|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
74-302 |
5.25e-111 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 322.42 E-value: 5.25e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRALVFQDPNLFPWRTVLDNVR 153
Cdd:COG1116 23 GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGVVFQEPALLPWLTVLDNVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LGPQARHRSRLDA-DRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELL 232
Cdd:COG1116 103 LGLELRGVPKAERrERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199741941 233 RLWQAERFTALLVTHDVDEALRLADRVVVLSDRPARVLADLTVDLDRPRDHAATD---YLSLRREILHLLGQD 302
Cdd:COG1116 183 RLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDRELRTspeFAALRAEILDLLREE 255
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
73-277 |
2.63e-97 |
|
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: 285.90 E-value: 2.63e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRALVFQDPNLFPWRTVLDNV 152
Cdd:cd03293 15 GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQQDALLPWLTVLDNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RLGPQARHRSRLDA-DRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDEL 231
Cdd:cd03293 95 ALGLELQGVPKAEArERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199741941 232 LRLWQAERFTALLVTHDVDEALRLADRVVVLSDRPARVLADLTVDL 277
Cdd:cd03293 175 LDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
78-299 |
5.16e-69 |
|
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: 214.64 E-value: 5.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRALVFQDPNLFPWRTVLDNVRLGPQ 157
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 158 ARHRSRLDADR---VRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRL 234
Cdd:TIGR01184 81 RVLPDLSKSERraiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 235 WQAERFTALLVTHDVDEALRLADRVVVLSDRPARVLAD-LTVDLDRPRDHAAT----DYLSLRREILHLL 299
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQiLEVPFPRPRDRLEVvedpSYYDLRNEALYFL 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
77-264 |
7.13e-67 |
|
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: 208.14 E-value: 7.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNVR 153
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrniGMVFQDYALFPHLTVAENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LGPQARHRSRLD-ADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELL 232
Cdd:cd03259 95 FGLKLRGVPKAEiRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELK 174
|
170 180 190
....*....|....*....|....*....|..
gi 1199741941 233 RLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03259 175 ELQRELGITTIYVTHDQEEALALADRIAVMNE 206
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
77-299 |
8.01e-67 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 209.60 E-value: 8.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRALVFQDPNLFPWRTVLDNVRLGP 156
Cdd:NF040729 20 VLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGPDRGFVFQNYALFPWMTVKENIEYPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 157 QARHRSRLDA-DRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRLW 235
Cdd:NF040729 100 KQQKMPKQEReKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEPLGAVDFQMRQILQEELESIW 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199741941 236 QAERFTALLVTHDVDEALRLADRVVVLSDRPARVLADLTVDLDRPRDHAATDYLSLRREILHLL 299
Cdd:NF040729 180 LKDKTTVLMVTHDVDEAVYLSDRVIVMSRDKGKILEDLKIDLPRPRNRESEKYLEYKDHLTNIL 243
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
77-264 |
9.06e-66 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 210.34 E-value: 9.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNVR 153
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKrnvGMVFQDYALFPHLTVAENVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LGPQARHRSRLDAD-RVRWALDLVGLTPFADALPATLSGG----------MaqraalaralVNRPRVFLLDEPLGKLDAL 222
Cdd:COG3842 100 FGLRMRGVPKAEIRaRVAELLELVGLEGLADRYPHQLSGGqqqrvalaraL----------APEPRVLLLDEPLSALDAK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199741941 223 TRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:COG3842 170 LREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
77-279 |
2.15e-65 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 206.25 E-value: 2.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRALVFQDPNLFPWRTVLDNVRLGP 156
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVFQKDALLPWLNVLDNVAFGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 157 QARHRSRldADRVRWA---LDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLR 233
Cdd:COG4525 102 RLRGVPK--AERRARAeelLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLD 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199741941 234 LWQAERFTALLVTHDVDEALRLADRVVVLSDRPARVLADLTVDLDR 279
Cdd:COG4525 180 VWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELDFSR 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
77-296 |
5.00e-64 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 202.60 E-value: 5.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRALVFQDPNLFPWRTVLDNVRLGP 156
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDARLLPWKKVIDNVGLGL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 157 QARHRsrldaDRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRLWQ 236
Cdd:PRK11247 107 KGQWR-----DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQ 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 237 AERFTALLVTHDVDEALRLADRVVVLSDrpARVLADLTVDLDRPRDHAATDYLSLRREIL 296
Cdd:PRK11247 182 QHGFTVLLVTHDVSEAVAMADRVLLIEE--GKIGLDLTVDLPRPRRRGSARLAELEAEVL 239
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
76-264 |
9.04e-59 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 191.90 E-value: 9.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR----ALVFQDPNLFPWRTVLDN 151
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRerrvGFVFQHYALFPHMTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQARHRSRLD-ADRVRWALDLVGLTPFADALPATLSGG---------MAqraalaralVNRPRVFLLDEPLGKLDA 221
Cdd:COG1118 96 IAFGLRVRPPSKAEiRARVEELLELVQLEGLADRYPSQLSGGqrqrvalarAL---------AVEPEVLLLDEPFGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1199741941 222 LTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:COG1118 167 KVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
77-264 |
9.71e-59 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 191.82 E-value: 9.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNVR 153
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDrniAMVFQSYALYPHMTVYENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LGPQARHRSRLDAD-RVRWALDLVGLTPFADALPATLSGG----------MaqraalaralVNRPRVFLLDEPLGKLDAL 222
Cdd:COG3839 98 FPLKLRKVPKAEIDrRVREAAELLGLEDLLDRKPKQLSGGqrqrvalgraL----------VREPKVFLLDEPLSNLDAK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199741941 223 TRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:COG3839 168 LRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND 209
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
77-264 |
6.85e-53 |
|
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: 172.44 E-value: 6.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNVR 153
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdiAMVFQNYALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LGPQARHRSRLDAD-RVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELL 232
Cdd:cd03301 95 FGLKLRKVPKDEIDeRVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELK 174
|
170 180 190
....*....|....*....|....*....|..
gi 1199741941 233 RLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03301 175 RLQQRLGTTTIYVTHDQVEAMTMADRIAVMND 206
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
77-264 |
9.48e-52 |
|
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: 170.11 E-value: 9.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA-PHPSRAL--VFQDPNLFPWRTVLDNVR 153
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPHKRPVntVFQNYALFPHLTVFENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LGPQARHRSRLD-ADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELL 232
Cdd:cd03300 95 FGLRLKKLPKAEiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELK 174
|
170 180 190
....*....|....*....|....*....|..
gi 1199741941 233 RLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03300 175 RLQKELGITFVFVTHDQEEALTMSDRIAVMNK 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
73-264 |
1.25e-51 |
|
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: 169.59 E-value: 1.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---------ALVFQDPNLF 143
Cdd:cd03255 15 EKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafrrrhiGFVFQSFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 144 PWRTVLDNVRLGPQ-ARHRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDAL 222
Cdd:cd03255 95 PDLTALENVELPLLlAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199741941 223 TRLTMQDELLRLWQAERFTALLVTHDVDEAlRLADRVVVLSD 264
Cdd:cd03255 175 TGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRD 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
77-279 |
3.53e-51 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 169.50 E-value: 3.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRALVFQDPNLFPWRTVLDNVRLGP 156
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAFGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 157 QARHRSRLD-ADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRLW 235
Cdd:PRK11248 96 QLAGVEKMQrLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLW 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1199741941 236 QAERFTALLVTHDVDEALRLADRVVVLSDRPARVLADLTVDLDR 279
Cdd:PRK11248 176 QETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLNFAR 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
77-276 |
3.20e-50 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 165.97 E-value: 3.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRA-----LVFQDPN--LF-PwrTV 148
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELrrkvgLVFQNPDdqLFaP--TV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGPQARHRSRLDAD-RVRWALDLVGLTPFADALPATLSGG------------MaqraalaralvnRPRVFLLDEP 215
Cdd:COG1122 94 EEDVAFGPENLGLPREEIReRVEEALELVGLEHLADRPPHELSGGqkqrvaiagvlaM------------EPEVLVLDEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199741941 216 LGKLDALTRLTMQDELLRLwQAERFTALLVTHDVDEALRLADRVVVLSDrpARVLADLTVD 276
Cdd:COG1122 162 TAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDD--GRIVADGTPR 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
78-263 |
1.06e-49 |
|
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: 165.20 E-value: 1.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNVRL 154
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnvGFVFQHYALFRHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 155 GPQARHRSRLD-----ADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQD 229
Cdd:cd03296 98 GLRVKPRSERPpeaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRR 177
|
170 180 190
....*....|....*....|....*....|....
gi 1199741941 230 ELLRLWQAERFTALLVTHDVDEALRLADRVVVLS 263
Cdd:cd03296 178 WLRRLHDELHVTTVFVTHDQEEALEVADRVVVMN 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
76-264 |
4.56e-48 |
|
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: 159.94 E-value: 4.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-----ALVFQDPNL-FPWRTVL 149
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrrkvGLVFQNPDDqFFGPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 150 DNVRLGPQARHRSRLDAD-RVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQ 228
Cdd:cd03225 95 EEVAFGLENLGLPEEEIEeRVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 1199741941 229 dELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03225 175 -ELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
77-264 |
5.23e-48 |
|
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: 160.93 E-value: 5.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-----ALVFQDPNLFPWRTVLDN 151
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrrkiGYVIQQIGLFPHMTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQARHRSRLDAD-RVRWALDLVGLTP--FADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQ 228
Cdd:cd03295 96 IALVPKLLKWPKEKIReRADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQ 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1199741941 229 DELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03295 176 EEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
77-276 |
6.93e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 160.23 E-value: 6.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDG-TVVTAPHPSRA---LVFQDPNLFPWRTVLDNV 152
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGeDVARDPAEVRRrigYVPQEPALYPDLTVRENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RLGPQARHRSRLDAD-RVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDEL 231
Cdd:COG1131 95 RFFARLYGLPRKEAReRIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199741941 232 LRLWQAERfTALLVTHDVDEALRLADRVVVLSDrpARVLADLTVD 276
Cdd:COG1131 175 RELAAEGK-TVLLSTHYLEEAERLCDRVAIIDK--GRIVADGTPD 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
73-264 |
8.24e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 159.82 E-value: 8.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA-PHPSRAL--------VFQDPNLF 143
Cdd:COG1136 19 GEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELARlrrrhigfVFQFFNLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 144 PWRTVLDNVRLGPQARHRSRLDA-DRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDAL 222
Cdd:COG1136 99 PELTALENVALPLLLAGVSRKERrERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199741941 223 TRLTMQDELLRLWQAERFTALLVTHDvDEALRLADRVVVLSD 264
Cdd:COG1136 179 TGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRD 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
80-264 |
9.30e-47 |
|
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: 158.58 E-value: 9.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 80 DVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---------ALVFQDPNLFPWRTVLD 150
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrkkiSMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGPQARHRSRLD-ADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQD 229
Cdd:cd03294 122 NVAFGLEVQGVPRAErEERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQD 201
|
170 180 190
....*....|....*....|....*....|....*
gi 1199741941 230 ELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03294 202 ELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKD 236
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
77-264 |
2.44e-46 |
|
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: 154.65 E-value: 2.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-------ALVFQDPNLFPWRTVL 149
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrrriGMVFQDFALFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 150 DNVRLGpqarhrsrldadrvrwaldlvgltpfadalpatLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQD 229
Cdd:cd03229 95 ENIALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRA 141
|
170 180 190
....*....|....*....|....*....|....*
gi 1199741941 230 ELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03229 142 LLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
77-263 |
2.98e-46 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 156.11 E-value: 2.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNVR 153
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDrkiGFVFQHYALFKHLTVRDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LGPQAR-HRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELL 232
Cdd:TIGR00968 95 FGLEIRkHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRKELRSWLR 174
|
170 180 190
....*....|....*....|....*....|.
gi 1199741941 233 RLWQAERFTALLVTHDVDEALRLADRVVVLS 263
Cdd:TIGR00968 175 KLHDEVHVTTVFVTHDQEEAMEVADRIVVMS 205
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
77-276 |
1.82e-45 |
|
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: 154.37 E-value: 1.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPS--RAL------VFQDPNLFPWRTV 148
Cdd:COG1127 20 VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelYELrrrigmLFQGGALFDSLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGPqaRHRSRLD----ADRVRWALDLVGLTPFADALPATLSGGMaqraalaralVNRPRVFLLDEPLGKLDALTR 224
Cdd:COG1127 100 FENVAFPL--REHTDLSeaeiRELVLEKLELVGLPGAADKMPSELSGGMrkrvalaralALDPEILLYDEPTAGLDPITS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1199741941 225 LTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSDRpaRVLADLTVD 276
Cdd:COG1127 178 AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG--KIIAEGTPE 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
77-264 |
2.84e-45 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 157.42 E-value: 2.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT-APHPSRAL--VFQDPNLFPWRTVLDNVR 153
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThVPAENRHVntVFQSYALFPHMTVFENVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LGPQARHRSRLD-ADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELL 232
Cdd:PRK09452 109 FGLRMQKTPAAEiTPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELK 188
|
170 180 190
....*....|....*....|....*....|..
gi 1199741941 233 RLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK09452 189 ALQRKLGITFVFVTHDQEEALTMSDRIVVMRD 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
77-276 |
1.42e-44 |
|
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: 151.89 E-value: 1.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR--------ALVFQDPNLFPWRTV 148
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrrrmGMLFQSGALFDSLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGpqARHRSRLDA----DRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTR 224
Cdd:cd03261 95 FENVAFP--LREHTRLSEeeirEIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIAS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1199741941 225 LTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSDRpaRVLADLTVD 276
Cdd:cd03261 173 GVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDG--KIVAEGTPE 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
74-264 |
6.42e-44 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 149.64 E-value: 6.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGL-----AQPSEGDVSVDGTVVTAPHPSR-------ALVFQDPN 141
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVlelrrrvGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 142 LFPwRTVLDNVRLGPQAR--HRSRLDADRVRWALDLVGLTP-FADALPAT-LSGGMAQRAALARALVNRPRVFLLDEPLG 217
Cdd:cd03260 92 PFP-GSIYDNVAYGLRLHgiKLKEELDERVEEALRKAALWDeVKDRLHALgLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199741941 218 KLDALTRLTMQDELLRLwqAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03260 171 ALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLN 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
74-264 |
8.22e-44 |
|
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: 149.22 E-value: 8.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPS----R---ALVFQDPNLFPWR 146
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRqkvGMVFQQFNLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 147 TVLDNVRLGP-QARHRSRLDAD-RVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDAltr 224
Cdd:cd03262 92 TVLENITLAPiKVKGMSKAEAEeRALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDP--- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1199741941 225 lTMQDELLRLWQA---ERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03262 169 -ELVGEVLDVMKDlaeEGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
78-288 |
9.71e-44 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 153.72 E-value: 9.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---------ALVFQDPNLFPWRTV 148
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrkkmSMVFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGPQARHRSRLD-ADRVRWALDLVGLTPFADALPATLSGGMaqraalaralvnRPRV------------FLLDEP 215
Cdd:COG4175 123 LENVAFGLEIQGVPKAErRERAREALELVGLAGWEDSYPDELSGGM------------QQRVglaralatdpdiLLMDEA 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199741941 216 LGKLDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSDrpARVladltVDLDRPRD---HAATDY 288
Cdd:COG4175 191 FSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKD--GRI-----VQIGTPEEiltNPANDY 259
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
74-264 |
2.25e-43 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 148.60 E-value: 2.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRA-------LVFQDPNLFPWR 146
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINklrrkvgMVFQQFNLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 147 TVLDNVRLGP-QARHRSRLDA-DRVRWALDLVGLTPFADALPATLSGG------------MaqraalaralvnRPRVFLL 212
Cdd:COG1126 93 TVLENVTLAPiKVKKMSKAEAeERAMELLERVGLADKADAYPAQLSGGqqqrvaiaralaM------------EPKVMLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199741941 213 DEPLGKLDAltrlTMQDELLRLWQ---AERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:COG1126 161 DEPTSALDP----ELVGEVLDVMRdlaKEGMTMVVVTHEMGFAREVADRVVFMDG 211
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
76-262 |
2.67e-43 |
|
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: 151.73 E-value: 2.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNV 152
Cdd:TIGR03265 18 TALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKrdyGIVFQSYALFPNLTVADNI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RLGPQARHRSRLDAD-RVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDEL 231
Cdd:TIGR03265 98 AYGLKNRGMGRAEVAeRVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEI 177
|
170 180 190
....*....|....*....|....*....|.
gi 1199741941 232 LRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:TIGR03265 178 RQLQRRLGVTTIMVTHDQEEALSMADRIVVM 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
77-263 |
8.98e-43 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 150.62 E-value: 8.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNVR 153
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDrkvGFVFQHYALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LG----PQarhRSRLDAD----RVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRL 225
Cdd:PRK10851 97 FGltvlPR---RERPNAAaikaKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1199741941 226 TMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLS 263
Cdd:PRK10851 174 ELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMS 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
77-262 |
2.35e-42 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 149.48 E-value: 2.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTapHPS---R--ALVFQDPNLFPWRTVLDN 151
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSiqqRdiCMVFQSYALFPHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQARHRSRLD-ADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDE 230
Cdd:PRK11432 99 VGYGLKMLGVPKEErKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREK 178
|
170 180 190
....*....|....*....|....*....|..
gi 1199741941 231 LLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK11432 179 IRELQQQFNITSLYVTHDQSEAFAVSDTVIVM 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
73-282 |
7.19e-42 |
|
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: 151.59 E-value: 7.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR--------ALVFQDPN--L 142
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelrrrvQMVFQDPYssL 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 143 FPWRTVLDNVRLGPQARHRSRLDA--DRVRWALDLVGLTP-FADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:COG1123 356 NPRMTVGDIIAEPLRLHGLLSRAErrERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199741941 220 DALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSDrpARVLADLTVD--LDRPRD 282
Cdd:COG1123 436 DVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD--GRIVEDGPTEevFANPQH 498
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
75-275 |
4.09e-41 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 142.96 E-value: 4.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 75 LAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR------ALVFQDPNLFPWRTV 148
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEiarlgiGRTFQIPRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGPQARHRSRLDA-----------DRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLG 217
Cdd:cd03219 93 LENVMVAAQARTGSGLLLararreerearERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199741941 218 KL-DALTRLTMqdELLRLWQAERFTALLVTHDVDEALRLADRVVVL-------SDRPARVLADLTV 275
Cdd:cd03219 173 GLnPEETEELA--ELIRELRERGITVLLVEHDMDVVMSLADRVTVLdqgrviaEGTPDEVRNNPRV 236
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
93-264 |
6.73e-41 |
|
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: 144.94 E-value: 6.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 93 LVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNVRLGPQARHRSRLDAD-R 168
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLrhiNMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKpR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 169 VRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRLWQAERFTALLVTHD 248
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170
....*....|....*.
gi 1199741941 249 VDEALRLADRVVVLSD 264
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRK 176
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
77-262 |
7.01e-41 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 145.37 E-value: 7.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNVR 153
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADrdiAMVFQNYALYPHMSVRENMA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LGPQARHRSRLDAD-RVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELL 232
Cdd:PRK11650 99 YGLKIRGMPKAEIEeRVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQ 178
|
170 180 190
....*....|....*....|....*....|
gi 1199741941 233 RLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK11650 179 RLHRRLKTTSLYVTHDQVEAMTLADRVVVM 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
82-289 |
7.13e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 142.20 E-value: 7.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 82 TLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNVRLGPQA 158
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAErpvSMLFQENNLFPHLTVAQNIGLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 159 RHR-SRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALV-NRPrVFLLDEPLGKLDALTRLTMQDELLRLWQ 236
Cdd:COG3840 99 GLKlTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPFSALDPALRQEMLDLVDELCR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199741941 237 AERFTALLVTHDVDEALRLADRVVVLSDRpaRVLADLTVD--LDRPRDHAATDYL 289
Cdd:COG3840 178 ERGLTVLMVTHDPEDAARIADRVLLVADG--RIAADGPTAalLDGEPPPALAAYL 230
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
74-264 |
2.02e-40 |
|
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: 142.21 E-value: 2.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAP-----HPSR---ALVFQDP--NLF 143
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKkkkklKDLRkkvGLVFQFPehQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 144 PwRTVLDNVRLGPQARHRSRLDAD-RVRWALDLVGLTP-FADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDA 221
Cdd:TIGR04521 97 E-ETVYKDIAFGPKNLGLSEEEAEeRVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1199741941 222 LTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:TIGR04521 176 KGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHK 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
77-288 |
6.62e-40 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 139.94 E-value: 6.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-----ALVFQDP--NLFPWRTVL 149
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrrvQMVFQDPyaSLHPRHTVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 150 DNVRLgPQARHRSRLDADRVRWALDLVGLTP-FADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQ 228
Cdd:COG1124 100 RILAE-PLRIHGLPDREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEIL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 229 DELLRLWQAERFTALLVTHDVDEALRLADRVVVLSDrpARVLADLTVdlDRPRDHAATDY 288
Cdd:COG1124 179 NLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN--GRIVEELTV--ADLLAGPKHPY 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
78-264 |
7.23e-40 |
|
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: 138.97 E-value: 7.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIP---PGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVV--------TAPHPSR-ALVFQDPNLFPW 145
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkinLPPQQRKiGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 146 RTVLDNVRLGPQaRHRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRL 225
Cdd:cd03297 90 LNVRENLAFGLK-RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1199741941 226 TMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMED 207
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
77-302 |
1.36e-39 |
|
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: 139.22 E-value: 1.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT--APHPSRALVF--QDPNLFPWRTVLDNV 152
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkePREARRQIGVlpDERGLYDRLTVRENI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 R-LGPQARHRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDEL 231
Cdd:COG4555 96 RyFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199741941 232 LRLWQAERfTALLVTHDVDEALRLADRVVVLSDrpARVLADLTVDLDRPRDHAAtdylSLRREILHLLGQD 302
Cdd:COG4555 176 RALKKEGK-TVLFSSHIMQEVEALCDRVVILHK--GKVVAQGSLDELREEIGEE----NLEDAFVALIGSE 239
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
75-272 |
2.06e-39 |
|
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: 139.02 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 75 LAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR------ALVFQDPNLFPWRTV 148
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRiarlgiARTFQNPRLFPELTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGPQARHRSRLDA----------------DRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLL 212
Cdd:COG0411 97 LENVLVAAHARLGRGLLAallrlprarreerearERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199741941 213 DEPLGKLDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVL-------SDRPARVLAD 272
Cdd:COG0411 177 DEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLdfgrviaEGTPAEVRAD 243
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
77-294 |
4.14e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 143.89 E-value: 4.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPS---EGDVSVDGTVVTAPHPSR-----ALVFQDP--NLFPWr 146
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALrgrriGMVFQDPmtQLNPV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 147 TVLDNVRLGPQARHRSRLDA-DRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRL 225
Cdd:COG1123 100 TVGDQIAEALENLGLSRAEArARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199741941 226 TMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSDrpARVLADLTVD--LDRPRDHAATDYLSLRRE 294
Cdd:COG1123 180 EILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDD--GRIVEDGPPEeiLAAPQALAAVPRLGAARG 248
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
77-264 |
1.05e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.71 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-----ALVFQDPNLFPwRTVLDN 151
Cdd:COG4619 15 ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrrqvAYVPQEPALWG-GTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQARHRsRLDADRVRWALDLVGLTP-FADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDE 230
Cdd:COG4619 94 LPFPFQLRER-KFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEEL 172
|
170 180 190
....*....|....*....|....*....|....
gi 1199741941 231 LLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:COG4619 173 LREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
76-264 |
2.05e-38 |
|
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: 143.82 E-value: 2.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-----ALVFQDPNLFPwRTVLD 150
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrrqiGVVLQDVFLFS-GTIRE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGpqarhRSRLDADRVRWALDLVGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:COG2274 568 NITLG-----DPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199741941 220 DALTRLTMQDELLRLwqAERFTALLVTHDvDEALRLADRVVVLSD 264
Cdd:COG2274 643 DAETEAIILENLRRL--LKGRTVIIIAHR-LSTIRLADRIIVLDK 684
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
77-264 |
2.42e-38 |
|
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: 135.94 E-value: 2.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPS-----RALVFQDPNL-FPWrTVLD 150
Cdd:COG1120 16 VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRelarrIAYVPQEPPApFGL-TVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGpQARHRSRL------DADRVRWALDLVGLTPFADALPATLSGG--------MaqraalarALVNRPRVFLLDEPL 216
Cdd:COG1120 95 LVALG-RYPHLGLFgrpsaeDREAVEEALERTGLEHLADRPVDELSGGerqrvliaR--------ALAQEPPLLLLDEPT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1199741941 217 GKLDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:COG1120 166 SHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKD 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
77-264 |
1.55e-37 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 131.37 E-value: 1.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR----ALVFQDPNLFPWRTVLDNV 152
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVkrriGYLPEEPSLYENLTVRENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RlgpqarhrsrldadrvrwaldlvgltpfadalpatLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELL 232
Cdd:cd03230 95 K-----------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLR 139
|
170 180 190
....*....|....*....|....*....|..
gi 1199741941 233 RLwQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03230 140 EL-KKEGKTILLSSHILEEAERLCDRVAILNN 170
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
74-264 |
1.81e-37 |
|
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: 133.09 E-value: 1.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR--------ALVFQDPNLFPW 145
Cdd:cd03258 17 KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkarrriGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 146 RTVLDNVRLGPQARHRSRLDAD-RVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTR 224
Cdd:cd03258 97 RTVFENVALPLEIAGVPKAEIEeRVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETT 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1199741941 225 LTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03258 177 QSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
77-265 |
2.04e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 133.29 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRALVFQDPNlFPWR---TVLDNVR 153
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAE-VDWDfpiTVRDVVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LG-----PQARHRSRLDADRVRWALDLVGLTPFADALPATLSGG----------MaqraalaralVNRPRVFLLDEPLGK 218
Cdd:COG1121 100 MGrygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGqqqrvllaraL----------AQDPDLLLLDEPFAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199741941 219 LDALTRLTMQDeLLRLWQAERFTALLVTHDVDEALRLADRVVVLSDR 265
Cdd:COG1121 170 VDAATEEALYE-LLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
77-262 |
2.32e-37 |
|
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: 132.63 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR--------ALVFQDP--NLFPWR 146
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirrkeiQMVFQDPmsSLNPRM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 147 TVLDNVRLGPQARHRSRLDADRVRWALDL---VGLTP-FADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDAL 222
Cdd:cd03257 100 TIGEQIAEPLRIHGKLSKKEARKEAVLLLlvgVGLPEeVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1199741941 223 TRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:cd03257 180 VQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
77-264 |
2.34e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.48 E-value: 2.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGT-VVTAPHPSRAL-------VFQDPNLFPWRTV 148
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdLSRLKRREIPYlrrrigvVFQDFRLLPDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGPQARHRSRLDA-DRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLtm 227
Cdd:COG2884 97 YENVALPLRVTGKSRKEIrRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSW-- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199741941 228 qdELLRLWqaERF-----TALLVTHDVDEALRLADRVVVLSD 264
Cdd:COG2884 175 --EIMELL--EEInrrgtTVLIATHDLELVDRMPKRVLELED 212
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
80-262 |
2.40e-37 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 136.70 E-value: 2.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 80 DVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNVRLGP 156
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAErgvGMVFQSYALYPHLSVAENMSFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 157 QARHRSRLDAD-RVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRLW 235
Cdd:PRK11000 101 KLAGAKKEEINqRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLH 180
|
170 180
....*....|....*....|....*..
gi 1199741941 236 QAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK11000 181 KRLGRTMIYVTHDQVEAMTLADKIVVL 207
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
78-264 |
3.08e-37 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 135.59 E-value: 3.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNVRL 154
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKrgiAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 155 GPQARHRSRLDADR-VRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLR 233
Cdd:NF040840 96 GLKLRKVPKEEIERkVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180 190
....*....|....*....|....*....|.
gi 1199741941 234 LWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIMLN 206
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
80-286 |
1.06e-36 |
|
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: 134.46 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 80 DVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVV--------TAPHPSR-ALVFQDPNLFPWRTVLD 150
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargifLPPHRRRiGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGpqaRHRSRLDADRVRWA--LDLVGLTPFADALPATLSGG-----------MAqraalaralvnRPRVFLLDEPLG 217
Cdd:COG4148 97 NLLYG---RKRAPRAERRISFDevVELLGIGHLLDRRPATLSGGerqrvaigralLS-----------SPRLLLMDEPLA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199741941 218 KLDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD-------RPARVLADLTVDLDRPRDHAAT 286
Cdd:COG4148 163 ALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQgrvvasgPLAEVLSRPDLLPLAGGEEAGS 238
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
76-264 |
1.23e-36 |
|
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: 131.15 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR--------ALVFQDPNLFPWRT 147
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrrqiGMIFQQFNLIERLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 148 VLDNVRLGPQARHR---------SRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGK 218
Cdd:cd03256 95 VLENVLSGRLGRRStwrslfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVAS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199741941 219 LD-ALTRLTMQDeLLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03256 175 LDpASSRQVMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKD 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
78-215 |
3.16e-36 |
|
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: 127.38 E-value: 3.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT-----APHPSRALVFQDPNLFPWRTVLDNV 152
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdderkSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199741941 153 RLGPQARHRSRLDAD-RVRWALDLVGLTPFAD----ALPATLSGGMAQRAALARALVNRPRVFLLDEP 215
Cdd:pfam00005 81 RLGLLLKGLSKREKDaRAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
76-263 |
3.50e-36 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 133.81 E-value: 3.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRA---LVFQDPNLFPWRTVLDNV 152
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRpinMMFQSYALFPHMTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RLGPQARHRSRLD-ADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDEL 231
Cdd:PRK11607 113 AFGLKQDKLPKAEiASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
|
170 180 190
....*....|....*....|....*....|..
gi 1199741941 232 LRLWQAERFTALLVTHDVDEALRLADRVVVLS 263
Cdd:PRK11607 193 VDILERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
77-264 |
8.01e-36 |
|
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: 128.39 E-value: 8.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT----APHPSRALVFQDPNLFPWRTVLDNV 152
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRtdrkAARQSLGYCPQFDALFDELTVREHL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RLGPQARHRSRLDADRVR-WALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDEL 231
Cdd:cd03263 97 RFYARLKGLPKSEIKEEVeLLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLI 176
|
170 180 190
....*....|....*....|....*....|...
gi 1199741941 232 LRLwQAERfTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03263 177 LEV-RKGR-SIILTTHSMDEAEALCDRIAIMSD 207
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
80-272 |
2.24e-35 |
|
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: 127.22 E-value: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 80 DVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNVRLGP 156
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADrpvSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 157 QAR-HRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRLW 235
Cdd:cd03298 96 SPGlKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 1199741941 236 QAERFTALLVTHDVDEALRLADRVVVLSDrpARVLAD 272
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDN--GRIAAQ 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
77-262 |
5.05e-35 |
|
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: 127.07 E-value: 5.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNVR 153
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKrdiSYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LGPQARHRSRLDADR-VRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELL 232
Cdd:cd03299 94 YGLKKRKVDKKEIERkVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190
....*....|....*....|....*....|
gi 1199741941 233 RLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVAIM 203
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
77-262 |
2.89e-34 |
|
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: 124.18 E-value: 2.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRALVFQDPNL---FPWrTVLDNVR 153
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRSIdrdFPI-SVRDVVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LGPQARHR-----SRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQ 228
Cdd:cd03235 93 MGLYGHKGlfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIY 172
|
170 180 190
....*....|....*....|....*....|....
gi 1199741941 229 dELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:cd03235 173 -ELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
78-264 |
4.12e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.90 E-value: 4.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAP-----HPSRALVFQDP-NLFPWRTVLDN 151
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtvwdvRRQVGMVFQNPdNQFVGATVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQARHRSRLD-ADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDE 230
Cdd:PRK13635 103 VAFGLENIGVPREEmVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLET 182
|
170 180 190
....*....|....*....|....*....|....
gi 1199741941 231 LLRLWQAERFTALLVTHDVDEALRlADRVVVLSD 264
Cdd:PRK13635 183 VRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNK 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
74-264 |
5.16e-34 |
|
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: 124.08 E-value: 5.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA-PHPSRAL--------VFQDPNLFP 144
Cdd:COG4181 24 ELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAlDEDARARlrarhvgfVFQSFQLLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 145 WRTVLDNVRLgPQARHRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTR 224
Cdd:COG4181 104 TLTALENVML-PLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1199741941 225 LTMQDELLRLWQAERFTALLVTHDVDEALRlADRVVVLSD 264
Cdd:COG4181 183 EQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRA 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
80-271 |
1.15e-33 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 126.38 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 80 DVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVV--------TAPHPSR-ALVFQDPNLFPWRTVLD 150
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkgifLPPEKRRiGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGpqaRHRSRLDADRVRWA--LDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQ 228
Cdd:TIGR02142 95 NLRYG---MKRARPSERRISFErvIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1199741941 229 DELLRLWQAERFTALLVTHDVDEALRLADRVVVLSDrpARVLA 271
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLED--GRVAA 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
77-260 |
2.66e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 122.51 E-value: 2.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-------ALVFQDPNLFPWRTVL 149
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqeaGMVFQQFYLFPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 150 DNVRLGP-QARHRSRLDADRV-RWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRltm 227
Cdd:PRK09493 96 ENVMFGPlRVRGASKEEAEKQaRELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELR--- 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 1199741941 228 qDELLRLWQA---ERFTALLVTHDVDEALRLADRVV 260
Cdd:PRK09493 173 -HEVLKVMQDlaeEGMTMVIVTHEIGFAEKVASRLI 207
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
77-264 |
1.42e-32 |
|
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: 118.64 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT--APHPSR---ALVFQDPNLFPwRTVLDN 151
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRdlDLESLRkniAYVPQDPFLFS-GTIREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQarhRSRLdadrvrwALdlvgltpfADALpatlsggmaqraalaralVNRPRVFLLDEPLGKLDALTRLTMQDEL 231
Cdd:cd03228 96 ILSGGQ---RQRI-------AI--------ARAL------------------LRDPPILILDEATSALDPETEALILEAL 139
|
170 180 190
....*....|....*....|....*....|...
gi 1199741941 232 LRLwqAERFTALLVTHDVdEALRLADRVVVLSD 264
Cdd:cd03228 140 RAL--AKGKTVIVIAHRL-STIRDADRIIVLDD 169
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
76-264 |
2.33e-32 |
|
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: 125.64 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-----ALVFQDPNLFPWrTVLD 150
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrrqiAWVPQNPYLFAG-TIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLG-PQArhrsrlDADRVRWALDLVGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVFLLDEPLGK 218
Cdd:COG4988 430 NLRLGrPDA------SDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAH 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199741941 219 LDALTRLTMQDELLRLWQaERfTALLVTHDvDEALRLADRVVVLSD 264
Cdd:COG4988 504 LDAETEAEILQALRRLAK-GR-TVILITHR-LALLAQADRILVLDD 546
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
77-264 |
2.44e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 122.49 E-value: 2.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTApHPSRAL---------VFQDPNLFPWRT 147
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTA-LSERELraarrkigmIFQHFNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 148 VLDNVRL-------GPQARHRsrldadRVRWALDLVGLTPFADALPATLSGG----------MaqraalaralVNRPRVF 210
Cdd:COG1135 99 VAENVALpleiagvPKAEIRK------RVAELLELVGLSDKADAYPSQLSGGqkqrvgiaraL----------ANNPKVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199741941 211 LLDEPLGKLDALTrlTmqDELLRLWQ--AERF--TALLVTHDVDEALRLADRVVVLSD 264
Cdd:COG1135 163 LCDEATSALDPET--T--RSILDLLKdiNRELglTIVLITHEMDVVRRICDRVAVLEN 216
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
78-265 |
4.21e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 118.35 E-value: 4.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQP---SEGDVSVDGTVVTA--PHPSR-ALVFQDPNLFPWRTVLDN 151
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAlpAEQRRiGILFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQARHRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDEL 231
Cdd:COG4136 97 LAFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFV 176
|
170 180 190
....*....|....*....|....*....|....
gi 1199741941 232 LRLWQAERFTALLVTHDVDEALrLADRVVVLSDR 265
Cdd:COG4136 177 FEQIRQRGIPALLVTHDEEDAP-AAGRVLDLGNW 209
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
78-263 |
2.92e-31 |
|
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: 116.70 E-value: 2.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDG-TVVTAPHPSRA---LVFQDPNLFPWRTVLDNVR 153
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhDVVREPREVRRrigIVFQDLSVDDELTGWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LgpQAR---HRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDE 230
Cdd:cd03265 96 I--HARlygVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY 173
|
170 180 190
....*....|....*....|....*....|...
gi 1199741941 231 LLRLWQAERFTALLVTHDVDEALRLADRVVVLS 263
Cdd:cd03265 174 IEKLKEEFGMTILLTTHYMEEAEQLCDRVAIID 206
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
76-264 |
4.27e-31 |
|
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: 115.97 E-value: 4.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR--------ALVFQDPNLFPWRT 147
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrrkiGVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 148 VLDNVRLGPQ-ARHRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLT 226
Cdd:cd03292 95 VYENVAFALEvTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1199741941 227 MQDeLLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03292 175 IMN-LLKKINKAGTTVVVATHAKELVDTTRHRVIALER 211
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
83-272 |
1.34e-30 |
|
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: 114.57 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 83 LDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNVRLGPQAR 159
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQrpvSMLFQENNLFAHLTVRQNIGLGLHPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 160 HR-SRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRLWQAE 238
Cdd:TIGR01277 99 LKlNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSER 178
|
170 180 190
....*....|....*....|....*....|....
gi 1199741941 239 RFTALLVTHDVDEALRLADRVVVLSDRPARVLAD 272
Cdd:TIGR01277 179 QRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
77-264 |
2.33e-30 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 112.91 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPS-----RALVFQdpnlfpwrtvldn 151
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKelarkIAYVPQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 vrlgpqarhrsrldadrvrwALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDaltrLTMQDEL 231
Cdd:cd03214 81 --------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD----IAHQIEL 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 1199741941 232 L----RLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03214 137 LellrRLARERGKTVVMVLHDLNLAARYADRVILLKD 173
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
77-265 |
2.81e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 113.73 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT----APHPSRALVFQDPNLFPWRTVLDNV 152
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRdareDYRRRLAYLGHADGLKPELTVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RLGpQARHRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQdELL 232
Cdd:COG4133 97 RFW-AALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLA-ELI 174
|
170 180 190
....*....|....*....|....*....|...
gi 1199741941 233 RLWQAERFTALLVTHDVDEAlrLADRVVVLSDR 265
Cdd:COG4133 175 AAHLARGGAVLLTTHQPLEL--AAARVLDLGDF 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
77-264 |
2.97e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 119.88 E-value: 2.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA-PHPS-R---ALVFQDPNLFPwRTVLDN 151
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESlRrqiGVVPQDTFLFS-GTIREN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGpqarhrsRLDADR--VRWALDLVGLTPFADALP-----------ATLSGG----------MaqraalaralVNRPR 208
Cdd:COG1132 434 IRYG-------RPDATDeeVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGqrqriaiaraL----------LKDPP 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199741941 209 VFLLDEPLGKLDALTRLTMQDELLRLwqAERFTALLVTHdvdealRL-----ADRVVVLSD 264
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERL--MKGRTTIVIAH------RLstirnADRILVLDD 549
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
77-264 |
1.73e-29 |
|
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: 111.58 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRA--LVFQDPN--LFPwRTVLDNV 152
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSigYVMQDVDyqLFT-DSVREEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RLGPQARHRSRLDADRVrwaLDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLD--ALTRLTmqdE 230
Cdd:cd03226 94 LLGLKELDAGNEQAETV---LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDykNMERVG---E 167
|
170 180 190
....*....|....*....|....*....|....
gi 1199741941 231 LLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03226 168 LIRELAAQGKAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
77-272 |
2.72e-29 |
|
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: 111.37 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR------ALVFQDPNLFPWRTVLD 150
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHEraragiGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGPQARHRSRLDAdRVRWALDLV-GLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQD 229
Cdd:cd03224 95 NLLLGAYARRRAKRKA-RLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1199741941 230 ELLRLwQAERFTALLVTHDVDEALRLADRV-------VVLSDRPARVLAD 272
Cdd:cd03224 174 AIREL-RDEGVTILLVEQNARFALEIADRAyvlergrVVLEGTAAELLAD 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
82-264 |
3.15e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 111.60 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 82 TLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---ALVFQDPNLFPWRTVLDNVRLG--P 156
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRrpvSMLFQENNLFSHLTVAQNIGLGlnP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 157 QARhrsrLDAD---RVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLR 233
Cdd:PRK10771 99 GLK----LNAAqreKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190
....*....|....*....|....*....|.
gi 1199741941 234 LWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVAD 205
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
77-264 |
4.83e-29 |
|
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: 110.38 E-value: 4.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR----ALVfQDPNLFPWRTVLDNV 152
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALrrigALI-EAPGFYPNLTARENL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RLGPQARHRSRLDADRVrwaLDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQdELL 232
Cdd:cd03268 94 RLLARLLGIRKKRIDEV---LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELR-ELI 169
|
170 180 190
....*....|....*....|....*....|..
gi 1199741941 233 RLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03268 170 LSLRDQGITVLISSHLLSEIQKVADRIGIINK 201
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
77-264 |
4.98e-29 |
|
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: 108.87 E-value: 4.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGtvvtaphpsralvfQDPNLFPWRTVLDNVRLGP 156
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG--------------KDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 157 QarhrsrldadrvrwaldlvgltpfadalpatLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRLwQ 236
Cdd:cd00267 80 Q-------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL-A 127
|
170 180
....*....|....*....|....*...
gi 1199741941 237 AERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd00267 128 EEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
77-262 |
1.30e-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: 109.29 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-ALVFQDPNLFPWRTVLDNVRLG 155
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRiGYLPEERGLYPKMKVIDQLVYL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 156 PQARHRSRLDA-DRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRL 234
Cdd:cd03269 95 AQLKGLKKEEArRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIREL 174
|
170 180
....*....|....*....|....*...
gi 1199741941 235 WQAERfTALLVTHDVDEALRLADRVVVL 262
Cdd:cd03269 175 ARAGK-TVILSTHQMELVEELCDRVLLL 201
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
77-264 |
1.41e-28 |
|
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: 109.62 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGT-VVTAPHPS-R---ALVFQDPNLFPwRTVLDN 151
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdIRDISRKSlRsmiGVVLQDTFLFS-GTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGpqarhRSRLDADRVRWALDLVGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVFLLDEPLGKLD 220
Cdd:cd03254 97 IRLG-----RPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1199741941 221 ALTRLTMQDELLRLWQAErfTALLVTHdvdealRL-----ADRVVVLSD 264
Cdd:cd03254 172 TETEKLIQEALEKLMKGR--TSIIIAH------RLstiknADKILVLDD 212
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
78-271 |
2.27e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.21 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-----ALVFQDPN--LFPwRTVLD 150
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrskvGLVFQDPDdqVFS-STVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGPQarhRSRLDAD----RVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLT 226
Cdd:PRK13647 100 DVAFGPV---NMGLDKDeverRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199741941 227 MQDELLRLWQAERfTALLVTHDVDEALRLADRVVVLSDrpARVLA 271
Cdd:PRK13647 177 LMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKE--GRVLA 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
74-264 |
2.37e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 111.82 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTApHPSRAL---------VFQDPNLFP 144
Cdd:PRK11153 17 TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTA-LSEKELrkarrqigmIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 145 WRTVLDNVRLGPQARHRSRLDAD-RVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLD-AL 222
Cdd:PRK11153 96 SRTVFDNVALPLELAGTPKAEIKaRVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDpAT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1199741941 223 TRLTMqdELLRLWQAE-RFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK11153 176 TRSIL--ELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDA 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
77-270 |
2.47e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 109.82 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPS-----RALVFQDPNL-FPWrTVLD 150
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarrRAVLPQHSSLaFPF-TVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLG--PQARHRSRlDADRVRWALDLVGLTPFADALPATLSGG--------------MAQRAAlaralvnRPRVFLLDE 214
Cdd:COG4559 95 VVALGraPHGSSAAQ-DRQIVREALALVGLAHLAGRSYQTLSGGeqqrvqlarvlaqlWEPVDG-------GPRWLFLDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199741941 215 PLGKLD-ALTRLTMQdeLLRLWQAERFTALLVTHDVDEALRLADRVVVLSD-------RPARVL 270
Cdd:COG4559 167 PTSALDlAHQHAVLR--LARQLARRGGGVVAVLHDLNLAAQYADRILLLHQgrlvaqgTPEEVL 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
77-262 |
3.28e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 109.36 E-value: 3.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLA--QPS---EGDVSVDGTVVTAPHPS----RA---LVFQDPNLFP 144
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGarvEGEILLDGEDIYDPDVDvvelRRrvgMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 145 WrTVLDNVRLGP---QARHRSRLDaDRVRWALDLVGLTP-FADAL--PAT-LSGG------------Maqraalaralvn 205
Cdd:COG1117 106 K-SIYDNVAYGLrlhGIKSKSELD-EIVEESLRKAALWDeVKDRLkkSALgLSGGqqqrlciaralaV------------ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199741941 206 RPRVFLLDEPLGKLDALTRLTMQDELLRLwqAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:COG1117 172 EPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQAARVSDYTAFF 226
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
74-264 |
8.70e-28 |
|
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: 107.44 E-value: 8.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---------ALVFQDPNLFP 144
Cdd:TIGR02211 17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNEraklrnkklGFIYQFHHLLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 145 WRTVLDNVRLGPQARHRSRLDADRVRWA-LDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALT 223
Cdd:TIGR02211 97 DFTALENVAMPLLIGKKSVKEAKERAYEmLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNN 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1199741941 224 RLTMQDELLRLWQAERFTALLVTHDVDEALRLaDRVVVLSD 264
Cdd:TIGR02211 177 AKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKD 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
78-262 |
9.13e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 108.95 E-value: 9.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRAL---------VFQDP--NLFPwR 146
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLkplrkkvgiVFQFPehQLFE-E 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 147 TVLDNVRLGPQARHRSRLDAD-RVRWALDLVGLTP-FADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTR 224
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDAKqKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1199741941 225 LTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK13634 182 KEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVM 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
76-262 |
1.47e-27 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 111.99 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-----ALVFQDPNLFPwRTVLD 150
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrdqiAWVPQHPFLFA-GTIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGpqarhRSRLDADRVRWALDLVGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:TIGR02857 415 NIRLA-----RPDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1199741941 220 DALTRLTMQDELLRLwqAERFTALLVTHDvDEALRLADRVVVL 262
Cdd:TIGR02857 490 DAETEAEVLEALRAL--AQGRTVLLVTHR-LALAALADRIVVL 529
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
76-276 |
1.80e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 107.48 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTApHPSRAL------VFQDPNLFPWRTVL 149
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT-TPSRELakrlaiLRQENHINSRLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 150 DNVRLGPQARHRSRL---DADRVRWALDLVGLTPFADALPATLSGGmaqraalaralvNRPRVF------------LLDE 214
Cdd:COG4604 94 ELVAFGRFPYSKGRLtaeDREIIDEAIAYLDLEDLADRYLDELSGG------------QRQRAFiamvlaqdtdyvLLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199741941 215 PLGKLD---------ALTRLTmqDELLRlwqaerfTALLVTHDVDEALRLADRVVVLSDrpARVLADLTVD 276
Cdd:COG4604 162 PLNNLDmkhsvqmmkLLRRLA--DELGK-------TVVIVLHDINFASCYADHIVAMKD--GRVVAQGTPE 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
73-272 |
1.81e-27 |
|
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: 106.52 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPS--RA---LVFQDPNLFpWRT 147
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRnigYVPQDVTLF-YGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 148 VLDNVRLGPQArhrsrLDADRVRWALDLVGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVFLLDEPL 216
Cdd:cd03245 94 LRDNITLGAPL-----ADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199741941 217 GKLDALTRLTMQDElLRLWQAERfTALLVTHDVdEALRLADRVVVLSDrpARVLAD 272
Cdd:cd03245 169 SAMDMNSEERLKER-LRQLLGDK-TLIIITHRP-SLLDLVDRIIVMDS--GRIVAD 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
75-285 |
2.10e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 107.47 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 75 LAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRA--------LVFQDP--NLFP 144
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRkafrrdiqMVFQDSisAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 145 WRTVLDNVRlgPQARHRSRLD----ADRVRWALDLVGLTP-FADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:PRK10419 105 RKTVREIIR--EPLRHLLSLDkaerLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199741941 220 DALTRLTMQDELLRLwQAERFTA-LLVTHDVDEALRLADRVVVLSDrpARVLADLTVDLDRPRDHAA 285
Cdd:PRK10419 183 DLVLQAGVIRLLKKL-QQQFGTAcLFITHDLRLVERFCQRVMVMDN--GQIVETQPVGDKLTFSSPA 246
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
80-264 |
2.16e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 110.12 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 80 DVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---------ALVFQDPNLFPWRTVLD 150
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrkkiAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLG-------PQARHRSRLDAdrvrwaLDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALT 223
Cdd:PRK10070 126 NTAFGmelaginAEERREKALDA------LRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1199741941 224 RLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
73-264 |
2.40e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.96 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGD---VSVDGTVVTAP-----HPSRALVFQDP-NLF 143
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKtvwdiREKVGIVFQNPdNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 144 PWRTVLDNVRLGPQARHRSRLDADR-VRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDAL 222
Cdd:PRK13640 98 VGATVGDDVAFGLENRAVPRPEMIKiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199741941 223 TRLTMQDELLRLWQAERFTALLVTHDVDEAlRLADRVVVLSD 264
Cdd:PRK13640 178 GKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDD 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
77-260 |
5.22e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 105.99 E-value: 5.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEG-----DVSVDGTVVTAPHPS--RAL------VFQDPNLF 143
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLSQQKGliRQLrqhvgfVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 144 PWRTVLDNVRLGP-QARHRSRLDA-DRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDA 221
Cdd:PRK11264 98 PHRTVLENIIEGPvIVKGEPKEEAtARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199741941 222 ltrlTMQDELL---RLWQAERFTALLVTHDVDEALRLADRVV 260
Cdd:PRK11264 178 ----ELVGEVLntiRQLAQEKRTMVIVTHEMSFARDVADRAI 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
77-264 |
6.37e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.72 E-value: 6.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRAL------VFQDPNLFPWRTVLD 150
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQaagiaiIHQELNLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGPQARHRSRLD----ADRVRWALDLVGLTPFADALPATLSGG---MaqraalaralV-------NRPRVFLLDEPl 216
Cdd:COG1129 99 NIFLGREPRRGGLIDwramRRRARELLARLGLDIDPDTPVGDLSVAqqqL----------VeiaralsRDARVLILDEP- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199741941 217 gkLDALTRltmqDE------LLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:COG1129 168 --TASLTE----REverlfrIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRD 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
76-264 |
7.94e-27 |
|
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: 110.24 E-value: 7.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-----ALVFQDPNLFPwRTVLD 150
Cdd:COG4987 349 PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrrriAVVPQRPHLFD-TTLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGpqarhRSRLDADRVRWALDLVGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:COG4987 428 NLRLA-----RPDATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGL 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199741941 220 DALTRLTMQDELLRlWQAERfTALLVTHDvDEALRLADRVVVLSD 264
Cdd:COG4987 503 DAATEQALLADLLE-ALAGR-TVLLITHR-LAGLERMDRILVLED 544
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
77-262 |
1.43e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 104.71 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGT---VVTAPHPSRAL--------VFQDPNLFPW 145
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdFSQKPSEKAIRllrqkvgmVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 146 RTVLDN-----VRLGPQARHRSRLDADRVrwaLDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLD 220
Cdd:COG4161 97 LTVMENlieapCKVLGLSKEQAREKAMKL---LARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1199741941 221 AltRLTMQ-DELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:COG4161 174 P--EITAQvVEIIRELSQTGITQVIVTHEVEFARKVASQVVYM 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
75-262 |
1.78e-26 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 105.27 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 75 LAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRA--------LVFQD-PNLF-P 144
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRrafrrdvqLVFQDsPSAVnP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 145 WRTVldNVRLGPQARHRSRLDA----DRVRWALDLVGLTP-FADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:TIGR02769 104 RMTV--RQIIGEPLRHLTSLDEseqkARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1199741941 220 DALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVM 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
74-273 |
2.02e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.21 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR---------ALVFQDP--NL 142
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqirkkvGLVFQFPesQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 143 FPwRTVLDNVRLGPQARHRSRLDADRV-RWALDLVGLTP-FADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLD 220
Cdd:PRK13649 99 FE-ETVLKDVAFGPQNFGVSQEEAEALaREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199741941 221 ALTRltmqDELLRLWQA---ERFTALLVTHDVDEALRLADRV-------VVLSDRPARVLADL 273
Cdd:PRK13649 178 PKGR----KELMTLFKKlhqSGMTIVLVTHLMDDVANYADFVyvlekgkLVLSGKPKDIFQDV 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
77-272 |
2.59e-26 |
|
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: 103.91 E-value: 2.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR------ALVFQDPNLFPWRTVLD 150
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRiarlgiGYVPEGRRIFPSLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGPQARHrsrlDADRVRWALDLVG-----LTPFADALPATLSGG----------MaqraalaralVNRPRVFLLDEP 215
Cdd:COG0410 98 NLLLGAYARR----DRAEVRADLERVYelfprLKERRRQRAGTLSGGeqqmlaigraL----------MSRPKLLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199741941 216 -LGkLDALTRLTMQDELLRLwQAERFTALLVTHDVDEALRLADRV-------VVLSDRPARVLAD 272
Cdd:COG0410 164 sLG-LAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAyvlergrIVLEGTAAELLAD 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
77-272 |
2.81e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.47 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHP-----SRALVFQDPNL-FPWrTVLD 150
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPaelarRRAVLPQHSSLsFPF-TVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGPQARHRSRLDADR-VRWALDLVGLTPFADALPATLSGG------MAQRAALARALVNRPRVFLLDEPLGKLDalt 223
Cdd:PRK13548 96 VVAMGRAPHGLSRAEDDAlVAAALAQVDLAHLAGRDYPQLSGGeqqrvqLARVLAQLWEPDGPPRWLLLDEPTSALD--- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199741941 224 rLTMQDELLRLwqAERFTA------LLVTHDVDEALRLADRVVVLSD-------RPARVLAD 272
Cdd:PRK13548 173 -LAHQHHVLRL--ARQLAHerglavIVVLHDLNLAARYADRIVLLHQgrlvadgTPAEVLTP 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
78-264 |
2.96e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.81 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPH-----PSRALVFQDP-NLFPWRTVLDN 151
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwdirHKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQARHRSRLD-ADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDE 230
Cdd:PRK13650 103 VAFGLENKGIPHEEmKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182
|
170 180 190
....*....|....*....|....*....|....
gi 1199741941 231 LLRLWQAERFTALLVTHDVDEaLRLADRVVVLSD 264
Cdd:PRK13650 183 IKGIRDDYQMTVISITHDLDE-VALSDRVLVMKN 215
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
77-262 |
3.71e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 103.56 E-value: 3.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSV-----DGTVVTAPHPSRAL------VFQDPNLFPW 145
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfDFSKTPSDKAIRELrrnvgmVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 146 RTVLDNVRLGP---------QARHRSRLDADRVRwaldlvgLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPL 216
Cdd:PRK11124 97 LTVQQNLIEAPcrvlglskdQALARAEKLLERLR-------LKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199741941 217 GKLDAltRLTMQ-DELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK11124 170 AALDP--EITAQiVSIIRELAETGITQVIVTHEVEVARKTASRVVYM 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
76-272 |
5.72e-26 |
|
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: 102.45 E-value: 5.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDG-TVVTAPHPSRA---LVFQDPNLFPWRTVLDN 151
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRrlgFVSDSTGLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VR-------LGPQARHrsrldaDRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTR 224
Cdd:cd03266 99 LEyfaglygLKGDELT------ARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1199741941 225 LTMQdELLRLWQAERFTALLVTHDVDEALRLADRVVVLSDrpARVLAD 272
Cdd:cd03266 173 RALR-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHR--GRVVYE 217
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
78-302 |
1.37e-25 |
|
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: 103.62 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDG-TVVTAPHPSR---ALVFQDPNLFPWRTVLDNVR 153
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGyDVVREPRKVRrsiGIVPQYASVDEDLTGRENLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LG------PQARHRSRldADRVrwaLDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTM 227
Cdd:TIGR01188 89 MMgrlyglPKDEAEER--AEEL---LELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 228 QDELLRLwQAERFTALLVTHDVDEALRLADRVVVLS-------DRPARVLADLTVDLDRPRDHAATDYLSLRREILHLLG 300
Cdd:TIGR01188 164 WDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDhgriiaeGTPEELKRRLGKDTLESRPRDIQSLKVEVSMLIAELG 242
|
..
gi 1199741941 301 QD 302
Cdd:TIGR01188 243 ET 244
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
77-264 |
2.16e-25 |
|
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: 100.73 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGqLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA-PHPSRALVF---QDPNLFPWRTVLDNV 152
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKqPQKLRRRIGylpQEFGVYPNFTVREFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RLgpQAR----HRSRLDAdRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQ 228
Cdd:cd03264 94 DY--IAWlkgiPSKEVKA-RVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFR 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1199741941 229 DELLRLwqAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03264 171 NLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNK 204
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
77-262 |
2.67e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 101.84 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPS-----EGDVSVDGTVVTAP--HPSR-----ALVFQDPNLFP 144
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPdvDPIEvrrevGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 145 WRTVLDNVRLGPQ----ARHRSRLDaDRVRWALDLVGL-TPFADAL---PATLSGGMAQRAALARALVNRPRVFLLDEPL 216
Cdd:PRK14267 99 HLTIYDNVAIGVKlnglVKSKKELD-ERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199741941 217 GKLDALTRLTMQDELLRLwqAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK14267 178 ANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFL 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
78-272 |
6.14e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.44 E-value: 6.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRA---------LVFQDP--NLFPwR 146
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlkklrkkvsLVFQFPeaQLFE-N 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 147 TVLDNVRLGPQARHRSRLDADR--VRWaLDLVGL-TPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALT 223
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSEDEAKEkaLKW-LKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199741941 224 RLTMQdELLRLWQAERFTALLVTHDVDEALRLADRVVVLS-------DRPARVLAD 272
Cdd:PRK13641 181 RKEMM-QLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEhgklikhASPKEIFSD 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
77-264 |
1.12e-24 |
|
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: 99.14 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTaphPSRALVFQDPNLfpwrTVLDNVRLGp 156
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS---LLGLGGGFNPEL----TGRENIYLN- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 157 qAR---HRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLR 233
Cdd:cd03220 109 -GRllgLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRE 187
|
170 180 190
....*....|....*....|....*....|.
gi 1199741941 234 LWQAERfTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03220 188 LLKQGK-TVILVSHDPSSIKRLCDRALVLEK 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
77-268 |
2.32e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.25 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-----ALVFQDPNLFPwRTVLDN 151
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrqqvSYCAQTPTLFG-DTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQARH----RSRLDADRVRWALDLVGLTPFADAlpatLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTM 227
Cdd:PRK10247 101 LIFPWQIRNqqpdPAIFLDDLERFALPDTILTKNIAE----LSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1199741941 228 QDELLRLWQAERFTALLVTHDVDEaLRLADRVVVLSDRPAR 268
Cdd:PRK10247 177 NEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQPHAGE 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
78-262 |
2.47e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 99.74 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRA-------LVFQDP--NLFPwRTV 148
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdirkkvgLVFQYPeyQLFE-ETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGPQARHRSRLD-ADRVRWALDLVGLT--PFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRL 225
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEiENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 1199741941 226 TMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVM 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
77-262 |
2.67e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.30 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRALVfqdPNLFPwRTVLDNVRLGP 156
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEV---PDSLP-LTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 157 QA-----RHRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMqDEL 231
Cdd:NF040873 83 WArrglwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI-IAL 161
|
170 180 190
....*....|....*....|....*....|.
gi 1199741941 232 LRLWQAERFTALLVTHDVDEAlRLADRVVVL 262
Cdd:NF040873 162 LAEEHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
74-272 |
4.22e-24 |
|
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: 97.79 E-value: 4.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVvtaPHPSR-------ALVFQDPNLFPWR 146
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV---PWKRRkkflrriGVVFGQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 147 -TVLDNVRLgpqARHRSRLDADRVRWAL----DLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDA 221
Cdd:cd03267 110 lPVIDSFYL---LAAIYDLPPARFKKRLdelsELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1199741941 222 LTRLTMQdELLRLWQAER-FTALLVTHDVDEALRLADRVVVLSDrpARVLAD 272
Cdd:cd03267 187 VAQENIR-NFLKEYNRERgTTVLLTSHYMKDIEALARRVLVIDK--GRLLYD 235
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
77-264 |
4.52e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.16 E-value: 4.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHP---SRALVF--QDPNLFPWRTVLDN 151
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrqlARRLALlpQHHLTPEGITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLG--PQARHRSRL---DADRVRWALDLVGLTPFADALPATLSGGmaqraalaralvNRPRVF------------LLDE 214
Cdd:PRK11231 97 VAYGrsPWLSLWGRLsaeDNARVNQAMEQTRINHLADRRLTDLSGG------------QRQRAFlamvlaqdtpvvLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199741941 215 PLGKLDaltrLTMQDELLRLW---QAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK11231 165 PTTYLD----INHQVELMRLMrelNTQGKTVVTVLHDLNQASRYCDHLVVLAN 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
78-274 |
5.64e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 101.80 E-value: 5.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSV----DGTVVTAPHP---SRA-----LVFQDPNLFPW 145
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPdgrGRAkryigILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 146 RTVLDNVRLGPQARHRSRLDADRVRWALDLVGLT-----PFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLD 220
Cdd:TIGR03269 380 RTVLDNLTEAIGLELPDELARMKAVITLKMVGFDeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199741941 221 ALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD-------RPARVLADLT 274
Cdd:TIGR03269 460 PITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDgkivkigDPEEIVEELT 520
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
77-262 |
5.83e-24 |
|
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: 99.36 E-value: 5.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQP---SEGDVSVDGTVVTAPHPSR---------ALVFQDP---- 140
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKElrkirgreiQMIFQDPmtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 141 NlfPWRTVLDNVRLgPQARHR--SRLDA-DRVRWALDLVGLTP---FADALPATLSGGMaqraalaralvnR-------- 206
Cdd:COG0444 100 N--PVMTVGDQIAE-PLRIHGglSKAEArERAIELLERVGLPDperRLDRYPHELSGGM------------Rqrvmiara 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199741941 207 ----PRVFLLDEPLGKLDAltrlTMQD---ELLRLWQAERFTA-LLVTHDVDEALRLADRVVVL 262
Cdd:COG0444 165 lalePKLLIADEPTTALDV----TIQAqilNLLKDLQRELGLAiLFITHDLGVVAEIADRVAVM 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
75-292 |
7.23e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.93 E-value: 7.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 75 LAVlDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQ--PS---EGDVSVDGTVVTAPH--PSR-----ALVFQDPNL 142
Cdd:PRK14243 24 LAV-KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDvdPVEvrrriGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 143 FPwRTVLDNVRLGPQAR----------HRSRLDA---DRVRWALDLVGLtpfadalpaTLSGGMAQRAALARALVNRPRV 209
Cdd:PRK14243 103 FP-KSIYDNIAYGARINgykgdmdelvERSLRQAalwDEVKDKLKQSGL---------SLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 210 FLLDEPLGKLDALTRLTMQDELLRLwqAERFTALLVTHDVDEALRLADRV----VVLSDRPAR----VLADLT-VDLDRP 280
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSDMTaffnVELTEGGGRygylVEFDRTeKIFNSP 250
|
250
....*....|..
gi 1199741941 281 RDHAATDYLSLR 292
Cdd:PRK14243 251 QQQATRDYVSGR 262
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
78-262 |
1.20e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.88 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAP------HPSR---ALVFQDP--NLFPwR 146
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkeiKPVRkkvGVVFQFPesQLFE-E 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 147 TVLDNVRLGPQARHRSRLDADRVRW-ALDLVGLTP-FADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTR 224
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAeKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 1199741941 225 LTMQDELLRLWQAERfTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK13643 181 IEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLL 217
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
78-261 |
2.29e-23 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 97.88 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPS--RAL------VFQDP--NLFPWRT 147
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRelRPLrrrmqmVFQDPyaSLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 148 V-------LDNVRLGPQARHRsrldaDRVRWALDLVGLTP-FADALPATLSGG-----------MAqraalaralvnRPR 208
Cdd:COG4608 114 VgdiiaepLRIHGLASKAERR-----ERVAELLELVGLRPeHADRYPHEFSGGqrqrigiaralAL-----------NPK 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199741941 209 VFLLDEPLGKLDA---------LTRLtmQDELlrlwqaeRFTALLVTHDvdeaLR----LADRVVV 261
Cdd:COG4608 178 LIVCDEPVSALDVsiqaqvlnlLEDL--QDEL-------GLTYLFISHD----LSvvrhISDRVAV 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
77-274 |
2.65e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 96.76 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR--------ALVFQDPNLFPWRTV 148
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlytvrkrmSMLFQSGALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLgPQARHrSRLDADRVR----WALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTR 224
Cdd:PRK11831 102 FDNVAY-PLREH-TQLPAPLLHstvmMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1199741941 225 LTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSDRpaRVLADLT 274
Cdd:PRK11831 180 GVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADK--KIVAHGS 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
80-262 |
4.10e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 97.64 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 80 DVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT--------APHPSR-ALVFQDPNLFPWRTVLD 150
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdaekgiclPPEKRRiGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGpqARHRSRLDADRVrwaLDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDaltrLTMQDE 230
Cdd:PRK11144 96 NLRYG--MAKSMVAQFDKI---VALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD----LPRKRE 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1199741941 231 LL----RLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK11144 167 LLpyleRLAREINIPILYVSHSLDEILRLADRVVVL 202
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
77-262 |
4.67e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 95.36 E-value: 4.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQ--PS---EGDVSVDGTVVTAPHPSR-----ALVFQDPNLFPWR 146
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIElrrrvQMVFQIPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 147 TVLDNVRLGPQ----ARHRSRLDAdRVRWALDLVGL----TPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGK 218
Cdd:PRK14247 98 SIFENVALGLKlnrlVKSKKELQE-RVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTAN 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1199741941 219 LDALTrlTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK14247 177 LDPEN--TAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFL 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
77-264 |
4.74e-23 |
|
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: 93.43 E-value: 4.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-----ALVFQDPNLFPwRTVLDN 151
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgdhvGYLPQDDELFS-GSIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQaRHRsrldadrvrwaldlVGLtpfADALpatlsggmaqraalaralVNRPRVFLLDEPLGKLDALTRLTMQDEL 231
Cdd:cd03246 96 ILSGGQ-RQR--------------LGL---ARAL------------------YGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|...
gi 1199741941 232 LRLwQAERFTALLVTHDVdEALRLADRVVVLSD 264
Cdd:cd03246 140 AAL-KAAGATRIVIAHRP-ETLASADRILVLED 170
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
73-264 |
5.06e-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: 94.99 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVV---TAPHPSR--ALVFQDPNLFPwRT 147
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdyTLASLRRqiGLVSQDVFLFN-DT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 148 VLDNVRLGpqarhRSRLDADRVRWALDLVGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVFLLDEPL 216
Cdd:cd03251 92 VAENIAYG-----RPGATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199741941 217 GKLDALTRLTMQDELLRLwqAERFTALLVTHdvdealRL-----ADRVVVLSD 264
Cdd:cd03251 167 SALDTESERLVQAALERL--MKNRTTFVIAH------RLstienADRIVVLED 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
78-272 |
6.01e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.46 E-value: 6.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLA---QPSEGDVSVDGTVVTAP-------HPSRA---LVFQDPNLFP 144
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREgrlardiRKSRAntgYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 145 WRTVLDNVRLGPQA---------RHRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEP 215
Cdd:PRK09984 100 RLSVLENVLIGALGstpfwrtcfSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199741941 216 LGKLDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLsdRPARVLAD 272
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL--RQGHVFYD 234
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
77-264 |
1.82e-22 |
|
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: 92.53 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVvtaphpsrALVFQdpnlFPW---RTVLDNVR 153
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--------AYVSQ----EPWiqnGTIRENIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LGpqarhrSRLDADRVRWALDLVGLTPFADALPA-----------TLSGGMAQRAALARALVNRPRVFLLDEPLGKLDAL 222
Cdd:cd03250 88 FG------KPFDEERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1199741941 223 T-RLTMQDELLRLWQAERfTALLVTHDVdEALRLADRVVVLSD 264
Cdd:cd03250 162 VgRHIFENCILGLLLNNK-TRILVTHQL-QLLPHADQIVVLDN 202
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
78-262 |
1.89e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.02 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRAL------VFQDPNLFPWRTVLDN 151
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIalgigmVHQHFMLVPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQARHRSRLDADRVR-----------WALDLvgltpfaDALPATLSGGMaqraalaralvnR------------PR 208
Cdd:COG3845 101 IVLGLEPTKGGRLDRKAARarirelserygLDVDP-------DAKVEDLSVGE------------QqrveilkalyrgAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199741941 209 VFLLDEPlgkldaLTRLTMQ--DEL---LRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:COG3845 162 ILILDEP------TAVLTPQeaDELfeiLRRLAAEGKSIIFITHKLREVMAIADRVTVL 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
76-248 |
2.94e-22 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 96.66 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-----ALVFQDPNLFPwRTVLD 150
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrrrvSVCAQDAHLFD-TTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGpqarhRSRLDADRVRWALDLVGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:TIGR02868 428 NLRLA-----RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180 190
....*....|....*....|....*....|.
gi 1199741941 220 DALTRltmqDELLR-LWQA-ERFTALLVTHD 248
Cdd:TIGR02868 503 DAETA----DELLEdLLAAlSGRTVVLITHH 529
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
78-264 |
3.61e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 92.63 E-value: 3.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT------APHPSR--ALVFQDPNLFPWRTVL 149
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknreVPFLRRqiGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 150 DNVRLGPQARHRSRLDADR-VRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDAltrlTMQ 228
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIRRrVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD----ALS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1199741941 229 DELLRLWqaERF-----TALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK10908 174 EGILRLF--EEFnrvgvTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
74-257 |
4.20e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 92.53 E-value: 4.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA-PHPSRA--------LVFQDPNLFP 144
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmDEEARAklrakhvgFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 145 WRTVLDNVRLGPQAR-HRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALT 223
Cdd:PRK10584 102 TLNALENVELPALLRgESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1199741941 224 RLTMQDELLRLWQAERFTALLVTHDV------DEALRLAD 257
Cdd:PRK10584 182 GDKIADLLFSLNREHGTTLILVTHDLqlaarcDRRLRLVN 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
77-264 |
1.01e-21 |
|
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: 91.45 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-----ALVFQDPNLFPwRTVLDN 151
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrsqiGLVSQEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGpqarhRSRLDADRVRWALDLVGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVFLLDEPLGKLD 220
Cdd:cd03249 97 IRYG-----KPDATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1199741941 221 ALTRLTMQDELLRLwqAERFTALLVTHdvdealRL-----ADRVVVLSD 264
Cdd:cd03249 172 AESEKLVQEALDRA--MKGRTTIVIAH------RLstirnADLIAVLQN 212
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
77-275 |
1.51e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.03 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT-------APHPSRAL--VFQDPNLFPWRT 147
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssaakAELRNQKLgfIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 148 VLDNVRLGPQARHRSRLDA-DRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLT 226
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEInSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1199741941 227 MQDELLRLWQAERFTALLVTHDVDEALRLADRvvvLSDRPARVLADLTV 275
Cdd:PRK11629 184 IFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ---LEMRDGRLTAELSL 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
74-272 |
1.64e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 91.59 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRA-----LVFQDP-NLFPWRT 147
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIrkkigIIFQNPdNQFIGAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 148 VLDNVRLGPQARHRSRLDADR-VRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLT 226
Cdd:PRK13632 101 VEDDIAFGLENKKVPPKKMKDiIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKRE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199741941 227 MQDELLRLWQAERFTALLVTHDVDEALrLADRVVVLSD-------RPARVLAD 272
Cdd:PRK13632 181 IKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEgkliaqgKPKEILNN 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
76-262 |
4.21e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.82 E-value: 4.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGtvvtAPHPSRA--------LVFQDPNLFPWRT 147
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG----VPVPARArlararigVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 148 VLDN-VRLGPQARHRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLT 226
Cdd:PRK13536 131 VRENlLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210
|
170 180 190
....*....|....*....|....*....|....*.
gi 1199741941 227 MQdELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK13536 211 IW-ERLRSLLARGKTILLTTHFMEEAERLCDRLCVL 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
78-264 |
7.33e-21 |
|
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: 92.44 E-value: 7.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLaQPSEGDVSVDGTVVTApHPSRAL---------VFQDPN--LFPWR 146
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDG-LSRRALrplrrrmqvVFQDPFgsLSPRM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 147 TVLDNVRLGPQArHRSRLDA----DRVRWALDLVGLTP-FADALPATLSGG----------MaqraalaralVNRPRVFL 211
Cdd:COG4172 380 TVGQIIAEGLRV-HGPGLSAaerrARVAEALEEVGLDPaARHRYPHEFSGGqrqriaiaraL----------ILEPKLLV 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199741941 212 LDEPLGKLDALTRLTMQDeLLRLWQAER-FTALLVTHDVDEALRLADRVVVLSD 264
Cdd:COG4172 449 LDEPTSALDVSVQAQILD-LLRDLQREHgLAYLFISHDLAVVRALAHRVMVMKD 501
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
77-264 |
8.90e-21 |
|
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: 87.10 E-value: 8.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRAL------VFQdpnlfpwrtvld 150
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARragiamVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 nvrlgpqarhrsrldadrvrwaldlvgltpfadalpatLSGGMAQRAALARALVNRPRVFLLDEPLGkldALTRLTMQD- 229
Cdd:cd03216 83 --------------------------------------LSVGERQMVEIARALARNARLLILDEPTA---ALTPAEVERl 121
|
170 180 190
....*....|....*....|....*....|....*.
gi 1199741941 230 -ELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03216 122 fKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRD 157
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
77-276 |
9.35e-21 |
|
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: 88.75 E-value: 9.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA-PHPSRA---LVF--QDPNLFPWRTVLD 150
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlPMHKRArlgIGYlpQEASIFRKLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLG------PQARHRSRLDAdrvrwALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTR 224
Cdd:cd03218 95 NILAVleirglSKKEREEKLEE-----LLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199741941 225 LTMQDELLRLwqAERFTALLVT-HDVDEALRLADRVVVLSDrpARVLADLTVD 276
Cdd:cd03218 170 QDIQKIIKIL--KDRGIGVLITdHNVRETLSITDRAYIIYE--GKVLAEGTPE 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
77-264 |
1.95e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 88.98 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-------ALVFQDPN--LF-Pwr 146
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLlevrktvGIVFQNPDdqLFaP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 147 TVLDNVRLGPQARHRSRLD-ADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRL 225
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEvEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1199741941 226 TMQdELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK13639 175 QIM-KLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSD 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
77-264 |
2.35e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.83 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVtaphpsrALV-----FqDPNLfpwrTVLDN 151
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS-------ALLelgagF-HPEL----TGREN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQARHRSRLDAD-RVRWALDLVGLTPFADaLPA-TLSGGMAQraalaralvnR----------PRVFLLDEPLGKL 219
Cdd:COG1134 109 IYLNGRLLGLSRKEIDeKFDEIVEFAELGDFID-QPVkTYSSGMRA----------RlafavatavdPDILLVDEVLAVG 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199741941 220 DALTRLTMQDELLRLWQAERfTALLVTHDVDEALRLADRVVVLSD 264
Cdd:COG1134 178 DAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWLEK 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
78-264 |
2.92e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 88.27 E-value: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-----ALVFQDP-NLFPWRTVLDN 151
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrkhiGIVFQNPdNQFVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQARHRSRLDADR-VRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDE 230
Cdd:PRK13648 105 VAFGLENHAVPYDEMHRrVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDL 184
|
170 180 190
....*....|....*....|....*....|....
gi 1199741941 231 LLRLWQAERFTALLVTHDVDEALRlADRVVVLSD 264
Cdd:PRK13648 185 VRKVKSEHNITIISITHDLSEAME-ADHVIVMNK 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
73-264 |
4.36e-20 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 86.90 E-value: 4.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDG---TVVTAPHPSRAL--VFQDPNLFPwRT 147
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSLRRAIgvVPQDTVLFN-DT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 148 VLDNVRLGpqarhrsRLDA--DRVRWALDLVGLTPFADALP---AT--------LSGGMAQRAALARALVNRPRVFLLDE 214
Cdd:cd03253 91 IGYNIRYG-------RPDAtdEEVIEAAKAAQIHDKIMRFPdgyDTivgerglkLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1199741941 215 PLGKLDALTRLTMQDELLRLwqAERFTALLVTHDVDEALRlADRVVVLSD 264
Cdd:cd03253 164 ATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKD 210
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
78-262 |
4.36e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.84 E-value: 4.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPH-----PSRALVFQDP-NLFPWRTVLDN 151
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQARHRSRLDA-DRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDE 230
Cdd:PRK13642 103 VAFGMENQGIPREEMiKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190
....*....|....*....|....*....|..
gi 1199741941 231 LLRLWQAERFTALLVTHDVDEALRlADRVVVL 262
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVM 213
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
78-258 |
7.11e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 86.75 E-value: 7.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLL--AGLAQPsegDVSVDGTVVTAPH----PSR---------ALVFQDPNL 142
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNP---EVTITGSIVYNGHniysPRTdtvdlrkeiGMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 143 FPWrTVLDNVRLGPQ---ARHRSRLDAdRVRWAL------DLVGLTPFADALpaTLSGGMAQRAALARALVNRPRVFLLD 213
Cdd:PRK14239 98 FPM-SIYENVVYGLRlkgIKDKQVLDE-AVEKSLkgasiwDEVKDRLHDSAL--GLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199741941 214 EPLGKLDALTRLTMQDELLRLwqAERFTALLVTHDVDEALRLADR 258
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDR 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
77-274 |
1.44e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 86.29 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA-PHPSRAL----VFQDPNL--FPWRTVL 149
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlPEYKRAKyigrVFQDPMMgtAPSMTIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 150 DNVRLGpQARHRSRldadRVRWA---------------LDL---------VGLtpfadalpatLSGG--------Maqra 197
Cdd:COG1101 101 ENLALA-YRRGKRR----GLRRGltkkrrelfrellatLGLglenrldtkVGL----------LSGGqrqalsllM---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 198 alarALVNRPRVFLLDEPLGKLD-----ALTRLTMqdellRLWQAERFTALLVTHDVDEALRLADRVVVLSDrpARVLAD 272
Cdd:COG1101 162 ----ATLTKPKLLLLDEHTAALDpktaaLVLELTE-----KIVEENNLTTLMVTHNMEQALDYGNRLIMMHE--GRIILD 230
|
..
gi 1199741941 273 LT 274
Cdd:COG1101 231 VS 232
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
77-262 |
1.70e-19 |
|
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: 85.22 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA-----PHPSRALVFQDPNLFPwRTVLDN 151
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkyLHSKVSLVGQEPVLFA-RSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQArhrsrLDADRVRWALDLVGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVFLLDEPLGKLD 220
Cdd:cd03248 108 IAYGLQS-----CSFECVKEAAQKAHAHSFISELAsgydtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199741941 221 ALTRLTMQdELLRLWQaERFTALLVTHDVDEALRlADRVVVL 262
Cdd:cd03248 183 AESEQQVQ-QALYDWP-ERRTVLVIAHRLSTVER-ADQILVL 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
77-276 |
2.20e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 86.32 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRalvF----QDPNLFPWRTVLDN- 151
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR---IgylpEERGLYPKMKVGEQl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGpQARHRSRLDADRV--RWaLDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQD 229
Cdd:COG4152 93 VYLA-RLKGLSKAEAKRRadEW-LERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1199741941 230 ELLRLwqAERFTA-LLVTHDVDEALRLADRVVVLSDrpARVLADLTVD 276
Cdd:COG4152 171 VIREL--AAKGTTvIFSSHQMELVEELCDRIVIINK--GRKVLSGSVD 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
77-262 |
2.97e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.01 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTvvtaPHPSRA--------LVFQDPNLFPWRTV 148
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGE----PVPSRArharqrvgVVPQFDNLDPDFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRL-GPQARHRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTM 227
Cdd:PRK13537 98 RENLLVfGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLM 177
|
170 180 190
....*....|....*....|....*....|....*
gi 1199741941 228 QdELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK13537 178 W-ERLRSLLARGKTILLTTHFMEEAERLCDRLCVI 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
73-264 |
4.24e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.14 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHP-----SRA-LVFQDP-NLFPW 145
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwdirNKAgMVFQNPdNQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 146 RTVLDNVRLGPQ------ARHRSRLDadrvrWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:PRK13633 101 TIVEEDVAFGPEnlgippEEIRERVD-----ESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199741941 220 DALTRLTMQDELLRLWQAERFTALLVTHDVDEALRlADRVVVLSD 264
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDS 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
74-270 |
4.67e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.82 E-value: 4.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVV---TAPHPSR--ALVFQDPNLFPWRTV 148
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealSARAASRrvASVPQDTSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGpQARHRSRLD----ADR--VRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDaL 222
Cdd:PRK09536 95 RQVVEMG-RTPHRSRFDtwteTDRaaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD-I 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199741941 223 TRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD-------RPARVL 270
Cdd:PRK09536 173 NHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADgrvraagPPADVL 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
78-264 |
6.12e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 87.21 E-value: 6.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAqPSEGDVSVDGTVVTAPHPSR-----ALVFQDPNLFPwRTVLDNV 152
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESwrkhlSWVGQNPQLPH-GTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RLGpqarhRSRLDADRVRWALDLVGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDA 221
Cdd:PRK11174 444 LLG-----NPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1199741941 222 LT-RLTMQdELLRLWQAErfTALLVTHDVDEaLRLADRVVVLSD 264
Cdd:PRK11174 519 HSeQLVMQ-ALNAASRRQ--TTLMVTHQLED-LAQWDQIWVMQD 558
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
77-262 |
6.21e-19 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 84.07 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDG--TVVTAPHPSRA---LVFQDPNLFPwRTVLDN 151
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdLALADPAWLRRqvgVVLQENVLFN-RSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQArhrsrLDADRVRWALDLVGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVFLLDEPLGKLD 220
Cdd:cd03252 96 IALADPG-----MSMERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199741941 221 ALTRLTMQDELLRLWQAErfTALLVTHDVdEALRLADRVVVL 262
Cdd:cd03252 171 YESEHAIMRNMHDICAGR--TVIIIAHRL-STVKNADRIIVM 209
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
73-264 |
6.51e-19 |
|
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: 87.08 E-value: 6.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGtvvtapHPSR-----------ALVFQDPN 141
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG------HDLAdytlaslrrqvALVSQDVV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 142 LFPwRTVLDNVRLGpqarHRSRLDADRVRWALDLVGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVF 210
Cdd:TIGR02203 417 LFN-DTIANNIAYG----RTEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPIL 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199741941 211 LLDEPLGKLDALTRLTMQDELLRLWQaERfTALLVTHDVdEALRLADRVVVLSD 264
Cdd:TIGR02203 492 ILDEATSALDNESERLVQAALERLMQ-GR-TTLVIAHRL-STIEKADRIVVMDD 542
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
74-262 |
8.07e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 84.25 E-value: 8.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRA------------------L 135
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkvadknqlrllrtrltM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 136 VFQDPNLFPWRTVLDNVRLGP-QARHRSRLDA-DRVRWALDLVGLTPFA-DALPATLSGGMAQRAALARALVNRPRVFLL 212
Cdd:PRK10619 97 VFQHFNLWSHMTVLENVMEAPiQVLGLSKQEArERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199741941 213 DEPLGKLDAltrlTMQDELLRLWQA---ERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK10619 177 DEPTSALDP----ELVGEVLRIMQQlaeEGKTMVVVTHEMGFARHVSSHVIFL 225
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
74-221 |
9.43e-19 |
|
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: 82.41 E-value: 9.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVV--TAPHPSRALVF--QDPNLFPWRTVL 149
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeQRDEPHENILYlgHLPGLKPELSAL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199741941 150 DNVRLgpqaRHRSRLDADRVRW-ALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDA 221
Cdd:TIGR01189 92 ENLHF----WAAIHGGAQRTIEdALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
73-262 |
1.40e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 84.37 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVvtaPHPSR-------ALVF-QDPNLFP 144
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV---PFKRRkefarriGVVFgQRSQLWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 145 WRTVLDNVRLG------PQARHRSRLD--ADRvrwaLDLVGL--TP-------------FADALpatlsggmaqraalar 201
Cdd:COG4586 110 DLPAIDSFRLLkaiyriPDAEYKKRLDelVEL----LDLGELldTPvrqlslgqrmrceLAAAL---------------- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199741941 202 alVNRPRVFLLDEP-LGkLDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:COG4586 170 --LHRPKILFLDEPtIG-LDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVI 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
77-279 |
2.94e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.73 E-value: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTaphpsrALVFQDPNLFPWRTVLDNVR--L 154
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRI------GYLPQEPPLDDDLTVLDTVLdgD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 155 GPQARHRSRL----------DADRVR-------------WALD------LVGL---TPFADALPATLSGGMAQRAALARA 202
Cdd:COG0488 87 AELRALEAELeeleaklaepDEDLERlaelqeefealggWEAEaraeeiLSGLgfpEEDLDRPVSELSGGWRRRVALARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199741941 203 LVNRPRVFLLDEPLGKLDALTRLTMQDELLRlwqaERFTALLVTHDVDealrLADRVVvlsdrparvlaDLTVDLDR 279
Cdd:COG0488 167 LLSEPDLLLLDEPTNHLDLESIEWLEEFLKN----YPGTVLVVSHDRY----FLDRVA-----------TRILELDR 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
77-271 |
4.11e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.14 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHpSRAL---VFQDPNLFPW---RTVLD 150
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS-SKAFarkVAYLPQQLPAaegMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGPQARHRS-----RLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRL 225
Cdd:PRK10575 105 LVAIGRYPWHGAlgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199741941 226 TMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLsdRPARVLA 271
Cdd:PRK10575 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVAL--RGGEMIA 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
76-262 |
6.21e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.63 E-value: 6.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVV-----------TAPHPSRALVFQDPNLFP 144
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifqidaIKLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 145 WRTVLDNVR--LGPQARHRSRLDADRVRWALDLVGL-TPFADAL--PAT-LSGGMAQRAALARALVNRPRVFLLDEPLGK 218
Cdd:PRK14246 104 HLSIYDNIAypLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLnsPASqLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1199741941 219 LDALTRLTMQDELLRLwqAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK14246 184 IDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFL 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
75-262 |
6.57e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.57 E-value: 6.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 75 LAVlDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVtAPHPSRAL-------VFQDPNLFPWRT 147
Cdd:PRK11300 19 LAV-NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI-EGLPGHQIarmgvvrTFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 148 VLDNVrLGPQARH----------------RSRLDA-DRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVF 210
Cdd:PRK11300 97 VIENL-LVAQHQQlktglfsgllktpafrRAESEAlDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1199741941 211 LLDEPLGKLDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
80-281 |
6.71e-18 |
|
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: 81.42 E-value: 6.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 80 DVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDG------TVVTAPHPSRALVFQDPNLFPWRTVLDNVR 153
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaelELYQLSEAERRRLMRTEWGFVHQNPRDGLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LGPQA-------------RHRSRLDADRVRWaLDLVGLTPF-ADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:TIGR02323 101 MRVSAganigerlmaigaRHYGNIRATAQDW-LEEVEIDPTrIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199741941 220 DALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSDrpARVLADLTVD--LDRPR 281
Cdd:TIGR02323 180 DVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQ--GRVVESGLTDqvLDDPQ 241
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
77-264 |
8.01e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 8.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVV---TAPHPSR--ALVFQDPNLFPWRTVLDN 151
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyASKEVARriGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLG-----PQARHRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLT 226
Cdd:PRK10253 102 VARGryphqPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1199741941 227 MQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK10253 182 LLELLSELNREKGYTLAAVLHDLNQACRYASHLIALRE 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
77-271 |
8.79e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.84 E-value: 8.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA-PHPSRAL-----VFQDPNLFpwR--TV 148
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlPMHKRARlgigyLPQEASIF--RklTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGPQARHRSRLD-ADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTM 227
Cdd:COG1137 96 EDNILAVLELRKLSKKErEERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199741941 228 QDELLRLwqAERFTALLVT-HDVDEALRLADRVVVLSDrpARVLA 271
Cdd:COG1137 176 QKIIRHL--KERGIGVLITdHNVRETLGICDRAYIISE--GKVLA 216
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
78-264 |
1.81e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 80.66 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAP-------HPSRALVFQDPN--LFPwRTV 148
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSrkglmklRESVGMVFQDPDnqLFS-ASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGPQARHRSRLDA-DRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTM 227
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEVrKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEI 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 1199741941 228 QDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK13636 181 MKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKE 217
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
75-263 |
2.28e-17 |
|
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: 78.75 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 75 LAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPS--EGDVSVDGTVVTAPHPSR--ALVFQDPNLFPWRTVLD 150
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSFRKiiGYVPQDDILHPTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLgpQARHRSrldadrvrwaldlvgltpfadalpatLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDE 230
Cdd:cd03213 102 TLMF--AAKLRG--------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153
|
170 180 190
....*....|....*....|....*....|....
gi 1199741941 231 LLRLWQAERfTALLVTHDV-DEALRLADRVVVLS 263
Cdd:cd03213 154 LRRLADTGR-TIICSIHQPsSEIFELFDKLLLLS 186
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
78-262 |
2.68e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 80.78 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGT-VVTAPHPSRAL-------VFQDP--NLFPWRT 147
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdLLKADPEAQKLlrqkiqiVFQNPygSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 148 V--------LDNVRLGPQARhrsrldADRVRWALDLVGLTP-FADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGK 218
Cdd:PRK11308 111 VgqileeplLINTSLSAAER------REKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1199741941 219 LDaltrLTMQDELLRLW---QAERFTA-LLVTHDVDEALRLADRVVVL 262
Cdd:PRK11308 185 LD----VSVQAQVLNLMmdlQQELGLSyVFISHDLSVVEHIADEVMVM 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
77-269 |
2.75e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.08 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQpSEGDVSVDGTV-----------VTAPHPSR--ALVFQDPNLF 143
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRVeffnqniyerrVNLNRLRRqvSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 144 PwRTVLDNVRLGPQA---RHRSRLDaDRVRWAL------DLVGLTPFADALpaTLSGGMAQRAALARALVNRPRVFLLDE 214
Cdd:PRK14258 101 P-MSVYDNVAYGVKIvgwRPKLEID-DIVESALkdadlwDEIKHKIHKSAL--DLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199741941 215 PLGKLDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSDRPARV 269
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRI 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
74-262 |
3.10e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.08 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA-----PHPSRALVFQDPNLFPwRTV 148
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhhyLHRQVALVGQEPVLFS-GSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGPQarhrsRLDADRVRWALDLVGLTPFADALPAT-----------LSGGMAQRAALARALVNRPRVFLLDEPLG 217
Cdd:TIGR00958 572 RENIAYGLT-----DTPDEEIMAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199741941 218 KLDALTRLTMQDELLRlwqAERfTALLVTHDVDEALRlADRVVVL 262
Cdd:TIGR00958 647 ALDAECEQLLQESRSR---ASR-TVLLIAHRLSTVER-ADQILVL 686
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
79-264 |
3.77e-17 |
|
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: 78.95 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 79 DDVTLDIPPGQLVALVGPSGCGKST----LLRLLAGLAQPSEGDVSVDGTVVtAPHPSR----ALVFQDP-NLF-PWRTV 148
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPL-LPLSIRgrhiATIMQNPrTAFnPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGPQARHRSRLDA-DRVRWALDLVGLTPFADAL---PATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTR 224
Cdd:TIGR02770 82 GNHAIETLRSLGKLSKQArALILEALEAVGLPDPEEVLkkyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1199741941 225 LTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:TIGR02770 162 ARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDD 201
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
78-275 |
3.97e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.65 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGtvVTAPHPSR--------ALVFQDPNL-FPWRTV 148
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKlqgirklvGIVFQNPETqFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGPQ------ARHRSRLDAdrvrwALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDAL 222
Cdd:PRK13644 96 EEDLAFGPEnlclppIEIRKRVDR-----ALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 223 TRLTMQDELLRLWQAERfTALLVTHDVDEaLRLADRV-------VVLSDRPARVLADLTV 275
Cdd:PRK13644 171 SGIAVLERIKKLHEKGK-TIVYITHNLEE-LHDADRIivmdrgkIVLEGEPENVLSDVSL 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
78-264 |
1.18e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 78.04 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGT------VVTAPHPSRALVFQDPNLFPWRTVLDN 151
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdLYALSEAERRRLLRTEWGFVHQHPRDG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQA-------------RHRSRLDADRVRWaLDLVGLTPF-ADALPATLSGGMAQRAALARALVNRPRVFLLDEPLG 217
Cdd:PRK11701 102 LRMQVSAggnigerlmavgaRHYGDIRATAGDW-LERVEIDAArIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199741941 218 KLDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK11701 181 GLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
74-275 |
1.24e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 77.61 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR------ALVFQDPNLFPWRT 147
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimreavAIVPEGRRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 148 VLDNVRLGPQARHRSRLDaDRVRWALDLVG-LTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLT 226
Cdd:PRK11614 97 VEENLAMGGFFAERDQFQ-ERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199741941 227 MQDELLRLwQAERFTALLVTHDVDEALRLADR-------VVVLSDRPARVLADLTV 275
Cdd:PRK11614 176 IFDTIEQL-REQGMTIFLVEQNANQALKLADRgyvlengHVVLEDTGDALLANEAV 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
73-276 |
1.31e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.31 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAP--HPSR---ALVFQDPN--LFPw 145
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEniREVRkfvGLVFQNPDdqIFS- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 146 RTVLDNVRLGPQarhRSRLD----ADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDA 221
Cdd:PRK13652 94 PTVEQDIAFGPI---NLGLDeetvAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199741941 222 LTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSDrpARVLADLTVD 276
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDK--GRIVAYGTVE 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
74-264 |
1.79e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.90 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAP------HPSR---ALVFQDP--NL 142
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyiRPVRkriGMVFQFPesQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 143 FPwRTVLDNVRLGPQarhRSRLDADRVR-----------WALDLVGLTPFadalpaTLSGGMAQRAALARALVNRPRVFL 211
Cdd:PRK13646 99 FE-DTVEREIIFGPK---NFKMNLDEVKnyahrllmdlgFSRDVMSQSPF------QMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199741941 212 LDEPLGKLDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKE 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
77-272 |
2.07e-16 |
|
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: 77.05 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEG-DVSVDGT---------------VVTaphPSRALVFQdP 140
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggedvwelrkrigLVS---PALQLRFP-R 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 141 NLFPWRTVL----DNVRLGPQArhrSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPL 216
Cdd:COG1119 94 DETVLDVVLsgffDSIGLYREP---TDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199741941 217 GKLDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLsdRPARVLAD 272
Cdd:COG1119 171 AGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL--KDGRVVAA 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
78-281 |
2.56e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.18 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT------APHPSRALVFQDPNLFPWRTVLDN 151
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfasttaALAAGVAIIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLG--PQAR---HRSRLDAdRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDAltRLT 226
Cdd:PRK11288 100 LYLGqlPHKGgivNRRLLNY-EAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA--REI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199741941 227 mqDELLRL---WQAERFTALLVTHDVDEALRLADRVVVLSD-RPARVLADLTvDLDRPR 281
Cdd:PRK11288 177 --EQLFRVireLRAEGRVILYVSHRMEEIFALCDAITVFKDgRYVATFDDMA-QVDRDQ 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
74-221 |
2.66e-16 |
|
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: 75.99 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPS--RALVF--QDPNLFPWRTVL 149
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiaRGLLYlgHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199741941 150 DNVRLgpqarHRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDA 221
Cdd:cd03231 92 ENLRF-----WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
74-264 |
2.66e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.38 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVtAPHPSRAL----------VFQDPNLF 143
Cdd:PRK10535 20 QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDV-ATLDADALaqlrrehfgfIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 144 PWRTVLDNVRL----GPQARHRSRldaDRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:PRK10535 99 SHLTAAQNVEVpavyAGLERKQRL---LRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199741941 220 DALTRLTMQDELLRLwQAERFTALLVTHDVDEALRlADRVVVLSD 264
Cdd:PRK10535 176 DSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRD 218
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
73-264 |
3.76e-16 |
|
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: 75.83 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHP---------SRALVFQDPNLF 143
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFeatrsrnrySVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 144 PwRTVLDNVRLGpqarhrSRLDADRVRWALDLVGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVFLL 212
Cdd:cd03290 92 N-ATVEENITFG------SPFNKQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199741941 213 DEPLGKLDA-LTRLTMQDELLRLWQAERFTALLVTHDVdEALRLADRVVVLSD 264
Cdd:cd03290 165 DDPFSALDIhLSDHLMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKD 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
77-264 |
4.30e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 78.71 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA--PHPSRA---LVFQDPNLFPwRTVLDN 151
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvtQASLRAaigIVPQDTVLFN-DTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGpqarhrsRLDADR--VRWALDLVGLTPFADALP---AT--------LSGGMAQRAALARALVNRPRVFLLDEPLGK 218
Cdd:COG5265 452 IAYG-------RPDASEeeVEAAARAAQIHDFIESLPdgyDTrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1199741941 219 LDALTRLTMQDELLRLwqAERFTALLVTHdvdealRL-----ADRVVVLSD 264
Cdd:COG5265 525 LDSRTERAIQAALREV--ARGRTTLVIAH------RLstivdADEILVLEA 567
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
74-263 |
6.37e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 76.81 E-value: 6.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSV---------DGTVVTAPHPSR----------- 133
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELITNPYSKkiknfkelrrr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 134 -ALVFQDP--NLFPwRTVLDNVRLGPQARHRSRLDA-DRVRWALDLVGL-TPFADALPATLSGGMAQRAALARALVNRPR 208
Cdd:PRK13631 118 vSMVFQFPeyQLFK-DTIEKDIMFGPVALGVKKSEAkKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199741941 209 VFLLDEPLGKLDALTRLTMQDeLLRLWQAERFTALLVTHDVDEALRLADRVVVLS 263
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
77-264 |
1.21e-15 |
|
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: 73.50 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR----ALVFQDPNLFPwRTVLDNv 152
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALssliSVLNQRPYLFD-TTLRNN- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 rLGPQarhrsrldadrvrwaldlvgltpfadalpatLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTrltmQDELL 232
Cdd:cd03247 95 -LGRR-------------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT----ERQLL 138
|
170 180 190
....*....|....*....|....*....|....
gi 1199741941 233 RLW--QAERFTALLVTHDVdEALRLADRVVVLSD 264
Cdd:cd03247 139 SLIfeVLKDKTLIWITHHL-TGIEHMDKILFLEN 171
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
77-262 |
1.24e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.07 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDG-TVVTAPHP----SRALVFQDPNLFPwRTVLDN 151
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrPLSSLSHSvlrqGVAMVQQDPVVLA-DTFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGpqaRHrsrLDADRVRWALDLVGLTPFADALPA-----------TLSGGMAQRAALARALVNRPRVFLLDEPLGKLD 220
Cdd:PRK10790 435 VTLG---RD---ISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199741941 221 ALTRLTMQdELLRLWQaERFTALLVTHdvdealRL-----ADRVVVL 262
Cdd:PRK10790 509 SGTEQAIQ-QALAAVR-EHTTLVVIAH------RLstiveADTILVL 547
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
73-264 |
1.28e-15 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 77.10 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT-------APH----PsralvfQDPN 141
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwdreelGRHigylP------QDVE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 142 LFPwRTVLDNV-RLGPqarhrsrLDADRVRWALDLVGLTPFADALP-----------ATLSGG----------MAqraal 199
Cdd:COG4618 417 LFD-GTIAENIaRFGD-------ADPEKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGqrqriglaraLY----- 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 200 aralvNRPRVFLLDEPLGKLD-----ALTRltmqdeLLRLWQAERFTALLVTHDVdEALRLADRVVVLSD 264
Cdd:COG4618 484 -----GDPRLVVLDEPNSNLDdegeaALAA------AIRALKARGATVVVITHRP-SLLAAVDKLLVLRD 541
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
77-264 |
1.86e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.13 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEG-----DVSVDGTV------VTAPHPSRALVFQDPNLFPw 145
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSifnyrdVLEFRRRVGMLFQRPNPFP- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 146 RTVLDNVRLGPQArHR--SRLDADRVRWA-LDLVGL-TPFADAL---PATLSGGMAQRAALARALVNRPRVFLLDEPLGK 218
Cdd:PRK14271 115 MSIMDNVLAGVRA-HKlvPRKEFRGVAQArLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199741941 219 LDALTRLTMQDELLRLwqAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK14271 194 LDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFD 237
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
77-263 |
2.38e-15 |
|
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: 76.32 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT--APHPSRAL---VFQDPNLFPwRTVLDN 151
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdiDRHTLRQFinyLPQEPYIFS-GSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGpqarHRSRLDADRVRWALDLVGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVFLLDEPLGKLD 220
Cdd:TIGR01193 568 LLLG----AKENVSQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1199741941 221 ALTRLTMQDELLRLWQAerfTALLVTHDVDEALRlADRVVVLS 263
Cdd:TIGR01193 644 TITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLD 682
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
77-271 |
2.42e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.66 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT-------APHPSRALVFQDPNLFPWRTVL 149
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrgllALRQQVATVFQDPEQQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 150 DN------VRLGPQARHRSRldadRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALT 223
Cdd:PRK13638 96 DSdiafslRNLGVPEAEITR----RVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1199741941 224 RLTMQDELLRLWQAERFTaLLVTHDVDEALRLADRVVVLsdRPARVLA 271
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVL--RQGQILT 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
76-264 |
2.53e-15 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 72.46 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRA------LVFQDPN---LFPWR 146
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiragiaYVPEDRKregLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 147 TVLDNVrlgpqarhrsrldadrvrwaldlvgltpfadALPATLSGGmaqraalaralvN------------RPRVFLLDE 214
Cdd:cd03215 94 SVAENI-------------------------------ALSSLLSGG------------NqqkvvlarwlarDPRVLILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1199741941 215 PLGKLDALTRLTMQDELLRLwqAERFTA-LLVTHDVDEALRLADRVVVLSD 264
Cdd:cd03215 131 PTRGVDVGAKAEIYRLIREL--ADAGKAvLLISSELDELLGLCDRILVMYE 179
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
79-221 |
5.04e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.53 E-value: 5.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 79 DDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPS--RALVF--QDPNLFPWRTVLDNVRL 154
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhQDLLYlgHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199741941 155 gpQARHRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDA 221
Cdd:PRK13538 98 --YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
78-193 |
5.20e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.55 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSV-DGTVVTAPHpsRALVFQD----P-----NLFPWRT 147
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlGGDMADARH--RRAVCPRiaymPqglgkNLYPTLS 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1199741941 148 VLDNV----RL-GPQARHRSRldadRVRWALDLVGLTPFADALPATLSGGM 193
Cdd:NF033858 95 VFENLdffgRLfGQDAAERRR----RIDELLRATGLAPFADRPAGKLSGGM 141
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
77-262 |
1.25e-14 |
|
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: 73.95 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKS----TLLRLLAGLAQPSEGDVSVDGT-VVTAPHPSR--------ALVFQDP--N 141
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQdLLGLSERELrrirgnriAMIFQEPmtS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 142 LFPWRTVldnvrlGPQ-----ARHR--SRLDA-DRVRWALDLVGLTPFA---DALPATLSGGMAQRAALARALVNRPRVF 210
Cdd:COG4172 105 LNPLHTI------GKQiaevlRLHRglSGAAArARALELLERVGIPDPErrlDAYPHQLSGGQRQRVMIAMALANEPDLL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199741941 211 LLDEPLGKLDAltrlTMQDELLRL---WQAERFTA-LLVTHDVDEALRLADRVVVL 262
Cdd:COG4172 179 IADEPTTALDV----TVQAQILDLlkdLQRELGMAlLLITHDLGVVRRFADRVAVM 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
73-264 |
1.27e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.81 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDV-----------------SVDGTVVTAPHPSRAL 135
Cdd:PRK13651 18 TELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekeKVLEKLVIQKTRFKKI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 136 ------------VFQ--DPNLFPwRTVLDNVRLGPQARHRSRLDA-DRVRWALDLVGL-TPFADALPATLSGGMAQRAAL 199
Cdd:PRK13651 98 kkikeirrrvgvVFQfaEYQLFE-QTIEKDIIFGPVSMGVSKEEAkKRAAKYIELVGLdESYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199741941 200 ARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRLWQAERfTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKD 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
78-263 |
1.28e-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: 74.66 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDG----TVVTAPHPSRALVFQDPNLFPWRTVLDNVR 153
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdieTNLDAVRQSLGMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LGPQARHRSRLDAD-RVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELL 232
Cdd:TIGR01257 1026 FYAQLKGRSWEEAQlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190
....*....|....*....|....*....|.
gi 1199741941 233 RlWQAERfTALLVTHDVDEALRLADRVVVLS 263
Cdd:TIGR01257 1106 K-YRSGR-TIIMSTHHMDEADLLGDRIAIIS 1134
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
74-264 |
1.48e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.73 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGL-----AQPSEGDVSVDGTVVTAPHPSR-----ALVFQDP--N 141
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetGQTIVGDYAIPANLKKIKEVKRlrkeiGLVFQFPeyQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 142 LFPwRTVLDNVRLGPQARHRSRLDA-DRVRWALDLVGL-TPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:PRK13645 103 LFQ-ETIEKDIAFGPVNLGENKQEAyKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199741941 220 DALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHE 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
78-267 |
1.63e-14 |
|
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: 71.67 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPG-----QLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVV-------TAPHPS--RALVFQdpnlf 143
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpqyiKADYEGtvRDLLSS----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 144 pwrtVLDNVRLGPQarhrsrldadrvrWALDLV---GLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLD 220
Cdd:cd03237 85 ----ITKDFYTHPY-------------FKTEIAkplQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199741941 221 ALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSDRPA 267
Cdd:cd03237 148 VEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
78-262 |
1.97e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.46 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT-----APHPSRALVFQDPNLFPwRTVLDNV 152
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRtvtraSLRRNIAVVFQDAGLFN-RSIEDNI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RLG-PQARHRSRLDADRVRWALDLV-----GLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLT 226
Cdd:PRK13657 430 RVGrPDATDEEMRAAAERAQAHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAK 509
|
170 180 190
....*....|....*....|....*....|....*.
gi 1199741941 227 MQDELLRLWQAErfTALLVTHDVdEALRLADRVVVL 262
Cdd:PRK13657 510 VKAALDELMKGR--TTFIIAHRL-STVRNADRILVF 542
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
77-263 |
3.33e-14 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 70.38 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSE---GDVSVDGTVVTaPHPSR---ALVFQDPNLFPWRTVLD 150
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRK-PDQFQkcvAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGPQARHRSRLD--ADRVRWA---LDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRL 225
Cdd:cd03234 101 TLTYTAILRLPRKSSdaIRKKRVEdvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1199741941 226 TMQDELLRLwqAERFTALLVT-HD-VDEALRLADRVVVLS 263
Cdd:cd03234 181 NLVSTLSQL--ARRNRIVILTiHQpRSDLFRLFDRILLLS 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
77-264 |
4.94e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAphpsralVF-QDP-NLFPWRTVLDNVR- 153
Cdd:COG0488 330 LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIG-------YFdQHQeELDPDKTVLDELRd 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LGPQARH---RSRL-----DADRVRwalDLVGltpfadalpaTLSGG----------MaqraalaralVNRPRVFLLDEP 215
Cdd:COG0488 403 GAPGGTEqevRGYLgrflfSGDDAF---KPVG----------VLSGGekarlalaklL----------LSPPNVLLLDEP 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1199741941 216 LGKLDALTRlTMQDELLRLWQAerfTALLVTHD---VDealRLADRVVVLSD 264
Cdd:COG0488 460 TNHLDIETL-EALEEALDDFPG---TVLLVSHDryfLD---RVATRILEFED 504
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
73-264 |
7.46e-14 |
|
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: 69.39 E-value: 7.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSV--DGTVV---TAPhPSRAL---------VFQ 138
Cdd:COG4778 22 KRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlaQAS-PREILalrrrtigyVSQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 139 DPNLFPWRTVLDNVRLGPQARHRSRLDA-DRVRWALDLVGLTP-FADALPATLSGGmaqraalARALVN-------RPRV 209
Cdd:COG4778 101 FLRVIPRVSALDVVAEPLLERGVDREEArARARELLARLNLPErLWDLPPATFSGG-------EQQRVNiargfiaDPPL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199741941 210 FLLDEPLGKLDALTRLTMQDELLRLWQaeRFTALL-VTHDVDEALRLADRVVVLSD 264
Cdd:COG4778 174 LLLDEPTASLDAANRAVVVELIEEAKA--RGTAIIgIFHDEEVREAVADRVVDVTP 227
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
77-264 |
7.66e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 69.71 E-value: 7.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLA--QPSEGDVSVDGTVVTA--PHpSRA-----LVFQDPNLFPWRT 147
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILElsPD-ERAragifLAFQYPVEIPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 148 VLDNVRLGPQARHRSRLDA----DRVRWALDLVGLTP-FAD-ALPATLSGG---------MAqraalaralVNRPRVFLL 212
Cdd:COG0396 94 VSNFLRTALNARRGEELSAreflKLLKEKMKELGLDEdFLDrYVNEGFSGGekkrneilqML---------LLEPKLAIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 213 DEP---LgKLDALTRLTmqdELLRLWQAERFTALLVTHdvdeALRL-----ADRVVVLSD 264
Cdd:COG0396 165 DETdsgL-DIDALRIVA---EGVNKLRSPDRGILIITH----YQRIldyikPDFVHVLVD 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
74-262 |
8.36e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.81 E-value: 8.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR--------ALVFQDP--NLF 143
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrrdiQFIFQDPyaSLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 144 PWRTVLDNVrLGPQARHR---SRLDADRVRWALDLVGLTP-FADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:PRK10261 416 PRQTVGDSI-MEPLRVHGllpGKAAAARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1199741941 220 DALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVM 537
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
73-264 |
8.47e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.73 E-value: 8.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKS-----TLLRLLAGLAQpSEGDVSVDGTVVtAPHPSR----ALVFQDPN-- 141
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPV-APCALRgrkiATIMQNPRsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 142 LFPWRTVLDNVRLGPQARHRSRLDAdRVRWALDLVGLTPFADAL---PATLSGGMAQRAALARALVNRPRVFLLDEPLGK 218
Cdd:PRK10418 92 FNPLHTMHTHARETCLALGKPADDA-TLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199741941 219 LDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSH 216
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
75-262 |
1.71e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.74 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 75 LAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT--APHPSRA------LVFQDP--NLFP 144
Cdd:PRK15079 34 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmKDDEWRAvrsdiqMIFQDPlaSLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 145 WRTVLDnVRLGPQARHRSRLDA----DRVRWALDLVGLTP-FADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:PRK15079 114 RMTIGE-IIAEPLRTYHPKLSRqevkDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199741941 220 DaltrLTMQDE---LLRLWQAERFTALL-VTHDVDEALRLADRVVVL 262
Cdd:PRK15079 193 D----VSIQAQvvnLLQQLQREMGLSLIfIAHDLAVVKHISDRVLVM 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
78-276 |
2.46e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRA------LVFQDPNLFPWRTVLDN 151
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlgigIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGpqaRHRSR--LDADRVRWA---------LDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKL- 219
Cdd:PRK09700 101 LYIG---RHLTKkvCGVNIIDWRemrvraammLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLt 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199741941 220 -DALTRLTMqdeLLRLWQAERFTALLVTHDVDEALRLADRVVVLSDRP---ARVLADLTVD 276
Cdd:PRK09700 178 nKEVDYLFL---IMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSsvcSGMVSDVSND 235
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
77-264 |
3.28e-13 |
|
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: 67.52 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT--APHPSR---ALVFQDPNLFPwRTVLDN 151
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkiGLHDLRsriSIIPQDPVLFS-GTIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 vrLGPQARHrsrldADRVRW-ALDLVGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:cd03244 98 --LDPFGEY-----SDEELWqALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILVLDEATASV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1199741941 220 DALTRLTMQdELLRLWQAERfTALLVTHdvdealRL-----ADRVVVLSD 264
Cdd:cd03244 171 DPETDALIQ-KTIREAFKDC-TVLTIAH------RLdtiidSDRILVLDK 212
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
76-272 |
3.55e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAG-LAQPSE-------GDVSVDGTVVTAPHPSR------ALVFQDPN 141
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRlarlraVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 142 LFPWrTVLDNVRLG--PQARH---RSRLDADRVRWALDLVGLTPFADALPATLSGG---------MAQRAALARALVNRP 207
Cdd:PRK13547 95 AFAF-SAREIVLLGryPHARRagaLTHRDGEIAWQALALAGATALVGRDVTTLSGGelarvqfarVLAQLWPPHDAAQPP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199741941 208 RVFLLDEPLGKLDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSDrpARVLAD 272
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLAD--GAIVAH 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
74-221 |
3.69e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.21 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRALVF---QD---PNLfpwrT 147
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYlghRNamkPAL----T 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199741941 148 VLDNVRLGPQARHRSRLDADRvrwALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDA 221
Cdd:PRK13539 90 VAENLEFWAAFLGGEELDIAA---ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
77-264 |
3.85e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRA------LVFQDPNLFPWRTVLD 150
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAhqlgiyLVPQEPLLFPNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGPQarhRSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGkldALT-----RL 225
Cdd:PRK15439 106 NILFGLP---KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTA---SLTpaeteRL 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1199741941 226 TMQdelLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK15439 180 FSR---IRELLAQGVGIVFISHKLPEIRQLADRISVMRD 215
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
74-263 |
4.86e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.29 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLA--QPSEGDVSVDgtvvtaphpsralvfqDPNLFPWRTVLDN 151
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVP----------------DNQFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VrlgpqARHRSRLDADRVrwaLDLVGLT--PFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQD 229
Cdd:COG2401 106 I-----GRKGDFKDAVEL---LNAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 1199741941 230 ELLRLWQAERFTALLVTH--DVDEALRlADRVVVLS 263
Cdd:COG2401 178 NLQKLARRAGITLVVATHhyDVIDDLQ-PDLLIFVG 212
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
77-275 |
5.48e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.23 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA-PHPSRAL-----VFQDPNLFPWRTVLD 150
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlPLHARARrgigyLPQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 NVRLGPQARH--RSRLDADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQ 228
Cdd:PRK10895 98 NLMAVLQIRDdlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIK 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199741941 229 dELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD-------RPARVLADLTV 275
Cdd:PRK10895 178 -RIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQghliahgTPTEILQDEHV 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
77-274 |
8.45e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.51 E-value: 8.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRAL---------------VFQDpn 141
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIragiayvpedrkgegLVLD-- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 142 lfpwRTVLDNVRLGPQARH------RSRLDADRVRWALDLVGL-TPFADALPATLSGGmaqraalaralvN--------- 205
Cdd:COG1129 345 ----LSIRENITLASLDRLsrggllDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGG------------Nqqkvvlakw 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 206 ---RPRVFLLDEPlgkldalTR----------LTMQDELlrlwqAERFTA-LLVTHDVDEALRLADRVVVLSDRpaRVLA 271
Cdd:COG1129 409 latDPKVLILDEP-------TRgidvgakaeiYRLIREL-----AAEGKAvIVISSELPELLGLSDRILVMREG--RIVG 474
|
...
gi 1199741941 272 DLT 274
Cdd:COG1129 475 ELD 477
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
77-248 |
1.18e-12 |
|
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: 68.04 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDvsvdgtVVTAPHPSRALVFQDPNLFPWRTVLDNVRLG- 155
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE------ARPQPGIKVGYLPQEPQLDPTKTVRENVEEGv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 156 -----------------------------PQARHRSRLDA-------DRVRWALDLVGLTPFaDALPATLSGGMAQRAAL 199
Cdd:TIGR03719 94 aeikdaldrfneisakyaepdadfdklaaEQAELQEIIDAadawdldSQLEIAMDALRCPPW-DADVTKLSGGERRRVAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1199741941 200 ARALVNRPRVFLLDEPLGKLDALTRLTMQDELlrlwqaERF--TALLVTHD 248
Cdd:TIGR03719 173 CRLLLSKPDMLLLDEPTNHLDAESVAWLERHL------QEYpgTVVAVTHD 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
78-264 |
1.28e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.15 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPS---EGDVSVDGTVVTAPHPSR--ALVFQDPNLFPWRTVLDN- 151
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAisAYVQQDDLFIPTLTVREHl 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 -----VRLGPQARHRSRLdaDRVRWALDLVGLTPFADALPAT------LSGGMAQRAALARALVNRPRVFLLDEPLGKLD 220
Cdd:TIGR00955 121 mfqahLRMPRRVTKKEKR--ERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199741941 221 ALTRLTMQDELLRLWQAERfTALLVTHD-VDEALRLADRVVVLSD 264
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGK-TIICTIHQpSSELFELFDKIILMAE 242
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
78-264 |
1.47e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.43 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVvtAPHPSRALVFQDpnlfpwrTVLDNVRLGPQ 157
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV--AYVPQQAWIQND-------SLRENILFGKA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 158 arhrsrLDADRVRWALDLVGLTPFADALPA-----------TLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLT 226
Cdd:TIGR00957 725 ------LNEKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190
....*....|....*....|....*....|....*....
gi 1199741941 227 MQDELL-RLWQAERFTALLVTHDVdEALRLADRVVVLSD 264
Cdd:TIGR00957 799 IFEHVIgPEGVLKNKTRILVTHGI-SYLPQVDVIIVMSG 836
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
78-262 |
1.62e-12 |
|
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: 68.12 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAphpSRALVFQDPNLFPWRTVLDNVRLGPQ 157
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT---NISDVHQNMGYCPQFDAIDDLLTGRE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 158 -----ARHRS--RLDADRV-RWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQD 229
Cdd:TIGR01257 2032 hlylyARLRGvpAEEIEKVaNWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 2111
|
170 180 190
....*....|....*....|....*....|...
gi 1199741941 230 ELLRLWQAERfTALLVTHDVDEALRLADRVVVL 262
Cdd:TIGR01257 2112 TIVSIIREGR-AVVLTSHSMEECEALCTRLAIM 2143
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
77-262 |
1.82e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.42 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKST----LLRLLAglaqpSEGDVSVDGTVVTAPHPSRAL--------VFQDPN--L 142
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLpvrhriqvVFQDPNssL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 143 FPWRTVLDNVRLGPQArHRSRLDA----DRVRWALDLVGLTPFA-DALPATLSGGMAQRAALARALVNRPRVFLLDEPLG 217
Cdd:PRK15134 376 NPRLNVLQIIEEGLRV-HQPTLSAaqreQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1199741941 218 KLDAltrlTMQDELL----RLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK15134 455 SLDK----TVQAQILallkSLQQKHQLAYLFISHDLHVVRALCHQVIVL 499
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
75-264 |
2.10e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.36 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 75 LAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR------ALVFQDPN---LFPW 145
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErrrlgvAYIPEDRLgrgLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 146 RTVLDNVRLG----PQARHRSRLDADRVR-WALDLVG----LTPFADALPATLSGGmaqraalaralvN----------- 205
Cdd:COG3845 351 MSVAENLILGryrrPPFSRGGFLDRKAIRaFAEELIEefdvRTPGPDTPARSLSGG------------Nqqkvilarels 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199741941 206 -RPRVFLLDEPLGKLDALTRLTMQDELLRLwqAERFTA-LLVTHDVDEALRLADRVVVLSD 264
Cdd:COG3845 419 rDPKLLIAAQPTRGLDVGAIEFIHQRLLEL--RDAGAAvLLISEDLDEILALSDRIAVMYE 477
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
74-266 |
2.54e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.87 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRALVFQD--PNLFPWRTVLDN 151
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGhlPGLKADLSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRL--GPQARHRSRLDADrvrwALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDaLTRLTMQD 229
Cdd:PRK13543 103 LHFlcGLHGRRAKQMPGS----ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD-LEGITLVN 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 1199741941 230 ELLRLWQAERFTALLVTHDVDEALRLADRVVVLSDRP 266
Cdd:PRK13543 178 RMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
77-265 |
3.13e-12 |
|
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: 63.24 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAphpsralVFqdpnlfpwrtvldnvrlgP 156
Cdd:cd03221 15 LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIG-------YF------------------E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 157 QarhrsrldadrvrwaldlvgltpfadalpatLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELlrlwQ 236
Cdd:cd03221 70 Q-------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL----K 114
|
170 180
....*....|....*....|....*....
gi 1199741941 237 AERFTALLVTHDVDEALRLADRVVVLSDR 265
Cdd:cd03221 115 EYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
77-262 |
4.06e-12 |
|
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: 66.86 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHpsralvfqdpnlFPW---RTVLDNVR 153
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQ------------TSWimpGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LG---PQARHRSRLDADRVRwalDLVGLTPFADALP-----ATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRL 225
Cdd:TIGR01271 509 FGlsyDEYRYTSVIKACQLE---EDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190
....*....|....*....|....*....|....*..
gi 1199741941 226 TMQDELLRLWQAERfTALLVTHDVdEALRLADRVVVL 262
Cdd:TIGR01271 586 EIFESCLCKLMSNK-TRILVTSKL-EHLKKADKILLL 620
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
80-262 |
7.41e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.43 E-value: 7.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 80 DVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT-APHPSRA----LVFQDP--NLFPWRTV---L 149
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDYSYRSqrirMIFQDPstSLNPRQRIsqiL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 150 D-----NVRLGPQARHRsrldadRVRWALDLVGLTP-FADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALT 223
Cdd:PRK15112 111 DfplrlNTDLEPEQREK------QIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 1199741941 224 RLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK15112 185 RSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVM 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
76-270 |
1.13e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.21 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVdgtvvtaPHPSRALVF-QDPNLfPWRTvLDNVRL 154
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR-------PAGARVLFLpQRPYL-PLGT-LREALL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 155 GPQArhRSRLDADRVRWALDLVGLTPFADAL------PATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDAltrlTMQ 228
Cdd:COG4178 448 YPAT--AEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE----ENE 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1199741941 229 DELLRLWQAERFTA--LLVTHDvDEALRLADRVVVLSDRPARVL 270
Cdd:COG4178 522 AALYQLLREELPGTtvISVGHR-STLAAFHDRVLELTGDGSWQL 564
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
76-262 |
1.21e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRalVFQDPNLfPWrTVLDNVRLG 155
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK--LYLDTTL-PL-TVNRFLRLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 156 PQARHRSRLDadrvrwALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRLW 235
Cdd:PRK09544 94 PGTKKEDILP------ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLR 167
|
170 180
....*....|....*....|....*..
gi 1199741941 236 QAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK09544 168 RELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
77-262 |
1.83e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 63.34 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHpsralvfqdpnlFPW---RTVLDNVR 153
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQ------------FSWimpGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LG---PQARHRSRLDADRVRWalDLVGLtPFADALP-----ATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRL 225
Cdd:cd03291 120 FGvsyDEYRYKSVVKACQLEE--DITKF-PEKDNTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190
....*....|....*....|....*....|....*..
gi 1199741941 226 TMQDELLRLWQAERfTALLVTHDVdEALRLADRVVVL 262
Cdd:cd03291 197 EIFESCVCKLMANK-TRILVTSKM-EHLKKADKILIL 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
74-264 |
1.90e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.46 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPS--RA---LVFQDPNLFPwRTV 148
Cdd:PRK11160 352 PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAalRQaisVVSQRVHLFS-ATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLG-PQArhrsrlDADRVRWALDLVGLTPFADALPA----------TLSGGMAQRAALARALVNRPRVFLLDEPLG 217
Cdd:PRK11160 431 RDNLLLAaPNA------SDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1199741941 218 KLDALT-RLTMQdeLLRLWQAERfTALLVTHDVdEALRLADRVVVLSD 264
Cdd:PRK11160 505 GLDAETeRQILE--LLAEHAQNK-TVLMITHRL-TGLEQFDRICVMDN 548
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
81-143 |
3.24e-11 |
|
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: 63.66 E-value: 3.24e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199741941 81 VTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPS--RAL---VFQDPNLF 143
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREayRQLfsaVFSDFHLF 418
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
77-248 |
3.88e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDvsvdgtVVTAPHPSRALVFQDPNLFPWRTVLDNVRLG- 155
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE------ARPAPGIKVGYLPQEPQLDPEKTVRENVEEGv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 156 -----------------------------PQARHRSRLDA-------DRVRWALDLVGLTPfADALPATLSGGMAQRAAL 199
Cdd:PRK11819 96 aevkaaldrfneiyaayaepdadfdalaaEQGELQEIIDAadawdldSQLEIAMDALRCPP-WDAKVTKLSGGERRRVAL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1199741941 200 ARALVNRPRVFLLDEPLGKLDALTRLTMQDELlrlwqaERF--TALLVTHD 248
Cdd:PRK11819 175 CRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL------HDYpgTVVAVTHD 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
78-276 |
8.96e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 8.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLaQPS---EGDVSVDGTVVTAPHPSR------ALVFQDPNLFPWRTV 148
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNIRDteragiAIIHQELALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGPQARHRSRLDADRV-----RWaLDLVGLtpfaDALPAT----LSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:PRK13549 100 LENIFLGNEITPGGIMDYDAMylraqKL-LAQLKL----DINPATpvgnLGLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199741941 220 -DALTRLTMqdELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD------RPArvlADLTVD 276
Cdd:PRK13549 175 tESETAVLL--DIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDgrhigtRPA---AGMTED 233
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
77-264 |
1.47e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 59.46 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLA--QPSEGDVSVDGTVVTAPHPS-RA-----LVFQDPNLFPWRTV 148
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEeRArlgifLAFQYPPEIPGVKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRlgpqarhrsrldadrvrwaldlvgltpfadALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDaLTRLTMQ 228
Cdd:cd03217 95 ADFLR------------------------------YVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD-IDALRLV 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 1199741941 229 DELLRLWQAERFTALLVTH--DVDEALRlADRVVVLSD 264
Cdd:cd03217 144 AEVINKLREEGKSVLIITHyqRLLDYIK-PDRVHVLYD 180
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
78-264 |
1.95e-10 |
|
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: 61.38 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLaQPS---EGDVSVDGTVVTAPHPSR------ALVFQDPNLFPWRTV 148
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASNIRDteragiVIIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGPQARHRSRLDAD-----RVRWALDLVGLTPFADALPATLSGGMAQRAALARALVN-RPRVFLLDEPLGKLDAL 222
Cdd:TIGR02633 96 AENIFLGNEITLPGGRMAYnamylRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNkQARLLILDEPSSSLTEK 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199741941 223 TRLTMQDeLLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:TIGR02633 176 ETEILLD-IIRDLKAHGVACVYISHKLNEVKAVCDTICVIRD 216
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
73-264 |
2.05e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEgDVSVD--GTVVTAPHpsralvfqdpnlFPW---RT 147
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-TSSVVirGSVAYVPQ------------VSWifnAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 148 VLDNVRLGpqarhrSRLDADRVRWALDLVGLTPFADALPA-----------TLSGGMAQRAALARALVNRPRVFLLDEPL 216
Cdd:PLN03232 695 VRENILFG------SDFESERYWRAIDVTALQHDLDLLPGrdlteigergvNISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199741941 217 GKLDA-----LTRLTMQDELlrlwqaERFTALLVTHDVdEALRLADRVVVLSD 264
Cdd:PLN03232 769 SALDAhvahqVFDSCMKDEL------KGKTRVLVTNQL-HFLPLMDRIILVSE 814
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
78-155 |
4.15e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRAL------VFQDPNLFPWRTVLDN 151
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALengismVHQELNLVLQRSVMDN 93
|
....
gi 1199741941 152 VRLG 155
Cdd:PRK10982 94 MWLG 97
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
74-221 |
7.28e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.14 E-value: 7.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAG-LAQPSEGDVSVDGTVVTAPHPSraLVFQdpnlfpwRTVLDNV 152
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTVAYVPQVS--WIFN-------ATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RLGpqarhrSRLDADRVRWALDLVGLTPFADALPA-----------TLSGGMAQRAALARALVNRPRVFLLDEPLGKLDA 221
Cdd:PLN03130 700 LFG------SPFDPERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
78-264 |
8.40e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 58.31 E-value: 8.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAqPSEGDVSVDGTVVTAPHPS-----RA-LVFQDPNLFPWRtVLDN 151
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAelarhRAyLSQQQSPPFAMP-VFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQARHRSRLDADRVRWALDLVGLTPFADALPATLSGG------MAQRAALARALVN-RPRVFLLDEPLGKLDALTR 224
Cdd:COG4138 90 LALHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGewqrvrLAAVLLQVWPTINpEGQLLLLDEPMNSLDVAQQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1199741941 225 LTMqDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:COG4138 170 AAL-DRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQ 208
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
77-128 |
1.10e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.18 E-value: 1.10e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA 128
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLA 388
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
78-248 |
1.97e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVdGTVVTAPH--PSRAlvfqdpNLFPWRTVLDNVRLG 155
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYfdQHRA------ELDPEKTVMDNLAEG 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 156 PQ-------ARH-------------RSRldadrvrwaldlvglTPFadalpATLSGGMAqraalaralvNR---PRVFL- 211
Cdd:PRK11147 408 KQevmvngrPRHvlgylqdflfhpkRAM---------------TPV-----KALSGGER----------NRlllARLFLk 457
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1199741941 212 ------LDEPLGKLDALTrLTMQDELLRLWQAerfTALLVTHD 248
Cdd:PRK11147 458 psnlliLDEPTNDLDVET-LELLEELLDSYQG---TVLLVSHD 496
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
84-267 |
3.07e-09 |
|
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: 55.27 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 84 DIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTaphpsralvfqdpnlfpwrtvldnvrLGPQArhrsr 163
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV--------------------------YKPQY----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 164 ldadrvrwaldlvgltpfadalpATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRLWQAERFTAL 243
Cdd:cd03222 70 -----------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTAL 126
|
170 180
....*....|....*....|....
gi 1199741941 244 LVTHDVDEALRLADRVVVLSDRPA 267
Cdd:cd03222 127 VVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
74-280 |
4.51e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVsvdgtVVTAPHPSR-----------ALVFQDPNL 142
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-----IINDSHNLKdinlkwwrskiGVVSQDPLL 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 143 FPwRTVLDNVRLG-------------------PQARHRSRLDADRVRWALDL---------------------------- 175
Cdd:PTZ00265 472 FS-NSIKNNIKYSlyslkdlealsnyynedgnDSQENKNKRNSCRAKCAGDLndmsnttdsneliemrknyqtikdsevv 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 176 -----VGLTPFADALP-----------ATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRLWQAER 239
Cdd:PTZ00265 551 dvskkVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEN 630
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1199741941 240 FTALLVTHDVdEALRLADRVVVLSDRPARVLADLTVDLDRP 280
Cdd:PTZ00265 631 RITIIIAHRL-STIRYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
81-143 |
4.58e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.29 E-value: 4.58e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199741941 81 VTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPS--RAL---VFQDPNLF 143
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLfsaVFTDFHLF 409
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
74-264 |
4.64e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.20 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPS--EGDVSVDGTVVTAPHPSR-ALVFQDPNLFPWRTVLD 150
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKRtGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 151 N------VRLgPQA--RHRSRLDADRVRWALDLV--GLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLD 220
Cdd:PLN03211 160 TlvfcslLRL-PKSltKQEKILVAESVISELGLTkcENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1199741941 221 ALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSE 282
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
78-262 |
6.19e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.04 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR--ALVFQDPNL---FPwRTVLDNV 152
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNlvAYVPQSEEVdwsFP-VLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RLG----------PQARHRSRLDAdrvrwALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDAL 222
Cdd:PRK15056 102 MMGryghmgwlrrAKKRDRQIVTA-----ALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1199741941 223 TRLTMQDeLLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK15056 177 TEARIIS-LLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
77-262 |
7.45e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.64 E-value: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKS----TLLRLLaglaqPS------EGDVSVDG-TVVTAPHPSR--------ALVF 137
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGeSLLHASEQTLrgvrgnkiAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 138 QDP--NLFPWRTV---LDNVrlgpQARHRS-RLDADRVRW--ALDLVGLTPFADAL---PATLSGGMAQRAALARALVNR 206
Cdd:PRK15134 99 QEPmvSLNPLHTLekqLYEV----LSLHRGmRREAARGEIlnCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 207 PRVFLLDEPLGKLDaltrLTMQDE---LLRLWQAERFTALL-VTHDVDEALRLADRVVVL 262
Cdd:PRK15134 175 PELLIADEPTTALD----VSVQAQilqLLRELQQELNMGLLfITHNLSIVRKLADRVAVM 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
78-220 |
1.03e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA---PHPSRAL---VF---------QDPNL 142
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVArlqQDPPRNVegtVYdfvaegieeQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 143 FPWRTVLDNVRLGPQARHRSRLDA--------------DRVRWALDLVGLTPfaDALPATLSGGMAQRAALARALVNRPR 208
Cdd:PRK11147 99 KRYHDISHLVETDPSEKNLNELAKlqeqldhhnlwqleNRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPD 176
|
170
....*....|..
gi 1199741941 209 VFLLDEPLGKLD 220
Cdd:PRK11147 177 VLLLDEPTNHLD 188
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
74-264 |
1.12e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.18 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSR-----ALVFQDPNLFPwRTV 148
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrnqvALVSQNVHLFN-DTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGPQARHrSRLD---ADRVRWALDLV-----GLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLD 220
Cdd:PRK11176 434 ANNIAYARTEQY-SREQieeAARMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1199741941 221 ALTRLTMQ---DELlrlwQAERfTALLVTHdvdealRL-----ADRVVVLSD 264
Cdd:PRK11176 513 TESERAIQaalDEL----QKNR-TSLVIAH------RLstiekADEILVVED 553
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
78-264 |
1.21e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT--APHPSRA----LVFQDPNLFPWRTVLDN 151
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQEagigIIHQELNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQARHR-SRLD-------ADRVrwaLDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPlgkLDALT 223
Cdd:PRK10762 100 IFLGREFVNRfGRIDwkkmyaeADKL---LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP---TDALT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1199741941 224 RlTMQDELLRL---WQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK10762 174 D-TETESLFRVireLKSQGRGIVYISHRLKEIFEICDDVTVFRD 216
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
78-262 |
1.24e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.52 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGL----AQPSEGDVSVDGTVVTAPHPSR---------ALVFQDP--NL 142
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKErrnlvgaevAMIFQDPmtSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 143 FPWRTV----LDNVRLGPQARHRSRldADRVRWALDLVGLTPFA---DALPATLSGGMAQRAALARALVNRPRVFLLDEP 215
Cdd:PRK11022 103 NPCYTVgfqiMEAIKVHQGGNKKTR--RQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199741941 216 LGKLDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVM 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
77-264 |
1.41e-08 |
|
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: 55.58 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQ--PSEGDV----------------SVDGT------------VV 126
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpSKVGEpcpvcggtlepeEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 127 TAPHPSR----------ALVFQDP-NLFPWRTVLDNV-RLGPQARHRSRLDADRVRWALDLVGLTPFADALPATLSGGMA 194
Cdd:TIGR03269 95 DFWNLSDklrrrirkriAIMLQRTfALYGDDTVLDNVlEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 195 QRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLEN 244
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
81-264 |
1.50e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.55 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 81 VTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAqPSEGDVSVDGTVV-TAPHPSRA-----LVFQDPNLF--PwrtVLDNV 152
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLeAWSAAELArhrayLSQQQTPPFamP---VFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RLGPQARHRSRLDADRVRWALDLVGLTPFADALPATLSGG------MAQRAALARALVN-RPRVFLLDEPLGKLDaLTRL 225
Cdd:PRK03695 91 TLHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGewqrvrLAAVVLQVWPDINpAGQLLLLDEPMNSLD-VAQQ 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 1199741941 226 TMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK03695 170 AALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQ 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
77-271 |
1.68e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.72 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVT--APHPSR---ALVFQDPNLFP--WRTVL 149
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAkiGLHDLRfkiTIIPQDPVLFSgsLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 150 DNVrlgpqarhrSRLDADRVRWALDLVGLTPFADALPA-----------TLSGGMAQRAALARALVNRPRVFLLDEPLGK 218
Cdd:TIGR00957 1381 DPF---------SQYSDEEVWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 219 LDALTRLTMQDELLRlwQAERFTALLVTHDVDEALRLAdRVVVLS-------DRPARVLA 271
Cdd:TIGR00957 1452 VDLETDNLIQSTIRT--QFEDCTVLTIAHRLNTIMDYT-RVIVLDkgevaefGAPSNLLQ 1508
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
79-125 |
2.20e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 2.20e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1199741941 79 DDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTV 125
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV 387
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
77-257 |
2.52e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.03 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVV----TAPHPSRALVFQDPNLFPWRTVLDNV 152
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdlCTYQKQLCFVGHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RLGPQARHRSRLDADRVRwaldLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELl 232
Cdd:PRK13540 96 LYDIHFSPGAVGITELCR----LFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI- 170
|
170 180
....*....|....*....|....*..
gi 1199741941 233 rlwQAERFT--ALLVTHDVDEALRLAD 257
Cdd:PRK13540 171 ---QEHRAKggAVLLTSHQDLPLNKAD 194
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
76-223 |
3.19e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.92 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQpSEGDVSVDGtvvtaphpsraLVFQDPNLFPWRTVLDNVrlg 155
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG-----------VSWNSVTLQTWRKAFGVI--- 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 156 PQ------ARHRSRLD-----ADRVRWAL-DLVGLTPFADALPA-----------TLSGGMAQRAALARALVNRPRVFLL 212
Cdd:TIGR01271 1298 PQkvfifsGTFRKNLDpyeqwSDEEIWKVaEEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSILSKAKILLL 1377
|
170
....*....|.
gi 1199741941 213 DEPLGKLDALT 223
Cdd:TIGR01271 1378 DEPSAHLDPVT 1388
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
77-247 |
3.27e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 52.16 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVdgtvvtapHPSRALVF--QDPNL----------FP 144
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--------PEGEDLLFlpQRPYLplgtlreqliYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 145 WRTVLDnvrLGPQARHRsrldadrvrwaldlvgltpFADALpatlsggmaqraalaralVNRPRVFLLDEPLGKLDAltr 224
Cdd:cd03223 88 WDDVLS---GGEQQRLA-------------------FARLL------------------LHKPKFVFLDEATSALDE--- 124
|
170 180
....*....|....*....|...
gi 1199741941 225 lTMQDELLRLWQAERFTALLVTH 247
Cdd:cd03223 125 -ESEDRLYQLLKELGITVISVGH 146
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
78-123 |
3.52e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 52.63 E-value: 3.52e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPS--EGDVSVDG 123
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILING 70
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
74-264 |
6.46e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.88 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLaqpSEGDVSVDGTVV--------TAPHPSRALVF--QDPNLF 143
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDIHyngipykeFAEKYPGEIIYvsEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 144 PWRTVldnvrlgpqarhRSRLDAdrvrwALDLVGltpfaDALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALT 223
Cdd:cd03233 96 PTLTV------------RETLDF-----ALRCKG-----NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199741941 224 RLTMQDELLRLWQAERFTALL-VTHDVDEALRLADRVVVLSD 264
Cdd:cd03233 154 ALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYE 195
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
158-276 |
7.29e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.20 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 158 ARHRSRLDADRVrwaLDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDElLRLWQA 237
Cdd:NF000106 117 SRKDARARADEL---LERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE-VRSMVR 192
|
90 100 110
....*....|....*....|....*....|....*....
gi 1199741941 238 ERFTALLVTHDVDEALRLADRVVVLsDRpARVLADLTVD 276
Cdd:NF000106 193 DGATVLLTTQYMEEAEQLAHELTVI-DR-GRVIADGKVD 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
78-268 |
2.02e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQL-----VALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHpsraLVFQDPNLfpwrTVLDNV 152
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ----YIKPDYDG----TVEDLL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RLGPQARHRSRLDADRVRwaldLVGLTPFADALPATLSGGmaqraalaralvNRPRV------------FLLDEPLGKLD 220
Cdd:PRK13409 422 RSITDDLGSSYYKSEIIK----PLQLERLLDKNVKDLSGG------------ELQRVaiaaclsrdadlYLLDEPSAHLD 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1199741941 221 ALTRLTMQDELLRLWQAERFTALLVTHDV---DealRLADRVVVLSDRPAR 268
Cdd:PRK13409 486 VEQRLAVAKAIRRIAEEREATALVVDHDIymiD---YISDRLMVFEGEPGK 533
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
87-258 |
2.08e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 49.68 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 87 PGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVdgtvvtaphpsralvfqdpnlfpwrtvldnvrlgpqarhrsrLDA 166
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY------------------------------------------IDG 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 167 DRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDA-----LTRLTMQDELLRLWQAERFT 241
Cdd:smart00382 39 EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEELRLLLLLKSEKNLT 118
|
170
....*....|....*..
gi 1199741941 242 ALLVTHDVDEALRLADR 258
Cdd:smart00382 119 VILTTNDEKDLGPALLR 135
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
76-271 |
2.08e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.43 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVlDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA-PHPSRALV---FQDPNLFPWRTVLDN 151
Cdd:NF033858 281 AV-DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAgDIATRRRVgymSQAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLgpQAR--HRSRLD-ADRVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQ 228
Cdd:NF033858 360 LEL--HARlfHLPAAEiAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFW 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1199741941 229 DELLRLWQAERFTALLVTHDVDEALRlADRV-------VVLSDRPARVLA 271
Cdd:NF033858 438 RLLIELSREDGVTIFISTHFMNEAER-CDRIslmhagrVLASDTPAALVA 486
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
81-284 |
2.14e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 81 VTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRA------LVFQD---PNLFPWRTVLDN 151
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAiragimLCPEDrkaEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 VRLGPQaRHRSRL-----------DADRVRWALDLVglTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLD 220
Cdd:PRK11288 352 INISAR-RHHLRAgclinnrweaeNADRFIRSLNIK--TPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199741941 221 ALTRLTMQDELLRLwqAERFTA-LLVTHDVDEALRLADRVVVLsdRPARVLADLtvdldrPRDHA 284
Cdd:PRK11288 429 VGAKHEIYNVIYEL--AAQGVAvLFVSSDLPEVLGVADRIVVM--REGRIAGEL------AREQA 483
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
77-264 |
2.23e-07 |
|
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: 50.49 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVV-----TAPHPSRALVFQDPNLF--PWRTVL 149
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIstiplEDLRSSLTIIPQDPTLFsgTIRSNL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 150 DNVrlgpqarhrSRLDADRVRWALDLV--GLtpfadalpaTLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTM 227
Cdd:cd03369 103 DPF---------DEYSDEEIYGALRVSegGL---------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199741941 228 QdELLRlwqaERF---TALLVTHdvdealRLA-----DRVVVLSD 264
Cdd:cd03369 165 Q-KTIR----EEFtnsTILTIAH------RLRtiidyDKILVMDA 198
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
77-262 |
2.74e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.34 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGlaqpsegdVSVDGTVVTA--------------PHPSRALV------ 136
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG--------VTKDNWRVTAdrmrfddidllrlsPRERRKLVghnvsm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 137 -FQDPnlfpwRTVLD-NVRLGPQ-----------ARHRSRLDAdRVRWALDL---VGLTPFADAL---PATLSGGMAQRA 197
Cdd:PRK15093 94 iFQEP-----QSCLDpSERVGRQlmqnipgwtykGRWWQRFGW-RKRRAIELlhrVGIKDHKDAMrsfPYELTEGECQKV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199741941 198 ALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
78-268 |
5.96e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQL-----VALVGPSGCGKSTLLRLLAGLAQPSEGdvSVDGTVVTAPHPSRALVFQDpnlfpwRTVLDNV 152
Cdd:COG1245 351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEG--EVDEDLKISYKPQYISPDYD------GTVEEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 153 RlgpqARHRSRLDAdrVRWALDLV---GLTPFADALPATLSGGmaqraalaralvNRPRV------------FLLDEPLG 217
Cdd:COG1245 423 R----SANTDDFGS--SYYKTEIIkplGLEKLLDKNVKDLSGG------------ELQRVaiaaclsrdadlYLLDEPSA 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199741941 218 KLDALTRLTMQDELLRLWQAERFTALLVTHDV---DealRLADRVVVLSDRPAR 268
Cdd:COG1245 485 HLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIyliD---YISDRLMVFEGEPGV 535
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
77-129 |
6.52e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 6.52e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLaglaqpsEGDVSVDGTVVTAP 129
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFP 61
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
76-268 |
7.61e-07 |
|
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: 49.47 E-value: 7.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQpSEGDVSVDGtvvtaphpsraLVFQDPNLFPWRTVLDNVrlg 155
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG-----------VSWNSVPLQKWRKAFGVI--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 156 PQ------ARHRSRLD-----ADRVRWAL-DLVGLTPFADALPA-----------TLSGGMAQRAALARALVNRPRVFLL 212
Cdd:cd03289 83 PQkvfifsGTFRKNLDpygkwSDEEIWKVaEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199741941 213 DEPLGKLDALTRLTMQDELLRLWQAerFTALLVTHDVdEALRLADRVVVLSDRPAR 268
Cdd:cd03289 163 DEPSAHLDPITYQVIRKTLKQAFAD--CTVILSEHRI-EAMLECQRFLVIEENKVR 215
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
77-264 |
8.35e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPsralvfqdpnlfPW---RTVLDNVR 153
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQ------------AWimnATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 LGPQARHRSRLDADRV-RWALDLV----GLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDA-LTRLTM 227
Cdd:PTZ00243 743 FFDEEDAARLADAVRVsQLEADLAqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVGERVV 822
|
170 180 190
....*....|....*....|....*....|....*..
gi 1199741941 228 QDELLRLWQAErfTALLVTHDVdEALRLADRVVVLSD 264
Cdd:PTZ00243 823 EECFLGALAGK--TRVLATHQV-HVVPRADYVVALGD 856
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
78-264 |
1.33e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLaQPS---EGDVSVDGTVVT--APHPSRAL----VFQDPNLFPWRTV 148
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCRfkDIRDSEALgiviIHQELALIPYLSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLGPQARHRSRLDADRV-RWALDL---VGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKL----- 219
Cdd:NF040905 96 AENIFLGNERAKRGVIDWNETnRRARELlakVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALneeds 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199741941 220 DALTrltmqdELLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:NF040905 176 AALL------DLLLELKAQGITSIIISHKLNEIRRVADSITVLRD 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
74-262 |
1.58e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.47 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVV-------------TAPHPSR------A 134
Cdd:PRK10261 28 KIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrsrqvielseqSAAQMRHvrgadmA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 135 LVFQDP--NLFPWRTV----LDNVRLGPQA-RHRSRLDADRVrwaLDLVGLtPFADAL----PATLSGGMAQRAALARAL 203
Cdd:PRK10261 108 MIFQEPmtSLNPVFTVgeqiAESIRLHQGAsREEAMVEAKRM---LDQVRI-PEAQTIlsryPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199741941 204 VNRPRVFLLDEPLGKLDaltrLTMQDELLR----LWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK10261 184 SCRPAVLIADEPTTALD----VTIQAQILQlikvLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
78-124 |
2.08e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.12 E-value: 2.08e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGT 124
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS 86
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
77-248 |
2.35e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRALVFQDPNLFPWRTVldnVRLGP 156
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHL---ARLAP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 157 QARHRSRLDAdrvrwaldLVGLTPFADALP---ATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLR 233
Cdd:PRK10636 404 QELEQKLRDY--------LGGFGFQGDKVTeetRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID 475
|
170
....*....|....*
gi 1199741941 234 LWQAerftALLVTHD 248
Cdd:PRK10636 476 FEGA----LVVVSHD 486
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
91-248 |
2.40e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 91 VALVGPSGCGKSTLLRLLAGLAQPSEGDV----SVDGTVVTAPHPSRALVFQDPNLFPWRTVLDnvrlGPQARHRSRLDA 166
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVfrsaKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPG----VPEQKLRAHLGS 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 167 DRVRWALDLVGLTpfadalpaTLSGGMAQRAALARALVNRPRVFLLDEPLGKLDaLTRLTMQDELLRLWQAerfTALLVT 246
Cdd:PLN03073 614 FGVTGNLALQPMY--------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD-LDAVEALIQGLVLFQG---GVLMVS 681
|
..
gi 1199741941 247 HD 248
Cdd:PLN03073 682 HD 683
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
77-180 |
2.67e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.71 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGlaQPS----EGDVSVDGTVVTAPHPS-RA-----LVFQDPNLFPWR 146
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEeRAhlgifLAFQYPIEIPGV 99
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1199741941 147 TVLDNVRLGPQARHRSR----LDA----DRVRWALDLVGLTP 180
Cdd:CHL00131 100 SNADFLRLAYNSKRKFQglpeLDPleflEIINEKLKLVGMDP 141
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
80-264 |
2.67e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.51 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 80 DVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHP----SRALVF-----QDPNLF-----PW 145
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlARGLVYlpedrQSSGLYldaplAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 146 RTV-LDNVRLG---PQARHRSRLDadRVRWALDLvgltPFADALPA--TLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:PRK15439 361 NVCaLTHNRRGfwiKPARENAVLE--RYRRALNI----KFNHAEQAarTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199741941 220 DALTRLTMQDeLLRLWQAERFTALLVTHDVDEALRLADRVVVLSD 264
Cdd:PRK15439 435 DVSARNDIYQ-LIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQ 478
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
77-262 |
3.68e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 47.98 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSegdvsvdgTVVTA--------------PHPSR-------AL 135
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN--------WHVTAdrfrwngidllklsPRERRkiigreiAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 136 VFQDPNlfpwrTVLD-NVRLGPQ---------------ARHRsrldaDRVRWALDL---VGLTPFAD---ALPATLSGGM 193
Cdd:COG4170 94 IFQEPS-----SCLDpSAKIGDQlieaipswtfkgkwwQRFK-----WRKKRAIELlhrVGIKDHKDimnSYPHELTEGE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199741941 194 AQRAALARALVNRPRVFLLDEPLGKLDALTRLTMQDELLRLWQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:COG4170 164 CQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
83-267 |
4.61e-06 |
|
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: 46.98 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 83 LDIP-PGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDvsvdgtvvtaphpsralvFQDPNlfPWRTVLDNVR-------- 153
Cdd:cd03236 20 LPVPrEGQVLGLVGPNGIGKSTALKILAGKLKPNLGK------------------FDDPP--DWDEILDEFRgselqnyf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 154 -----------LGPQ----------ARHRSRLDADRVRWALDLV----GLTPFADALPATLSGGMAQRAALARALVNRPR 208
Cdd:cd03236 80 tkllegdvkviVKPQyvdlipkavkGKVGELLKKKDERGKLDELvdqlELRHVLDRNIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199741941 209 VFLLDEPLGKLDALTRLTMQDELLRLWQAERFTaLLVTHDVDEALRLADRVVVLSDRPA 267
Cdd:cd03236 160 FYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV-LVVEHDLAVLDYLSDYIHCLYGEPG 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
78-273 |
5.06e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.90 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGlAQPS--EGDVSVDGTVVTAPHPSRA------LVFQD---PNLFPWR 146
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGkfEGNVFINGKPVDIRNPAQAiragiaMVPEDrkrHGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 147 TVLDNVRLGPQARH--RSRLDA----DRVRWALDLVGLTPFADALP-ATLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:TIGR02633 355 GVGKNITLSVLKSFcfKMRIDAaaelQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199741941 220 DALTRLTMQdELLRLWQAERFTALLVTHDVDEALRLADRVVVLSDrpARVLADL 273
Cdd:TIGR02633 435 DVGAKYEIY-KLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGE--GKLKGDF 485
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
73-158 |
6.20e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.40 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPH----PSR-ALVFQDPNLFPwRT 147
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldswRSRlAVVSQTPFLFS-DT 404
|
90
....*....|..
gi 1199741941 148 VLDNVRLG-PQA 158
Cdd:PRK10789 405 VANNIALGrPDA 416
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
78-262 |
9.12e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.92 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTAPHPSRAL------VFQD---PNLFPWRTV 148
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLangivyISEDrkrDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 149 LDNVRLgPQARHRS----RLDADRVRWAL-DLVGL----TPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:PRK10762 348 KENMSL-TALRYFSraggSLKHADEQQAVsDFIRLfnikTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199741941 220 DaltrLTMQDELLRL---WQAERFTALLVTHDVDEALRLADRVVVL 262
Cdd:PRK10762 427 D----VGAKKEIYQLinqFKAEGLSIILVSSEMPEVLGMSDRILVM 468
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
77-264 |
1.28e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 45.67 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA-P-HPSR---ALVFQDPNLFPWRTVLDn 151
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlPlHTLRsrlSIILQDPILFSGSIRFN- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 vrLGPQArhrsRLDADRVRWALDLVGLTPFADALPATL-----------SGGMAQRAALARALVNRPRVFLLDEPLGKLD 220
Cdd:cd03288 115 --LDPEC----KCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASID 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1199741941 221 ALTRLTMQDELLRLWqAERfTALLVTHDVDEALRlADRVVVLSD 264
Cdd:cd03288 189 MATENILQKVVMTAF-ADR-TVVTIAHRVSTILD-ADLVLVLSR 229
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
78-125 |
1.91e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.19 E-value: 1.91e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTV 125
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV 87
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
74-223 |
2.44e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQP---SEGDVSVDGTVVTAPHPSRALVFQDPNL-FPWRTVL 149
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQRSIGYVQQQDLhLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 150 DNVRLGP---QARHRSRLDADR-VRWALDLVGLTPFADALPATLSGGMAQRAALARA----LVNRPRVFL-LDEPLGKLD 220
Cdd:TIGR00956 855 ESLRFSAylrQPKSVSKSEKMEyVEEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTigveLVAKPKLLLfLDEPTSGLD 934
|
...
gi 1199741941 221 ALT 223
Cdd:TIGR00956 935 SQT 937
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
77-119 |
3.73e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.88 E-value: 3.73e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDV 119
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
76-262 |
4.25e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.72 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVlDDVTLDIPPGQLVALVGPSGCGKS-TLLRLLAGLAQPS--EGDVSVDGT-VVTAPHPS----RA----LVFQDP--N 141
Cdd:PRK09473 31 AV-NDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFNGReILNLPEKElnklRAeqisMIFQDPmtS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 142 LFPWRTV--------------------------LDNVRLgPQARHRSRLdadrvrwaldlvgltpfadaLPATLSGGMAQ 195
Cdd:PRK09473 110 LNPYMRVgeqlmevlmlhkgmskaeafeesvrmLDAVKM-PEARKRMKM--------------------YPHEFSGGMRQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199741941 196 RAALARALVNRPRVFLLDEPLGKLDALTR---LTMQDELLRlwqaERFTA-LLVTHDVDEALRLADRVVVL 262
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQaqiMTLLNELKR----EFNTAiIMITHDLGVVAGICDKVLVM 235
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
74-224 |
4.40e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.71 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 74 ELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSV-DGTVVTAPHPSRALVFQDPNLFPWRTVLDNV 152
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYkNCNINNIAKPYCTYIGHNLGLKLEMTVFENL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199741941 153 RLGPQARHRSRLdadrVRWALDLVGLTPFADALPATLSGGMAQRAALARALVNRPRVFLLDEPLGKLDALTR 224
Cdd:PRK13541 92 KFWSEIYNSAET----LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
93-155 |
7.93e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 7.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199741941 93 LVGPSGCGKSTLLRLLAGLAQPSEGDVSVDgtvvtaPHPSRALVFQDPNLFPWRTVLDNVRLG 155
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD------PNERLGKLRQDQFAFEEFTVLDTVIMG 88
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
73-123 |
1.03e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.07 E-value: 1.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPS--EGDVSVDG 123
Cdd:PLN03140 891 DRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISG 943
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
76-165 |
1.25e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.86 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 76 AVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLA--QPSEGDVSVDGTVVTAPHPS-RA-----LVFQDP------- 140
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEdRAgegifMAFQYPveipgvs 94
|
90 100
....*....|....*....|....*
gi 1199741941 141 NLFPWRTVLDNVRlgpQARHRSRLD 165
Cdd:PRK09580 95 NQFFLQTALNAVR---SYRGQEPLD 116
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
77-271 |
1.73e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTA---PHPSRAL--VFQDPNLFPwRTVLDN 151
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfglTDLRRVLsiIPQSPVLFS-GTVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 152 vrLGPQARHRsrlDADrvRW-AL------DLVGLTPFA-DALPA----TLSGGMAQRAALARALVNRPRVFLLDEPLGKL 219
Cdd:PLN03232 1330 --IDPFSEHN---DAD--LWeALerahikDVIDRNPFGlDAEVSeggeNFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199741941 220 DALTrltmqDELLRLWQAERF---TALLVTH------DVDEALRLADRVVVLSDRPARVLA 271
Cdd:PLN03232 1403 DVRT-----DSLIQRTIREEFkscTMLVIAHrlntiiDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
73-123 |
1.80e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.30 E-value: 1.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1199741941 73 TELAVLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPS---EGDVSVDG 123
Cdd:PLN03140 176 TKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNG 229
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
78-113 |
2.35e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 2.35e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLR--LLAGLAQ 113
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtLYPALAN 661
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
77-111 |
2.73e-04 |
|
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: 42.43 E-value: 2.73e-04
10 20 30
....*....|....*....|....*....|....*
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGL 111
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL 501
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
84-108 |
3.58e-04 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 42.42 E-value: 3.58e-04
10 20
....*....|....*....|....*
gi 1199741941 84 DIPPGQLVALVGPSGCGKSTLLRLL 108
Cdd:COG5192 65 DLPPPFIVAVVGPPGTGKSTLIRSL 89
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
78-113 |
7.97e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 7.97e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLR--LLAGLAQ 113
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNdiLYPALAR 658
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
78-113 |
1.02e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.91 E-value: 1.02e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLR--LLAGLAQ 113
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtLYPALAR 48
|
|
| BMS1 |
cd01882 |
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ... |
80-108 |
1.04e-03 |
|
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subumit. The C-terminal domain of Bms1 contains a GTPase-activating protein (GAP) that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes.
Pssm-ID: 206669 [Multi-domain] Cd Length: 231 Bit Score: 39.63 E-value: 1.04e-03
10 20
....*....|....*....|....*....
gi 1199741941 80 DVTLDIPPGQLVALVGPSGCGKSTLLRLL 108
Cdd:cd01882 31 DRTPEEPPPLVVVVVGPPGVGKSTLIRSL 59
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
78-113 |
1.10e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 1.10e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTLLR--LLAGLAQ 113
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINetLYKALAR 662
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
88-120 |
1.14e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.06 E-value: 1.14e-03
10 20 30
....*....|....*....|....*....|...
gi 1199741941 88 GQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVS 120
Cdd:pfam03193 106 GKTTVLAGQSGVGKSTLLNALLPELDLRTGEIS 138
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
88-120 |
1.58e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.92 E-value: 1.58e-03
10 20 30
....*....|....*....|....*....|...
gi 1199741941 88 GQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVS 120
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPELVLATGEIS 117
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
78-104 |
1.64e-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: 40.00 E-value: 1.64e-03
10 20
....*....|....*....|....*..
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTL 104
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
83-124 |
2.68e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.41 E-value: 2.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1199741941 83 LDIP-PGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGT 124
Cdd:PRK13409 93 LPIPkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPS 135
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
83-124 |
2.68e-03 |
|
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: 39.38 E-value: 2.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1199741941 83 LDIP-PGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGT 124
Cdd:COG1245 93 LPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPS 135
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-268 |
3.57e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.24 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 134 ALVFQDPNLFPwRTVLDNVRLGpqarhrsRLDADR--VRWALDLVGLTPFADALP-----------ATLSGGMAQRAALA 200
Cdd:PTZ00265 1299 SIVSQEPMLFN-MSIYENIKFG-------KEDATRedVKRACKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIA 1370
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199741941 201 RALVNRPRVFLLDEPLGKLDALTRLTMQDELLRLWQAERFTALLVTHDVdEALRLADRVVVLSDrPAR 268
Cdd:PTZ00265 1371 RALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFNN-PDR 1436
|
|
| gmk |
PRK00300 |
guanylate kinase; Provisional |
87-121 |
4.11e-03 |
|
guanylate kinase; Provisional
Pssm-ID: 234719 Cd Length: 205 Bit Score: 37.76 E-value: 4.11e-03
10 20 30
....*....|....*....|....*....|....*
gi 1199741941 87 PGQLVALVGPSGCGKSTLLRLLagLAQPSEGDVSV 121
Cdd:PRK00300 4 RGLLIVLSGPSGAGKSTLVKAL--LERDPNLQLSV 36
|
|
| endolysin_R21-like |
cd16900 |
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ... |
76-110 |
4.66e-03 |
|
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
Pssm-ID: 381619 [Multi-domain] Cd Length: 142 Bit Score: 36.77 E-value: 4.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1199741941 76 AVLDDVTLDIPPGQLVAL------VGPSGCGKSTLLRLL-AG 110
Cdd:cd16900 66 AVDRCVKVPLPDPQRAALasfaynVGVGAFCRSTLLRKLnAG 107
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
79-105 |
5.76e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.50 E-value: 5.76e-03
10 20
....*....|....*....|....*..
gi 1199741941 79 DDVTLDIPPGQLVALVGPSGCGKSTLL 105
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
77-247 |
6.25e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.07 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLlaglaqpsegdvsvdgtvVTAPHP---SRALVfqdpnLFP--------- 144
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSL------------------ITGDHPqgySNDLT-----LFGrrrgsgeti 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 145 W-----------------------RTVL-----DNVRLGPQARHRSRLDADRvrWaLDLVGL-TPFADALPATLSGGMAQ 195
Cdd:PRK10938 332 WdikkhigyvssslhldyrvstsvRNVIlsgffDSIGIYQAVSDRQQKLAQQ--W-LDILGIdKRTADAPFHSLSWGQQR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1199741941 196 RAALARALVNRPRVFLLDEPLGKLDALTRLtmqdeLLRlwqaeRFTALLVTH 247
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQ-----LVR-----RFVDVLISE 450
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
78-104 |
6.26e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 37.24 E-value: 6.26e-03
10 20
....*....|....*....|....*..
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTL 104
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL 37
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
77-178 |
6.33e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.22 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199741941 77 VLDDVTLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDVSVDGTVVTApHPSRAL------VFQDPNLFPwRTVLD 150
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGA-YGLRELrrqfsmIPQDPVLFD-GTVRQ 1402
|
90 100
....*....|....*....|....*...
gi 1199741941 151 NVRLGPQArhrsrlDADRVRWALDLVGL 178
Cdd:PTZ00243 1403 NVDPFLEA------SSAEVWAALELVGL 1424
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
83-113 |
6.62e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.99 E-value: 6.62e-03
10 20 30
....*....|....*....|....*....|....
gi 1199741941 83 LDIPPGQLVALVGPSGCGKSTL---LRLLAGLAQ 113
Cdd:COG4637 16 LELPLGPLTVLIGANGSGKSNLldaLRFLSDAAR 49
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
82-119 |
8.13e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 36.36 E-value: 8.13e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1199741941 82 TLDIPPGQLVALVGPSGCGKSTLLRLLAGLAQPSEGDV 119
Cdd:cd00009 13 ALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPF 50
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
78-104 |
8.72e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 8.72e-03
10 20
....*....|....*....|....*..
gi 1199741941 78 LDDVTLDIPPGQLVALVGPSGCGKSTL 104
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| |
