|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
20-271 |
1.46e-156 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 436.06 E-value: 1.46e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 20 TFSQPKLEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSD 99
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 100 RGMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLL 179
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 180 MDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMIANPGRIKDEFKIELPPERDLEIKMSEDF 259
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDRELRTSPEF 241
|
250
....*....|..
gi 2225592549 260 WQIKRQILKSLQ 271
Cdd:COG1116 242 AALRAEILDLLR 253
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
26-245 |
8.90e-136 |
|
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: 381.82 E-value: 8.90e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDRGMVFQ 105
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 106 NYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFG 185
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 186 ALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMIANPGRIKDEFKIEL 245
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-270 |
1.92e-113 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 326.82 E-value: 1.92e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 24 PKLEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDRGMV 103
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 104 FQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEP 183
Cdd:COG4525 82 FQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 184 FGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMIANPGRIKDEFkiELP---------PERdlEIK 254
Cdd:COG4525 162 FGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERL--ELDfsrrflageDAR--AIK 237
|
250
....*....|....*.
gi 2225592549 255 MSEDFWQIKRQILKSL 270
Cdd:COG4525 238 SDPAFIALREELLDII 253
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
22-237 |
3.58e-100 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 296.62 E-value: 3.58e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFphlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE-PGSDR 100
Cdd:COG3842 2 AMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 --GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVL 178
Cdd:COG3842 78 nvGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2225592549 179 LMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVM--NDGRI 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
26-237 |
6.76e-91 |
|
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: 267.85 E-value: 6.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI-EEPGSDR--GM 102
Cdd:cd03259 1 LELKGLSKTYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVtGVPPERRniGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 103 VFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDE 182
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2225592549 183 PFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVM--NEGRI 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
26-237 |
2.72e-90 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 271.25 E-value: 2.72e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPhlktNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEV--IEEPGSDR--G 101
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlfTNLPPRERrvG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 102 MVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMD 181
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2225592549 182 EPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVM--NQGRI 212
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
25-252 |
6.36e-89 |
|
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: 264.30 E-value: 6.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 25 KLEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDRGMVF 104
Cdd:NF040729 1 KLKIQNISKTFINNKKENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGPDRGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 105 QNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPF 184
Cdd:NF040729 81 QNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEPL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2225592549 185 GALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMIANPGRIKDEFKIELPPERDLE 252
Cdd:NF040729 161 GAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRDKGKILEDLKIDLPRPRNRE 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
45-270 |
1.43e-85 |
|
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: 255.08 E-value: 1.43e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDRGMVFQNYTLFPWLTVADNVAFGLK 124
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 125 --LRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLEL 202
Cdd:TIGR01184 81 rvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 203 WEQTHITVLMITHDVEEAVFLSGRVYVMIANPG-RIKDEFKIELPPERD-LEIKMSEDFWQIKRQILKSL 270
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAaNIGQILEVPFPRPRDrLEVVEDPSYYDLRNEALYFL 230
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
23-240 |
1.14e-81 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 244.95 E-value: 1.14e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 23 QPKLEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR-- 100
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 -------GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALAN 173
Cdd:COG1136 82 rlrrrhiGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2225592549 174 HPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDvEEAVFLSGRVYVMIAnpGRIKDE 240
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRD--GRIVSD 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
26-237 |
4.29e-81 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 244.61 E-value: 4.29e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPhlktNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDRGMVFQ 105
Cdd:PRK11248 2 LQISHLYADYG----GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 106 NYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFG 185
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2225592549 186 ALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMIANPGRI 237
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRV 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
26-237 |
6.02e-81 |
|
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: 243.30 E-value: 6.02e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG-EVIEEPGSDR--GM 102
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkDITNLPPHKRpvNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 103 VFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDE 182
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2225592549 183 PFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVM--NKGKI 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
28-237 |
6.91e-81 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 247.29 E-value: 6.91e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 28 VEKVFKHFPHLKtnlsvleDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI-EEPGSDRG--MVF 104
Cdd:COG3839 9 VSKSYGGVEALK-------DIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtDLPPKDRNiaMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 105 QNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPF 184
Cdd:COG3839 82 QSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 185 GALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:COG3839 162 SNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVM--NDGRI 212
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
26-230 |
3.08e-78 |
|
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: 235.85 E-value: 3.08e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR----- 100
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ----GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPE 176
Cdd:cd03255 81 rrhiGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2225592549 177 VLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDvEEAVFLSGRVYVM 230
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIEL 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
22-237 |
1.74e-77 |
|
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: 238.78 E-value: 1.74e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFphlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI--EEPGS- 98
Cdd:TIGR03265 1 SSPYLSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDItrLPPQKr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 99 DRGMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVL 178
Cdd:TIGR03265 77 DYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2225592549 179 LMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:TIGR03265 157 LLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVM--NHGVI 213
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
24-230 |
2.26e-73 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 229.22 E-value: 2.26e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 24 PKLEVE---KVF-----KHFPHLKTNLS---VLE---------DINIQVYPNE-FVsIVGASGCGKSTLLNIIAGLIPPS 82
Cdd:COG4175 2 PKIEVRnlyKIFgkrpeRALKLLDQGKSkdeILEktgqtvgvnDASFDVEEGEiFV-IMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 83 AGQVLMNGEVIEEPGSDR---------GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAY 153
Cdd:COG4175 81 AGEVLIDGEDITKLSKKElrelrrkkmSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2225592549 154 PKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:COG4175 161 PDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIM 237
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
26-237 |
2.84e-73 |
|
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: 224.14 E-value: 2.84e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPhlktNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGE-VIEEPGSDR--GM 102
Cdd:cd03296 3 IEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdATDVPVQERnvGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 103 VFQNYTLFPWLTVADNVAFGLKLR----GLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVL 178
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVKprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2225592549 179 LMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVM--NKGRI 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
22-237 |
8.38e-72 |
|
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: 229.02 E-value: 8.38e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLKTN-LSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR 100
Cdd:COG1123 257 AEPLLEVRNLSKRYPVRGKGgVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 --------GMVFQN-YT-LFPWLTVADNVAFGLKLRGLSSG-EIKEQVFYYLSIVGL-TQFAKAYPKQLSGGMKQRVAIA 168
Cdd:COG1123 337 lrelrrrvQMVFQDpYSsLNPRMTVGDIIAEPLRLHGLLSRaERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2225592549 169 RALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVM--YDGRI 483
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
44-237 |
8.03e-70 |
|
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: 214.89 E-value: 8.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR-----GMVFQN--YTLF-PwlTV 115
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrrkvGLVFQNpdDQLFaP--TV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 116 ADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQM 195
Cdd:COG1122 94 EEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRREL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2225592549 196 QQFFLELwEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:COG1122 174 LELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVL--DDGRI 212
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
27-237 |
2.15e-69 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 216.50 E-value: 2.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 27 EVEKVFKHFPHLKTnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGE-VIEEPGSD--RGM- 102
Cdd:COG1125 3 EFENVTKRYPDGTV---AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEdIRDLDPVElrRRIg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 103 -VFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGL--TQFAKAYPKQLSGGMKQRVAIARALANHPEVLL 179
Cdd:COG1125 80 yVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2225592549 180 MDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:COG1125 160 MDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM--REGRI 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
22-237 |
7.30e-69 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 212.92 E-value: 7.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFphlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR- 100
Cdd:COG1127 2 SEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 -------GMVFQNYTLFPWLTVADNVAFGLK-LRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALA 172
Cdd:COG1127 78 yelrrriGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2225592549 173 NHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYvMIANpGRI 237
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVA-VLAD-GKI 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
39-237 |
1.10e-68 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 213.27 E-value: 1.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 39 KTNLSV-LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG---------EVIEEPGSDRGMVFQNYT 108
Cdd:cd03294 33 KTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkELRELRRKKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 109 LFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALD 188
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2225592549 189 AQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:cd03294 193 PLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIM--KDGRL 239
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
26-237 |
2.33e-68 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 211.58 E-value: 2.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFphlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG-EVIEEPGSDR--GM 102
Cdd:TIGR00968 1 IEIANISKRF----GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGqDATRVHARDRkiGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 103 VFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDE 182
Cdd:TIGR00968 77 VFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2225592549 183 PFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:TIGR00968 157 PFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVM--SNGKI 209
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
26-237 |
4.37e-68 |
|
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: 209.80 E-value: 4.37e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPhlktNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE-PGSDR--GM 102
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlPPKDRdiAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 103 VFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDE 182
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2225592549 183 PFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM--NDGQI 209
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
60-237 |
4.54e-68 |
|
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: 213.89 E-value: 4.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 60 IVGASGCGKSTLLNIIAGLIPPSAGQVLMNGE-VIEEPGSDR--GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQ 136
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEdVTNVPPHLRhiNMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 137 VFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHD 216
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180
....*....|....*....|.
gi 2225592549 217 VEEAVFLSGRVYVMiaNPGRI 237
Cdd:TIGR01187 161 QEEAMTMSDRIAIM--RKGKI 179
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
23-237 |
4.83e-68 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 215.20 E-value: 4.83e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 23 QPKLEVEKVFKHFPHlKTnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE-PGSDRG 101
Cdd:PRK09452 12 SPLVELRGISKSFDG-KE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 102 M--VFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLL 179
Cdd:PRK09452 88 VntVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2225592549 180 MDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRI 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
26-249 |
1.63e-66 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 207.61 E-value: 1.63e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHlKTnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDRGMVFQ 105
Cdd:PRK11247 13 LLLNAVSKRYGE-RT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 106 NYTLFPWLTVADNVAFGLKlrglssGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFG 185
Cdd:PRK11247 89 DARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2225592549 186 ALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVyVMIANpGRIKDEFKIELPPER 249
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRV-LLIEE-GKIGLDLTVDLPRPR 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
26-218 |
3.11e-65 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 202.98 E-value: 3.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPhlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG-EVIEEPGSDR---- 100
Cdd:COG2884 2 IRFENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqDLSRLKRREIpylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ---GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEV 177
Cdd:COG2884 79 rriGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2225592549 178 LLMDEPFGALDAQTREQMQQFFLELwEQTHITVLMITHDVE 218
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLE 198
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
26-244 |
9.19e-65 |
|
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: 202.04 E-value: 9.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG-EVIEEPGSDR---- 100
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtDLTLLSGKELrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ---GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEV 177
Cdd:cd03258 82 rriGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2225592549 178 LLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMIAnpGRIKDEFKIE 244
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK--GEVVEEGTVE 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
27-230 |
3.22e-64 |
|
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: 200.00 E-value: 3.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 27 EVEKVFKHFPHLKTNlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR-----G 101
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrrkvG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 102 MVFQN--YTLFPwLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLL 179
Cdd:cd03225 79 LVFQNpdDQFFG-PTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2225592549 180 MDEPFGALDAQTREQMQQFFLELWEQtHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
26-230 |
3.88e-64 |
|
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: 198.57 E-value: 3.88e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR----- 100
Cdd:cd03229 1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 --GMVFQNYTLFPWLTVADNVAFGLklrglssgeikeqvfyylsivgltqfakaypkqlSGGMKQRVAIARALANHPEVL 178
Cdd:cd03229 77 riGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2225592549 179 LMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVL 174
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
26-237 |
8.28e-64 |
|
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: 199.65 E-value: 8.28e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR----- 100
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ---GMVFQNY--TLFPWLTVADNVAFGLKLRGLSSGE--IKEQVFYYLSIVGL-TQFAKAYPKQLSGGMKQRVAIARALA 172
Cdd:cd03257 82 keiQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKeaRKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2225592549 173 NHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMIAnpGRI 237
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYA--GKI 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
26-237 |
2.19e-63 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 199.06 E-value: 2.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE--PGSDR--- 100
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqdPVELRrki 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGL--TQFAKAYPKQLSGGMKQRVAIARALANHPEVL 178
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2225592549 179 LMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIM--KNGEI 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
26-237 |
4.10e-63 |
|
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: 198.11 E-value: 4.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR----- 100
Cdd:cd03261 1 IELRGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ---GMVFQNYTLFPWLTVADNVAFGLKLRG-LSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPE 176
Cdd:cd03261 77 rrmGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2225592549 177 VLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYvMIANpGRI 237
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIA-VLYD-GKI 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
26-237 |
7.62e-63 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 197.21 E-value: 7.62e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGE-VIEEPGSDR---G 101
Cdd:COG1131 1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdVARDPAEVRrriG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 102 MVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMD 181
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2225592549 182 EPFGALDAQTREQMQQFFLELWEQTHiTVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGK-TVLLSTHYLEEAERLCDRVAII--DKGRI 209
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
26-218 |
8.17e-63 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 200.69 E-value: 8.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE-PGSDR---- 100
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ---GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEV 177
Cdd:COG1135 82 rkiGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2225592549 178 LLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVE 218
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMD 202
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
26-242 |
1.28e-62 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 200.30 E-value: 1.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsvLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGE-VIEEPGSDRGM-- 102
Cdd:NF040840 2 IRIENLSKDWKEFK-----LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKdITNLPPEKRGIay 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 103 VFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDE 182
Cdd:NF040840 77 VYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2225592549 183 PFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM----IANPGRIKDEFK 242
Cdd:NF040840 157 PLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMlngrLSQVGDVREVFR 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
24-230 |
1.89e-62 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 200.83 E-value: 1.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 24 PKLEVEKVFKHFphlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE-PGSDR-- 100
Cdd:PRK11607 18 PLLEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvPPYQRpi 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLM 180
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2225592549 181 DEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIM 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
26-237 |
2.21e-62 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 199.92 E-value: 2.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG-EVIEEPGSDR--GM 102
Cdd:PRK10851 3 IEIANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtDVSRLHARDRkvGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 103 VFQNYTLFPWLTVADNVAFGLKL----RGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVL 178
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2225592549 179 LMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVM--SQGNI 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
54-230 |
2.38e-61 |
|
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: 192.90 E-value: 2.38e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 54 PNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEV-------IEEPGSDR--GMVFQNYTLFPWLTVADNVAFGLK 124
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkINLPPQQRkiGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 125 lrGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWE 204
Cdd:cd03297 102 --RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180
....*....|....*....|....*.
gi 2225592549 205 QTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
26-248 |
1.74e-60 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 191.12 E-value: 1.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTNlsvledINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGE-VIEEPGSDRG--M 102
Cdd:COG3840 2 LRLDDLTYRYGDFPLR------FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdLTALPPAERPvsM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 103 VFQNYTLFPWLTVADNVAFGL--KLRgLSSGEiKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLM 180
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLGLrpGLK-LTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2225592549 181 DEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYV----MIANPGRIKDEFKIELPPE 248
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLvadgRIAADGPTAALLDGEPPPA 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
26-188 |
2.81e-60 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 190.98 E-value: 2.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR----- 100
Cdd:COG1126 2 IEIENLHKSFGDLE----VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInklrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 --GMVFQNYTLFPWLTVADNVAFGL-KLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEV 177
Cdd:COG1126 78 kvGMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170
....*....|.
gi 2225592549 178 LLMDEPFGALD 188
Cdd:COG1126 158 MLFDEPTSALD 168
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
23-237 |
7.88e-60 |
|
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: 197.82 E-value: 7.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 23 QPKLEVEKVFKHFPHLKTNlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSA---GQVLMNGEVI-----E 94
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLlelseA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 95 EPGSDRGMVFQNYT--LFPwLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALA 172
Cdd:COG1123 80 LRGRRIGMVFQDPMtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2225592549 173 NHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM--DDGRI 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
26-244 |
1.93e-59 |
|
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: 188.86 E-value: 1.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR----- 100
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 GMVFQNYT--LFPWLTVADNVAFGLKLRGLssGEIKEQVFYYLSIVGLT-QFAKAYPKQLSGGMKQRVAIARALANHPEV 177
Cdd:COG1124 82 QMVFQDPYasLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2225592549 178 LLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMIAnpGRIKDEFKIE 244
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN--GRIVEELTVA 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
26-237 |
7.13e-58 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 183.88 E-value: 7.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSD----R- 100
Cdd:cd03262 1 IEIKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 --GMVFQNYTLFPWLTVADNVAFGL-KLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEV 177
Cdd:cd03262 77 kvGMVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 178 LLMDEPFGALDAQTREQMQQFFLELwEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFM--DDGRI 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
26-240 |
7.96e-58 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 185.71 E-value: 7.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTNlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG------EVIEEPGSD 99
Cdd:TIGR04520 1 IEVENVSFSYPESEKP--ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtldeENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 100 RGMVFQNytlfP-----WLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANH 174
Cdd:TIGR04520 79 VGMVFQN----PdnqfvGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2225592549 175 PEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVfLSGRVYVMiaNPGRIKDE 240
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVM--NKGKIVAE 217
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
39-230 |
2.15e-57 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 187.37 E-value: 2.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 39 KTNLSV-LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR---------GMVFQNYT 108
Cdd:TIGR01186 2 KTGGKKgVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevrrkkiGMVFQQFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 109 LFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALD 188
Cdd:TIGR01186 82 LFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2225592549 189 AQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:TIGR01186 162 PLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIM 203
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
33-237 |
1.26e-56 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 184.92 E-value: 1.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 33 KHFPHLKT------NLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPG---SDRGMV 103
Cdd:PRK11432 4 KNFVVLKNitkrfgSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqqRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 104 FQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEP 183
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2225592549 184 FGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVM--NKGKI 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
22-237 |
2.50e-56 |
|
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: 180.71 E-value: 2.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI----EEP- 96
Cdd:COG4181 5 SAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldEDAr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 97 ----GSDRGMVFQNYTLFPWLTVADNVAFGLKLRGLssGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALA 172
Cdd:COG4181 85 arlrARHVGFVFQSFQLLPTLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2225592549 173 NHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVfLSGRVYVMIAnpGRI 237
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRA--GRL 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
26-237 |
3.30e-56 |
|
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: 182.95 E-value: 3.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPP---SAGQVLMNGEVI-----EEP- 96
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklseKELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 97 ---GSDRGMVFQN-YT-LFPWLTVADNVAFGLKL-RGLSSGEIKEQVFYYLSIVGLT---QFAKAYPKQLSGGMKQRVAI 167
Cdd:COG0444 82 kirGREIQMIFQDpMTsLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 168 ARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMIAnpGRI 237
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYA--GRI 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
41-237 |
4.83e-56 |
|
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: 179.68 E-value: 4.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 41 NLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIP-----PSAGQVLMNGEVIEEPGSDR-------GMVFQNYT 108
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVlelrrrvGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 109 LFPwLTVADNVAFGLKLRGLSSG-EIKEQVFYYLSIVGLTQFAK--AYPKQLSGGMKQRVAIARALANHPEVLLMDEPFG 185
Cdd:cd03260 92 PFP-GSIYDNVAYGLRLHGIKLKeELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2225592549 186 ALDAQTREQMQQFFLELWEQthITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:cd03260 171 ALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFL--LNGRL 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
44-237 |
5.70e-56 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 183.51 E-value: 5.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI--EEPgSDRG--MVFQNYTLFPWLTVADNV 119
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVneLEP-ADRDiaMVFQNYALYPHMSVRENM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 120 AFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFF 199
Cdd:PRK11650 98 AYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEI 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 2225592549 200 LELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:PRK11650 178 QRLHRRLKTTSLYVTHDQVEAMTLADRVVVM--NGGVA 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
27-218 |
2.04e-54 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 179.23 E-value: 2.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 27 EVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR------ 100
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 --GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVL 178
Cdd:PRK11153 83 qiGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2225592549 179 LMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVE 218
Cdd:PRK11153 163 LCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMD 202
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
26-218 |
2.12e-54 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 175.13 E-value: 2.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPhlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE-PGSD----R 100
Cdd:TIGR02673 2 IEFHNVSKAYP---GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlRGRQlpllR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ---GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEV 177
Cdd:TIGR02673 79 rriGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2225592549 178 LLMDEPFGALDAQTREQMQQFFLELwEQTHITVLMITHDVE 218
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILDLLKRL-NKRGTTVIVATHDLS 198
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
44-242 |
5.08e-54 |
|
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: 174.83 E-value: 5.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR---GMVFQNYTLFPWLTVADNVA 120
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKrdiSYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 121 FGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFL 200
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2225592549 201 ELWEQTHITVLMITHDVEEAVFLSGRVYVM----IANPGRIKDEFK 242
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVAIMlngkLIQVGKPEEVFK 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
26-220 |
5.49e-54 |
|
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: 174.68 E-value: 5.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPG-------- 97
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkalrqlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 98 SDRGMVFQNYTLFPWLTVADNVAFGL--------KLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIAR 169
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2225592549 170 ALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEA 220
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLA 208
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
24-220 |
6.93e-53 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 172.16 E-value: 6.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 24 PKLEVEKVFKHFPhlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG-EVIEEPGSDR-- 100
Cdd:COG3638 1 PMLELRNLSKRYP---GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGqDVTALRGRALrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 -----GMVFQNYTLFPWLTVADNVAFGL--------KLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAI 167
Cdd:COG3638 78 lrrriGMIFQQFNLVPRLSVLTNVLAGRlgrtstwrSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 168 ARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEA 220
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLA 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
44-237 |
1.32e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.38 E-value: 1.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE-PGSD-R---GMVFQNYTLFPwLTVADN 118
Cdd:COG4619 15 ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEwRrqvAYVPQEPALWG-GTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFGLKLRGLSSGEikEQVFYYLSIVGLTQFAKAYP-KQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQ 197
Cdd:COG4619 94 LPFPFQLRERKFDR--ERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2225592549 198 FFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:COG4619 172 LLREYLAEEGRAVLWVSHDPEQIERVADRVLTL--EAGRL 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
22-230 |
2.96e-52 |
|
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: 170.99 E-value: 2.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR- 100
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLV----AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ---GMV--FQNYTLFPWLTVADNVA---------------FGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGG 160
Cdd:COG0411 77 arlGIArtFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2225592549 161 MKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVeEAVF-LSGRVYVM 230
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDM-DLVMgLADRIVVL 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
45-236 |
4.51e-52 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 168.81 E-value: 4.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPP---SAGQVLMNGEVIEE-PGSDR--GMVFQNYTLFPWLTVADN 118
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAlPAEQRriGILFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFGLKlRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQF 198
Cdd:COG4136 97 LAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREF 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 2225592549 199 FLELWEQTHITVLMITHDVEEAVfLSGRVyVMIANPGR 236
Cdd:COG4136 176 VFEQIRQRGIPALLVTHDEEDAP-AAGRV-LDLGNWQH 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
44-237 |
5.28e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 169.88 E-value: 5.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDRGMVFQNYTL---FPwLTVADNVA 120
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAEVdwdFP-ITVRDVVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 121 FGL----KLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQ 196
Cdd:COG1121 100 MGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALY 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2225592549 197 QFFLELWEQtHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:COG1121 180 ELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL--NRGLV 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
47-238 |
8.69e-52 |
|
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: 172.59 E-value: 8.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 47 DINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI--EEPGSDR-------GMVFQNYTLFPWLTVAD 117
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLpphrrriGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFGLKLRGLSSGEIK-EQVfyyLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQ 196
Cdd:COG4148 97 NLLYGRKRAPRAERRISfDEV---VELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2225592549 197 QFFLELWEQTHITVLMITHDVEEAVFLSGRVyVMIANpGRIK 238
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSLDEVARLADHV-VLLEQ-GRVV 213
|
|
| ABC_choXWV_ATP |
TIGR03415 |
choline ABC transporter, ATP-binding protein; Members of this protein family are the ... |
46-237 |
1.09e-51 |
|
choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 188317 [Multi-domain] Cd Length: 382 Bit Score: 173.04 E-value: 1.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 46 EDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLM---NGEV----IEEPGSDR------GMVFQNYTLFPW 112
Cdd:TIGR03415 41 HNASLDIEEGEICVLMGLSGSGKSTLLRAVNGLNPVSRGSVLVkdgDGSVdvanCDAATLRRlrthrvSMVFQQFALLPW 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 113 LTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTR 192
Cdd:TIGR03415 121 RTVEENVAFGLEMQGMPKAERRKRVDEQLELVGLAQWADRKPGELSGGMQQRVGLARAFATEAPILLMDEPFSALDPLIR 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2225592549 193 EQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:TIGR03415 201 TQLQDELLELQSKLKKTIVFVSHDLDEALKIGNRIAIM--EGGRI 243
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
47-237 |
2.46e-51 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 171.75 E-value: 2.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 47 DINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE-PGSDR--GMVFQNYTLFPWLTVADNVAFGL 123
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvPPAERgvGMVFQSYALYPHLSVAENMSFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 124 KLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELW 203
Cdd:PRK11000 101 KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLH 180
|
170 180 190
....*....|....*....|....*....|....
gi 2225592549 204 EQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:PRK11000 181 KRLGRTMIYVTHDQVEAMTLADKIVVL--DAGRV 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
47-237 |
5.17e-51 |
|
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: 166.13 E-value: 5.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 47 DINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG-EVIEEPGSDR--GMVFQNYTLFPWLTVADNVAFG- 122
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPADRpvSMLFQENNLFAHLTVEQNVGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 123 ---LKLRGLSSGEIKEQvfyyLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFF 199
Cdd:cd03298 96 spgLKLTAEDRQAIEVA----LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 2225592549 200 LELWEQTHITVLMITHDVEEAVFLSGRVyVMIANpGRI 237
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRV-VFLDN-GRI 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
26-237 |
5.74e-51 |
|
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: 166.84 E-value: 5.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFphlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR----- 100
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEiarlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 -GMVFQNYTLFPWLTVADNVAFGLKLRGLSS----------GEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIAR 169
Cdd:cd03219 77 iGRTFQIPRLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2225592549 170 ALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQtHITVLMITHDVeEAVF-LSGRVYVMiaNPGRI 237
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDM-DVVMsLADRVTVL--DQGRV 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-240 |
1.34e-50 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 167.50 E-value: 1.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 23 QPKLEVEKVFKHFPHLKTnlSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI-EEPGSD-R 100
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAT--YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLsEETVWDvR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ---GMVFQNY-TLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPE 176
Cdd:PRK13635 81 rqvGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2225592549 177 VLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFlSGRVYVMiaNPGRIKDE 240
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVM--NKGEILEE 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
26-237 |
6.70e-50 |
|
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: 162.18 E-value: 6.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGE-VIEEPGSDR---G 101
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKdIKKEPEEVKrriG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 102 MVFQNYTLFPWLTVADNVafglklrglssgeikeqvfyylsivgltqfakaypkQLSGGMKQRVAIARALANHPEVLLMD 181
Cdd:cd03230 77 YLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2225592549 182 EPFGALDAQTREQMQQFFLELwEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:cd03230 121 EPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAIL--NNGRI 173
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
26-237 |
1.58e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 163.34 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR----- 100
Cdd:PRK09493 2 IEFKNVSKHFGPTQ----VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 --GMVFQNYTLFPWLTVADNVAFG-LKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEV 177
Cdd:PRK09493 78 eaGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 178 LLMDEPFGALDAQTREQMQQFFLELWEQThITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFI--DKGRI 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
26-230 |
9.38e-49 |
|
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: 160.75 E-value: 9.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPhlKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG-EVIEEPGSDR---G 101
Cdd:cd03263 1 LQIRNLTKTYK--KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGySIRTDRKAARqslG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 102 MVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMD 181
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2225592549 182 EPFGALDAQTREQMQQFFLElwEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILE--VRKGRSIILTTHSMDEAEALCDRIAIM 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
45-184 |
2.21e-48 |
|
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: 157.42 E-value: 2.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI-----EEPGSDRGMVFQNYTLFPWLTVADNV 119
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdderKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2225592549 120 AFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAK----AYPKQLSGGMKQRVAIARALANHPEVLLMDEPF 184
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
26-218 |
3.18e-48 |
|
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: 159.11 E-value: 3.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHlktNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE------PGSD 99
Cdd:cd03292 1 IEFINVTKTYPN---GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraiPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 100 R--GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEV 177
Cdd:cd03292 78 RkiGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2225592549 178 LLMDEPFGALDAQTREQMqqffLELWEQTH---ITVLMITHDVE 218
Cdd:cd03292 158 LIADEPTGNLDPDTTWEI----MNLLKKINkagTTVVVATHAKE 197
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
44-237 |
3.25e-47 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 157.90 E-value: 3.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE-PGSDR----GMVFQNYTLFPWLTVADN 118
Cdd:COG1120 16 VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELarriAYVPQEPPAPFGLTVREL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFG----LKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQ 194
Cdd:COG1120 96 VALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2225592549 195 MQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:COG1120 176 VLELLRRLARERGRTVVMVLHDLNLAARYADRLVLL--KDGRI 216
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
26-220 |
1.08e-46 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 156.30 E-value: 1.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG-EVIEEPGSDR---- 100
Cdd:TIGR02315 2 LEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtDITKLRGKKLrklr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ---GMVFQNYTLFPWLTVADNVAFGL--------KLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIAR 169
Cdd:TIGR02315 79 rriGMIFQHYNLIERLTVLENVLHGRlgykptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2225592549 170 ALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEA 220
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLA 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
44-218 |
1.12e-46 |
|
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: 155.00 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDRGMVFQNYTL---FPwLTVADNVA 120
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRSIdrdFP-ISVRDVVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 121 FGL--KLRGLS--SGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQmq 196
Cdd:cd03235 93 MGLygHKGLFRrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQED-- 170
|
170 180
....*....|....*....|....*
gi 2225592549 197 qfFLEL---WEQTHITVLMITHDVE 218
Cdd:cd03235 171 --IYELlreLRREGMTILVVTHDLG 193
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
26-230 |
1.18e-46 |
|
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: 156.17 E-value: 1.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR----G 101
Cdd:COG4555 2 IEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREArrqiG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 102 MVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMD 181
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2225592549 182 EPFGALDAQTREQMQQFFLELWEQTHiTVLMITHDVEEAVFLSGRVYVM 230
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEALCDRVVIL 205
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
44-216 |
2.99e-46 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 154.41 E-value: 2.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEviEEPGSDR----------GMVFQNYTLFPWL 113
Cdd:TIGR02982 20 VLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQ--ELHGASKkqlvqlrrriGYIFQAHNLLGFL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 114 TVADNVAFGLKL-RGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTR 192
Cdd:TIGR02982 98 TARQNVQMALELqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSG 177
|
170 180
....*....|....*....|....
gi 2225592549 193 EQMQQFFLELWEQTHITVLMITHD 216
Cdd:TIGR02982 178 RDVVELMQKLAKEQGCTILMVTHD 201
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
26-239 |
4.60e-46 |
|
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: 154.05 E-value: 4.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR----- 100
Cdd:TIGR02211 2 LKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNEraklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ----GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPE 176
Cdd:TIGR02211 82 nkklGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 177 VLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSgRVYVMiaNPGRIKD 239
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLD-RVLEM--KDGQLFN 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
49-237 |
6.37e-46 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 153.97 E-value: 6.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 49 NIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEV-IEEPGSDR--GMVFQNYTLFPWLTVADNVAFG--- 122
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhTTTPPSRRpvSMLFQENNLFSHLTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 123 -LKLrglsSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLE 201
Cdd:PRK10771 99 gLKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 2225592549 202 LWEQTHITVLMITHDVEEAVFLSGRVyVMIANpGRI 237
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRS-LVVAD-GRI 208
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-251 |
8.15e-45 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 153.73 E-value: 8.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPhLKTNL--------SVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI 93
Cdd:COG4608 4 AEPLLEVRDLKKHFP-VRGGLfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 94 EE-PGSDR-------GMVFQN-YT-LFPWLTVADNVAFGLKLRGL-SSGEIKEQVFYYLSIVGL-TQFAKAYPKQLSGGM 161
Cdd:COG4608 83 TGlSGRELrplrrrmQMVFQDpYAsLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 162 KQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHD---VEeavFLSGRVYVMIAnpGRIk 238
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDlsvVR---HISDRVAVMYL--GKI- 236
|
250
....*....|...
gi 2225592549 239 defkIELPPERDL 251
Cdd:COG4608 237 ----VEIAPRDEL 245
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
44-230 |
1.27e-44 |
|
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: 148.16 E-value: 1.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEpgsdrgmvfqnytlfpwltvadnvafgl 123
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK---------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 124 klrgLSSGEIKEQVFYYLsivgltqfakaypkQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELW 203
Cdd:cd00267 66 ----LPLEELRRRIGYVP--------------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA 127
|
170 180
....*....|....*....|....*..
gi 2225592549 204 EQtHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:cd00267 128 EE-GRTVIIVTHDPELAELAADRVIVL 153
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
44-218 |
3.59e-44 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 148.53 E-value: 3.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR---------GMVFQNYTLFPWLT 114
Cdd:TIGR03608 13 ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrreklGYLFQNFALIENET 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 115 VADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQ 194
Cdd:TIGR03608 93 VEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDE 172
|
170 180
....*....|....*....|....
gi 2225592549 195 MQQFFLELWEQTHiTVLMITHDVE 218
Cdd:TIGR03608 173 VLDLLLELNDEGK-TIIIVTHDPE 195
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
44-216 |
4.03e-44 |
|
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: 148.40 E-value: 4.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR----GMVFQNYTLFPWLTVADNV 119
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYrrrlAYLGHADGLKPELTVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 120 AFGLKLRGLSSGEikEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFF 199
Cdd:COG4133 97 RFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELI 174
|
170 180
....*....|....*....|.
gi 2225592549 200 lelweQTHI----TVLMITHD 216
Cdd:COG4133 175 -----AAHLarggAVLLTTHQ 190
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
23-237 |
6.36e-44 |
|
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: 158.07 E-value: 6.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 23 QPKLEVEKVFKHFPHLKTNlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE--PGSDR 100
Cdd:COG2274 471 KGDIELENVSFRYPGDSPP--VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQidPASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ---GMVFQNYTLFPwLTVADNVAFGLKLRGLssgeikEQVFYYLSIVGLTQFAKAYPK-----------QLSGGMKQRVA 166
Cdd:COG2274 549 rqiGVVLQDVFLFS-GTIRENITLGDPDATD------EEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2225592549 167 IARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQthITVLMITHDvEEAVFLSGRVYVMiaNPGRI 237
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHR-LSTIRLADRIIVL--DKGRI 687
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
39-230 |
1.74e-43 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 152.11 E-value: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 39 KTNLSV-LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG---------EVIEEPGSDRGMVFQNYT 108
Cdd:PRK10070 37 KTGLSLgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaELREVRRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 109 LFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALD 188
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2225592549 189 AQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
47-244 |
3.15e-43 |
|
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: 150.26 E-value: 3.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 47 DINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE-------PGSDR--GMVFQNYTLFPWLTVAD 117
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgiflPPEKRriGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFGLK-LRGLSSGEIKEQVfyyLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQ 196
Cdd:TIGR02142 95 NLRYGMKrARPSERRISFERV---IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2225592549 197 QFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMIAnpGRIKDEFKIE 244
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLED--GRVAAAGPIA 217
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
26-237 |
5.13e-43 |
|
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: 145.98 E-value: 5.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFphlKTNLSVlEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG-EVIEEPGSDR---G 101
Cdd:cd03265 1 IEVENLVKKY---GDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhDVVREPREVRrriG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 102 MVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMD 181
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2225592549 182 EPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAII--DHGRI 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
26-230 |
5.23e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 147.96 E-value: 5.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFpHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPG-----SDR 100
Cdd:PRK13650 5 IEVKNLTFKY-KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwdirHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 GMVFQNY-TLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLL 179
Cdd:PRK13650 84 GMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2225592549 180 MDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEaVFLSGRVYVM 230
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVM 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
22-227 |
4.30e-42 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 144.79 E-value: 4.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEkvfkhfphlktNLSV-------LEDINIQVYPNEFVSIVGASGCGKSTLL---NIIAGLIPpSA---GQVLM 88
Cdd:COG1117 8 LEPKIEVR-----------NLNVyygdkqaLKDINLDIPENKVTALIGPSGCGKSTLLrclNRMNDLIP-GArveGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 89 NGEVIEEPGSD----R---GMVFQNYTLFPwLTVADNVAFGLKLRGLSS-GEIKEQVFYYLSIVG--------LTQFAKA 152
Cdd:COG1117 76 DGEDIYDPDVDvvelRrrvGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSkSELDEIVEESLRKAAlwdevkdrLKKSALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 153 ypkqLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQthITVLMITHDVEEA--------VFLS 224
Cdd:COG1117 155 ----LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAarvsdytaFFYL 228
|
...
gi 2225592549 225 GRV 227
Cdd:COG1117 229 GEL 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
26-238 |
1.05e-41 |
|
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: 142.33 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsVLEDINIQVyPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGE-VIEEPGSDRGMVF 104
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdVLKQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 105 ---QNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMD 181
Cdd:cd03264 76 ylpQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2225592549 182 EPFGALDAQTREQMQQFFLELWEQThiTVLMITHDVEEAVFLSGRVYVMiaNPGRIK 238
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVL--NKGKLV 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-237 |
1.06e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 143.98 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLKTNlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI-----EEP 96
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIskenlKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 97 GSDRGMVFQNY-TLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHP 175
Cdd:PRK13632 82 RKKIGIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2225592549 176 EVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVfLSGRVYVMiaNPGRI 237
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVF--SEGKL 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
26-230 |
1.28e-41 |
|
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: 140.60 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR----- 100
Cdd:cd03228 1 IEFKNVSFSYPG--RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrkni 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 GMVFQNYTLFPwLTVADNVafglklrglssgeikeqvfyylsivgltqfakaypkqLSGGMKQRVAIARALANHPEVLLM 180
Cdd:cd03228 79 AYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2225592549 181 DEPFGALDAQTREQMQQFFLELweQTHITVLMITHDVeEAVFLSGRVYVM 230
Cdd:cd03228 121 DEATSALDPETEALILEALRAL--AKGKTVIVIAHRL-STIRDADRIIVL 167
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
45-237 |
2.18e-41 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 141.94 E-value: 2.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI------EEPGSDR--GMVFQNYTLFPWLTVA 116
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlknrEVPFLRRqiGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 117 DNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQ 196
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2225592549 197 QFFlELWEQTHITVLMITHDVEeavFLSGRVY-VMIANPGRI 237
Cdd:PRK10908 178 RLF-EEFNRVGVTVLMATHDIG---LISRRSYrMLTLSDGHL 215
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
30-272 |
3.70e-41 |
|
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: 143.68 E-value: 3.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 30 KVFKHFPHLKtnlsvleDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG-EVIEEPGSDR---GMVFQ 105
Cdd:TIGR01188 1 KVYGDFKAVD-------GVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGyDVVREPRKVRrsiGIVPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 106 NYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFG 185
Cdd:TIGR01188 74 YASVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 186 ALDAQTREQMQQFFLELWEQTHiTVLMITHDVEEAVFLSGRVYVMiaNPGRIkdeFKIELPPErdLEIKMSEDFWQIKRQ 265
Cdd:TIGR01188 154 GLDPRTRRAIWDYIRALKEEGV-TILLTTHYMEEADKLCDRIAII--DHGRI---IAEGTPEE--LKRRLGKDTLESRPR 225
|
....*..
gi 2225592549 266 ILKSLQP 272
Cdd:TIGR01188 226 DIQSLKV 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
44-237 |
2.04e-40 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 139.76 E-value: 2.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEV-----------IEEPGSDRGMVFQNYTLFPW 112
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfsktpsdkaIRELRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 113 LTVADN-VAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQT 191
Cdd:PRK11124 97 LTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2225592549 192 REQMQQFFLELwEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:PRK11124 177 TAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYM--ENGHI 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-220 |
4.56e-40 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 138.76 E-value: 4.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI----EEP----- 96
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEAraklr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 97 GSDRGMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPE 176
Cdd:PRK10584 87 AKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2225592549 177 VLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEA 220
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
26-242 |
5.10e-40 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 139.19 E-value: 5.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFphlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE---------P 96
Cdd:TIGR03005 1 VRFSDVTKRF----GILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHmpgrngplvP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 97 GSDR---------GMVFQNYTLFPWLTVADNVAFG-LKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVA 166
Cdd:TIGR03005 77 ADEKhlrqmrnkiGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2225592549 167 IARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRvyVMIANPGRIKDEFK 242
Cdd:TIGR03005 157 IARALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADR--VCFFDKGRIVEQGK 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
45-237 |
6.02e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 140.18 E-value: 6.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR-------GMVFQ--NYTLFPwLTV 115
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdirkkvGLVFQypEYQLFE-ETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 116 ADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLT--QFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTRE 193
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2225592549 194 QMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVM--NKGKC 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-224 |
1.32e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 137.64 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGS--- 98
Cdd:PRK11629 2 NKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaak 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 99 ------DRGMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALA 172
Cdd:PRK11629 82 aelrnqKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2225592549 173 NHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLS 224
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
26-216 |
1.75e-39 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 145.25 E-value: 1.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR----- 100
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ----GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPE 176
Cdd:PRK10535 85 rehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2225592549 177 VLLMDEPFGALDAQTREQMQQFFLELWEQTHiTVLMITHD 216
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHD 203
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
44-240 |
1.99e-39 |
|
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: 144.13 E-value: 1.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE--PGSDRGMVF---QNYTLFPWlTVADN 118
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDldPASWRRQIAwvpQNPYLFAG-TIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFGlkLRGLSSGEIkEQVfyyLSIVGLTQFAKAYPK-----------QLSGGMKQRVAIARALANHPEVLLMDEPFGAL 187
Cdd:COG4988 431 LRLG--RPDASDEEL-EAA---LEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHL 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 188 DAQTREQMQQFFLELWEQThiTVLMITHDVEEAVFlSGRVYVMiaNPGRIKDE 240
Cdd:COG4988 505 DAETEAEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVL--DDGRIVEQ 552
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
44-237 |
3.06e-39 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 137.07 E-value: 3.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI---EEPGSDR--------GMVFQNYTLFPW 112
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAirllrqkvGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 113 LTVADN-VAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQT 191
Cdd:COG4161 97 LTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2225592549 192 REQMQQFFLELwEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:COG4161 177 TAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYM--EKGRI 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
41-233 |
2.73e-38 |
|
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: 133.15 E-value: 2.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 41 NLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIeePGSDR----GMVFQN--YTLFPwLT 114
Cdd:cd03226 12 GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI--KAKERrksiGYVMQDvdYQLFT-DS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 115 VADNVAFGLKLRGLSSGEIKEqvfyYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQ 194
Cdd:cd03226 89 VREELLLGLKELDAGNEQAET----VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 2225592549 195 MQQFFLELWEQTHiTVLMITHDVEEAVFLSGRVyVMIAN 233
Cdd:cd03226 165 VGELIRELAAQGK-AVIVITHDYEFLAKVCDRV-LLLAN 201
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
44-237 |
5.00e-38 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 131.79 E-value: 5.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEpgsdrgmvfqnytlFPWLTVADNVAFgl 123
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS--------------LSPKELARKIAY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 124 klrgLSsgeikeQVfyyLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELW 203
Cdd:cd03214 78 ----VP------QA---LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLA 144
|
170 180 190
....*....|....*....|....*....|....
gi 2225592549 204 EQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:cd03214 145 RERGKTVVMVLHDLNLAARYADRVILL--KDGRI 176
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
22-237 |
2.14e-37 |
|
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: 138.75 E-value: 2.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVfkHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE-PGSDR 100
Cdd:COG4987 330 GGPSLELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ----GMVFQNytlfPWL---TVADNVAFGLKlrGLSSGEIkEQVfyyLSIVGLTQFAKAYPK-----------QLSGGMK 162
Cdd:COG4987 408 rrriAVVPQR----PHLfdtTLRENLRLARP--DATDEEL-WAA---LERVGLGDWLAALPDgldtwlgeggrRLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 163 QRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQThiTVLMITHDveeavfLSG-----RVYVMiaNPGRI 237
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHR------LAGlermdRILVL--EDGRI 547
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
44-241 |
2.46e-37 |
|
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: 130.80 E-value: 2.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR---GMVFQNYTLFPWLTVADNVA 120
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALrriGALIEAPGFYPNLTARENLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 121 FGLKLRGLSSGEIKEqvfyYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFL 200
Cdd:cd03268 95 LLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELIL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2225592549 201 ELWEQThITVLMITHDVEEAVFLSGRVyVMIANpGRIKDEF 241
Cdd:cd03268 171 SLRDQG-ITVLISSHLLSEIQKVADRI-GIINK-GKLIEEG 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-230 |
4.90e-37 |
|
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: 128.70 E-value: 4.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEepgsdrgmvfq 105
Cdd:cd03216 1 LELRGITKRFGGVK----ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 106 nytlfpWLTVADNVAFGLKLrglssgeikeqVFyylsivgltqfakaypkQLSGGMKQRVAIARALANHPEVLLMDEPFG 185
Cdd:cd03216 66 ------FASPRDARRAGIAM-----------VY-----------------QLSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2225592549 186 ALDAQTREQMQQFFLELWEQtHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:cd03216 112 ALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVL 155
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
44-240 |
5.67e-37 |
|
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: 130.25 E-value: 5.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGE-VIEEPGSDR-----GMVFQNYTLFPWLTVAD 117
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRdITGLPPHERaragiGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFGLKLRGLSSG-EIKEQVFYYLSIvgLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQ 196
Cdd:cd03224 95 NLLLGAYARRRAKRkARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2225592549 197 QFFLELwEQTHITVLMITHDVEEAVFLSGRVYVMIAnpGRIKDE 240
Cdd:cd03224 173 EAIREL-RDEGVTILLVEQNARFALEIADRAYVLER--GRVVLE 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
44-215 |
1.21e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 136.45 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE--PGSDR---GMVFQNYTLFPwLTVADN 118
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDltLESLRrqiGVVPQDTFLFS-GTIREN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFGLKlrGLSSGEIKEqvfyYLSIVGLTQFAKAYPK-----------QLSGGMKQRVAIARALANHPEVLLMDEPFGAL 187
Cdd:COG1132 434 IRYGRP--DATDEEVEE----AAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSAL 507
|
170 180
....*....|....*....|....*...
gi 2225592549 188 DAQTREQMQQFFLELWEQThiTVLMITH 215
Cdd:COG1132 508 DTETEALIQEALERLMKGR--TTIVIAH 533
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-230 |
3.21e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 134.38 E-value: 3.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLKTNlsvlEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIeEPGSDR- 100
Cdd:COG3845 2 MPPALELRGITKRFGGVVAN----DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPRd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ------GMVFQNYTLFPWLTVADNVAFGL---KLRGLSSGEIKEQVfyylsivglTQFAKAYP---------KQLSGGMK 162
Cdd:COG3845 77 aialgiGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARI---------RELSERYGldvdpdakvEDLSVGEQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2225592549 163 QRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHiTVLMITHDVEEAVFLSGRVYVM 230
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGK-SIIFITHKLREVMAIADRVTVL 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-230 |
1.26e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.83 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIeEPGSDR- 100
Cdd:COG1129 1 AEPLLEMRGISKSFGGVK----ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSPRd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ------GMVFQNYTLFPWLTVADNVAFGLKLRG---LSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARAL 171
Cdd:COG1129 76 aqaagiAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 172 ANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQtHITVLMITHDVEEaVF-LSGRVYVM 230
Cdd:COG1129 156 SRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDE-VFeIADRVTVL 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
44-230 |
1.93e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 127.90 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG------EVIEEPGSDRGMVFQN------YTLfp 111
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENLWDIRNKAGMVFQNpdnqivATI-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 112 wltVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQT 191
Cdd:PRK13633 103 ---VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 2225592549 192 REQMQQFFLELWEQTHITVLMITHDVEEAVfLSGRVYVM 230
Cdd:PRK13633 180 RREVVNTIKELNKKYGITIILITHYMEEAV-EADRIIVM 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
44-237 |
2.03e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 127.54 E-value: 2.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE-PGSD----RGMVFQNYTL-FPWlTVAD 117
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwSPWElarrRAVLPQHSSLaFPF-TVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFA-KAYPkQLSGGMKQRVAIARALA-------NHPEVLLMDEPFGALD- 188
Cdd:COG4559 95 VVALGRAPHGSSAAQDRQIVREALALVGLAHLAgRSYQ-TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDl 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2225592549 189 AQtreqmQQFFLEL---WEQTHITVLMITHDVEEAVFLSGRVYVMIAnpGRI 237
Cdd:COG4559 174 AH-----QHAVLRLarqLARRGGGVVAVLHDLNLAAQYADRILLLHQ--GRL 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-230 |
4.55e-35 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 131.73 E-value: 4.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKS-TLLNIIaGLIPPSA----GQVLMNG-EVIEE 95
Cdd:COG4172 3 SMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDPAahpsGSILFDGqDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 96 P--------GSDRGMVFQ------NytlfPWLTVADNVAFGLKL-RGLSSGEIKEQVFYYLSIVGLTQFA---KAYPKQL 157
Cdd:COG4172 82 SerelrrirGNRIAMIFQepmtslN----PLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2225592549 158 SGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHD---VEEavfLSGRVYVM 230
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvVRR---FADRVAVM 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
22-248 |
4.60e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 126.62 E-value: 4.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDRG 101
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 102 ------------------MVFQNYTLFPWLTVADNVAFG-LKLRGLSSGEIKEQVFYYLSIVGLTQFAKA-YPKQLSGGM 161
Cdd:PRK10619 78 qlkvadknqlrllrtrltMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 162 KQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHiTVLMITHDVEEAVFLSGrvYVMIANPGRIKDEF 241
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSS--HVIFLHQGKIEEEG 234
|
....*..
gi 2225592549 242 kielPPE 248
Cdd:PRK10619 235 ----APE 237
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
32-240 |
5.43e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 126.84 E-value: 5.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 32 FKH--FPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQ--------VLMNGEVIEEPGSDRG 101
Cdd:PRK13640 8 FKHvsFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVWDIREKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 102 MVFQNY-TLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLM 180
Cdd:PRK13640 88 IVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 181 DEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAvflSGRVYVMIANPGRIKDE 240
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA---NMADQVLVLDDGKLLAQ 224
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
26-216 |
5.99e-35 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 126.49 E-value: 5.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHlKTNLS------VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEePGSD 99
Cdd:COG4167 5 LEVRNLSKTFKY-RTGLFrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLE-YGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 100 RG------MVFQ--NYTLFPWLTVADNVAFGLKLR-GLSSGEIKEQVFYYLSIVGL-TQFAKAYPKQLSGGMKQRVAIAR 169
Cdd:COG4167 83 KYrckhirMIFQdpNTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALAR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2225592549 170 ALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHD 216
Cdd:COG4167 163 ALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQH 209
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-242 |
9.62e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 125.58 E-value: 9.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHF----PHLKTnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGE-VIEEPGSDR 100
Cdd:COG1101 2 LELKNLSKTFnpgtVNEKR---ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ----GMVFQNYTL--FPWLTVADNVAFGL---KLRGLSSGEIKEQVFYY---LSIVG------LTQFAkaypKQLSGGmk 162
Cdd:COG1101 79 akyiGRVFQDPMMgtAPSMTIEENLALAYrrgKRRGLRRGLTKKRRELFrelLATLGlglenrLDTKV----GLLSGG-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 163 QRVAIARALA--NHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRIKDE 240
Cdd:COG1101 153 QRQALSLLMAtlTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMM--HEGRIILD 230
|
..
gi 2225592549 241 FK 242
Cdd:COG1101 231 VS 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-230 |
1.81e-34 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 124.72 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLktnLSVlEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIE-EPG--- 97
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGL---LAV-NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEgLPGhqi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 98 SDRGMV--FQNYTLFPWLTVADN--VAFGLKLR-GLSSGEIK------------EQVFYYLSIVGLTQFAKAYPKQLSGG 160
Cdd:PRK11300 78 ARMGVVrtFQHVRLFREMTVIENllVAQHQQLKtGLFSGLLKtpafrraesealDRAATWLERVGLLEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 161 MKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
26-240 |
3.18e-34 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 123.25 E-value: 3.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG-EVIEEPGSDR---G 101
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARrrlG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 102 MVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMD 181
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2225592549 182 EPFGALDAQTREQMQQFFLELWEQTHiTVLMITHDVEEAVFLSGRVyVMIANpGRIKDE 240
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRV-VVLHR-GRVVYE 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
26-230 |
4.93e-34 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 129.03 E-value: 4.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFP-----------HLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPpSAGQVLMNGEVIE 94
Cdd:COG4172 276 LEARDLKVWFPikrglfrrtvgHVK----AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 95 EpGSDRGM---------VFQN-Y-TLFPWLTVADNVAFGLKL--RGLSSGEIKEQVFYYLSIVGLT-QFAKAYPKQLSGG 160
Cdd:COG4172 351 G-LSRRALrplrrrmqvVFQDpFgSLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGG 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2225592549 161 MKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVeeAV--FLSGRVYVM 230
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDL--AVvrALAHRVMVM 499
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
43-230 |
6.85e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 124.03 E-value: 6.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 43 SVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR-------GMVFQNY--TLF-Pw 112
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLlevrktvGIVFQNPddQLFaP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 113 lTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTR 192
Cdd:PRK13639 95 -TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 2225592549 193 EQMQQFFLELWEQThITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK13639 174 SQIMKLLYDLNKEG-ITIIISTHDVDLVPVYADKVYVM 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
26-237 |
1.16e-33 |
|
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: 121.62 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGE-VIEEPGSDRGMVF 104
Cdd:cd03269 1 LEVENVTKRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpLDIAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 105 QNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPF 184
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 185 GALDAQTREQMQQFFLELWEQThITVLMITHDVEEAVFLSGRVyVMIaNPGRI 237
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAG-KTVILSTHQMELVEELCDRV-LLL-NKGRA 206
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-249 |
1.46e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 122.64 E-value: 1.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIP--PSA---GQVLMNGEVIEEPGSDR-------GMVFQNYTLFP 111
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYSPDVDPievrrevGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 112 WLTVADNVAFGLKLRGL--SSGEIKEQVFYYLSIVGLTQFAKA----YPKQLSGGMKQRVAIARALANHPEVLLMDEPFG 185
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDrlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2225592549 186 ALDAQTREQMQQFFLELweQTHITVLMITHDVEEAVFLSGrvYVMIANPGRIkdefkIELPPER 249
Cdd:PRK14267 179 NIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSD--YVAFLYLGKL-----IEVGPTR 233
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
41-230 |
2.15e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 122.57 E-value: 2.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 41 NLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR--------GMVFQNYTLFPW 112
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlytvrkrmSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 113 LTVADNVAFGLKLRG-LSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQT 191
Cdd:PRK11831 99 MNVFDNVAYPLREHTqLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 2225592549 192 REQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK11831 179 MGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIV 217
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
44-237 |
3.34e-33 |
|
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: 120.73 E-value: 3.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIE-EPGSDR---GMVF--QNYTLFPWLTVAD 117
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITkLPMHKRarlGIGYlpQEASIFRKLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQ 197
Cdd:cd03218 95 NILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQK 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2225592549 198 FFLELWEQtHITVLMITHDVEEAVFLSGRVYVMIAnpGRI 237
Cdd:cd03218 175 IIKILKDR-GIGVLITDHNVRETLSITDRAYIIYE--GKV 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
44-220 |
3.47e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 119.65 E-value: 3.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGqvlmngEVIEEPGSDRGMVFQNYTL---FPwLTVADNVA 120
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG------TVRRAGGARVAYVPQRSEVpdsLP-LTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 121 FGL-KLRGLS---SGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQ 196
Cdd:NF040873 80 MGRwARRGLWrrlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180
....*....|....*....|....
gi 2225592549 197 QFFLElWEQTHITVLMITHDVEEA 220
Cdd:NF040873 160 ALLAE-EHARGATVVVVTHDLELV 182
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
47-238 |
4.91e-33 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 123.45 E-value: 4.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 47 DINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEV-------IEEPGSDR--GMVFQNYTLFPWLTVAD 117
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgICLPPEKRriGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFGLKlrglssGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDA-QTREQMQ 196
Cdd:PRK11144 96 NLRYGMA------KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLpRKRELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2225592549 197 qfFLE-LWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRIK 238
Cdd:PRK11144 170 --YLErLAREINIPILYVSHSLDEILRLADRVVVL--EQGKVK 208
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
45-237 |
6.43e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 121.01 E-value: 6.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI-----EEPGSDRGMVFQN-YTLFPWLTVADN 118
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnfEKLRKHIGIVFQNpDNQFVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQF 198
Cdd:PRK13648 105 VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDL 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 2225592549 199 FLELWEQTHITVLMITHDVEEAVflsGRVYVMIANPGRI 237
Cdd:PRK13648 185 VRKVKSEHNITIISITHDLSEAM---EADHVIVMNKGTV 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
44-219 |
1.86e-32 |
|
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: 119.42 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVL------MNGEVIEEPGSDRGMV----FQNYTlfPWL 113
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWELRKRIGLVspalQLRFP--RDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 114 TVADNV---AFGlklrglSSG-------EIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEP 183
Cdd:COG1119 96 TVLDVVlsgFFD------SIGlyreptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 2225592549 184 FGALDAQTREQMQQFFLELWEQTHITVLMITHDVEE 219
Cdd:COG1119 170 TAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEE 205
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
45-230 |
1.90e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 120.51 E-value: 1.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEePGSDR----------GMVFQ--NYTLFPw 112
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVIT-AGKKNkklkplrkkvGIVFQfpEHQLFE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 113 LTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQ--FAKAyPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQ 190
Cdd:PRK13634 101 ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEelLARS-PFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2225592549 191 TREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVM 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
26-237 |
2.60e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 119.08 E-value: 2.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFpHLKTnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMnGEVI--------EEPG 97
Cdd:PRK11264 4 IEVKNLVKKF-HGQT---VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITidtarslsQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 98 SDR------GMVFQNYTLFPWLTVADNVAFG-LKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARA 170
Cdd:PRK11264 79 LIRqlrqhvGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2225592549 171 LANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHiTVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFM--DQGRI 222
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
24-237 |
3.03e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 118.59 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 24 PKLEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIeepgSD---- 99
Cdd:COG1137 2 MTLEAENLVKSYGKRT----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI----THlpmh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 100 ----RGM--------VFQNytlfpwLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAI 167
Cdd:COG1137 74 krarLGIgylpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2225592549 168 ARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQtHITVLmIT-HDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKER-GIGVL-ITdHNVRETLGICDRAYII--SEGKV 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
44-218 |
3.30e-32 |
|
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: 123.94 E-value: 3.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR-----GMVFQNYTLFPWlTVADN 118
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrdqiAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFGlkLRGLSSGEIKEQvfyyLSIVGLTQFAKAYPKQ-----------LSGGMKQRVAIARALANHPEVLLMDEPFGAL 187
Cdd:TIGR02857 416 IRLA--RPDASDAEIREA----LERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190
....*....|....*....|....*....|.
gi 2225592549 188 DAQTREQMQQFFLELwEQTHiTVLMITHDVE 218
Cdd:TIGR02857 490 DAETEAEVLEALRAL-AQGR-TVLLVTHRLA 518
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
45-230 |
4.84e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 119.16 E-value: 4.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR---------GMVFQnytlFPWL-- 113
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklrkkvSLVFQ----FPEAql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 114 ---TVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGL-TQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDA 189
Cdd:PRK13641 99 fenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2225592549 190 QTREQMQQFFLELWEQTHiTVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVL 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
44-218 |
5.84e-32 |
|
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: 117.25 E-value: 5.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVieepgsdRGMVFQNYTLFPWLTVADNVAFGL 123
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV-------SSLLGLGGGFNPELTGRENIYLNG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 124 KLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELW 203
Cdd:cd03220 110 RLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL 189
|
170
....*....|....*
gi 2225592549 204 EQTHiTVLMITHDVE 218
Cdd:cd03220 190 KQGK-TVILVSHDPS 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-259 |
7.02e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 119.06 E-value: 7.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFphlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI------------ 93
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLdpedrrrigylp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 94 EEPGsdrgmvfqnytLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALAN 173
Cdd:COG4152 78 EERG-----------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 174 HPEVLLMDEPFGALDAQTREQMQQFFLELWEQThITVLMITHD---VEEavfLSGRVyVMIANpGR---------IKDEF 241
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAKG-TTVIFSSHQmelVEE---LCDRI-VIINK-GRkvlsgsvdeIRRQF 220
|
250
....*....|....*...
gi 2225592549 242 KielppERDLEIKMSEDF 259
Cdd:COG4152 221 G-----RNTLRLEADGDA 233
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
25-237 |
1.47e-31 |
|
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: 116.15 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 25 KLEVEKVFKHFPHLKTNlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE-PGSDR--- 100
Cdd:cd03245 2 RIEFRNVSFSYPNQEIP--ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLrrn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 -GMVFQNYTLFpWLTVADNVAFGLKLrgLSSGEIKEQVfyylSIVGLTQFAKAYPK-----------QLSGGMKQRVAIA 168
Cdd:cd03245 80 iGYVPQDVTLF-YGTLRDNITLGAPL--ADDERILRAA----ELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2225592549 169 RALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEqtHITVLMITHdveEAVFLS--GRVYVMiaNPGRI 237
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITH---RPSLLDlvDRIIVM--DSGRI 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-226 |
1.58e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.18 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLKTnlsvLEDINIQVYPNEFVSIVGASGCGKSTLL---NIIAGLIP--PSAGQVLMNGEVIEEP 96
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKA----LNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLNPevTITGSIVYNGHNIYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 97 GSDR-------GMVFQNYTLFPwLTVADNVAFGLKLRGLSSGEIKEQVFYYlSIVGLTQFAKAYPK------QLSGGMKQ 163
Cdd:PRK14239 78 RTDTvdlrkeiGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGASIWDEVKDRlhdsalGLSGGQQQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 164 RVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQthITVLMITHDVEEAVFLSGR 226
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDR 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
44-237 |
3.29e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.41 E-value: 3.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE-PGSD----RGMVFQNYTL-FPWlTVAD 117
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAElarrRAVLPQHSSLsFPF-TVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFA-KAYPkQLSGGMKQRVAIARALA------NHPEVLLMDEPFGALDAQ 190
Cdd:PRK13548 96 VVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAgRDYP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2225592549 191 TREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVyVMIANpGRI 237
Cdd:PRK13548 175 HQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRI-VLLHQ-GRL 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
26-232 |
4.00e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 116.73 E-value: 4.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEK-VFKHfpHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPG-----SD 99
Cdd:PRK13642 5 LEVENlVFKY--EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 100 RGMVFQNY-TLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVL 178
Cdd:PRK13642 83 IGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2225592549 179 LMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFlSGRVYVMIA 232
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKA 215
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
39-237 |
5.66e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 116.44 E-value: 5.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 39 KTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI-----EEPGSDRGMVFQNY--TLFP 111
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItkeniREVRKFVGLVFQNPddQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 112 wLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQT 191
Cdd:PRK13652 94 -PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2225592549 192 REQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVM--DKGRI 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
24-216 |
7.39e-31 |
|
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: 120.16 E-value: 7.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 24 PKLEVEKVFKHFPhlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR--- 100
Cdd:TIGR02868 333 PTLELRDLSAGYP---GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrr 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 --GMVFQNYTLFPwLTVADNVAFGlklRGLSSGeikEQVFYYLSIVGLTQFAKAYP-----------KQLSGGMKQRVAI 167
Cdd:TIGR02868 410 rvSVCAQDAHLFD-TTVRENLRLA---RPDATD---EELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2225592549 168 ARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQThiTVLMITHD 216
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHH 529
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-230 |
1.03e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 116.44 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFphlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIeePGSDR- 100
Cdd:PRK13537 4 SVAPIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV--PSRARh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 -----GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHP 175
Cdd:PRK13537 78 arqrvGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2225592549 176 EVLLMDEPFGALDAQTREQMqqfflelWEQTHI------TVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLM-------WERLRSllargkTILLTTHFMEEAERLCDRLCVI 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
26-242 |
1.62e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 114.02 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFP-------HLKTNLS-----------VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVL 87
Cdd:COG1134 5 IEVENVSKSYRlyhepsrSLKELLLrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 88 MNGEV---IEepgsdRGMVFQnytlfPWLTVADNVAFGLKLRGLSSGEIKEQvfyYLSIV---GLTQFAKAyP-KQLSGG 160
Cdd:COG1134 85 VNGRVsalLE-----LGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEK---FDEIVefaELGDFIDQ-PvKTYSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 161 MKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHiTVLMITHD---VEE----AVFLS-GRVyVMIA 232
Cdd:COG1134 151 MRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSmgaVRRlcdrAIWLEkGRL-VMDG 228
|
250
....*....|
gi 2225592549 233 NPGRIKDEFK 242
Cdd:COG1134 229 DPEEVIAAYE 238
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
31-215 |
2.57e-30 |
|
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: 113.48 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 31 VFKH--FPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE--PGSDR---GMV 103
Cdd:cd03251 2 EFKNvtFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytLASLRrqiGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 104 FQNYTLFPWlTVADNVAFGLklrglsSGEIKEQVFYYLSIVGLTQFAKAYPK-----------QLSGGMKQRVAIARALA 172
Cdd:cd03251 82 SQDVFLFND-TVAENIAYGR------PGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2225592549 173 NHPEVLLMDEPFGALDAQTREQMQQFFLELWEqtHITVLMITH 215
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH 195
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
26-243 |
3.71e-30 |
|
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: 113.75 E-value: 3.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPH-----LKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE--PGS 98
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 99 DRG------MVFQN-YTLF-PWLTVADNVAFGLK-LRGLSSGEIKEQVFYYLSIVGL-TQFAKAYPKQLSGGMKQRVAIA 168
Cdd:TIGR02769 83 RRAfrrdvqLVFQDsPSAVnPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2225592549 169 RALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRIKDEFKI 243
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVM--DKGQIVEECDV 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
41-230 |
5.08e-30 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 114.80 E-value: 5.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 41 NLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVL--------MNGEVIEEPGSDRGMVFQN--YTLF 110
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllgMKDDEWRAVRSDIQMIFQDplASLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 111 PWLTVADNVAFGLKLR--GLSSGEIKEQVFYYLSIVGL-TQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGAL 187
Cdd:PRK15079 113 PRMTIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2225592549 188 DAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
44-227 |
5.56e-30 |
|
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: 112.18 E-value: 5.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPG-----SDRGMVFQNYTLFPwLTVADN 118
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEhkylhSKVSLVGQEPVLFA-RSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFGLKlrGLSSGEIKEQVFYYLSIVGLTQFAKAYPK-------QLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQT 191
Cdd:cd03248 108 IAYGLQ--SCSFECVKEAAQKAHAHSFISELASGYDTevgekgsQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2225592549 192 REQMQQFFLElWEQTHiTVLMITH---DVEEA----VFLSGRV 227
Cdd:cd03248 186 EQQVQQALYD-WPERR-TVLVIAHrlsTVERAdqilVLDGGRI 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-251 |
5.77e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 113.08 E-value: 5.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 41 NLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLI-----PPSAGQVLMNGEVI-----EEPGSDRGMVFQNYTLF 110
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfkmdvIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 111 PWLTVADNVAFGLKLRGL--SSGEIKEQVFYYLSIVGLTQFAK----AYPKQLSGGMKQRVAIARALANHPEVLLMDEPF 184
Cdd:PRK14247 95 PNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKdrldAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2225592549 185 GALDAQTREQMQQFFLELweQTHITVLMITHDVEEAVFLSGrvYVMIANPGRIkdefkIELPPERDL 251
Cdd:PRK14247 175 ANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISD--YVAFLYKGQI-----VEWGPTREV 232
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
26-240 |
7.49e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 113.24 E-value: 7.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPH-----LKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE-PGSD 99
Cdd:PRK10419 4 LNVSGLSHHYAHgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 100 RG-------MVFQNY--TLFPWLTVADNVAFGLK-LRGLSSGEIKEQVFYYLSIVGLT-QFAKAYPKQLSGGMKQRVAIA 168
Cdd:PRK10419 84 RKafrrdiqMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2225592549 169 RALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRIKDE 240
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVM--DNGQIVET 233
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
44-230 |
1.12e-29 |
|
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: 111.61 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR------GMVFQNYTLFPWLTVAD 117
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRiarlgiGYVPEGRRIFPSLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFGLKLRGLSSG--EIKEQVFYYLSIvgLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQM 195
Cdd:COG0410 98 NLLLGAYARRDRAEvrADLERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEI 175
|
170 180 190
....*....|....*....|....*....|....*
gi 2225592549 196 QQFFLELWEQtHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:COG0410 176 FEIIRRLNRE-GVTILLVEQNARFALEIADRAYVL 209
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
26-230 |
1.97e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 112.25 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPhlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIE-------EPGS 98
Cdd:PRK13636 6 LKVEELNYNYS---DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkglmKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 99 DRGMVFQ--NYTLFPwLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPE 176
Cdd:PRK13636 83 SVGMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2225592549 177 VLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVM 215
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
26-215 |
3.85e-29 |
|
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: 108.46 E-value: 3.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFkhFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR----- 100
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgdhv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 GMVFQNYTLFPWlTVADNVafglklrglssgeikeqvfyylsivgltqfakaypkqLSGGMKQRVAIARALANHPEVLLM 180
Cdd:cd03246 79 GYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 2225592549 181 DEPFGALDAQTREQMQQFFLELwEQTHITVLMITH 215
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAH 154
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
41-237 |
8.78e-29 |
|
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: 107.90 E-value: 8.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 41 NLSV---LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGS----DRGMVF-----QNYT 108
Cdd:cd03215 9 GLSVkgaVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrdaiRAGIAYvpedrKREG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 109 LFPWLTVADNVAFGLklrglssgeikeqvfyylsivgltqfakaypkQLSGGMKQRVAIARALANHPEVLLMDEPFGALD 188
Cdd:cd03215 89 LVLDLSVAENIALSS--------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2225592549 189 AQTREQMQQFFLELWEQTHiTVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:cd03215 137 VGAKAEIYRLIRELADAGK-AVLLISSELDELLGLCDRILVM--YEGRI 182
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
26-252 |
8.81e-29 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 109.03 E-value: 8.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFphlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMN------------GEVI 93
Cdd:TIGR03740 1 LETKNLSKRF----GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDghpwtrkdlhkiGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 94 EEPgsdrgmvfqnyTLFPWLTVADNVAFGLKLRGLSSGEIKEqvfyYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALAN 173
Cdd:TIGR03740 77 ESP-----------PLYENLTARENLKVHTTLLGLPDSRIDE----VLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLN 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2225592549 174 HPEVLLMDEPFGALDAQTREQMQQFFLELWEQThITVLMITHDVEEAVFLSGrvYVMIANPGRIKDEFKIElpPERDLE 252
Cdd:TIGR03740 142 HPKLLILDEPTNGLDPIGIQELRELIRSFPEQG-ITVILSSHILSEVQQLAD--HIGIISEGVLGYQGKIN--KSENLE 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-249 |
8.97e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 114.57 E-value: 8.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFP-------HLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIE 94
Cdd:PRK10261 310 GEPILQVRNLVTRFPlrsgllnRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 95 E-PGS-------DRGMVFQN--YTLFPWLTVADNVAFGLKLRGLSSGE-IKEQVFYYLSIVGLT-QFAKAYPKQLSGGMK 162
Cdd:PRK10261 390 TlSPGklqalrrDIQFIFQDpyASLDPRQTVGDSIMEPLRVHGLLPGKaAAARVAWLLERVGLLpEHAWRYPHEFSGGQR 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 163 QRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRIkdefk 242
Cdd:PRK10261 470 QRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVM--YLGQI----- 542
|
....*..
gi 2225592549 243 IELPPER 249
Cdd:PRK10261 543 VEIGPRR 549
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
47-237 |
9.16e-29 |
|
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: 109.38 E-value: 9.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 47 DINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPP----SAGQVLMNGEVIEEP---GSDRGMVFQN-YTLF-PWLTVAD 117
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLsirGRHIATIMQNpRTAFnPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFA---KAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQ 194
Cdd:TIGR02770 84 HAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2225592549 195 MQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMIAnpGRI 237
Cdd:TIGR02770 164 VLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDD--GRI 204
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
38-232 |
1.07e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 109.87 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 38 LKT-NLSV-------LEDINIQVYPNEFVSIVGASGCGKSTLL---NIIAGLIPP--SAGQVLMNGEVIEEPGSDR---- 100
Cdd:PRK14243 11 LRTeNLNVyygsflaVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGfrVEGKVTFHGKNLYAPDVDPvevr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 ---GMVFQNYTLFPwLTVADNVAFGLKLRGLSsGEIKEQVFYYLSIVGLTQFAKAYPKQ----LSGGMKQRVAIARALAN 173
Cdd:PRK14243 91 rriGMVFQKPNPFP-KSIYDNIAYGARINGYK-GDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2225592549 174 HPEVLLMDEPFGALDAQTREQMQQFFLELWEQthITVLMITHDVEEAvflsGRVYVMIA 232
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQA----ARVSDMTA 221
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
60-216 |
1.78e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 110.82 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 60 IVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPgsDRG----------MVFQN-Y-TLFPWLTVADNVAFGLKLR- 126
Cdd:PRK11308 46 VVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA--DPEaqkllrqkiqIVFQNpYgSLNPRKKVGQILEEPLLINt 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 127 GLSSGEIKEQVFYYLSIVGL-TQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQ 205
Cdd:PRK11308 124 SLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQE 203
|
170
....*....|.
gi 2225592549 206 THITVLMITHD 216
Cdd:PRK11308 204 LGLSYVFISHD 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-215 |
2.65e-28 |
|
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: 106.87 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 20 TFSQPKLEVEKVFKHFPHLKTnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSA--GQVLMNGEVIEEPG 97
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKSGKQ---LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 98 SDR--GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKeqvfyylsivgltqfakaypkqlsggmkqRVAIARALANHP 175
Cdd:cd03213 80 FRKiiGYVPQDDILHPTLTVRETLMFAAKLRGLSGGERK-----------------------------RVSIALELVSNP 130
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2225592549 176 EVLLMDEPFGALDAQTREQMQQFFLELwEQTHITVLMITH 215
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIH 169
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
47-230 |
3.92e-28 |
|
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: 107.99 E-value: 3.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 47 DINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQV--LMNG----EVIEEPGSDR--------GMVFQNYTLFPW 112
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyIMRSgaelELYQLSEAERrrlmrtewGFVHQNPRDGLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 113 LTVADNVAFGLKLRGLSS---GEIKEQVFYYLSIVGLTQF-AKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALD 188
Cdd:TIGR02323 101 MRVSAGANIGERLMAIGArhyGNIRATAQDWLEEVEIDPTrIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLD 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2225592549 189 AQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:TIGR02323 181 VSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
26-230 |
5.01e-28 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 106.40 E-value: 5.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKV-FKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVieepgsdrGMVF 104
Cdd:cd03250 1 ISVEDAsFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--------AYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 105 QNytlfPWL---TVADNVAFGLK------------------LRGLSSG---EIKEQvfyylsivGLTqfakaypkqLSGG 160
Cdd:cd03250 73 QE----PWIqngTIRENILFGKPfdeeryekvikacalepdLEILPDGdltEIGEK--------GIN---------LSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 161 MKQRVAIARALANHPEVLLMDEPFGALDAQTREQ-MQQFFLELWEQtHITVLMITHDVEeavFLS--GRVYVM 230
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHiFENCILGLLLN-NKTRILVTHQLQ---LLPhaDQIVVL 200
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
44-219 |
6.79e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.72 E-value: 6.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE--PGSDRGMV---FQNYTLFPwLTVADN 118
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlkPEIYRQQVsycAQTPTLFG-DTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFGLKLRGLSSgeiKEQVFyylsIVGLTQFA------KAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTR 192
Cdd:PRK10247 101 LIFPWQIRNQQP---DPAIF----LDDLERFAlpdtilTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180
....*....|....*....|....*..
gi 2225592549 193 EQMQQFFLELWEQTHITVLMITHDVEE 219
Cdd:PRK10247 174 HNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-230 |
7.94e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 107.32 E-value: 7.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLKTnlsvLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG------EVIEE 95
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlrDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 96 PGSDR--------GMVFQNYT--LFPWLTVADNVafGLKLRGLSS---GEIKEQVFYYLSIVgltQFAKA----YPKQLS 158
Cdd:PRK11701 79 SEAERrrllrtewGFVHQHPRdgLRMQVSAGGNI--GERLMAVGArhyGDIRATAGDWLERV---EIDAAriddLPTTFS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2225592549 159 GGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-230 |
8.69e-28 |
|
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: 111.43 E-value: 8.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 23 QPKLEVEKVFKHFPHLKTNL-SVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQ--VLMNGEVIE--EPG 97
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDmtKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 98 SDR--------GMVFQNYTLFPWLTVADNV--AFGLKLrglsSGEI-KEQVFYYLSIVGLTQfAKA------YPKQLSGG 160
Cdd:TIGR03269 357 PDGrgrakryiGILHQEYDLYPHRTVLDNLteAIGLEL----PDELaRMKAVITLKMVGFDE-EKAeeildkYPDELSEG 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 161 MKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM 501
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
25-239 |
1.00e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 108.25 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 25 KLEVEKVFKHF-PHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQV----------------- 86
Cdd:PRK13651 2 QIKVKNIVKIFnKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 87 -LMNGEVIEEPGSDR-----------GMVFQ--NYTLFPwLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQ-FAK 151
Cdd:PRK13651 82 kVLEKLVIQKTRFKKikkikeirrrvGVVFQfaEYQLFE-QTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 152 AYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHiTVLMITHDVEEAVFLSGRVYVMi 231
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFF- 238
|
....*....
gi 2225592549 232 aNPGR-IKD 239
Cdd:PRK13651 239 -KDGKiIKD 246
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
44-215 |
1.49e-27 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 106.08 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE--PGSDR---GMVFQNYTLFPwLTVADN 118
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlnLRWLRsqiGLVSQEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFGLklRGLSSGEIKE---QVFYYLSIVGL-----TQfAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQ 190
Cdd:cd03249 97 IRYGK--PDATDEEVEEaakKANIHDFIMSLpdgydTL-VGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180
....*....|....*....|....*
gi 2225592549 191 TREQMQQFFLELWEQThiTVLMITH 215
Cdd:cd03249 174 SEKLVQEALDRAMKGR--TTIVIAH 196
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
44-237 |
1.52e-27 |
|
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: 106.03 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGE--VIEEPGSDR---GMVFQNYTLFPwLTVADN 118
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlALADPAWLRrqvGVVLQENVLFN-RSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFGlklrglSSGEIKEQVFYYLSIVGLTQFAKAYPK-----------QLSGGMKQRVAIARALANHPEVLLMDEPFGAL 187
Cdd:cd03252 96 IALA------DPGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2225592549 188 DAQTREQMQQFFLELWEQThiTVLMITHDVeEAVFLSGRVYVMiaNPGRI 237
Cdd:cd03252 170 DYESEHAIMRNMHDICAGR--TVIIIAHRL-STVKNADRIIVM--EKGRI 214
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
46-215 |
2.00e-27 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 104.89 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 46 EDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDrgmvFQNYTLF--------PWLTVAD 117
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE----YHQDLLYlghqpgikTELTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFGLKLRGLSSgeiKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQ 197
Cdd:PRK13538 94 NLRFYQRLHGPGD---DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEA 170
|
170
....*....|....*...
gi 2225592549 198 FFLELWEQTHItVLMITH 215
Cdd:PRK13538 171 LLAQHAEQGGM-VILTTH 187
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
26-247 |
2.93e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 107.52 E-value: 2.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIP-P---SAGQVLMNGE---VIEEP-- 96
Cdd:PRK11022 4 LNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQdlqRISEKer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 97 ----GSDRGMVFQN--YTLFPWLTVADNVAFGLKL-RGLSSGEIKEQVFYYLSIVGLTQFAK---AYPKQLSGGMKQRVA 166
Cdd:PRK11022 84 rnlvGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASrldVYPHQLSGGMSQRVM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 167 IARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHD---VEEAvflSGRVYVMIA----NPGRIKD 239
Cdd:PRK11022 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlalVAEA---AHKIIVMYAgqvvETGKAHD 240
|
....*...
gi 2225592549 240 EFKIELPP 247
Cdd:PRK11022 241 IFRAPRHP 248
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
33-237 |
3.24e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 105.11 E-value: 3.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 33 KHFPHLKTNL-SVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVieePGSDR-------GMVF 104
Cdd:cd03267 24 KSLFKRKYREvEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV---PWKRRkkflrriGVVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 105 QNYTLFPW-LTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEP 183
Cdd:cd03267 101 GQKTQLWWdLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2225592549 184 FGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRvyVMIANPGRI 237
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARR--VLVIDKGRL 232
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
44-230 |
3.48e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 104.91 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE-PGSDR-----GMVFQNYTLFPWLTVAD 117
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKlPPHERaragiAYVPQGREIFPRLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFGLKLRGLSSGEIKEQVFYYLSIvgLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQ 197
Cdd:TIGR03410 95 NLLTGLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGR 172
|
170 180 190
....*....|....*....|....*....|...
gi 2225592549 198 FFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:TIGR03410 173 VIRRLRAEGGMAILLVEQYLDFARELADRYYVM 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-240 |
5.46e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 105.84 E-value: 5.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPhlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG----EVIEEPGSDR- 100
Cdd:PRK13644 2 IRLENVSYSYP---DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgDFSKLQGIRKl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 -GMVFQN-YTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVL 178
Cdd:PRK13644 79 vGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2225592549 179 LMDEPFGALDAQTREQMQQFFLELWEQTHiTVLMITHDVEEaVFLSGRVYVMiaNPGRIKDE 240
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEE-LHDADRIIVM--DRGKIVLE 216
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
44-215 |
2.61e-26 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 102.69 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGevieEPGSDR---------GMVFQNYTLFPWlT 114
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDG----IDIRDIsrkslrsmiGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 115 VADNVAFGlklrglSSGEIKEQVFYYLSIVGLTQFAKAYPK-----------QLSGGMKQRVAIARALANHPEVLLMDEP 183
Cdd:cd03254 93 IMENIRLG------RPNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190
....*....|....*....|....*....|..
gi 2225592549 184 FGALDAQTREQMQQFFLELWEQThiTVLMITH 215
Cdd:cd03254 167 TSNIDTETEKLIQEALEKLMKGR--TSIIIAH 196
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
26-230 |
3.46e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.05 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKV-FKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR---- 100
Cdd:PRK13643 2 IKFEKVnYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 -----GMVFQ--NYTLFPWlTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLT-QFAKAYPKQLSGGMKQRVAIARALA 172
Cdd:PRK13643 82 vrkkvGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2225592549 173 NHPEVLLMDEPFGALDAQTREQMQQFFlELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLF-ESIHQSGQTVVLVTHLMDDVADYADYVYLL 217
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
25-251 |
3.75e-26 |
|
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: 107.11 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 25 KLEVEKVFKHFPhlKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR---- 100
Cdd:TIGR02203 330 DVEFRNVTFRYP--GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrrq 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 -GMVFQNYTLFPwLTVADNVAFGlKLRGLSSGEIKEQvfyyLSIVGLTQFAKAYPK-----------QLSGGMKQRVAIA 168
Cdd:TIGR02203 408 vALVSQDVVLFN-DTIANNIAYG-RTEQADRAEIERA----LAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 169 RALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQThiTVLMITH---DVEEAvflsGRVYVMiaNPGRIkdefkIEL 245
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHrlsTIEKA----DRIVVM--DDGRI-----VER 548
|
....*.
gi 2225592549 246 PPERDL 251
Cdd:TIGR02203 549 GTHNEL 554
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-191 |
4.30e-26 |
|
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: 101.96 E-value: 4.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 25 KLEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSA---GQVLMNGEVIEEPGSDR- 100
Cdd:cd03234 3 VLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQKc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 -GMVFQNYTLFPWLTVADNVAFGLKLRG--LSSGEIKEQV--FYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHP 175
Cdd:cd03234 83 vAYVRQDDILLPGLTVRETLTYTAILRLprKSSDAIRKKRveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDP 162
|
170
....*....|....*.
gi 2225592549 176 EVLLMDEPFGALDAQT 191
Cdd:cd03234 163 KVLILDEPTSGLDSFT 178
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
26-221 |
5.08e-26 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 101.92 E-value: 5.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKV-FKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE--PGSDR-- 100
Cdd:cd03253 1 IEFENVtFAYDPGRP----VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtLDSLRra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 -GMVFQNYTLFPwLTVADNVAFGlklrGLSSGEikEQVFYYLSIVGLTQFAKAYPKQ-----------LSGGMKQRVAIA 168
Cdd:cd03253 77 iGVVPQDTVLFN-DTIGYNIRYG----RPDATD--EEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 169 RALANHPEVLLMDEPFGALDAQTREQMQQFFLELweQTHITVLMITHDVEEAV 221
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIV 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-244 |
5.61e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.26 E-value: 5.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 24 PKLEVEkvfkhfphlktNLSV---LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEePGS-- 98
Cdd:COG1129 255 VVLEVE-----------GLSVggvVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR-IRSpr 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 99 ---DRGMVF-----QNYTLFPWLTVADNVAFGL-----KLRGLSSGEIKEQVFYY---LSIV--GLTQFAKaypkQLSGG 160
Cdd:COG1129 323 daiRAGIAYvpedrKGEGLVLDLSIRENITLASldrlsRGGLLDRRRERALAEEYikrLRIKtpSPEQPVG----NLSGG 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 161 MKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQThITVLMITHDVEEAVFLSGRVYVMiaNPGRIKDE 240
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEG-KAVIVISSELPELLGLSDRILVM--REGRIVGE 475
|
....
gi 2225592549 241 FKIE 244
Cdd:COG1129 476 LDRE 479
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
44-223 |
9.99e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.53 E-value: 9.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNgevieePGSDRGMVFQNYTLFPWLTVADNVAFGL 123
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------KGLRIGYLPQEPPLDDDLTVLDTVLDGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 124 K-LRGL-------------SSGEIKEQVFYY------------------LSIVGLTQFAKAYP-KQLSGGMKQRVAIARA 170
Cdd:COG0488 87 AeLRALeaeleeleaklaePDEDLERLAELQeefealggweaearaeeiLSGLGFPEEDLDRPvSELSGGWRRRVALARA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 171 LANHPEVLLMDEPFGALDAQTREQMQQFFLelweQTHITVLMITHDVEeavFL 223
Cdd:COG0488 167 LLSEPDLLLLDEPTNHLDLESIEWLEEFLK----NYPGTVLVVSHDRY---FL 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
45-230 |
1.38e-25 |
|
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: 105.87 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEP----GSDRGMVFQNYTLFPWLTVADNVA 120
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNldavRQSLGMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 121 FGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFL 200
Cdd:TIGR01257 1026 FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190
....*....|....*....|....*....|
gi 2225592549 201 ELweQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:TIGR01257 1106 KY--RSGRTIIMSTHHMDEADLLGDRIAII 1133
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-220 |
1.84e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 101.28 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 43 SVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIE-----------EPGSDRGMVFQNYTLFP 111
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqidaiKLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 112 WLTVADNVAFGLKLRGLSSG-EIKEQVFYYLSIVGLTQFA----KAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGA 186
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190
....*....|....*....|....*....|....
gi 2225592549 187 LDAQTREQMQQFFLELweQTHITVLMITHDVEEA 220
Cdd:PRK14246 184 IDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQV 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
44-215 |
2.90e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 99.18 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDRGMVF---QNyTLFPWLTVADNVA 120
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYlghRN-AMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 121 FGLKLRGLSSGEIKEQvfyyLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTreqmQQFFL 200
Cdd:PRK13539 96 FWAAFLGGEELDIAAA----LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA----VALFA 167
|
170
....*....|....*....
gi 2225592549 201 ELWeQTHI----TVLMITH 215
Cdd:PRK13539 168 ELI-RAHLaqggIVIAATH 185
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
23-230 |
2.93e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 100.86 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 23 QPKLEVEKVFKHFPHLKTnlsvLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLI---PPSAGQVLMNGEVIEEPG-- 97
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQA----LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 98 --------SDRGMVFQNYTLFPWLTVADNVAFGLK---------LRGLSSGEiKEQVFYYLSIVGLTQFAKAYPKQLSGG 160
Cdd:PRK09984 78 ardirksrANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQ-KQRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 161 MKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
26-251 |
4.38e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.58 E-value: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFphlKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPG-----SDR 100
Cdd:PRK13647 5 IEVEDLHFRY---KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENekwvrSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 GMVFQNY--TLFPwLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVL 178
Cdd:PRK13647 82 GLVFQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 179 LMDEPFGALDAQTREQMQQFFLELWEQTHiTVLMITHDVEEAVflSGRVYVMIANPGRIKDEFKIELPPERDL 251
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAA--EWADQVIVLKEGRVLAEGDKSLLTDEDI 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
23-230 |
6.45e-25 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 99.05 E-value: 6.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 23 QPKLEVEKVFKHFP-HLK--TNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMN--GEVIEEPG 97
Cdd:COG4778 2 TTLLEVENLSKTFTlHLQggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 98 -SDR----------GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQ-FAKAYPKQLSGGMKQRV 165
Cdd:COG4778 82 aSPReilalrrrtiGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPErLWDLPPATFSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2225592549 166 AIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELwEQTHITVLMITHDVE--EAVflSGRVYVM 230
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEvrEAV--ADRVVDV 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
42-230 |
6.62e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.08 E-value: 6.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 42 LSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQV----LMNGEVIEEPGSDR----------------- 100
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITnpyskkiknfkelrrrv 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 GMVFQ--NYTLFPwLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGL-TQFAKAYPKQLSGGMKQRVAIARALANHPEV 177
Cdd:PRK13631 119 SMVFQfpEYQLFK-DTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 178 LLMDEPFGALDAQTREQMQQFFLELWEQTHiTVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVM 249
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
44-230 |
8.09e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 99.70 E-value: 8.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEpgSDRGM---------VFQN--YTLFpW 112
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY--SKRGLlalrqqvatVFQDpeQQIF-Y 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 113 LTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTR 192
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 2225592549 193 EQMQQFFLELWEQTHiTVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK13638 173 TQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVL 209
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
27-217 |
9.13e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 99.00 E-value: 9.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 27 EVEKVFKHFphlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG-EVIEEPGSDRGMVF- 104
Cdd:COG4604 3 EIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGlDVATTPSRELAKRLa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 105 ---QNYTLFPWLTVADNVAFGlklR-----GLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPE 176
Cdd:COG4604 79 ilrQENHINSRLTVRELVAFG---RfpyskGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2225592549 177 VLLMDEPFGALD-AQTREQMQQffL-ELWEQTHITVLMITHDV 217
Cdd:COG4604 156 YVLLDEPLNNLDmKHSVQMMKL--LrRLADELGKTVVIVLHDI 196
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
44-215 |
1.03e-24 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 97.81 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE--PGSDRGMVFQNYT--LFPWLTVADNV 119
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEqrDEPHENILYLGHLpgLKPELSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 120 AFglkLRGLSSGEiKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFF 199
Cdd:TIGR01189 95 HF---WAAIHGGA-QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
170
....*....|....*.
gi 2225592549 200 LELWEQTHItVLMITH 215
Cdd:TIGR01189 171 RAHLARGGI-VLLTTH 185
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
45-251 |
1.70e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.05 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR---------GMVFQnytlFPWL-- 113
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqirkkvGLVFQ----FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 114 ---TVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQ--FAKAyPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALD 188
Cdd:PRK13649 99 feeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEslFEKN-PFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2225592549 189 AQTREQMQQFFLELwEQTHITVLMITHDVEEAVFLSGRVYVM----IANPGRIKDEF-KIELPPERDL 251
Cdd:PRK13649 178 PKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLekgkLVLSGKPKDIFqDVDFLEEKQL 244
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
44-230 |
1.87e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 100.29 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEviEEPGSDR------GMVFQNYTLFPWLTVAD 117
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV--PVPARARlarariGVVPQFDNLDLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 N-VAFGlKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQmq 196
Cdd:PRK13536 134 NlLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL-- 210
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2225592549 197 qffleLWEQTH------ITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK13536 211 -----IWERLRsllargKTILLTTHFMEEAERLCDRLCVL 245
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-237 |
1.94e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.57 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIaGLIPPSAGQVLMNGEV-------------IEEPGSDRGMVFQNYTLF 110
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVeffnqniyerrvnLNRLRRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 111 PwLTVADNVAFGLKLRG--------------LSSGEIKEQVFYYLSIVGLtqfakaypkQLSGGMKQRVAIARALANHPE 176
Cdd:PRK14258 101 P-MSVYDNVAYGVKIVGwrpkleiddivesaLKDADLWDEIKHKIHKSAL---------DLSGGQQQRLCIARALAVKPK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2225592549 177 VLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMIANPGRI 237
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRI 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
42-215 |
2.40e-24 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 96.79 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 42 LSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE--PGSDRGMVFQNYT--LFPWLTVAD 117
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFqrDSIARGLLYLGHApgIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFglkLRGLSSgeiKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQ 197
Cdd:cd03231 93 NLRF---WHADHS---DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
170
....*....|....*...
gi 2225592549 198 FFLELWEQTHItVLMITH 215
Cdd:cd03231 167 AMAGHCARGGM-VVLTTH 183
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-230 |
9.81e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.78 E-value: 9.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKS-TLLNIIAGLIPPSA----GQVLMNGEVI--- 93
Cdd:PRK15134 2 TQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLlha 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 94 EEP------GSDRGMVFQN--YTLFPWLTVADNVAFGLKL-RGLSSGEIKEQVFYYLSIVGLTQFAK---AYPKQLSGGM 161
Cdd:PRK15134 82 SEQtlrgvrGNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKrltDYPHQLSGGE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2225592549 162 KQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
45-230 |
1.13e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 97.00 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLM-------NGEVIEEPGSDR---GMVFQ--NYTLFPw 112
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipaNLKKIKEVKRLRkeiGLVFQfpEYQLFQ- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 113 LTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQ-FAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQT 191
Cdd:PRK13645 106 ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 2225592549 192 REQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
45-254 |
1.88e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.39 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR---------GMVFQnytlFPWL-- 113
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpvrkriGMVFQ----FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 114 ---TVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQ-FAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDA 189
Cdd:PRK13646 99 fedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 190 QTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRIKDE---------------FKIELPP----ERD 250
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVM--KEGSIVSQtspkelfkdkkkladWHIGLPEivqlQYD 256
|
....
gi 2225592549 251 LEIK 254
Cdd:PRK13646 257 FEQK 260
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
26-230 |
3.70e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 95.24 E-value: 3.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHL-----KTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIE----EP 96
Cdd:PRK15112 5 LEVRNLSKTFRYRtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 97 GSDR-GMVFQN--YTLFPWLTVADNVAFGLKLR-GLSSGEIKEQVFYYLSIVGL-TQFAKAYPKQLSGGMKQRVAIARAL 171
Cdd:PRK15112 85 RSQRiRMIFQDpsTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2225592549 172 ANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK15112 165 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVM 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
41-215 |
6.33e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.87 E-value: 6.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 41 NLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPG-----SDRGMVFQNYTLFPWlTV 115
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhhylhRQVALVGQEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 116 ADNVAFGLKLRGlssgeiKEQVFYYLSIVGLTQFAKAYPK-----------QLSGGMKQRVAIARALANHPEVLLMDEPF 184
Cdd:TIGR00958 572 RENIAYGLTDTP------DEEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190
....*....|....*....|....*....|.
gi 2225592549 185 GALDAQTreqmQQFFLELWEQTHITVLMITH 215
Cdd:TIGR00958 646 SALDAEC----EQLLQESRSRASRTVLLIAH 672
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
44-215 |
8.60e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.19 E-value: 8.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMngevieePGSDRgMVF---QNYtlFPWLTVADNVA 120
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR-------PAGAR-VLFlpqRPY--LPLGTLREALL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 121 FGLKLRGLSSGEIKEqvfyYLSIVGLTQFA------KAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQ 194
Cdd:COG4178 448 YPATAEAFSDAELRE----ALEAVGLGHLAerldeeADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAA 523
|
170 180
....*....|....*....|.
gi 2225592549 195 MQQFFLElwEQTHITVLMITH 215
Cdd:COG4178 524 LYQLLRE--ELPGTTVISVGH 542
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-215 |
1.15e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 96.82 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 14 SSQTGETFSQPKLEVEKVfkHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI 93
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 94 EE--PGSDRGM---VFQNYTLFPwLTVADNVAFGLKLrglSSGEIKEQVfyyLSIVGLTQFAKAYP----------KQLS 158
Cdd:PRK11160 405 ADysEAALRQAisvVSQRVHLFS-ATLRDNLLLAAPN---ASDEALIEV---LQQVGLEKLLEDDKglnawlgeggRQLS 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2225592549 159 GGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEqtHITVLMITH 215
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH 532
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
26-216 |
1.28e-22 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 90.59 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPhlktNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVlmngevieepgsdrgmvfq 105
Cdd:cd03221 1 IELENLSKTYG----GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 106 nytlfpwlTVADNVAFGlklrglssgeikeqvfyYLSivgltqfakaypkQLSGGMKQRVAIARALANHPEVLLMDEPFG 185
Cdd:cd03221 58 --------TWGSTVKIG-----------------YFE-------------QLSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190
....*....|....*....|....*....|.
gi 2225592549 186 ALDAQTREQMQQFFLELweqtHITVLMITHD 216
Cdd:cd03221 100 HLDLESIEALEEALKEY----PGTVILVSHD 126
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-230 |
2.51e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 96.08 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 15 SQTGETFSQPKLEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQV-------- 86
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 87 LMNGEVIEEP-----------GSDRGMVFQN--YTLFPWLTVADNVAFGLKL-RGLSSGEIKEQVFYYLSIVGLTQ---F 149
Cdd:PRK10261 82 RRSRQVIELSeqsaaqmrhvrGADMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEaqtI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 150 AKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYV 229
Cdd:PRK10261 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLV 241
|
.
gi 2225592549 230 M 230
Cdd:PRK10261 242 M 242
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-236 |
4.65e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 93.25 E-value: 4.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPS---AGQVLMNG-EVIEEPG 97
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGrEILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 98 SD----RG----MVFQN--YTLFPWLTVADNVAFGLKL-RGLSSGEIKEQVFYYLSIVGLTQFAK---AYPKQLSGGMKQ 163
Cdd:PRK09473 89 KElnklRAeqisMIFQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKrmkMYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 164 RVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMIAnpGR 236
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA--GR 239
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
45-259 |
6.48e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 92.84 E-value: 6.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVieePGSDR-------GMVF-QNYTLFPWLTVA 116
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV---PFKRRkefarriGVVFgQRSQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 117 DNvaFGL--KLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQ 194
Cdd:COG4586 115 DS--FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 195 MQQFFLELWEQTHITVLMITH---DVEEavfLSGRVyVMIANpGRI-----KDEFKIELPPERDLEIKMSEDF 259
Cdd:COG4586 193 IREFLKEYNRERGTTILLTSHdmdDIEA---LCDRV-IVIDH-GRIiydgsLEELKERFGPYKTIVLELAEPV 260
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-218 |
8.85e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.39 E-value: 8.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLKTNL-------SVLEDINIQVYPNEFVSIVGASGCGKST----LLNIIAglippSAGQVLMNG 90
Cdd:PRK15134 272 ASPLLDVEQLQVAFPIRKGILkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 91 EVIEEpGSDRGM---------VFQ--NYTLFPWLTVADNVAFGLKL--RGLSSGEIKEQVFYYLSIVGLTQFAKA-YPKQ 156
Cdd:PRK15134 347 QPLHN-LNRRQLlpvrhriqvVFQdpNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETRHrYPAE 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2225592549 157 LSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVE 218
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLH 487
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
48-219 |
1.08e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 94.14 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 48 INIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPpSAGQVLMNGevIE----EPGSDR---GMVFQNYTLFPWlTVADNVA 120
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKING--IElrelDPESWRkhlSWVGQNPQLPHG-TLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 121 FGlklRGLSSGEIKEQVfyyLSIVGLTQFAKAYPK-----------QLSGGMKQRVAIARALANHPEVLLMDEPFGALDA 189
Cdd:PRK11174 445 LG---NPDASDEQLQQA---LENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190
....*....|....*....|....*....|
gi 2225592549 190 QTREQMQQFFLELWEQThiTVLMITHDVEE 219
Cdd:PRK11174 519 HSEQLVMQALNAASRRQ--TTLMVTHQLED 546
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
26-239 |
1.40e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVlmngevieEPGSDrgmVFQ 105
Cdd:COG0488 316 LELEGLSKSYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------KLGET---VKI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 106 NY------TLFPWLTVADNvafglkLRGLSSGEIKEQVFYYLSIVGLT---QFAKAypKQLSGGMKQRVAIARALANHPE 176
Cdd:COG0488 381 GYfdqhqeELDPDKTVLDE------LRDGAPGGTEQEVRGYLGRFLFSgddAFKPV--GVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2225592549 177 VLLMDEPFGALDAQTREQMQQfFLELWEQthiTVLMITHDVEeavFLSG---RVYVMiaNPGRIKD 239
Cdd:COG0488 453 VLLLDEPTNHLDIETLEALEE-ALDDFPG---TVLLVSHDRY---FLDRvatRILEF--EDGGVRE 509
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
41-220 |
1.74e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.82 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 41 NLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR-----GMVFQNYTLFPWLTV 115
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvarriGLLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 116 ADNVAFG----LKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQT 191
Cdd:PRK10253 99 QELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180
....*....|....*....|....*....
gi 2225592549 192 REQMQQFFLELWEQTHITVLMITHDVEEA 220
Cdd:PRK10253 179 QIDLLELLSELNREKGYTLAAVLHDLNQA 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
34-215 |
1.99e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 88.52 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 34 HFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR----GMVFQNYTL 109
Cdd:cd03247 7 SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALssliSVLNQRPYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 110 FPwLTVADNVAfglklrglssgeikeqvfyylsivgltqfakaypKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDA 189
Cdd:cd03247 87 FD-TTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180
....*....|....*....|....*..
gi 2225592549 190 QT-REQMQQFFLELWEQthiTVLMITH 215
Cdd:cd03247 132 ITeRQLLSLIFEVLKDK---TLIWITH 155
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
40-218 |
3.32e-21 |
|
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: 88.93 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 40 TNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDRGMVFQNYTLF-----PWL- 113
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAyaaqkPWLl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 114 --TVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGL-----TQFAKAyPKQLSGGMKQRVAIARALANHPEVLLMDEPFGA 186
Cdd:cd03290 92 naTVEENITFGSPFNKQRYKAVTDACSLQPDIDLLpfgdqTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190
....*....|....*....|....*....|...
gi 2225592549 187 LDAQTREQ-MQQFFLELWEQTHITVLMITHDVE 218
Cdd:cd03290 171 LDIHLSDHlMQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
44-230 |
3.42e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.57 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIE-EPGSDR-----GMVFQNYTLFPWLTVAD 117
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISlLPLHARarrgiGYLPQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFGLKLR-GLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQ 196
Cdd:PRK10895 98 NLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIK 177
|
170 180 190
....*....|....*....|....*....|....
gi 2225592549 197 QfFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK10895 178 R-IIEHLRDSGLGVLITDHNVRETLAVCERAYIV 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
23-216 |
5.88e-21 |
|
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: 91.73 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 23 QPKLEVEKVFKHFPHlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI-----EEPG 97
Cdd:COG4618 328 KGRLSVENLTVVPPG--SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwdrEELG 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 98 SDRGMVFQNYTLFPWlTVADNVA-FGlklrglssgEIK-EQVFYYLSIVGL----TQFAKAY-------PKQLSGGMKQR 164
Cdd:COG4618 406 RHIGYLPQDVELFDG-TIAENIArFG---------DADpEKVVAAAKLAGVhemiLRLPDGYdtrigegGARLSGGQRQR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2225592549 165 VAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQtHITVLMITHD 216
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHR 526
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
24-241 |
6.28e-21 |
|
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: 87.93 E-value: 6.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 24 PKLEVEKV-FKHFPHLKTnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPG----- 97
Cdd:cd03244 1 GDIEFKNVsLRYRPNLPP---VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGlhdlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 98 SDRGMVFQNYTLFPWlTVADNVA-FGLKlrglSSGEIKEqvfyYLSIVGLTQFAKAYPKQL-----------SGGMKQRV 165
Cdd:cd03244 78 SRISIIPQDPVLFSG-TIRSNLDpFGEY----SDEELWQ----ALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 166 AIARALANHPEVLLMDEPFGALDAQTREQMQQ----FFlelweqTHITVLMITHDVeEAVFLSGRVYVMiaNPGRIKdEF 241
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKtireAF------KDCTVLTIAHRL-DTIIDSDRILVL--DKGRVV-EF 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
27-220 |
8.16e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 87.71 E-value: 8.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 27 EVEKVFKHF--PHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIP--PSAGQVlmngEVIEEP-GSDRg 101
Cdd:COG2401 26 RVAIVLEAFgvELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCV----DVPDNQfGREA- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 102 mvfqnytlfpwlTVADNVAfglklrglSSGEIKeQVFYYLSIVGLT--QFAKAYPKQLSGGMKQRVAIARALANHPEVLL 179
Cdd:COG2401 101 ------------SLIDAIG--------RKGDFK-DAVELLNAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2225592549 180 MDEpFGA-LDAQTREQMQQFFLELWEQTHITVLMITH--DVEEA 220
Cdd:COG2401 160 IDE-FCShLDRQTAKRVARNLQKLARRAGITLVVATHhyDVIDD 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
26-263 |
2.51e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.86 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGL--IPPSAGQVLMNGEVIE-----EPGS 98
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEkcgyvERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 99 DRG----------------------------------MVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKEQVFYYLSIV 144
Cdd:TIGR03269 77 KVGepcpvcggtlepeevdfwnlsdklrrrirkriaiMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 145 GLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITH-------DV 217
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpeviedLS 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2225592549 218 EEAVFLSGRVYVMIANPGRIKDEFKIELP-PERDLEIKMSEDFWQIK 263
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVAVFMEGVSeVEKECEVEVGEPIIKVR 283
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
38-237 |
3.22e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 87.06 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 38 LKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPP----SAGQVLMNGEVIEePGSDRG----MVFQN-YT 108
Cdd:PRK10418 12 LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVA-PCALRGrkiaTIMQNpRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 109 LF-PWLTVADNVAFGLKLRGLSSGEikEQVFYYLSIVGLT---QFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPF 184
Cdd:PRK10418 91 AFnPLHTMHTHARETCLALGKPADD--ATLTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2225592549 185 GALD--AQTReqmqqfFLELWE---QTH-ITVLMITHDVEEAVFLSGRVYVMIAnpGRI 237
Cdd:PRK10418 169 TDLDvvAQAR------ILDLLEsivQKRaLGMLLVTHDMGVVARLADDVAVMSH--GRI 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
44-215 |
3.24e-20 |
|
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: 84.90 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMngevieePGSDRgmvfqnyTLF----PWLTVadnv 119
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-------PEGED-------LLFlpqrPYLPL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 120 afglklrglssGEIKEQVfyylsivgltqfakAYP--KQLSGGMKQRVAIARALANHPEVLLMDEPFGALDaqtrEQMQQ 197
Cdd:cd03223 78 -----------GTLREQL--------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESED 128
|
170
....*....|....*...
gi 2225592549 198 FFLELWEQTHITVLMITH 215
Cdd:cd03223 129 RLYQLLKELGITVISVGH 146
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
44-215 |
4.90e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 89.39 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPG-----SDRGMVFQNYTLFPwLTVADN 118
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsvlrQGVAMVQQDPVVLA-DTFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFGlklRGLSsgeiKEQVFYYLSIVGLTQFAKAYPK-----------QLSGGMKQRVAIARALANHPEVLLMDEPFGAL 187
Cdd:PRK10790 435 VTLG---RDIS----EEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANI 507
|
170 180
....*....|....*....|....*...
gi 2225592549 188 DAQTREQMQQFFLELWEQThiTVLMITH 215
Cdd:PRK10790 508 DSGTEQAIQQALAAVREHT--TLVVIAH 533
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-244 |
3.74e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.62 E-value: 3.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 24 PKLEVEkvfkhfphlktNLSV--------LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE 95
Cdd:COG3845 256 VVLEVE-----------NLSVrddrgvpaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 96 PGS----DRGMVF-----QNYTLFPWLTVADNVAFGL-------KLRGLSSGEIKEQV------FyylSIVGLTQFAKAy 153
Cdd:COG3845 325 LSPrerrRLGVAYipedrLGRGLVPDMSVAENLILGRyrrppfsRGGFLDRKAIRAFAeelieeF---DVRTPGPDTPA- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 154 pKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQThITVLMITHDVEEAVFLSGRVYVMiaN 233
Cdd:COG3845 401 -RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAG-AAVLLISEDLDEILALSDRIAVM--Y 476
|
250
....*....|.
gi 2225592549 234 PGRIKDEFKIE 244
Cdd:COG3845 477 EGRIVGEVPAA 487
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-244 |
3.89e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.38 E-value: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 43 SVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAG-----QVLMNGEVI------EEPGSDRGMVFQNYTLFP 111
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyrdvLEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 112 wLTVADNVAFGLKLRGL-SSGEIKEQVFYYLSIVGLTQFAKA----YPKQLSGGMKQRVAIARALANHPEVLLMDEPFGA 186
Cdd:PRK14271 115 -MSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLWDAVKDrlsdSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2225592549 187 LDAQTREQMQQFFLELWEQthITVLMITHDVEEAVFLSGRVYVMIanPGRIKDEFKIE 244
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFF--DGRLVEEGPTE 247
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
47-230 |
1.11e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.10 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 47 DINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGS----DRGMVF-----QNYTLF-----PW 112
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlARGLVYlpedrQSSGLYldaplAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 113 ----LTVADNvafGLKLRGLSSGEIKEQVFYYLSI--VGLTQFAKAypkqLSGGMKQRVAIARALANHPEVLLMDEPFGA 186
Cdd:PRK15439 361 nvcaLTHNRR---GFWIKPARENAVLERYRRALNIkfNHAEQAART----LSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2225592549 187 LDAQTREQMQQFFLELWEQtHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVM 476
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
43-239 |
1.32e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.51 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 43 SVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIE-----EPGSDRGMVFQNYTLFPWLTVAD 117
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEalsarAASRRVASVPQDTSLSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFGL---KLRGLSSGEIKEQ-VFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTRE 193
Cdd:PRK09536 97 VVEMGRtphRSRFDTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQV 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2225592549 194 QMQQFFLELWEqTHITVLMITHDVEEAVFLSGRVyVMIANpGRIKD 239
Cdd:PRK09536 177 RTLELVRRLVD-DGKTAVAAIHDLDLAARYCDEL-VLLAD-GRVRA 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
44-216 |
2.62e-18 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 84.22 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSagqvlmNGEVIEEPGSDRGMVFQNYTLFPWLTVADNVAFGL 123
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDF------NGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 124 klrglssGEIKEQVFYYLSIVGL-----TQFAKAYPKQ-------------------------------------LSGGM 161
Cdd:TIGR03719 94 -------AEIKDALDRFNEISAKyaepdADFDKLAAEQaelqeiidaadawdldsqleiamdalrcppwdadvtkLSGGE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2225592549 162 KQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELweqtHITVLMITHD 216
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY----PGTVVAVTHD 217
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
43-220 |
2.63e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.60 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 43 SVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSD---RGMVF--QNYTLFPWLTVAD 117
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRqlaRRLALlpQHHLTPEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFG----LKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTRE 193
Cdd:PRK11231 96 LVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQV 175
|
170 180
....*....|....*....|....*....
gi 2225592549 194 QMQQFFLELWEQ--THITVLmitHDVEEA 220
Cdd:PRK11231 176 ELMRLMRELNTQgkTVVTVL---HDLNQA 201
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
44-215 |
3.20e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 84.10 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE--PGSDR---GMVFQNYTLFPwLTVADN 118
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvtQASLRaaiGIVPQDTVLFN-DTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFGlklR-GLSSGEIKE-----QvfyylsivgLTQFAKAYPKQ-----------LSGGMKQRVAIARALANHPEVLLMD 181
Cdd:COG5265 452 IAYG---RpDASEEEVEAaaraaQ---------IHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFD 519
|
170 180 190
....*....|....*....|....*....|....
gi 2225592549 182 EPFGALDAQTrEQMQQFFLELWEQTHiTVLMITH 215
Cdd:COG5265 520 EATSALDSRT-ERAIQAALREVARGR-TTLVIAH 551
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-215 |
3.29e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.94 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 25 KLEVEKVFKHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPS---AGQVLMNGEVIEEPGSDR- 100
Cdd:TIGR00955 21 KQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 -GMVFQNYTLFPWLTVADNVAFGLKLR---GLSSGEIKEQVFYYLSIVGLTQFAK------AYPKQLSGGMKQRVAIARA 170
Cdd:TIGR00955 101 sAYVQQDDLFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2225592549 171 LANHPEVLLMDEPFGALDAQTREQMQQFFLELwEQTHITVLMITH 215
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIH 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-215 |
7.13e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 82.76 E-value: 7.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 5 LFAIDSLDLSSQTGetfsqpKLEVEKV-----FKH--FPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAG 77
Cdd:PRK11176 318 LFAILDLEQEKDEG------KRVIERAkgdieFRNvtFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 78 LIPPSAGQVLMNGEVIEE--PGSDR---GMVFQNYTLFPwLTVADNVAFGLKLRgLSSGEIKE--QVFYYLSIV-----G 145
Cdd:PRK11176 392 FYDIDEGEILLDGHDLRDytLASLRnqvALVSQNVHLFN-DTIANNIAYARTEQ-YSREQIEEaaRMAYAMDFInkmdnG 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 146 LTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELweQTHITVLMITH 215
Cdd:PRK11176 470 LDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAH 537
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
44-217 |
8.74e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.16 E-value: 8.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGqvlmngeVIEEPGSDR-GMVFQNYTLFPwlTVADNVAFG 122
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-------VIKRNGKLRiGYVPQKLYLDT--TLPLTVNRF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 123 LKLRGlssGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLEL 202
Cdd:PRK09544 90 LRLRP---GTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQL 166
|
170
....*....|....*
gi 2225592549 203 WEQTHITVLMITHDV 217
Cdd:PRK09544 167 RRELDCAVLMVSHDL 181
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
45-227 |
1.13e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 82.32 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPG--SDR---GMVFQNYTLFPwLTVADNV 119
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTraSLRrniAVVFQDAGLFN-RSIEDNI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 120 AFGLKlrGLSSGEIKEQV-------FYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTR 192
Cdd:PRK13657 430 RVGRP--DATDEEMRAAAeraqahdFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2225592549 193 EQMQQFFLELWEQThiTVLMITH---DVEEA----VFLSGRV 227
Cdd:PRK13657 508 AKVKAALDELMKGR--TTFIIAHrlsTVRNAdrilVFDNGRV 547
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
40-216 |
1.27e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.88 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 40 TNLSV---LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIpPSAGQVLMNGEVIEE-PGSD----RGMVFQNYTLFP 111
Cdd:COG4138 4 NDVAVagrLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwSAAElarhRAYLSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 112 WLTVADNVAfgLKLRGLSSGEIKEQVFYYLSivGLTQFAKAYPK---QLSGGMKQRVAIARALAN-HPEV------LLMD 181
Cdd:COG4138 83 AMPVFQYLA--LHQPAGASSEAVEQLLAQLA--EALGLEDKLSRpltQLSGGEWQRVRLAAVLLQvWPTInpegqlLLLD 158
|
170 180 190
....*....|....*....|....*....|....*
gi 2225592549 182 EPFGALDAQTREQMQQFFLELWEQThITVLMITHD 216
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELCQQG-ITVVMSSHD 192
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-229 |
1.44e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.88 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLKTnlsvLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVieepgsdrg 101
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKA----LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 102 MVFQNYT---------------LFPWLTVADNVAFG-LKLRG--LSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQ 163
Cdd:PRK11288 68 MRFASTTaalaagvaiiyqelhLVPEMTVAENLYLGqLPHKGgiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2225592549 164 RVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHItVLMITHDVEEAVFLSGRVYV 229
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITV 212
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
43-230 |
3.00e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.08 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 43 SVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPS--AGQVLMNGEVIEEPGSDR-GMVFQNYTLFPWLTVADNV 119
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKRtGFVTQDDILYPHLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 120 AFGLKLRGLSSGEIKEQVFYYLSIV---GLTQ-----FAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQT 191
Cdd:PLN03211 162 VFCSLLRLPKSLTKQEKILVAESVIselGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180 190
....*....|....*....|....*....|....*....
gi 2225592549 192 REQMQQFFLELwEQTHITVLMITHDVeeavflSGRVYVM 230
Cdd:PLN03211 242 AYRLVLTLGSL-AQKGKTIVTSMHQP------SSRVYQM 273
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
16-230 |
3.83e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 16 QTGETFSQPKLEVEKVFKHFphlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEE 95
Cdd:PRK15439 2 QTSDTTAPPLLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 96 --PGSDRGM----VFQNYTLFPWLTVADNVAFGLKLRGLSSGEikeqvfyylsivgLTQFAKAYPKQLSGGMK------- 162
Cdd:PRK15439 78 ltPAKAHQLgiylVPQEPLLFPNLSVKENILFGLPKRQASMQK-------------MKQLLAALGCQLDLDSSagsleva 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2225592549 163 --QRVAIARALANHPEVLLMDEPFGALD-AQTREQMQQffLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK15439 145 drQIVEILRGLMRDSRILILDEPTASLTpAETERLFSR--IRELLAQGVGIVFISHKLPEIRQLADRISVM 213
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
60-220 |
5.93e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.29 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 60 IVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSD---RGMVF--QNYTLFPWLTVADNVAFGlklR-------G 127
Cdd:PRK10575 42 LIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafaRKVAYlpQQLPAAEGMTVRELVAIG---RypwhgalG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 128 LSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTH 207
Cdd:PRK10575 119 RFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERG 198
|
170
....*....|...
gi 2225592549 208 ITVLMITHDVEEA 220
Cdd:PRK10575 199 LTVIAVLHDINMA 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
44-220 |
1.51e-16 |
|
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: 79.01 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEpgSDRGMVFQNYTLFPWL------TVAD 117
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD--IDRHTLRQFINYLPQEpyifsgSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFGLKlRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQL-------SGGMKQRVAIARALANHPEVLLMDEPFGALDAQ 190
Cdd:TIGR01193 567 NLLLGAK-ENVSQDEIWAACEIAEIKDDIENMPLGYQTELseegssiSGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190
....*....|....*....|....*....|
gi 2225592549 191 TREQMQQFFLELweqTHITVLMITHDVEEA 220
Cdd:TIGR01193 646 TEKKIVNNLLNL---QDKTIIFVAHRLSVA 672
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-216 |
1.85e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 78.62 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 30 KVFKHFPHLKTnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSagqvlmNGEVIEEPGSDRGMVFQNYTL 109
Cdd:PRK11819 11 RVSKVVPPKKQ---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEF------EGEARPAPGIKVGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 110 FPWLTVADNVAFGLklrglssGEIKEQVFYYLSIVGL-----TQFAKAYPKQ---------------------------- 156
Cdd:PRK11819 82 DPEKTVRENVEEGV-------AEVKAALDRFNEIYAAyaepdADFDALAAEQgelqeiidaadawdldsqleiamdalrc 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2225592549 157 ---------LSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFlelwEQTHITVLMITHD 216
Cdd:PRK11819 155 ppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYPGTVVAVTHD 219
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
44-188 |
2.39e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 75.66 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDRGMVFQNY--TLFPWLTVADNVAF 121
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHlpGLKADLSTLENLHF 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2225592549 122 glkLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALD 188
Cdd:PRK13543 106 ---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-195 |
4.89e-16 |
|
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: 76.05 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 18 GETFSQPKLEVEK----------VFKHFPHLKTnlSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVL 87
Cdd:cd03291 18 GELLEKAKQENNDrkhssddnnlFFSNLCLVGA--PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 88 MNGEVIEEPGsdrgmvfqnytlFPWL---TVADNVAFglklrGLSSGEikeqvFYYLSIVGLTQFAK---AYPKQ----- 156
Cdd:cd03291 96 HSGRISFSSQ------------FSWImpgTIKENIIF-----GVSYDE-----YRYKSVVKACQLEEditKFPEKdntvl 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2225592549 157 ------LSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQM 195
Cdd:cd03291 154 geggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-230 |
5.38e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.13 E-value: 5.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 24 PKLEVEKVFKHFPHLKTnlsvLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGevIEEPGSDR--- 100
Cdd:PRK09700 4 PYISMAGIGKSFGPVHA----LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN--INYNKLDHkla 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 -----GMVFQNYTLFPWLTVADNVAFGL----KLRGLSS---GEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIA 168
Cdd:PRK09700 78 aqlgiGIIYQELSVIDELTVLENLYIGRhltkKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2225592549 169 RALANHPEVLLMDEPFGALdaqTREQMQQFFLEL--WEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMnqLRKEGTAIVYISHKLAEIRRICDRYTVM 218
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
39-198 |
6.25e-16 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 73.82 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 39 KTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIA-----GLIppsAGQVLMNGEVIEEPGSDR-GMVFQNYTLFPW 112
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGVI---TGEILINGRPLDKNFQRStGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 113 LTVADNVAFGLKLRGLSSGEikeqvfyylsivgltqfakaypkqlsggmKQRVAIARALANHPEVLLMDEPFGALDAQTR 192
Cdd:cd03232 94 LTVREALRFSALLRGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
....*.
gi 2225592549 193 EQMQQF 198
Cdd:cd03232 145 YNIVRF 150
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
25-215 |
2.02e-15 |
|
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: 72.83 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 25 KLEVEK-VFKHFPHLKtnlSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR--- 100
Cdd:cd03369 6 EIEVENlSVRYAPDLP---PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 101 --GMVFQNYTLFpwltvadnvafglklrglsSGEIK-----------EQVFYYLSIvgltqfaKAYPKQLSGGMKQRVAI 167
Cdd:cd03369 83 slTIIPQDPTLF-------------------SGTIRsnldpfdeysdEEIYGALRV-------SEGGLNLSQGQRQLLCL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2225592549 168 ARALANHPEVLLMDEPFGALDAQTREQMQQFFLElwEQTHITVLMITH 215
Cdd:cd03369 137 ARALLKRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAH 182
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
50-231 |
2.18e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 75.82 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 50 IQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDrgmVFQNYTLFPWLTVADNVAFG------- 122
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD---VHQNMGYCPQFDAIDDLLTGrehlyly 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 123 LKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLEL 202
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
|
170 180
....*....|....*....|....*....
gi 2225592549 203 WEQTHITVLMiTHDVEEAVFLSGRVYVMI 231
Cdd:TIGR01257 2117 IREGRAVVLT-SHSMEECEALCTRLAIMV 2144
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
23-230 |
4.07e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.60 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 23 QPKLEVEKVFKHFPHLKtnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDRGM 102
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQ----ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 103 ------VFQNYTLFPWLTVADNVAFGlklrglssGEIKEQVFYYLSIVGLTQ-FAKAYPKQ------LSGGMKQRVAIAR 169
Cdd:PRK11614 79 reavaiVPEGRRVFSRMTVEENLAMG--------GFFAERDQFQERIKWVYElFPRLHERRiqragtMSGGEQQMLAIGR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 170 ALANHPEVLLMDEPFGALDAQTreqMQQFF--LELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK11614 151 ALMSQPRLLLLDEPSLGLAPII---IQQIFdtIEQLREQGMTIFLVEQNANQALKLADRGYVL 210
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
12-236 |
1.18e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 73.28 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 12 DLSSQTGETFSQPKLEVEKVFKHFPHLKtnLSVLEDiniQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGE 91
Cdd:COG1245 328 EVHAPRREKEEETLVEYPDLTKSYGGFS--LEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 92 VIEEP---GSDRGMvfqnytlfpwlTVADNvafglkLRGLSSGEIkEQVFYYLSIV---GLTQFAKAYPKQLSGGMKQRV 165
Cdd:COG1245 403 ISYKPqyiSPDYDG-----------TVEEF------LRSANTDDF-GSSYYKTEIIkplGLEKLLDKNVKDLSGGELQRV 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2225592549 166 AIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVMIANPGR 236
Cdd:COG1245 465 AIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEGEPGV 535
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
33-215 |
1.33e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 73.21 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 33 KHFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI-----EEPGSDRGMVFQNY 107
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtklqlDSWRSRLAVVSQTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 108 TLFPwLTVADNVAFGlklRGLSSGEIKEQVFYYLS----IVGLTQfakAYPKQ-------LSGGMKQRVAIARALANHPE 176
Cdd:PRK10789 399 FLFS-DTVANNIALG---RPDATQQEIEHVARLASvhddILRLPQ---GYDTEvgergvmLSGGQKQRISIARALLLNAE 471
|
170 180 190
....*....|....*....|....*....|....*....
gi 2225592549 177 VLLMDEPFGALDAQTREQMQQfFLELWEQtHITVLMITH 215
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILH-NLRQWGE-GRTVIISAH 508
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
39-240 |
1.40e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 73.62 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 39 KTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPP-SAGQVLMNGEVIEEPGsdrgmvfqnytlFPWL---T 114
Cdd:PLN03130 627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGTVAYVPQ------------VSWIfnaT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 115 VADNVAFGLKLrglssgeikEQVFYYLSI--VGLTQFAKAYPK-----------QLSGGMKQRVAIARALANHPEVLLMD 181
Cdd:PLN03130 695 VRDNILFGSPF---------DPERYERAIdvTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFD 765
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2225592549 182 EPFGALDAQTREQMQQFFL--ELWEQTHITVLMITHdveeavFLSGRVYVMIANPGRIKDE 240
Cdd:PLN03130 766 DPLSALDAHVGRQVFDKCIkdELRGKTRVLVTNQLH------FLSQVDRIILVHEGMIKEE 820
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
44-237 |
1.84e-14 |
|
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: 70.25 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGlIP---PSAGQVLMNGEVIEE-PGSDR-----GMVFQNYTLFPWLT 114
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDITDlPPEERarlgiFLAFQYPPEIPGVK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 115 VADnvaFglkLRGLSSGeikeqvfyylsivgltqfakaypkqLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQ 194
Cdd:cd03217 94 NAD---F---LRYVNEG-------------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2225592549 195 MQQFFLELWEQThITVLMITHDVEEAVFLSG-RVYVMIAnpGRI 237
Cdd:cd03217 143 VAEVINKLREEG-KSVLIITHYQRLLDYIKPdRVHVLYD--GRI 183
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
45-219 |
2.00e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 71.00 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVieepgsdrGMVFQNYTLFPWLTVADNVAFGLK 124
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV--------SVIAISAGLSGQLTGIENIEFKML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 125 LRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWE 204
Cdd:PRK13546 112 CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKE 191
|
170
....*....|....*
gi 2225592549 205 QTHiTVLMITHDVEE 219
Cdd:PRK13546 192 QNK-TIFFVSHNLGQ 205
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-219 |
2.52e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 23 QPKLEVEKVFKHFPHLKTnlsvLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI--------E 94
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKA----LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 95 EPGSdrGMVFQNYTLFPWLTVADNVAFGLKLRGlSSGEIKEQVFY-----YLSIVGLTQFAKAYPKQLSGGMKQRVAIAR 169
Cdd:PRK10762 78 EAGI--GIIHQELNLIPQLTIAENIFLGREFVN-RFGRIDWKKMYaeadkLLARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2225592549 170 ALANHPEVLLMDEPFGAL-DAQTrEQMQQFFLELWEQTHITVlMITHDVEE 219
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALtDTET-ESLFRVIRELKSQGRGIV-YISHRLKE 203
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
32-195 |
2.57e-14 |
|
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: 72.64 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 32 FKHFPHLKTnlSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGsdrgmvfqnytlFP 111
Cdd:TIGR01271 431 FSNFSLYVT--PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQ------------TS 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 112 WL---TVADNVAFglklrGLSSGEikeqvFYYLSIVGLTQFAK---AYPKQ-----------LSGGMKQRVAIARALANH 174
Cdd:TIGR01271 497 WImpgTIKDNIIF-----GLSYDE-----YRYTSVIKACQLEEdiaLFPEKdktvlgeggitLSGGQRARISLARAVYKD 566
|
170 180
....*....|....*....|.
gi 2225592549 175 PEVLLMDEPFGALDAQTREQM 195
Cdd:TIGR01271 567 ADLYLLDSPFTHLDVVTEKEI 587
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
36-244 |
5.07e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.57 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 36 PHLKTNLSV-------LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIE----EPGSDRGMVF 104
Cdd:PRK10762 252 APGEVRLKVdnlsgpgVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspQDGLANGIVY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 105 QNytlfpwltvADNVAFGLKLrGLSsgeIKEQvfyyLSIVGLTQFAKAY-----------------------PKQ----- 156
Cdd:PRK10762 332 IS---------EDRKRDGLVL-GMS---VKEN----MSLTALRYFSRAGgslkhadeqqavsdfirlfniktPSMeqaig 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 157 -LSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQfFLELWEQTHITVLMITHDVEEAVFLSGRVYVMiaNPG 235
Cdd:PRK10762 395 lLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ-LINQFKAEGLSIILVSSEMPEVLGMSDRILVM--HEG 471
|
....*....
gi 2225592549 236 RIKDEFKIE 244
Cdd:PRK10762 472 RISGEFTRE 480
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-230 |
6.38e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 71.01 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTnlsvLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSA--GQVLMNGEVIEEPG----SD 99
Cdd:TIGR02633 2 LEMKGIVKTFGGVKA----LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNirdtER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 100 RGMVF--QNYTLFPWLTVADNVAFG--LKLRG--LSSGEIKEQVFYYLSIVGLTQFAKAYP-KQLSGGMKQRVAIARALA 172
Cdd:TIGR02633 78 AGIVIihQELTLVPELSVAENIFLGneITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2225592549 173 NHPEVLLMDEPFGALDAQTREQMQQFFLELwEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVI 214
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
42-230 |
6.46e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 70.32 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 42 LSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPS----AGQVLMNG------------EVIeepGSDRGMVFQ 105
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGidllklsprerrKII---GREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 106 NYT--LFPWLTVADNVAFGLKLRGLSS------GEIKEQVFYYLSIVGLTQ---FAKAYPKQLSGGMKQRVAIARALANH 174
Cdd:COG4170 97 EPSscLDPSAKIGDQLIEAIPSWTFKGkwwqrfKWRKKRAIELLHRVGIKDhkdIMNSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2225592549 175 PEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
62-220 |
7.95e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 62 GASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEepGSDR------GMVFQNYTLFPWLTVADNVAFGLKLRGLSSGEIKE 135
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD--AGDIatrrrvGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAA 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 136 QVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITH 215
Cdd:NF033858 377 RVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTH 456
|
....*
gi 2225592549 216 DVEEA 220
Cdd:NF033858 457 FMNEA 461
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
52-248 |
8.62e-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: 68.97 E-value: 8.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 52 VYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGqvlmngevieEPGSDRGMVfqNYTlfPWLTVADnvaFGLKLRGLSSG 131
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG----------DIEIELDTV--SYK--PQYIKAD---YEGTVRDLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 132 EIK---EQVFYYLSIVGLTQFAKAYPKQ---LSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQ 205
Cdd:cd03237 85 ITKdfyTHPYFKTEIAKPLQIEQILDREvpeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAEN 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2225592549 206 THITVLMITHDVEEAVFLSGRVYVMIANPGrikdEFKIELPPE 248
Cdd:cd03237 165 NEKTAFVVEHDIIMIDYLADRLIVFEGEPS----VNGVANPPQ 203
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
35-191 |
1.06e-13 |
|
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: 68.06 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 35 FPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSA---GQVLMNG----EVIEEPGSDRGMVFQNY 107
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGipykEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 108 TLFPWLTVADNVAFGLKLRGlssgeikeqvfyylsivgltqfaKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGAL 187
Cdd:cd03233 93 VHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
....
gi 2225592549 188 DAQT 191
Cdd:cd03233 150 DSST 153
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
38-240 |
1.25e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.78 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 38 LKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPS-AGQVLMNGEVIEEPGsdrgmvfqnytlFPWL--- 113
Cdd:PLN03232 626 SKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVPQ------------VSWIfna 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 114 TVADNVAFGLKLRglssgeiKEQVFYYLSIVGLTQFAKAYPKQ-----------LSGGMKQRVAIARALANHPEVLLMDE 182
Cdd:PLN03232 694 TVRENILFGSDFE-------SERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 183 PFGALDAQTREQMQQFFL--ELWEQTHITVLMITHdveeavFLSGRVYVMIANPGRIKDE 240
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMkdELKGKTRVLVTNQLH------FLPLMDRIILVSEGMIKEE 820
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-219 |
1.75e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.82 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHLKTnlsvLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPS--AGQVLMNGEVIE-------Ep 96
Cdd:NF040905 2 LEMRGITKTFPGVKA----LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRfkdirdsE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 97 gsDRGMVF--QNYTLFPWLTVADNV-------AFGLKLRGLSSGEIKEqvfyYLSIVGLTQFAKAYPKQLSGGMKQRVAI 167
Cdd:NF040905 77 --ALGIVIihQELALIPYLSIAENIflgneraKRGVIDWNETNRRARE----LLAKVGLDESPDTLVTDIGVGKQQLVEI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2225592549 168 ARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQThITVLMITHDVEE 219
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQG-ITSIIISHKLNE 201
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
44-237 |
1.96e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSA--------GQVLMNGE---VIEEP--GSDRGMVFQ-NYTL 109
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEplaAIDAPrlARLRAVLPQaAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 110 FPWlTVADNVAFGLKLRGLSSGEI----KEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALAN---------HPE 176
Cdd:PRK13547 96 FAF-SAREIVLLGRYPHARRAGALthrdGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2225592549 177 VLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVyVMIANpGRI 237
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRI-AMLAD-GAI 233
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
54-219 |
3.59e-13 |
|
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: 65.47 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 54 PNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLM-NGEVIEEPGSDRGMVFQNYTlfpwltvadnvafglklrglssge 132
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLLLIIVGG------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 133 ikeqvfyylsivgltqfakaYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQ-----QFFLELWEQTH 207
Cdd:smart00382 57 --------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLLKSEKN 116
|
170
....*....|..
gi 2225592549 208 ITVLMITHDVEE 219
Cdd:smart00382 117 LTVILTTNDEKD 128
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
47-216 |
4.70e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.82 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 47 DINIQvyPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI------EEPGSDRGMVFqnytlfpwltvaDNVA 120
Cdd:PRK11147 23 ELHIE--DNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvarlqqDPPRNVEGTVY------------DFVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 121 FGLKlrglssgEIKEQVFYY-------------------------LSIVGLTQF--------------AKAYPKQLSGGM 161
Cdd:PRK11147 89 EGIE-------EQAEYLKRYhdishlvetdpseknlnelaklqeqLDHHNLWQLenrinevlaqlgldPDAALSSLSGGW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2225592549 162 KQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELweqtHITVLMITHD 216
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF----QGSIIFISHD 212
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-193 |
7.76e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 65.66 E-value: 7.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 34 HFPHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVL---MNGEVIEEPGSdrGMVFQNYTLF 110
Cdd:PRK13541 5 HQLQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYyknCNINNIAKPYC--TYIGHNLGLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 111 PWLTVADNVAFGLKLRGlSSGEIKEQVFYYlsivGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQ 190
Cdd:PRK13541 83 LEMTVFENLKFWSEIYN-SAETLYAAIHYF----KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
...
gi 2225592549 191 TRE 193
Cdd:PRK13541 158 NRD 160
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
46-240 |
7.82e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.01 E-value: 7.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 46 EDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGE--VIEEPGS--DRGMVF-----QNYTLFPWLTVA 116
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDaiRAGIMLcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 117 DNVA---------FGLKLRGLSSGEIKEQVFYYLSIVglTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGAL 187
Cdd:PRK11288 350 DNINisarrhhlrAGCLINNRWEAENADRFIRSLNIK--TPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 188 DAQTREQMQQFFLELWEQThITVLMITHDVEEAVFLSGRVYVMiaNPGRIKDE 240
Cdd:PRK11288 428 DVGAKHEIYNVIYELAAQG-VAVLFVSSDLPEVLGVADRIVVM--REGRIAGE 477
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
37-216 |
1.05e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.11 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 37 HLKtNLSV---LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIpPSAGQVLMNGEVIEE-PGSD----RGmvfqnyt 108
Cdd:PRK03695 2 QLN-DVAVstrLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwSAAElarhRA------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 109 lfpWLTVADNVAFG------LKLR---GLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARAL-----ANH 174
Cdd:PRK03695 73 ---YLSQQQTPPFAmpvfqyLTLHqpdKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDIN 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2225592549 175 PE--VLLMDEPFGALDAQTREQMQQFFLELWEQThITVLMITHD 216
Cdd:PRK03695 150 PAgqLLLLDEPMNSLDVAQQAALDRLLSELCQQG-IAVVMSSHD 192
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-219 |
1.49e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 22 SQPKLEVEKVFKHFPHLKTnlsvLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSA--GQVLMNGEVIEEPG-- 97
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKA----LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNir 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 98 --SDRGMV--FQNYTLFPWLTVADNVAFGLKLrgLSSGEIKEQVFY-----YLSIVGLTQFAKAYPKQLSGGMKQRVAIA 168
Cdd:PRK13549 78 dtERAGIAiiHQELALVKELSVLENIFLGNEI--TPGGIMDYDAMYlraqkLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2225592549 169 RALANHPEVLLMDEPFGALDAQTREQMQQFFLELweQTH-ITVLMITHDVEE 219
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDL--KAHgIACIYISHKLNE 205
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
43-217 |
1.81e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.67 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 43 SVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDR--GMVFQNYTL---FPWLtVAD 117
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNlvAYVPQSEEVdwsFPVL-VED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFG----LKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTRE 193
Cdd:PRK15056 100 VVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180
....*....|....*....|....
gi 2225592549 194 QMQQFFLELWEQTHiTVLMITHDV 217
Cdd:PRK15056 180 RIISLLRELRDEGK-TMLVSTHNL 202
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-236 |
3.98e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 25 KLEVEKVfkHFPHL-KTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAG---------LIPPSAGQVLMNGEVIE 94
Cdd:PTZ00265 1165 KIEIMDV--NFRYIsRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhIVFKNEHTNDMTNEQDY 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 95 EPGSDRGMVFQN---------------YTLFP-----WLTVADNVAFGLK-LRGLSSGEIKEQVFYYLSIVGLTQFAK-- 151
Cdd:PTZ00265 1243 QGDEEQNVGMKNvnefsltkeggsgedSTVFKnsgkiLLDGVDICDYNLKdLRNLFSIVSQEPMLFNMSIYENIKFGKed 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 152 -------------------------------AYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFL 200
Cdd:PTZ00265 1323 atredvkrackfaaidefieslpnkydtnvgPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402
|
250 260 270
....*....|....*....|....*....|....*.
gi 2225592549 201 ELWEQTHITVLMITHDVeEAVFLSGRVyVMIANPGR 236
Cdd:PTZ00265 1403 DIKDKADKTIITIAHRI-ASIKRSDKI-VVFNNPDR 1436
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
51-236 |
5.25e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 51 QVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEP---GSDRGMvfqnytlfpwlTVADNvafglklrg 127
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPqyiKPDYDG-----------TVEDL--------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 128 LSSgeIKEQV---FYYLSIV---GLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLE 201
Cdd:PRK13409 421 LRS--ITDDLgssYYKSEIIkplQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 498
|
170 180 190
....*....|....*....|....*....|....*
gi 2225592549 202 LWEQTHITVLMITHDVEEAVFLSGRVYVMIANPGR 236
Cdd:PRK13409 499 IAEEREATALVVDHDIYMIDYISDRLMVFEGEPGK 533
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
25-216 |
6.68e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.99 E-value: 6.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 25 KLEVEKVFKHFPhlKTNLSVlEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI--EEPGSDRGM 102
Cdd:PRK10522 322 TLELRNVTFAYQ--DNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtaEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 103 ---VFQNYTLFPWLtvadnvafgLKLRGLSSGEikEQVFYYLSIVGLT-----QFAKAYPKQLSGGMKQRVAIARALANH 174
Cdd:PRK10522 399 fsaVFTDFHLFDQL---------LGPEGKPANP--ALVEKWLERLKMAhklelEDGRISNLKLSKGQKKRLALLLALAEE 467
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2225592549 175 PEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHD 216
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
26-216 |
7.01e-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: 64.96 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHlKTnlsVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMnGEVIeepgsDRGMVFQ 105
Cdd:TIGR03719 323 IEAENLTKAFGD-KL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-----KLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 106 NY-TLFPWLTVADNVAFGLKLRGLSSGEIKEQVfyYLS---IVGLTQFAKAypKQLSGGMKQRVAIARALANHPEVLLMD 181
Cdd:TIGR03719 393 SRdALDPNKTVWEEISGGLDIIKLGKREIPSRA--YVGrfnFKGSDQQKKV--GQLSGGERNRVHLAKTLKSGGNVLLLD 468
|
170 180 190
....*....|....*....|....*....|....*
gi 2225592549 182 EPFGALDAQTREQMQQFFLELWEqthiTVLMITHD 216
Cdd:TIGR03719 469 EPTNDLDVETLRALEEALLNFAG----CAVVISHD 499
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
26-225 |
7.56e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.91 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPhlktNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLM--NGEVIEEPgSDRGMV 103
Cdd:PRK15064 320 LEVENLTKGFD----NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWseNANIGYYA-QDHAYD 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 104 FQN-YTLFPWL----TVADNvafGLKLRGL------SSGEIKEQVfyylsivgltqfakaypKQLSGGMKQRVAIARALA 172
Cdd:PRK15064 395 FENdLTLFDWMsqwrQEGDD---EQAVRGTlgrllfSQDDIKKSV-----------------KVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 173 NHPEVLLMDEPFGALDAQTREQMqQFFLELWEQTHITVlmiTHDVEeavFLSG 225
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIESL-NMALEKYEGTLIFV---SHDRE---FVSS 500
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
45-220 |
2.14e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVlmngEVIEEPGSDRGMVFQNYT------------LFPW 112
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV----EVLGGDMADARHRRAVCPriaympqglgknLYPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 113 LTVADNVAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTR 192
Cdd:NF033858 93 LSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSR 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 2225592549 193 eqmQQFflelWE--------QTHITVLMITHDVEEA 220
Cdd:NF033858 173 ---RQF----WElidriraeRPGMSVLVATAYMEEA 201
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
47-240 |
2.17e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 47 DINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEePGSD-----RGMVF-----QNYTLFPWLTVA 116
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS-PRSPldavkKGMAYitesrRDNGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 117 DNVAFG--LKLRGL--------SSGEIK----EQVFYYLSIVGLTQFAKaypkQLSGGMKQRVAIARALANHPEVLLMDE 182
Cdd:PRK09700 360 QNMAISrsLKDGGYkgamglfhEVDEQRtaenQRELLALKCHSVNQNIT----ELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2225592549 183 PFGALDAQTREQMQQFFLELWEQThITVLMITHDVEE--------AVFLSGRVYVMIANPGRIKDE 240
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDG-KVILMVSSELPEiitvcdriAVFCEGRLTQILTNRDDMSEE 500
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
41-215 |
3.16e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 61.62 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 41 NLSV-------LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGlIP---PSAGQVLMNGE-VIEEPGSDR-----GMVF 104
Cdd:COG0396 5 NLHVsvegkeiLKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPkyeVTSGSILLDGEdILELSPDERaragiFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 105 QNYTLFPWLTVAD--NVAFGlKLRG--LSSGEIKEQVFYYLSIVGLtqfAKAYPKQ-----LSGGMKQRVAIARALANHP 175
Cdd:COG0396 84 QYPVEIPGVSVSNflRTALN-ARRGeeLSAREFLKLLKEKMKELGL---DEDFLDRyvnegFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2225592549 176 EVLLMDEPFGALD-------AQTREQMQqfflelweQTHITVLMITH 215
Cdd:COG0396 160 KLAILDETDSGLDidalrivAEGVNKLR--------SPDRGILIITH 198
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
151-230 |
3.86e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.51 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 151 KAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
45-190 |
3.94e-11 |
|
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: 63.04 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPgsdRGMVFQNYTLfpwltvADNVAFGLK 124
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVP---QQAWIQNDSL------RENILFGKA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 125 LrglssgeikeQVFYYLSIV---GLTQFAKAYPK-----------QLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQ 190
Cdd:TIGR00957 725 L----------NEKYYQQVLeacALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
44-220 |
4.81e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.34 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPpsagqvlmngevieepgsdrgmvfQNYTlfpwltvADNVAFGl 123
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP------------------------QGYS-------NDLTLFG- 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 124 KLRGlsSGE----IKEQVFY-------------------------------------------YLSIVGL-TQFAKAYPK 155
Cdd:PRK10938 323 RRRG--SGEtiwdIKKHIGYvssslhldyrvstsvrnvilsgffdsigiyqavsdrqqklaqqWLDILGIdKRTADAPFH 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2225592549 156 QLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITHDVEEA 220
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
56-252 |
1.25e-10 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 59.12 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 56 EFVSIVGASGCGKSTLLNIIAGLIPPsagqvlmNGEVIEEPGsdrgmvfqnytlfpwLTVAdnvafglklrglssgeIKE 135
Cdd:cd03222 26 EVIGIVGPNGTGKTTAVKILAGQLIP-------NGDNDEWDG---------------ITPV----------------YKP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 136 QvfyYLSivgltqfakaypkqLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLMITH 215
Cdd:cd03222 68 Q---YID--------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEH 130
|
170 180 190
....*....|....*....|....*....|....*..
gi 2225592549 216 DVEEAVFLSGRVYVMIANPGRikdeFKIELPPERDLE 252
Cdd:cd03222 131 DLAVLDYLSDRIHVFEGEPGV----YGIASQPKGTRE 163
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
52-191 |
1.66e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 52 VYPNEFVSIVGASGCGKSTLLNIIA-----GLIppSAGQVLMNGEVIEEPGSDR-GMVFQNYTLFPWLTVADNVAFGLKL 125
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAervttGVI--TGGDRLVNGRPLDSSFQRSiGYVQQQDLHLPTSTVRESLRFSAYL 863
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2225592549 126 RGLSSGEIKEQ---VFYYLSIVGLTQFAKAY---PKQ-LSGGMKQRVAIARALANHPEVLL-MDEPFGALDAQT 191
Cdd:TIGR00956 864 RQPKSVSKSEKmeyVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
48-110 |
1.75e-10 |
|
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: 60.97 E-value: 1.75e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2225592549 48 INIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSD--RGM---VFQNYTLF 110
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREayRQLfsaVFSDFHLF 418
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
58-216 |
1.78e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.03 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 58 VSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVieepgsdRGMVFQNYTLfPWLTVADNVAfgLKLRGLSSGEIKEQV 137
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV-------RMAVFSQHHV-DGLDLSSNPL--LYMMRCFPGVPEQKL 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 138 FYYLSIVGLTQFAKAYPK-QLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQfFLELWEQthiTVLMITHD 216
Cdd:PLN03073 608 RAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQ-GLVLFQG---GVLMVSHD 683
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
44-215 |
1.81e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.11 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSdRGMVFQnYTLFPwltvADNVAFGL 123
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGL-HDLRFK-ITIIP----QDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 124 KLR-GLS--SGEIKEQVFYYLSIVGLTQFAKAYP-----------KQLSGGMKQRVAIARALANHPEVLLMDEPFGALDA 189
Cdd:TIGR00957 1375 SLRmNLDpfSQYSDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180
....*....|....*....|....*.
gi 2225592549 190 QTREQMQQFFLELWEQThiTVLMITH 215
Cdd:TIGR00957 1455 ETDNLIQSTIRTQFEDC--TVLTIAH 1478
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-230 |
1.96e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 29 EKVFKHF--PHLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSA----GQVLMNGEVIEEPGSD-RG 101
Cdd:TIGR00956 59 TRGFRKLkkFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHigveGVITYDGITPEEIKKHyRG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 102 MVF---QNYTLFPWLTVADNVAFGLKLR-------GLSSGE-IKEQVFYYLSIVGL-----TQFAKAYPKQLSGGMKQRV 165
Cdd:TIGR00956 139 DVVynaETDVHFPHLTVGETLDFAARCKtpqnrpdGVSREEyAKHIADVYMATYGLshtrnTKVGNDFVRGVSGGERKRV 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2225592549 166 AIARALANHPEVLLMDEPFGALDAQTreqMQQFFLELWEQTHI---TVLM-ITHDVEEAVFLSGRVYVM 230
Cdd:TIGR00956 219 SIAEASLGGAKIQCWDNATRGLDSAT---ALEFIRALKTSANIldtTPLVaIYQCSQDAYELFDKVIVL 284
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
44-188 |
2.04e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEpgsDRGmVFQNYTLF--------PWLTV 115
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK---DLC-TYQKQLCFvghrsginPYLTL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2225592549 116 ADNVAFGLKlrgLSSG--EIKEQVfyylSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALD 188
Cdd:PRK13540 92 RENCLYDIH---FSPGavGITELC----RLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-215 |
2.64e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.81 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 14 SSQTGETFSQ-PKLEVEKVFKHFPHLKtNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMN--- 89
Cdd:PTZ00265 370 NNDDGKKLKDiKKIQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdsh 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 90 --------------GEVIEEPgsdrgMVFQN-------YTLFPW--LTVADNVA------------------------FG 122
Cdd:PTZ00265 449 nlkdinlkwwrskiGVVSQDP-----LLFSNsiknnikYSLYSLkdLEALSNYYnedgndsqenknkrnscrakcagdLN 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 123 LKLRGLSSGEIKEQVFYYLSI-----------VGLTQFAKAYP-----------KQLSGGMKQRVAIARALANHPEVLLM 180
Cdd:PTZ00265 524 DMSNTTDSNELIEMRKNYQTIkdsevvdvskkVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILIL 603
|
250 260 270
....*....|....*....|....*....|....*
gi 2225592549 181 DEPFGALDAQTREQMQQFFLELWEQTHITVLMITH 215
Cdd:PTZ00265 604 DEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
45-219 |
3.84e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.90 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVieepgsdrGMVFQNYTLFPWLTVADNVAFGLK 124
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA--------ALIAISSGLNGQLTGIENIELKGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 125 LRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDaQT-----REQMQQFf 199
Cdd:PRK13545 112 MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD-QTftkkcLDKMNEF- 189
|
170 180
....*....|....*....|
gi 2225592549 200 lelwEQTHITVLMITHDVEE 219
Cdd:PRK13545 190 ----KEQGKTIFFISHSLSQ 205
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
54-235 |
6.61e-10 |
|
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: 58.15 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 54 PNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG---EVIEEpgsDRGMVFQNY-------TLFP-----WLTVADN 118
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdEILDE---FRGSELQNYftkllegDVKVivkpqYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFGLKLRGLSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQF 198
Cdd:cd03236 102 AVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARL 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 2225592549 199 FLELWEQTHiTVLMITHDVEEAVFLSGRVYVMIANPG 235
Cdd:cd03236 182 IRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLYGEPG 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
58-235 |
4.50e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 58 VSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNG---EVIEEpgsDRGMVFQNYtlfpwltvadnvafglkLRGLSSGEIK 134
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdEVLKR---FRGTELQNY-----------------FKKLYNGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 135 -----------EQVF------------------YYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFG 185
Cdd:PRK13409 162 vvhkpqyvdliPKVFkgkvrellkkvdergkldEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2225592549 186 ALDAQTREQMQQFFLELWEQthITVLMITHDVeeAV--FLSGRVYVMIANPG 235
Cdd:PRK13409 242 YLDIRQRLNVARLIRELAEG--KYVLVVEHDL--AVldYLADNVHIAYGEPG 289
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
58-235 |
6.98e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.95 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 58 VSIVGASGCGKSTLLNIIAGLIPPsagqvlmN-GEVIEEPGSD------RGMVFQNYtlfpwltvadnvafglkLRGLSS 130
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKP-------NlGDYDEEPSWDevlkrfRGTELQDY-----------------FKKLAN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 131 GEIK-----------EQVF------------------YYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMD 181
Cdd:COG1245 158 GEIKvahkpqyvdliPKVFkgtvrellekvdergkldELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2225592549 182 EPFGALDAQTREQMQQFFLELWEQTHiTVLMITHDVeeAV--FLSGRVYVMIANPG 235
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELAEEGK-YVLVVEHDL--AIldYLADYVHILYGEPG 290
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
32-215 |
7.42e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 55.91 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 32 FKHFPHLKTNLSVL-EDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGE-----VIEEPGSDRGmVFQ 105
Cdd:TIGR00954 454 FENIPLVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKgklfyVPQRPYMTLG-TLR 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 106 NYTLFPwltvaDNVaFGLKLRGLSSGEIKEqvfyYLSIVGLTQFAKA---------YPKQLSGGMKQRVAIARALANHPE 176
Cdd:TIGR00954 533 DQIIYP-----DSS-EDMKRRGLSDKDLEQ----ILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQ 602
|
170 180 190
....*....|....*....|....*....|....*....
gi 2225592549 177 VLLMDEPFGALDAqtreQMQQFFLELWEQTHITVLMITH 215
Cdd:TIGR00954 603 FAILDECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
45-216 |
1.28e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 45 LEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMnGEVIEepgsdrgmV--FQNY--TLFPWLTVADNVA 120
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLE--------VayFDQHraELDPEKTVMDNLA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 121 FGlKLRGLSSGeIKEQVFYYLSivgltQF------AKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQ 194
Cdd:PRK11147 406 EG-KQEVMVNG-RPRHVLGYLQ-----DFlfhpkrAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLEL 478
|
170 180
....*....|....*....|..
gi 2225592549 195 MQqfflELWEQTHITVLMITHD 216
Cdd:PRK11147 479 LE----ELLDSYQGTVLLVSHD 496
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
39-218 |
2.29e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.71 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 39 KTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNiiaglippsagqvlmngEVIEEPGSDRGMVFQNyTLFPWLTVA-D 117
Cdd:cd03238 5 GANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------------EGLYASGKARLISFLP-KFSRNKLIFiD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 118 NVAFGLKLrGLSsgeikeqvfyYLSivgLTQFAKAypkqLSGGMKQRVAIARALANHPE--VLLMDEPFGALDAQTREQM 195
Cdd:cd03238 67 QLQFLIDV-GLG----------YLT---LGQKLST----LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL 128
|
170 180
....*....|....*....|...
gi 2225592549 196 QQFFLELWEQTHiTVLMITHDVE 218
Cdd:cd03238 129 LEVIKGLIDLGN-TVILIEHNLD 150
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
44-200 |
3.20e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSdrgmvfqnytlfPWL---TVADNVA 120
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQ------------AWImnaTVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 121 F------------------GLKLRGLSSG---EIKEQvfyylsivGLtqfakaypkQLSGGMKQRVAIARALANHPEVLL 179
Cdd:PTZ00243 743 FfdeedaarladavrvsqlEADLAQLGGGletEIGEK--------GV---------NLSGGQKARVSLARAVYANRDVYL 805
|
170 180
....*....|....*....|..
gi 2225592549 180 MDEPFGALDAQTREQ-MQQFFL 200
Cdd:PTZ00243 806 LDDPLSALDAHVGERvVEECFL 827
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
31-230 |
4.42e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 31 VFKHFPHLKTnlsvLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPGSDRG------MVF 104
Cdd:PRK10982 4 ISKSFPGVKA----LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEAlengisMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 105 QNYTLFPWLTVADNVAFG-LKLRGLSSGEIK-----EQVFYYLSIvgltqfaKAYPKQ----LSGGMKQRVAIARALANH 174
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGrYPTKGMFVDQDKmyrdtKAIFDELDI-------DIDPRAkvatLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2225592549 175 PEVLLMDEPFGALDAQTREQMQQFFLELWEQThITVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERG-CGIVYISHKMEEIFQLCDEITIL 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
156-244 |
8.73e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 8.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 156 QLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQtHITVLMITHDVEEAVFLSGRVYVMiaNPG 235
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVM--HEG 481
|
....*....
gi 2225592549 236 RIKDEFKIE 244
Cdd:PRK13549 482 KLKGDLINH 490
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-241 |
9.91e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.52 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPhLKTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPS-AGQVLMNGE------------- 91
Cdd:TIGR02633 258 LEARNLTCWDV-INPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvdirnpaqaira 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 92 ---VIEEPGSDRGM-----VFQNYTL-----FPWLTVADNVA-FGLKLRGLSSGEIKeQVFYYLSIVGLtqfakaypkql 157
Cdd:TIGR02633 337 giaMVPEDRKRHGIvpilgVGKNITLsvlksFCFKMRIDAAAeLQIIGSAIQRLKVK-TASPFLPIGRL----------- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 158 SGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELwEQTHITVLMITHDVEEAVFLSGRVYVMiaNPGRI 237
Cdd:TIGR02633 405 SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQL-AQEGVAIIVVSSELAEVLGLSDRVLVI--GEGKL 481
|
....
gi 2225592549 238 KDEF 241
Cdd:TIGR02633 482 KGDF 485
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
44-215 |
2.13e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPG-SDRGMVF----QNYTLFpwltvADN 118
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGlTDLRRVLsiipQSPVLF-----SGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFGLK----------LRGLSSGEIKEQVfyYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALD 188
Cdd:PLN03232 1326 VRFNIDpfsehndadlWEALERAHIKDVI--DRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180
....*....|....*....|....*..
gi 2225592549 189 AQTREQMQQFFLElwEQTHITVLMITH 215
Cdd:PLN03232 1404 VRTDSLIQRTIRE--EFKSCTMLVIAH 1428
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
39-212 |
2.69e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 39 KTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPS---AGQVLMNGEVIEE--PGSDRGMVFQNYTLFPWL 113
Cdd:PLN03140 175 KTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEfvPRKTSAYISQNDVHVGVM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 114 TVADNVAFGLKLRG----------LSSGEIKEQVF------------------------YYLSIVGL-----TQFAKAYP 154
Cdd:PLN03140 255 TVKETLDFSARCQGvgtrydllseLARREKDAGIFpeaevdlfmkatamegvksslitdYTLKILGLdickdTIVGDEMI 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2225592549 155 KQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHITVLM 212
Cdd:PLN03140 335 RGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLM 392
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
26-191 |
3.18e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 26 LEVEKVFKHFPHlktnlSVL-EDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMnGEVIEepgsdRGMVF 104
Cdd:PRK11819 325 IEAENLSKSFGD-----RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK-----LAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 105 QNY-TLFPWLTVADNVAFGLKLRGLSSGEIKEQVfyYLSIVGLT---QFAKAypKQLSGGMKQRVAIARALANHPEVLLM 180
Cdd:PRK11819 394 QSRdALDPNKTVWEEISGGLDIIKVGNREIPSRA--YVGRFNFKggdQQKKV--GVLSGGERNRLHLAKTLKQGGNVLLL 469
|
170
....*....|.
gi 2225592549 181 DEPFGALDAQT 191
Cdd:PRK11819 470 DEPTNDLDVET 480
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
43-218 |
3.67e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.06 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 43 SVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPpsagqvlMNGEVieepgSDRGMVFQNYTLFPWltvadNVAFG 122
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-------TEGEI-----QIDGVSWNSVTLQTW-----RKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 123 LKLRG--LSSGEIK-----------EQVFYYLSIVGLTQFAKAYPKQL-----------SGGMKQRVAIARALANHPEVL 178
Cdd:TIGR01271 1296 VIPQKvfIFSGTFRknldpyeqwsdEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2225592549 179 LMDEPFGALDAQT----REQMQQFFlelweqTHITVLMITHDVE 218
Cdd:TIGR01271 1376 LLDEPSAHLDPVTlqiiRKTLKQSF------SNCTVILSEHRVE 1413
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
128-244 |
4.47e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.12 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 128 LSSGEIKEQVFYYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREqmqqfflELWEQTH 207
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRN-------EVWDEVR 188
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2225592549 208 ------ITVLMITHDVEEAVFLSGRVYVMiaNPGRIKDEFKIE 244
Cdd:NF000106 189 smvrdgATVLLTTQYMEEAEQLAHELTVI--DRGRVIADGKVD 229
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
61-216 |
1.13e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 61 VGASGCGKSTLLNIIAGLIPPSAGQVLMngevieEPGSDRGMVFQNYTLFPWLTVADNVAFG-LKL--------RGLSSG 131
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSL------DPNERLGKLRQDQFAFEEFTVLDTVIMGhTELwevkqerdRIYALP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 132 EIKEQVFY--------YLSIVGLTQFAKA--------YP--------KQLSGGMKQRVAIARALANHPEVLLMDEPFGAL 187
Cdd:PRK15064 107 EMSEEDGMkvadlevkFAEMDGYTAEARAgelllgvgIPeeqhyglmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNL 186
|
170 180
....*....|....*....|....*....
gi 2225592549 188 DAQTREQMQQfflELwEQTHITVLMITHD 216
Cdd:PRK15064 187 DINTIRWLED---VL-NERNSTMIIISHD 211
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
40-214 |
1.67e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 40 TNLSVLEDINIQvyPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQ--------VLMNGEVIEEPGSDRgmvFQ-NYTLf 110
Cdd:PRK10938 16 TKTLQLPSLTLN--AGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLVSDE---WQrNNTD- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 111 pwLTVADNVAFGLKLRGLSSGEIK-----EQVFYYLSIVGL--TQFakaypKQLSGGMKQRVAIARALANHPEVLLMDEP 183
Cdd:PRK10938 90 --MLSPGEDDTGRTTAEIIQDEVKdparcEQLAQQFGITALldRRF-----KYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190
....*....|....*....|....*....|.
gi 2225592549 184 FGALDAQTREQMQQFFLELWEQTHITVLMIT 214
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHQSGITLVLVLN 193
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
43-218 |
2.98e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 47.54 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 43 SVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLippsagqVLMNGEVieepgSDRGMVFQNYTLFPWltvadNVAFG 122
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-------LNTEGDI-----QIDGVSWNSVPLQKW-----RKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 123 LKLRG--LSSGEIK-----------EQVFYYLSIVGLTQFAKAYPKQL-----------SGGMKQRVAIARALANHPEVL 178
Cdd:cd03289 81 VIPQKvfIFSGTFRknldpygkwsdEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2225592549 179 LMDEPFGALDAQT----REQMQQFFlelweqTHITVLMITHDVE 218
Cdd:cd03289 161 LLDEPSAHLDPITyqviRKTLKQAF------ADCTVILSEHRIE 198
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
41-188 |
4.26e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.94 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 41 NLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGliPPS----AGQVLMNGEVI--EEPG--SDRG--MVFQNYTLF 110
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESIldLEPEerAHLGifLAFQYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 111 PWLTVAD--NVAFGLKLRGLSSGEIKEQVFY-----YLSIVGLTQ-FAKAYPKQ-LSGGMKQRVAIARALANHPEVLLMD 181
Cdd:CHL00131 97 PGVSNADflRLAYNSKRKFQGLPELDPLEFLeiineKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMALLDSELAILD 176
|
....*..
gi 2225592549 182 EPFGALD 188
Cdd:CHL00131 177 ETDSGLD 183
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
157-230 |
5.27e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 5.27e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2225592549 157 LSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHiTVLMITHDVEEAVFLSGRVYVM 230
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVM 464
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
155-210 |
6.25e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 6.25e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2225592549 155 KQLSGGMKQRVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLElWEQTHITV 210
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK-WPKTFIVV 397
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
44-215 |
1.30e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.27 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPG-----SDRGMVFQNYTLFpwltvADN 118
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlmdlrKVLGIIPQAPVLF-----SGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFGLK----------LRGLSSGEIKEQVfyYLSIVGLTQFAKAYPKQLSGGMKQRVAIARALANHPEVLLMDEPFGALD 188
Cdd:PLN03130 1329 VRFNLDpfnehndadlWESLERAHLKDVI--RRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
170 180
....*....|....*....|....*..
gi 2225592549 189 AQTREQMQQFFLElwEQTHITVLMITH 215
Cdd:PLN03130 1407 VRTDALIQKTIRE--EFKSCTMLIIAH 1431
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-201 |
1.62e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 19 ETFSQPKLEVEKVFKHFphlkTNLSVLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPsagqvlMNGEVIEEPGS 98
Cdd:PRK10636 306 ESLPNPLLKMEKVSAGY----GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP------VSGEIGLAKGI 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 99 DRGMVFQNYTLFpwlTVADNVAFGLKLRgLSSGEIKEQVFYYLSIVGLTQFAKAYP-KQLSGGMKQRVAIARALANHPEV 177
Cdd:PRK10636 376 KLGYFAQHQLEF---LRADESPLQHLAR-LAPQELEQKLRDYLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQRPNL 451
|
170 180
....*....|....*....|....
gi 2225592549 178 LLMDEPFGALDAQTREQMQQFFLE 201
Cdd:PRK10636 452 LLLDEPTNHLDLDMRQALTEALID 475
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
44-216 |
2.54e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVI------EEPGSDRGMVfqNYT--------- 108
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQlawvnqETPALPQPAL--EYVidgdreyrq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 109 LFPWLTVA----DNVAFGL---KLRGLSSGEIKEQVFYYLSIVGLTQFAKAYP-KQLSGGMKQRVAIARALANHPEVLLM 180
Cdd:PRK10636 94 LEAQLHDAnernDGHAIATihgKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLL 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 2225592549 181 DEPFGALDAQTreqmqQFFLELWEQTHI-TVLMITHD 216
Cdd:PRK10636 174 DEPTNHLDLDA-----VIWLEKWLKSYQgTLILISHD 205
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
60-228 |
3.36e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.75 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 60 IVGASGCGKSTLLNIIA----GLIPPSAGQVLMNGEVIEEpGSDRGMV---FQN-----YTLFPWLTVADNVAFglklrg 127
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyaltGELPPNSKGGAHDPKLIRE-GEVRAQVklaFENangkkYTITRSLAILENVIF------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 128 LSSGEIKeqvfyylSIVGLTqfakayPKQLSGGMKQ------RVAIARALANHPEVLLMDEPFGALDAQTRE-QMQQFFL 200
Cdd:cd03240 100 CHQGESN-------WPLLDM------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIE 166
|
170 180
....*....|....*....|....*...
gi 2225592549 201 ELWEQTHITVLMITHDvEEAVFLSGRVY 228
Cdd:cd03240 167 ERKSQKNFQLIVITHD-EELVDAADHIY 193
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
44-215 |
3.79e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.77 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEPG-----SDRGMVFQNYTLFPWlTVADN 118
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGlrelrRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 119 VAFGLKlrgLSSGEikeqVFYYLSIVGLTQFAKAYPKQL-----------SGGMKQRVAIARALANHPE-VLLMDEPFGA 186
Cdd:PTZ00243 1404 VDPFLE---ASSAE----VWAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMARALLKKGSgFILMDEATAN 1476
|
170 180
....*....|....*....|....*....
gi 2225592549 187 LDAQTREQMQQFFLELWeqTHITVLMITH 215
Cdd:PTZ00243 1477 IDPALDRQIQATVMSAF--SAYTVITIAH 1503
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
33-233 |
4.78e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.73 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 33 KHFPHLKTNLSVLEDiniqvyPNEFVSIVGASGCGKSTLLNIIAglippsagqvlmngevieepgsdrgmvfqnytlfpw 112
Cdd:cd03227 5 GRFPSYFVPNDVTFG------EGSLTIITGPNGSGKSTILDAIG------------------------------------ 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 113 LTVADNVAFGLKLRGLSSGEIKEQV--FYYLSIVgltqfakaypkQLSGGMKQRVAIARALANH---PEVL-LMDEPFGA 186
Cdd:cd03227 43 LALGGAQSATRRRSGVKAGCIVAAVsaELIFTRL-----------QLSGGEKELSALALILALAslkPRPLyILDEIDRG 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2225592549 187 LDAQ--------TREQMQQFFlelweqthiTVLMITHDVEEAVFLSG--RVYVMIAN 233
Cdd:cd03227 112 LDPRdgqalaeaILEHLVKGA---------QVIVITHLPELAELADKliHIKKVITG 159
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
44-217 |
2.58e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 41.43 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 44 VLEDINIQVYPNEFVSIVGASGCGKSTLLNIIAGLIPPSAGQVLMNGEVIEEpgsdrgmvfqnytlFPWLTVADNVAFGL 123
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISK--------------LPLHTLRSRLSIIL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 124 KLRGLSSGEIK-----------EQVFYYLSIVGLTQFAKAYPKQL-----------SGGMKQRVAIARALANHPEVLLMD 181
Cdd:cd03288 102 QDPILFSGSIRfnldpeckctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 2225592549 182 EPFGALDAQTREQMQQFFLELWEQThiTVLMITHDV 217
Cdd:cd03288 182 EATASIDMATENILQKVVMTAFADR--TVVTIAHRV 215
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
154-208 |
4.40e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.38 E-value: 4.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2225592549 154 PKQLSGGMKQRVAIARALAnhpevLLMDepFGALDAQTREQMQQFFLELWEQTHI 208
Cdd:COG0419 156 IETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELAIITHV 203
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-243 |
6.68e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225592549 157 LSGGMKQRVAIARAL---ANHPEVLLMDEPFGALDAQTREQMQQFFLELWEQTHiTVLMITHDVEeavFLSGRVYVMIAN 233
Cdd:PRK00635 1700 LSLSEKIAIKIAKFLylpPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGH-SVIYIDHDPA---LLKQADYLIEMG 1775
|
90
....*....|
gi 2225592549 234 PGRIKDEFKI 243
Cdd:PRK00635 1776 PGSGKTGGKI 1785
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
154-220 |
1.05e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 1.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2225592549 154 PKQLSGGMK-Q-----RVAIARALANHPEVLLMDEPFGALDAQTREQMQQFFLELweQTHITVLMITHDVEEA 220
Cdd:COG4717 556 VEELSRGTReQlylalRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAEL--AKGRQVIYFTCHEELV 626
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
155-205 |
5.51e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 35.29 E-value: 5.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2225592549 155 KQLSGGMKQR---VAIARALA----------NHPEVLLMDEPFGALDAQTREQMqqffLELWEQ 205
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTA----LELLRA 90
|
|
| CpaF |
COG4962 |
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ... |
60-82 |
9.42e-03 |
|
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443988 [Multi-domain] Cd Length: 386 Bit Score: 37.07 E-value: 9.42e-03
|
| |
