVEENIAF-GLKAQGIYK 134
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--------PELKISYKPQYIKPDYDGTVEDLLRSiTDDLGSSYY 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 135 EHEadaarYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSftradlQDRLL------DIWEQ 208
Cdd:PRK13409 434 KSE-----IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV------EQRLAvakairRIAEE 502
|
170 180 190
....*....|....*....|....*....|.
gi 505262942 209 YHMTMILVTHDVDEAIYLGSRVVIMTPRPGR 239
Cdd:PRK13409 503 REATALVVDHDIYMIDYISDRLMVFEGEPGK 533
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
107-263 |
3.73e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.89 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 107 VFQQGSLFPwLTVEENIAFGlkaqgiyKEHEA--DAARYIEMVGLHGFEQAYPHQ-----------ISGGMAQRVAIARA 173
Cdd:PTZ00265 1301 VSQEPMLFN-MSIYENIKFG-------KEDATreDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARA 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 174 LIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILVTHDVdEAIYLGSRVVIMTpRPGRIKEIVPINLDARDR 253
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFN-NPDRTGSFVQAHGTHEEL 1450
|
170
....*....|
gi 505262942 254 VSDEFAAYRK 263
Cdd:PTZ00265 1451 LSVQDGVYKK 1460
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
46-238 |
3.86e-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: 60.66 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 46 VHALSDVSLSIYP-----GELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIegpnpkrgyvfqqgslfpwltve 120
Cdd:cd03222 7 VKRYGVFFLLVELgvvkeGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP----------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 121 eniafglkaqgIYKeheadaARYIEMvglhgfeqayphqiSGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQD 200
Cdd:cd03222 64 -----------VYK------PQYIDL--------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAAR 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 505262942 201 RLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMTPRPG 238
Cdd:cd03222 113 AIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
49-192 |
8.46e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.87 E-value: 8.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLsLAGEPIegpnpkrGYVFQQgslfPWL---TVEENIAF 125
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSI-------AYVPQQ----AWImnaTVRGNILF 743
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262942 126 glkaqgIYKEHEADAARYIEMVGLH--------GFEQAYPHQ---ISGGMAQRVAIARALIDHPDVLLLDEPMGALDS 192
Cdd:PTZ00243 744 ------FDEEDAARLADAVRVSQLEadlaqlggGLETEIGEKgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
41-218 |
9.15e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 62.46 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 41 PDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLagepiegpnPKRG---YVFQQgslfPWL 117
Cdd:TIGR00954 462 PNGDVL--IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGklfYVPQR----PYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 118 TVEEniafgLKAQGIYKE----------HEADAARYIEMVGLH-------GFE--QAYPHQISGGMAQRVAIARALIDHP 178
Cdd:TIGR00954 527 TLGT-----LRDQIIYPDssedmkrrglSDKDLEQILDNVQLThileregGWSavQDWMDVLSGGEKQRIAMARLFYHKP 601
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505262942 179 DVLLLDEPMGALDsftrADLQDRLLDIWEQYHMTMILVTH 218
Cdd:TIGR00954 602 QFAILDECTSAVS----VDVEGYMYRLCREFGITLFSVSH 637
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-194 |
1.77e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 10 AVASGRQTLADVP-AGVNPelsIEHVSREFTAPDGSV-VHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAG-LDHPQ 86
Cdd:TIGR00956 39 GVAADSDYQPTFPnALLKI---LTRGFRKLKKFRDTKtFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFH 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 87 ---SGTLSLAG-EPIEGPNPKRGYVFQQGSL---FPWLTVEENIAFGLKAQG-----------IYKEHEADAarYIEMVG 148
Cdd:TIGR00956 116 igvEGVITYDGiTPEEIKKHYRGDVVYNAETdvhFPHLTVGETLDFAARCKTpqnrpdgvsreEYAKHIADV--YMATYG 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505262942 149 L-HGFEQA----YPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFT 194
Cdd:TIGR00956 194 LsHTRNTKvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT 244
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
29-236 |
2.74e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.68 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREFtapDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAgepiegPNPKRGYVF 108
Cdd:PRK15064 320 LEVENLTKGF---DNGPL--FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS------ENANIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 109 QQGS--------LFPWLtveeniafglkAQGIYKEHEADAARyiEMVGLHGFEQ----AYPHQISGGMAQRVAIARALID 176
Cdd:PRK15064 389 QDHAydfendltLFDWM-----------SQWRQEGDDEQAVR--GTLGRLLFSQddikKSVKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 177 HPDVLLLDEPMGALDSFTRADLQDRLldiwEQYHMTMILVTHDVDEAIYLGSRVVIMTPR 236
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLNMAL----EKYEGTLIFVSHDREFVSSLATRIIEITPD 511
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
49-219 |
3.53e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSlAGEPIEgpnpkRGYvFQQ--GSLFPWLTVEENIAFG 126
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKLE-----VAY-FDQhrAELDPEKTVMDNLAEG 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 127 LKAQGI--YKEHeadAARYIEMVGLHGFEQAYP-HQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTrADLQDRLL 203
Cdd:PRK11147 408 KQEVMVngRPRH---VLGYLQDFLFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET-LELLEELL 483
|
170
....*....|....*.
gi 505262942 204 DiweQYHMTMILVTHD 219
Cdd:PRK11147 484 D---SYQGTVLLVSHD 496
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
48-242 |
4.36e-10 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 58.66 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTT----LLRLIagldHPQSGTLSLAGEPIE--GPNPKR---GYVFQQGSLFPWlT 118
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISkiGLHDLRsriSIIPQDPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 119 VEENIAfglkaqgIYKEH-EADAARYIEMVGLHGFEQAYPHQI-----------SGGMAQRVAIARALIDHPDVLLLDEP 186
Cdd:cd03244 94 IRSNLD-------PFGEYsDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505262942 187 MGALDSFTRADLQDRLLDiwEQYHMTMILVTH------DVDeaiylgsRVVIMTprPGRIKE 242
Cdd:cd03244 167 TASVDPETDALIQKTIRE--AFKDCTVLTIAHrldtiiDSD-------RILVLD--KGRVVE 217
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
47-220 |
5.42e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 58.67 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 47 HALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPiegpnpkrGYVFQQGSLFPWLTVEENIAFG 126
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV--------SVIAISAGLSGQLTGIENIEFK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 127 LKAQGI-YKEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALD-SFTRADLqDRLLD 204
Cdd:PRK13546 110 MLCMGFkRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDqTFAQKCL-DKIYE 188
|
170
....*....|....*.
gi 505262942 205 IWEQyHMTMILVTHDV 220
Cdd:PRK13546 189 FKEQ-NKTIFFVSHNL 203
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
28-243 |
9.44e-10 |
|
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: 57.42 E-value: 9.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 28 ELSIEHVSREFtAPDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGE-----PIEGPNP 102
Cdd:cd03369 6 EIEVENLSVRY-APDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 103 KRGYVFQQGSLFPWlTVEENiafgLKAQGIYKEHEADAARYIEMVGLHgfeqayphqISGGMAQRVAIARALIDHPDVLL 182
Cdd:cd03369 83 SLTIIPQDPTLFSG-TIRSN----LDPFDEYSDEEIYGALRVSEGGLN---------LSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505262942 183 LDEPMGALDSFTRADLQDrllDIWEQY-HMTMILVTHDVDEAIYLgSRVVIMTprPGRIKEI 243
Cdd:cd03369 149 LDEATASIDYATDALIQK---TIREEFtNSTILTIAHRLRTIIDY-DKILVMD--AGEVKEY 204
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
49-221 |
1.16e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAG---------EPIEGPNPKRGYVFQQGSLFPWLTV 119
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqETPALPQPALEYVIDGDREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 120 EENIAF----GLKAQGIYKEHEADAARYIE------MVGLhGFEQAYPHQ----ISGGMAQRVAIARALIDHPDVLLLDE 185
Cdd:PRK10636 97 QLHDANerndGHAIATIHGKLDAIDAWTIRsraaslLHGL-GFSNEQLERpvsdFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505262942 186 PMGALDsftradlqdrlLD--IW-----EQYHMTMILVTHDVD 221
Cdd:PRK10636 176 PTNHLD-----------LDavIWlekwlKSYQGTLILISHDRD 207
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
49-219 |
1.96e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAG---LDhpqSGTLSLAGEPI----EGPNPKRgyvfQQGSLFPWltvee 121
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLD---DGRIIYEQDLIvarlQQDPPRN----VEGTVYDF----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 122 nIAFGLKAQGIYKEHEADAARYIE-------MVGLHGFEQAYPHQ--------------------------ISGGMAQRV 168
Cdd:PRK11147 87 -VAEGIEEQAEYLKRYHDISHLVEtdpseknLNELAKLQEQLDHHnlwqlenrinevlaqlgldpdaalssLSGGWLRKA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505262942 169 AIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDiweqYHMTMILVTHD 219
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT----FQGSIIFISHD 212
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
49-218 |
4.77e-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: 55.23 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGldHPqsgtlslagepieGPNPKRGYVFQQGSLFPWLTVEENIAFGL- 127
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HP-------------KYEVTEGEILFKGEDITDLPPEERARLGIf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 128 -------KAQGIykeHEADAARYIEMvglhGFeqayphqiSGGMAQRVAIARALIDHPDVLLLDEPMGALDsFTRADLQD 200
Cdd:cd03217 81 lafqyppEIPGV---KNADFLRYVNE----GF--------SGGEKKRNEILQLLLLEPDLAILDEPDSGLD-IDALRLVA 144
|
170
....*....|....*...
gi 505262942 201 RLLDIWEQYHMTMILVTH 218
Cdd:cd03217 145 EVINKLREEGKSVLIITH 162
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
65-219 |
1.64e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.28 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 65 IGPSGCGKTTLLRLIAGLDHPQSGTLSLAgepiegPNPKRGYVFQQGSLFPWLTVEENIAFG------LKAQ--GIYKEH 136
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLD------PNERLGKLRQDQFAFEEFTVLDTVIMGhtelweVKQErdRIYALP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 137 EADAARYI----------EMVG----------LHGF----EQAYP--HQISGGMAQRVAIARALIDHPDVLLLDEPMGAL 190
Cdd:PRK15064 107 EMSEEDGMkvadlevkfaEMDGytaearagelLLGVgipeEQHYGlmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNL 186
|
170 180
....*....|....*....|....*....
gi 505262942 191 DSFTRADLQDRLldiwEQYHMTMILVTHD 219
Cdd:PRK15064 187 DINTIRWLEDVL----NERNSTMIIISHD 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
46-218 |
2.41e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 46 VHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTL------SLAGEPIEGPNPKRGYVFQQGSLFPwLTV 119
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshNLKDINLKWWRSKIGVVSQDPLLFS-NSI 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 120 EENIAFGL--------------------------------KAQGIYKE--HEADAARYIEM------------------V 147
Cdd:PTZ00265 477 KNNIKYSLyslkdlealsnyynedgndsqenknkrnscraKCAGDLNDmsNTTDSNELIEMrknyqtikdsevvdvskkV 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 148 GLHGFEQAYP-----------HQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQYHMTMILV 216
Cdd:PTZ00265 557 LIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIII 636
|
..
gi 505262942 217 TH 218
Cdd:PTZ00265 637 AH 638
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-233 |
4.14e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.06 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 29 LSIEHVSREftAPDGSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQ-SGTLSLAGEPIEGPNP----K 103
Cdd:TIGR02633 258 LEARNLTCW--DVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPaqaiR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 104 RGYVF-----QQGSLFPWLTVEENI------AFGLKAQgIYKEHEADA-ARYIEMVGLHGFEQAYP-HQISGGMAQRVAI 170
Cdd:TIGR02633 336 AGIAMvpedrKRHGIVPILGVGKNItlsvlkSFCFKMR-IDAAAELQIiGSAIQRLKVKTASPFLPiGRLSGGNQQKAVL 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505262942 171 ARALIDHPDVLLLDEPMGALDSFTRADLQdRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIM 233
Cdd:TIGR02633 415 AKMLLTNPRVLILDEPTRGVDVGAKYEIY-KLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
49-194 |
3.01e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAG---LDHPQSGTLSLAGEPIEGPNPKR-GYVFQQGSLFPWLTVEENI- 123
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErvtTGVITGGDRLVNGRPLDSSFQRSiGYVQQQDLHLPTSTVRESLr 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 124 --AFGLKAQGIYKEHEADAARYI----EM-------VGLHG----FEQayphqisggmAQRVAIARALIDHPDVLL-LDE 185
Cdd:TIGR00956 859 fsAYLRQPKSVSKSEKMEYVEEVikllEMesyadavVGVPGeglnVEQ----------RKRLTIGVELVAKPKLLLfLDE 928
|
....*....
gi 505262942 186 PMGALDSFT 194
Cdd:TIGR00956 929 PTSGLDSQT 937
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
58-238 |
3.80e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.44 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 58 PGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRGYVFQQgslfpWLT--VEENIAFGLKAQG---- 131
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQN-----YFTklLEGDVKVIVKPQYvdli 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 132 -----------IYKEHEADAA-RYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALD---SFTRA 196
Cdd:cd03236 100 pkavkgkvgelLKKKDERGKLdELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDikqRLNAA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505262942 197 DLQDRLLdiweQYHMTMILVTHDVDEAIYLGSRVVIMTPRPG 238
Cdd:cd03236 180 RLIRELA----EDDNYVLVVEHDLAVLDYLSDYIHCLYGEPG 217
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
53-222 |
6.10e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 53 SLSIYPGELVSIIGPSGCGKTTLLRLIAGldhpqSGTLsLAGEpiegpnpkRGYVFQQGSLFP-----------W----- 116
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG-----ELPL-LSGE--------RQSQFSHITRLSfeqlqklvsdeWqrnnt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 117 --LTVEENiAFGLKAQGIYKEHEADAARYIEMVGLHGFEQAYPH---QISGGMAQRVAIARALIDHPDVLLLDEPMGALD 191
Cdd:PRK10938 89 dmLSPGED-DTGRTTAEIIQDEVKDPARCEQLAQQFGITALLDRrfkYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190
....*....|....*....|....*....|.
gi 505262942 192 SFTRADLQDRLLDIWEQyHMTMILVTHDVDE 222
Cdd:PRK10938 168 VASRQQLAELLASLHQS-GITLVLVLNRFDE 197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
28-232 |
6.18e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.68 E-value: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 28 ELSIEHVSREFTApDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLrliagldhpqSGTLSLAGepIEGPNPKRGYV 107
Cdd:TIGR01271 1217 QMDVQGLTAKYTE-AGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLL----------SALLRLLS--TEGEIQIDGVS 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 108 FQQGSLFPWLTveeniAFGLKAQGIY------------KEHEADAA--RYIEMVGLHGFEQAYPHQ-----------ISG 162
Cdd:TIGR01271 1282 WNSVTLQTWRK-----AFGVIPQKVFifsgtfrknldpYEQWSDEEiwKVAEEVGLKSVIEQFPDKldfvlvdggyvLSN 1356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 163 GMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEqyHMTMILVTHDVDEAIYLGSRVVI 232
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFS--NCTVILSEHRVEALLECQQFLVI 1424
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
64-219 |
9.19e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 48.37 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 64 IIGPSGCGKTTLLRLI-AGL--DHPQSGTLSLAGEPIEGPNPKRGYVfqqgslfpwltveeNIAFGLKAQGIYKeheadA 140
Cdd:cd03240 27 IVGQNGAGKTTIIEALkYALtgELPPNSKGGAHDPKLIREGEVRAQV--------------KLAFENANGKKYT-----I 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 141 ARYIEMvglhgFEQA-YPHQ-------------ISGG------MAQRVAIARALIDHPDVLLLDEPMGALDSFTRAdlqD 200
Cdd:cd03240 88 TRSLAI-----LENViFCHQgesnwplldmrgrCSGGekvlasLIIRLALAETFGSNCGILALDEPTTNLDEENIE---E 159
|
170 180
....*....|....*....|...
gi 505262942 201 RLLDIWE----QYHMTMILVTHD 219
Cdd:cd03240 160 SLAEIIEerksQKNFQLIVITHD 182
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
51-241 |
9.86e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 51 DVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQS-GTLSLAGEPIEGPNP----KRGYVF------QQGsLFPWLTV 119
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIRNPqqaiAQGIAMvpedrkRDG-IVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 120 EENIAFGL-----KAQGIYKEHEADAARYiEMVGLHgFEQAYPHQ----ISGGMAQRVAIARALIDHPDVLLLDEPMGAL 190
Cdd:PRK13549 359 GKNITLAAldrftGGSRIDDAAELKTILE-SIQRLK-VKTASPELaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505262942 191 DSFTRADLQdRLLDIWEQYHMTMILVTHDVDEAIYLGSRVVIMtpRPGRIK 241
Cdd:PRK13549 437 DVGAKYEIY-KLINQLVQQGVAIIVISSELPEVLGLSDRVLVM--HEGKLK 484
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
37-191 |
1.73e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 37 EFTAPD---GSVVHALSDVSLSiYPG---------------ELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAgepie 98
Cdd:PLN03073 496 EFPTPDdrpGPPIISFSDASFG-YPGgpllfknlnfgidldSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRS----- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 99 gpnPK-RGYVFQQGSLFPWLTVEENIAFGLKAQGIYKEHEADAarYIEMVGLHGFEQAYP-HQISGGMAQRVAIARALID 176
Cdd:PLN03073 570 ---AKvRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRA--HLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFK 644
|
170
....*....|....*
gi 505262942 177 HPDVLLLDEPMGALD 191
Cdd:PLN03073 645 KPHILLLDEPSNHLD 659
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
28-194 |
4.40e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 47.16 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 28 ELSIEHVSREFTApDGSVVhaLSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLdhpqsgtLSLAGE-PIEGPNpkrgy 106
Cdd:cd03289 2 QMTVKDLTAKYTE-GGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-------LNTEGDiQIDGVS----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 107 vFQQGSLFPWLTveeniAFGLKAQGIY--------------KEHEADAARYIEMVGLHGFEQAYPHQ-----------IS 161
Cdd:cd03289 67 -WNSVPLQKWRK-----AFGVIPQKVFifsgtfrknldpygKWSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLS 140
|
170 180 190
....*....|....*....|....*....|...
gi 505262942 162 GGMAQRVAIARALIDHPDVLLLDEPMGALDSFT 194
Cdd:cd03289 141 HGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
46-239 |
1.01e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.01 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 46 VHALSDVSLSIYPGELVSIIGPSGCGKTTLLRliAGLDhpQSGTLSLAGEPiegPNPKRGYVFQQGSLfpwltvEENIAF 125
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLY--ASGKARLISFL---PKFSRNKLIFIDQL------QFLIDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 126 GLKaqgiykeheadaarYIEMvglhgfEQAYPhQISGGMAQRVAIARALI--DHPDVLLLDEPMGALDSFTRADLQDRLL 203
Cdd:cd03238 75 GLG--------------YLTL------GQKLS-TLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIK 133
|
170 180 190
....*....|....*....|....*....|....*.
gi 505262942 204 DIWEQYHmTMILVTHDVDeAIYLGSRVVIMTPRPGR 239
Cdd:cd03238 134 GLIDLGN-TVILIEHNLD-VLSSADWIIDFGPGSGK 167
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
49-192 |
1.17e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.76 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQ--SGTLSLAGEPIEGPNPKR--GYVFQQGSLFPWLTVEENI- 123
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETFARisGYCEQNDIHSPQVTVRESLi 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 124 --AFGLKAQGIYKEHEA----DAARYIEM-------VGLHGFEqayphQISGGMAQRVAIARALIDHPDVLLLDEPMGAL 190
Cdd:PLN03140 976 ysAFLRLPKEVSKEEKMmfvdEVMELVELdnlkdaiVGLPGVT-----GLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
..
gi 505262942 191 DS 192
Cdd:PLN03140 1051 DA 1052
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
159-218 |
1.40e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 159 QISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDiWEQyhmTMILVTH 218
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK-WPK---TFIVVSH 399
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
48-244 |
2.43e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 48 ALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRGyvFQQGslFPWLTVEEniafgl 127
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEA--INHG--FALVTEER------ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 128 KAQGIYKEHE-------ADAARYIEMVGLHGFEQAYP---------------HQ-----ISGGMAQRVAIARALIDHPDV 180
Cdd:PRK10982 333 RSTGIYAYLDigfnsliSNIRNYKNKVGLLDNSRMKSdtqwvidsmrvktpgHRtqigsLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505262942 181 LLLDEPMGALDSFTRADLQDRLLDIwEQYHMTMILVTHDVDEAIYLGSRVVIMTprPGRIKEIV 244
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMS--NGLVAGIV 473
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
49-218 |
2.71e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.63 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGldHPQ----SGTLSLAGEPIEGPNP----KRG--YVFQQGSLFPWLT 118
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPeeraHLGifLAFQYPIEIPGVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 119 VEE--NIAFGLKaQGIYKEHEADAARYIEMVG----LHGFEQAYPHQ-----ISGGMAQRVAIARALIDHPDVLLLDEPM 187
Cdd:CHL00131 101 NADflRLAYNSK-RKFQGLPELDPLEFLEIINeklkLVGMDPSFLSRnvnegFSGGEKKRNEILQMALLDSELAILDETD 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 505262942 188 GALDSftradlqDRLLDIWEQYHMTM------ILVTH 218
Cdd:CHL00131 180 SGLDI-------DALKIIAEGINKLMtsensiILITH 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
31-190 |
2.73e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 31 IEHVSREFTApdgsvVHALSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTLSLAGEPIEGPNPKRG----- 105
Cdd:PRK10982 1 MSNISKSFPG-----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEAlengi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 106 -YVFQQGSLFPWLTVEENIAFG-LKAQGIYKEHEA---DAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDV 180
Cdd:PRK10982 76 sMVHQELNLVLQRSVMDNMWLGrYPTKGMFVDQDKmyrDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170
....*....|
gi 505262942 181 LLLDEPMGAL 190
Cdd:PRK10982 156 VIMDEPTSSL 165
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
134-233 |
3.47e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 134 KEHEADAARYIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTRADLQDRLLDIWEQyHMTM 213
Cdd:NF000106 119 KDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATV 197
|
90 100
....*....|....*....|
gi 505262942 214 ILVTHDVDEAIYLGSRVVIM 233
Cdd:NF000106 198 LLTTQYMEEAEQLAHELTVI 217
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
51-219 |
3.72e-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: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 51 DVSLSiyPGELVSIIGPSGCGKTTLLR---LIAGLDHPQSGtlslagepiegpnpkRGYVFQQGslfpwltveENIAfgl 127
Cdd:cd03227 15 DVTFG--EGSLTIITGPNGSGKSTILDaigLALGGAQSATR---------------RRSGVKAG---------CIVA--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 128 kaqgiykeheADAARYIEMVglhgfeqaypHQISGGMAQRVAIARALIDH---PDVL-LLDEPMGALDSFTRADLQDRLL 203
Cdd:cd03227 66 ----------AVSAELIFTR----------LQLSGGEKELSALALILALAslkPRPLyILDEIDRGLDPRDGQALAEAIL 125
|
170
....*....|....*.
gi 505262942 204 DIWEQyHMTMILVTHD 219
Cdd:cd03227 126 EHLVK-GAQVIVITHL 140
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
58-238 |
5.69e-05 |
|
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: 44.39 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 58 PGELVSIIGPSGCGKTTLLRLIAGLDHPQSGTlslagepIEGPnPKRGYVFQ--QGS-LFPWLT--VEENIAFGLKAQGI 132
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGD-------YDEE-PSWDEVLKrfRGTeLQDYFKklANGEIKVAHKPQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 133 Y---------------KEHEADAAR-YIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTR- 195
Cdd:COG1245 170 DlipkvfkgtvrelleKVDERGKLDeLAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRl 249
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505262942 196 --ADLQDRLLDIweqyHMTMILVTHDVdeAI--YLGSRVVIMTPRPG 238
Cdd:COG1245 250 nvARLIRELAEE----GKYVLVVEHDL--AIldYLADYVHILYGEPG 290
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
58-238 |
1.42e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 58 PGELVSIIGPSGCGKTTLLRLIAGLDHPQsgtlslAGEPIEGPNPKRGYVFQQGS-LFPWLT--VEENIAFGLKAQGI-- 132
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPN------LGDYEEEPSWDEVLKRFRGTeLQNYFKklYNGEIKVVHKPQYVdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 133 -------------YKEHEADAAR-YIEMVGLHGFEQAYPHQISGGMAQRVAIARALIDHPDVLLLDEPMGALDSFTR--- 195
Cdd:PRK13409 172 ipkvfkgkvrellKKVDERGKLDeVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRlnv 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505262942 196 ADLQDRLLDiwEQYhmtMILVTHDVdeAI--YLGSRVVIMTPRPG 238
Cdd:PRK13409 252 ARLIRELAE--GKY---VLVVEHDL--AVldYLADNVHIAYGEPG 289
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
49-194 |
2.59e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 49 LSDVSLSIYPGELVSIIGPSGCGKTTLLRLIAGLDHPQ---SGTLSLAGEPIEGPNPKR--GYVFQQGSLFPWLTVEENI 123
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRKtsAYISQNDVHVGVMTVKETL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 124 AFGLKAQGIYKEH-----------------EADAARYIEMVGLHGFEQA----YPHQ-------------------ISGG 163
Cdd:PLN03140 261 DFSARCQGVGTRYdllselarrekdagifpEAEVDLFMKATAMEGVKSSlitdYTLKilgldickdtivgdemirgISGG 340
|
170 180 190
....*....|....*....|....*....|.
gi 505262942 164 MAQRVAIARALIDHPDVLLLDEPMGALDSFT 194
Cdd:PLN03140 341 QKKRVTTGEMIVGPTKTLFMDEISTGLDSST 371
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
59-81 |
1.53e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 39.68 E-value: 1.53e-03
10 20
....*....|....*....|....*
gi 505262942 59 GELVSII--GPSGCGKTTLLRLIAG 81
Cdd:PRK13342 34 GRLSSMIlwGPPGTGKTTLARIIAG 58
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
59-81 |
3.97e-03 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 38.50 E-value: 3.97e-03
10 20
....*....|....*....|....*
gi 505262942 59 GELVSII--GPSGCGKTTLLRLIAG 81
Cdd:COG2256 47 GRLSSMIlwGPPGTGKTTLARLIAN 71
|
|
| SpoIIIAA |
COG3854 |
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome ... |
64-80 |
5.01e-03 |
|
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443063 Cd Length: 309 Bit Score: 37.82 E-value: 5.01e-03
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
5-76 |
5.31e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.61 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262942 5 ELDHLAVASGRQTlaDVPAGVNPELSIEHVSREFTAPD----GSVVH-------------ALSDVSLSIYPGELVSIIGP 67
Cdd:PTZ00243 1267 ELDEEVDALERRT--GMAADVTGTVVIEPASPTSAAPHpvqaGSLVFegvqmryreglplVLRGVSFRIAPREKVGIVGR 1344
|
....*....
gi 505262942 68 SGCGKTTLL 76
Cdd:PTZ00243 1345 TGSGKSTLL 1353
|
|
| MobB |
COG1763 |
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ... |
61-82 |
6.15e-03 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 441369 [Multi-domain] Cd Length: 162 Bit Score: 36.70 E-value: 6.15e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
43-76 |
6.22e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 6.22e-03
10 20 30
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gi 505262942 43 GSVVHALSDVSLSIYPGELVSIIGPSGCGKTTLL 76
Cdd:TIGR00630 618 GARENNLKNITVSIPLGLFTCITGVSGSGKSTLI 651
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