|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-210 |
9.63e-67 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 208.38 E-value: 9.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGE--IFDKDklLQSENRSI------M 73
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEvrVLGED--VARDPAEVrrrigyV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 FQKTMFPDQLKVIEIINLYQSFYENPLP-----LEEIIELTKFDSsQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDE 148
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKearerIDELLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446537461 149 PTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIR 210
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-232 |
4.20e-57 |
|
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: 183.91 E-value: 4.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI----FDKDKLLQSENRSI--MF 74
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgEDVRKEPREARRQIgvLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 75 QKTMFPDQLKVIEIINLYQSFY-----ENPLPLEEIIELTKFDSsQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEP 149
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYglfdeELKKRIEELIELLGLEE-FLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 150 TSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQQSQiTLSDEYIRKLKL 229
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE-NLEDAFVALIGS 238
|
...
gi 446537461 230 DKD 232
Cdd:COG4555 239 EEG 241
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-200 |
2.78e-53 |
|
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: 171.81 E-value: 2.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF------DKDKLLQSENRSIMFQ 75
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkdiKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 76 KTMFPDQLKVIEIInlyqsfyenplpleeiieltkfdssqlnqfvnKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDI 155
Cdd:cd03230 81 EPSLYENLTVRENL--------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446537461 156 EIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:cd03230 129 ESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-210 |
3.22e-48 |
|
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: 160.36 E-value: 3.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRC--VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF------DKDKLLQSENRSIM 73
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYingysiRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 FQKTMFPDQLKVIEIINLY---QSFYENPLPLEEIIELTKFD-SSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEP 149
Cdd:cd03263 81 PQFDALFDELTVREHLRFYarlKGLPKSEIKEEVELLLRVLGlTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446537461 150 TSTMDIEIREYFWSIIENLKEdNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIR 210
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-273 |
1.08e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 135.24 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSI-------- 72
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 73 -MFQKtmfpdqLKVIEIInLYqsFYE-NPLPLEEIIE-----LTKFD-SSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLI 144
Cdd:COG4152 81 gLYPK------MKVGEQL-VY--LARlKGLSKAEAKRradewLERLGlGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 145 LLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIR----------TNQQ 214
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRrqfgrntlrlEADG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446537461 215 SQITLSDEY-IRKLKLDKDDLVIQKNHNGTIKIITSNVND--TILYLQQLHINLDDIEIQKV 273
Cdd:COG4152 232 DAGWLRALPgVTVVEEDGDGAELKLEDGADAQELLRALLArgPVREFEEVRPSLNEIFIEVV 293
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-202 |
2.16e-37 |
|
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: 132.02 E-value: 2.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMF----QKT 77
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGylpeERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 78 MFPDQlKVIEIINLYQSFYEnpLPLEEIIE-----LTKFD-SSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTS 151
Cdd:cd03269 81 LYPKM-KVIDQLVYLAQLKG--LKKEEARRridewLERLElSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446537461 152 TMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIIL 202
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-199 |
3.68e-37 |
|
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: 129.67 E-value: 3.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 3 QISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFdkdkllqsenrsimfqktmfpdq 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 83 lkvieiINLYQSFYENPLPLEEIIeltkfdssqlnQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFW 162
Cdd:cd00267 58 ------IDGKDIAKLPLEELRRRI-----------GYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|....*..
gi 446537461 163 SIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGE 199
Cdd:cd00267 121 ELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-201 |
7.51e-37 |
|
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: 131.70 E-value: 7.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENR-------SIM 73
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrelarriAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 FQKTMFPDQLKVIEIINL----YQSFYENPLP-LEEIIE--LTKFDSSQL-NQFVNKLSGGQ-QRlldfVL---SLIGQP 141
Cdd:COG1120 81 PQEPPAPFGLTVRELVALgrypHLGLFGRPSAeDREAVEeaLERTGLEHLaDRPVDELSGGErQR----VLiarALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446537461 142 QLILLDEPTSTMDI----EIREyfwsIIENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:COG1120 157 PLLLLDEPTSHLDLahqlEVLE----LLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-209 |
1.08e-36 |
|
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: 130.53 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSF-NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRS-------IM 73
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRelrrkvgLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 FQktmFPD-QL---KVIEIInlyqSFY-EN-PLPLEEIIE-----LTKFD-SSQLNQFVNKLSGGQQRLLDF--VLSLig 139
Cdd:COG1122 81 FQ---NPDdQLfapTVEEDV----AFGpENlGLPREEIRErveeaLELVGlEHLADRPPHELSGGQKQRVAIagVLAM-- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 140 QPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHI 209
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-200 |
1.40e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.94 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSEN-----RSIMF-- 74
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppewrRQVAYvp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 75 -QKTMFPDqlKVIEIINLYQSFYENPLPLEEIIELTK---FDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPT 150
Cdd:COG4619 81 qEPALWGG--TVRDNLPFPFQLRERKFDRERALELLErlgLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446537461 151 STMDIEIREYFWSII-ENLKEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:COG4619 159 SALDPENTRRVEELLrEYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-213 |
1.92e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.59 E-value: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSI--MFQKTM 78
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIgyVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 79 FPDQ--LKVIEIINLYQSFYENPLPL---------EEIIE---LTKFDSSQLNQfvnkLSGGQ-QRLLdFVLSLIGQPQL 143
Cdd:COG1121 86 VDWDfpITVRDVVLMGRYGRRGLFRRpsradreavDEALErvgLEDLADRPIGE----LSGGQqQRVL-LARALAQDPDL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 144 ILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIeNGEIILNDSTSHIRTNQ 213
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPE 229
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-199 |
1.35e-35 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 127.20 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 3 QISNINKSFNK--RCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENR-------SIM 73
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkelrrkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 FQktmFPDQ----LKVIEII-----NLYqsfyenpLPLEEIIE-----LTKFD-SSQLNQFVNKLSGGQQRLLDFVLSLI 138
Cdd:cd03225 81 FQ---NPDDqffgPTVEEEVafgleNLG-------LPEEEIEErveeaLELVGlEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446537461 139 GQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGE 199
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-275 |
3.04e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 129.44 E-value: 3.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSF-------------------NKRCV--LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI- 58
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkgalkglfrrEYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 59 ---FDKDKLLQSENRSI---MFQKT-MFPDqLKVIEIINLYQSFYEnpLP-------LEEIIELtkFD-SSQLNQFVNKL 123
Cdd:COG4586 81 vlgYVPFKRRKEFARRIgvvFGQRSqLWWD-LPAIDSFRLLKAIYR--IPdaeykkrLDELVEL--LDlGELLDTPVRQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 124 SGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREyfwSIIENLKEDNR----TILYTSHYIEEVERMSDKIILIENGE 199
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKE---AIREFLKEYNRergtTILLTSHDMDDIEALCDRVIVIDHGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 200 IILNDSTSHIRTN--QQSQITLS-DEYIRKLKLDKDDLVIQKNhNGTIKIITS---NVNDTILYLQQlHINLDDIEIQKV 273
Cdd:COG4586 233 IIYDGSLEELKERfgPYKTIVLElAEPVPPLELPRGGEVIERE-GNRVRLEVDpreSLAEVLARLLA-RYPVRDLTIEEP 310
|
..
gi 446537461 274 SI 275
Cdd:COG4586 311 PI 312
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-206 |
1.97e-34 |
|
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: 124.40 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGE--IFDKDKLLQS----ENRSIMFQ 75
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatVAGHDVVREPrevrRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 76 KTMFPDQLKVIEIINLYQSFYENPLPL--EEIIELTKFdsSQLNQFVNKL----SGGQQRLLDFVLSLIGQPQLILLDEP 149
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAErrERIDELLDF--VGLLEAADRLvktySGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 150 TSTMDIEIREYFWSIIENLKED-NRTILYTSHYIEEVERMSDKIILIENGEIILNDST 206
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-201 |
2.41e-34 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 122.93 E-value: 2.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 3 QISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQS-------ENRSIMFQ 75
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlspkelaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 76 ktmfpdQLKVIEIINLyqsfyenplpleeiieltkfdssqLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDI 155
Cdd:cd03214 81 ------ALELLGLAHL------------------------ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446537461 156 --EIReyFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:cd03214 131 ahQIE--LLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-180 |
3.61e-34 |
|
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: 123.36 E-value: 3.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF------DKDKLLQSENRSIMF 74
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwngepiRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 75 QKTMFPDQLKVIEIINLYQSFYENPLPLEEIIE-LTKFD-SSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTST 152
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREAIDEaLEAVGlAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180
....*....|....*....|....*...
gi 446537461 153 MDIEIREYFWSIIENLKEDNRTILYTSH 180
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-209 |
1.41e-32 |
|
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: 119.98 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDIL------------IGNVNANSGEIFDKDKLLQSEN 69
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndlipgapdEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 70 RSI-M-FQK-TMFPdqlkvieiinlyQSFYEN---PLPL---------EEIIE--LTK---FDSSQLNQFVNKLSGGQQR 129
Cdd:cd03260 81 RRVgMvFQKpNPFP------------GSIYDNvayGLRLhgiklkeelDERVEeaLRKaalWDEVKDRLHALGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 130 LLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDnRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHI 209
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-201 |
3.33e-32 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 116.76 E-value: 3.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSimfqktmfpD 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR---------D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 82 QLKV-IEIInlYQsfyenplpleeiieltkfdssqlnqfvnkLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREY 160
Cdd:cd03216 72 ARRAgIAMV--YQ-----------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446537461 161 FWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:cd03216 121 LFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-199 |
7.79e-32 |
|
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: 116.52 E-value: 7.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSImfqktmfPD 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDEL-------PP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 82 QLKVIEIInlYQSFYENPLpleeiieLTKFDSSQLnqfvnKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYF 161
Cdd:cd03229 74 LRRRIGMV--FQDFALFPH-------LTVLENIAL-----GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREV 139
|
170 180 190
....*....|....*....|....*....|....*....
gi 446537461 162 WSIIENLKE-DNRTILYTSHYIEEVERMSDKIILIENGE 199
Cdd:cd03229 140 RALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-201 |
8.43e-32 |
|
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: 117.25 E-value: 8.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 3 QISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSI--MFQK---- 76
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIgyVPQRrsid 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 TMFPdqLKVIEII--NLY----------QSFYENPLPLEEIIELTKFDSSQLNQfvnkLSGGQ-QRLLdFVLSLIGQPQL 143
Cdd:cd03235 81 RDFP--ISVRDVVlmGLYghkglfrrlsKADKAKVDEALERVGLSELADRQIGE----LSGGQqQRVL-LARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 144 ILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIeNGEII 201
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-201 |
1.18e-31 |
|
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: 117.61 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSF----NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQSENR----- 70
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIiFDGKDLLKLSRRlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 71 ----SIMFQKTM--FPDQLKVIEIIN---LYQSFYENPLPLEEIIELTKF----DSSQLNQFVNKLSGGQ-QRLLdFVLS 136
Cdd:cd03257 81 rkeiQMVFQDPMssLNPRMTIGEQIAeplRIHGKLSKKEARKEAVLLLLVgvglPEEVLNRYPHELSGGQrQRVA-IARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446537461 137 LIGQPQLILLDEPTSTMDIEIREYFWSIIENLKED-NRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-214 |
1.71e-31 |
|
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: 117.15 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKL--LQSENRSIM----- 73
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlFDGEDItgLPPHEIARLgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 FQKT-MFPDqLKVIEiiNL---YQSFYENPLPL--------------EEIIELTKFDSsQLNQFVNKLSGGQQRLLDFVL 135
Cdd:cd03219 81 FQIPrLFPE-LTVLE--NVmvaAQARTGSGLLLararreereareraEELLERVGLAD-LADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446537461 136 SLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQQ 214
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-201 |
3.93e-31 |
|
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: 115.69 E-value: 3.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQS---ENRSI--MFQK 76
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvppERRNIgmVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 -TMFPDqLKVIEiiNLYQSFYENPLPLEEI-------IELTKFDsSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDE 148
Cdd:cd03259 81 yALFPH-LTVAE--NIAFGLKLRGVPKAEIrarvrelLELVGLE-GLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446537461 149 PTSTMD----IEIREYFWSIIENLKednRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:cd03259 157 PLSALDaklrEELREELKELQRELG---ITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-227 |
4.28e-31 |
|
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: 116.44 E-value: 4.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSF----NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQSENRS---- 71
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtFDGRPVTRRRRKAfrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 72 --IMFQktmfpD-------QLKVIEIIN--LY-QSFYENPLPLEEIIELTKFDSSQLNQFVNKLSGGQ-QRLLdFVLSLI 138
Cdd:COG1124 81 vqMVFQ-----DpyaslhpRHTVDRILAepLRiHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQrQRVA-IARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 139 GQPQLILLDEPTSTMDIEIREYFWSIIENLKED-NRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTnqqsqi 217
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA------ 228
|
250
....*....|
gi 446537461 218 TLSDEYIRKL 227
Cdd:COG1124 229 GPKHPYTREL 238
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-233 |
1.66e-30 |
|
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: 115.18 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSG---EIFDKDklLQSEN-----RSI 72
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFGER--RGGEDvwelrKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 73 ------MFQKtmFPDQLKVIEII--NLYQSF--YENPLPL-----EEIIELtkFDSSQL-NQFVNKLSGGQQRLldfVL- 135
Cdd:COG1119 81 glvspaLQLR--FPRDETVLDVVlsGFFDSIglYREPTDEqreraRELLEL--LGLAHLaDRPFGTLSQGEQRR---VLi 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 136 --SLIGQPQLILLDEPTSTMDIEIREYFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTN 212
Cdd:COG1119 154 arALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTS 233
|
250 260
....*....|....*....|.
gi 446537461 213 QqsqiTLSDEYIRKLKLDKDD 233
Cdd:COG1119 234 E----NLSEAFGLPVEVERRD 250
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-201 |
3.54e-30 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 113.06 E-value: 3.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGkCIALIGKNGAGKSTLIDILIGNVNANSGEI-FD--KDKLLQSENRSI---MFQ 75
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIrIDgqDVLKQPQKLRRRigyLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 76 KTMFPDQLKVIEIINlYQSFY------ENPLPLEEIIELTkfdssQLNQF----VNKLSGGQQRLLDFVLSLIGQPQLIL 145
Cdd:cd03264 80 EFGVYPNFTVREFLD-YIAWLkgipskEVKARVDEVLELV-----NLGDRakkkIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446537461 146 LDEPTSTMDIEIREYFWSIIENLKEDnRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-204 |
8.64e-30 |
|
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: 112.81 E-value: 8.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-------FDKDKLLQSENRSIMFQKTMFPDQLKVIEI 88
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvaglvpWKRRKKFLRRIGVVFGQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 89 INLYQSFY--------ENPLPLEEIIELTKFdssqLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDI----E 156
Cdd:cd03267 116 FYLLAAIYdlpparfkKRLDELSELLDLEEL----LDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVvaqeN 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446537461 157 IREYfwsiienLKEDNR----TILYTSHYIEEVERMSDKIILIENGEIILND 204
Cdd:cd03267 192 IRNF-------LKEYNRergtTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-217 |
1.30e-29 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 112.21 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----DKDKLLQSENR------S 71
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgeDISGLSEAELYrlrrrmG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 72 IMFQKTMFPDQLKVIEII--NLYQSFyenPLPLEEIIELT--KFDSSQLNQFVNK----LSGGQQRLLDFVLSLIGQPQL 143
Cdd:cd03261 81 MLFQSGALFDSLTVFENVafPLREHT---RLSEEEIREIVleKLEAVGLRGAEDLypaeLSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446537461 144 ILLDEPTSTMDIEIREYFWSIIENLKED-NRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQQSQI 217
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPLV 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-201 |
3.00e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 113.77 E-value: 3.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQKTMFP- 80
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPq 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 81 -DQLK----VIEIINLYQSFYE-NPLPLEEII-ELTKFD--SSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTS 151
Cdd:PRK13536 122 fDNLDleftVRENLLVFGRYFGmSTREIEAVIpSLLEFArlESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446537461 152 TMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-214 |
8.59e-29 |
|
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: 110.51 E-value: 8.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKL--LQSENRSIM---- 73
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlFDGRDItgLPPHRIARLgiar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 -FQKT-MFPDqLKVIEiiNLY--------QSFYENPLPL--------------EEIIELTKFDSsQLNQFVNKLSGGQQR 129
Cdd:COG0411 84 tFQNPrLFPE-LTVLE--NVLvaaharlgRGLLAALLRLprarreereareraEELLERVGLAD-RADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 130 LLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKED-NRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSH 208
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
....*.
gi 446537461 209 IRTNQQ 214
Cdd:COG0411 240 VRADPR 245
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-217 |
2.43e-28 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 109.38 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSF-NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI--FDKD--KLLQSENRSIM-- 73
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEIlvDGQDvtALRGRALRRLRrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 ----FQKTMFPDQLKVIEIINL----YQSFYE---NPLPLEEIIE----LTKFD-SSQLNQFVNKLSGGQQ------RLL 131
Cdd:COG3638 82 igmiFQQFNLVPRLSVLTNVLAgrlgRTSTWRsllGLFPPEDRERaleaLERVGlADKAYQRADQLSGGQQqrvaiaRAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 132 dfvlslIGQPQLILLDEPTSTMDIEIREyfwSIIENLK----EDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTS 207
Cdd:COG3638 162 ------VQEPKLILADEPVASLDPKTAR---QVMDLLRriarEDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPA 232
|
250
....*....|
gi 446537461 208 HIRTNQQSQI 217
Cdd:COG3638 233 ELTDAVLREI 242
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-203 |
3.20e-28 |
|
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: 107.69 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENrsimfqktmfpD 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-----------E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 82 QLKVIEIINLYQSFYENPLPLEEIIELTK---FDSSQLNQF-------------VNKLSGGQQRLLDFVLSLIGQPQLIL 145
Cdd:cd03268 70 ALRRIGALIEAPGFYPNLTARENLRLLARllgIRKKRIDEVldvvglkdsakkkVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446537461 146 LDEPTSTMD----IEIREyfwsIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILN 203
Cdd:cd03268 150 LDEPTNGLDpdgiKELRE----LILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-201 |
7.14e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.03 E-value: 7.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLL------QSENR--SI 72
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrsprDAQAAgiAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 73 MFQK-TMFPDqLKVIEiiNLYQSFYENPLPL----------EEIIELTKFDSSqLNQFVNKLSGGQQRLLDFVLSLIGQP 141
Cdd:COG1129 84 IHQElNLVPN-LSVAE--NIFLGREPRRGGLidwramrrraRELLARLGLDID-PDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 142 QLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-200 |
1.58e-27 |
|
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: 106.42 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSF----NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF--DKDKLLQSENRSIMFQ 75
Cdd:cd03255 1 IELKNLSKTYggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 76 KtmfpDQLKVIeiinlYQSF--------YEN---PL-----PLEEIIE-----LTKFD-SSQLNQFVNKLSGGQQ----- 128
Cdd:cd03255 81 R----RHIGFV-----FQSFnllpdltaLENvelPLllagvPKKERREraeelLERVGlGDRLNHYPSELSGGQQqrvai 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446537461 129 -RlldfvlSLIGQPQLILLDEPTSTMDIEIREYFWSIIENL-KEDNRTILYTSHYiEEVERMSDKIILIENGEI 200
Cdd:cd03255 152 aR------ALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-201 |
1.66e-27 |
|
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: 106.88 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSF-NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKD----KLLQSENRSI---- 72
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinKLKGKALRQLrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 73 --MFQKTMFPDQLKVIEII--------NLYQSFYeNPLPLEEIIE----LTKFD-SSQLNQFVNKLSGGQQRLLDFVLSL 137
Cdd:cd03256 81 gmIFQQFNLIERLSVLENVlsgrlgrrSTWRSLF-GLFPKEEKQRalaaLERVGlLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 138 IGQPQLILLDEPTSTMDIEIREyfwSIIENLK----EDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSR---QVMDLLKrinrEEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-201 |
2.16e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.92 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI----------FDKDKLLQSENR 70
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklgetvkigyFDQHQEELDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 71 SIM--FQKTMfpDQLKVIEIINLYQSFyenpLpleeiieltkFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDE 148
Cdd:COG0488 395 TVLdeLRDGA--PGGTEQEVRGYLGRF----L----------FSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446537461 149 PTSTMDIEIREyfwSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:COG0488 459 PTNHLDIETLE---ALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-201 |
3.71e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 106.33 E-value: 3.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRC----VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQ--SENRSIMF 74
Cdd:COG1116 7 ALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTgpGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 75 QK-TMFPdQLKVIEiiNLYqsfyenpLPLE--------------EIIELTkfdssQLNQFVNK----LSGGQQ------R 129
Cdd:COG1116 87 QEpALLP-WLTVLD--NVA-------LGLElrgvpkaerrerarELLELV-----GLAGFEDAyphqLSGGMRqrvaiaR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446537461 130 lldfvlSLIGQPQLILLDEPTSTMDIEIREYFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIILIEN--GEII 201
Cdd:COG1116 152 ------ALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-201 |
3.99e-27 |
|
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: 105.14 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSF--NKRCV--LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI----FD--KDKLLQSENR 70
Cdd:cd03266 1 MITADALTKRFrdVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAtvdgFDvvKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 71 SIMFQKTMFPDQLKVIEIINLYQSFY-----ENPLPLEEIIELTKFDSSqLNQFVNKLSGGQQRLLDFVLSLIGQPQLIL 145
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYglkgdELTARLEELADRLGMEEL-LDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446537461 146 LDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-218 |
9.92e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 104.69 E-value: 9.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSI-------- 72
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInklrrkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 73 M-FQK-TMFPDqLKVIE-IInlyqsfyENP-----LPLEEIIE-----LTKFD-SSQLNQFVNKLSGGQQ------Rlld 132
Cdd:COG1126 81 MvFQQfNLFPH-LTVLEnVT-------LAPikvkkMSKAEAEEramelLERVGlADKADAYPAQLSGGQQqrvaiaR--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 133 fvlSLIGQPQLILLDEPTSTMDIE-IREYFwSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRT 211
Cdd:COG1126 150 ---ALAMEPKVMLFDEPTSALDPElVGEVL-DVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
|
....*..
gi 446537461 212 NQQSQIT 218
Cdd:COG1126 226 NPQHERT 232
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-230 |
1.50e-26 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 105.23 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNK-----RCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENR------ 70
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkklkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 71 ----SIMFQktmFPDqlkvieiinlYQSFYEN--------P----LPLEEI-------IELTKFDSSQLNQFVNKLSGGQ 127
Cdd:TIGR04521 81 rkkvGLVFQ---FPE----------HQLFEETvykdiafgPknlgLSEEEAeervkeaLELVGLDEEYLERSPFELSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 128 QRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDST 206
Cdd:TIGR04521 148 MRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTP 227
|
250 260
....*....|....*....|....
gi 446537461 207 SHIRTNQqsqitlsdEYIRKLKLD 230
Cdd:TIGR04521 228 REVFSDV--------DELEKIGLD 243
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-212 |
1.73e-26 |
|
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: 103.67 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQS-------------- 67
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlppheraragigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 68 -ENRSImfqktmFPdQLKVIEiiNLYQSFY-----ENPLPLEEIIELtkFD--SSQLNQFVNKLSGGQQRLLDFVLSLIG 139
Cdd:cd03224 81 pEGRRI------FP-ELTVEE--NLLLGAYarrraKRKARLERVYEL--FPrlKERRKQLAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446537461 140 QPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTN 212
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-225 |
2.22e-26 |
|
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: 103.91 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF---------DKDKLLQSENR- 70
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvdgqditglSEKELYELRRRi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 71 SIMFQK-TMFpDQLKVieiinlyqsfYEN---PL------PLEEIIEL--TKFDSSQLNQFVNK----LSGGQQ------ 128
Cdd:COG1127 85 GMLFQGgALF-DSLTV----------FENvafPLrehtdlSEAEIRELvlEKLELVGLPGAADKmpseLSGGMRkrvala 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 129 RlldfvlSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKED-NRTILYTSHYIEEVERMSDKIILIENGEIILNDSTS 207
Cdd:COG1127 154 R------ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPE 227
|
250
....*....|....*...
gi 446537461 208 HIRTNQqsqitlsDEYIR 225
Cdd:COG1127 228 ELLASD-------DPWVR 238
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-227 |
2.52e-26 |
|
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: 108.07 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRC-----VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----DKDKLLQSENR- 70
Cdd:COG1123 260 LLEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgkDLTKLSRRSLRe 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 71 -----SIMFQ--KTMFPDQLKVIEIInlyqsfyENPLPL-------------EEIIELTKFDSSQLNQFVNKLSGGQ-QR 129
Cdd:COG1123 340 lrrrvQMVFQdpYSSLNPRMTVGDII-------AEPLRLhgllsraerrervAELLERVGLPPDLADRYPHELSGGQrQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 130 LldfvlS----LIGQPQLILLDEPTSTMDIEIREyfwSIIENLK----EDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:COG1123 413 V-----AiaraLALEPKLLILDEPTSALDVSVQA---QILNLLRdlqrELGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
250 260
....*....|....*....|....*.
gi 446537461 202 LNDSTSHIRTNQQsqitlsDEYIRKL 227
Cdd:COG1123 485 EDGPTEEVFANPQ------HPYTRAL 504
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-201 |
3.28e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 104.89 E-value: 3.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQKTMFP- 80
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 81 -DQL----KVIEIINLYQSFYEnpLPLEEI-------IELTKFDSSQLNQfVNKLSGGQQRLLDFVLSLIGQPQLILLDE 148
Cdd:PRK13537 88 fDNLdpdfTVRENLLVFGRYFG--LSAAAAralvpplLEFAKLENKADAK-VGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446537461 149 PTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKI 217
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-202 |
3.46e-26 |
|
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: 101.62 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSF--NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIfdkdkLLQSENRSImFQKTMf 79
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-----TLDGVPVSD-LEKAL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 80 pdqLKVIEIINlyQSFYenplpleeiieltKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMD-IEIR 158
Cdd:cd03247 74 ---SSLISVLN--QRPY-------------LFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDpITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446537461 159 EYFWSIIENLKedNRTILYTSHYIEEVERMsDKIILIENGEIIL 202
Cdd:cd03247 136 QLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-201 |
4.66e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 105.23 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF--DKDKL--LQSENRSI--MFQ 75
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVlnGRDLFtnLPPRERRVgfVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 76 KTM-FPDqLKVieiinlyqsfYEN--------PLPLEEIIE-----LTKFDSSQL-NQFVNKLSGGQQ------Rlldfv 134
Cdd:COG1118 83 HYAlFPH-MTV----------AENiafglrvrPPSKAEIRArveelLELVQLEGLaDRYPSQLSGGQRqrvalaR----- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446537461 135 lSLIGQPQLILLDEPTSTMDI----EIREyfWsIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:COG1118 147 -ALAVEPEVLLLDEPFGALDAkvrkELRR--W-LRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIE 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-201 |
1.68e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 101.27 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSF----NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF--DKD--KLLQSE---- 68
Cdd:COG1136 4 LLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidGQDisSLSERElarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 69 -NRSIMFqktmfpdqlkvieiinLYQSFY--------EN---PL-----PLEEIIE-----LTKFD-SSQLNQFVNKLSG 125
Cdd:COG1136 84 rRRHIGF----------------VFQFFNllpeltalENvalPLllagvSRKERRErarelLERVGlGDRLDHRPSQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 126 GQQ------RlldfvlSLIGQPQLILLDEPTSTMDIEIREYFWSIIENL-KEDNRTILYTSHYiEEVERMSDKIILIENG 198
Cdd:COG1136 148 GQQqrvaiaR------ALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHD-PELAARADRVIRLRDG 220
|
...
gi 446537461 199 EII 201
Cdd:COG1136 221 RIV 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-200 |
2.07e-25 |
|
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: 100.68 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQSENR--------SI 72
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiIDGLKLTDDKKNinelrqkvGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 73 MFQK-TMFPdQLKVIEIINLYQSFYENpLPLEEIIE-----LTKFD-SSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLIL 145
Cdd:cd03262 81 VFQQfNLFP-HLTVLENITLAPIKVKG-MSKAEAEEralelLEKVGlADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446537461 146 LDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-201 |
2.38e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.51 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSF-NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI--FDKD--------------- 62
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvNGQDlsrlkrreipylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 63 --------KLLqsENRSImFQKTMFPdqLKVIEiinlyqsfyenpLPLEEIIE-----LTKFD-SSQLNQFVNKLSGG-Q 127
Cdd:COG2884 81 igvvfqdfRLL--PDRTV-YENVALP--LRVTG------------KSRKEIRRrvrevLDLVGlSDKAKALPHELSGGeQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446537461 128 QRLldfVL--SLIGQPQLILLDEPTSTMDieiREYFWSIIENLKEDNR---TILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:COG2884 144 QRV---AIarALVNRPELLLADEPTGNLD---PETSWEIMELLEEINRrgtTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-217 |
5.73e-25 |
|
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: 100.07 E-value: 5.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSF-NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF--------DKDKLLQSENRS 71
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILlegtditkLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 72 I--MFQKTMFPDQLKVIEiiNL------YQSFYE---NPLPLEEIIE----LTKFDSSQL-NQFVNKLSGGQQRLLDFVL 135
Cdd:TIGR02315 81 IgmIFQHYNLIERLTVLE--NVlhgrlgYKPTWRsllGRFSEEDKERalsaLERVGLADKaYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 136 SLIGQPQLILLDEPTSTMDIEIREYFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQQ 214
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVL 238
|
...
gi 446537461 215 SQI 217
Cdd:TIGR02315 239 RHI 241
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-199 |
1.03e-24 |
|
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: 97.45 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSF--NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----DKDKLLQSENR---SI 72
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvDLRDLDLESLRkniAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 73 MFQKT-MFPDqlkvieiinlyqSFYENplpleeIieltkfdssqlnqfvnkLSGGQQRLLDFVLSLIGQPQLILLDEPTS 151
Cdd:cd03228 81 VPQDPfLFSG------------TIREN------I-----------------LSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446537461 152 TMDIEIREYFWSIIENLKEDnRTILYTSHYIEEVERMsDKIILIENGE 199
Cdd:cd03228 126 ALDPETEALILEALRALAKG-KTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-151 |
1.53e-24 |
|
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: 96.56 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIM-------FQKTMFPDQLKVIEII 89
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrkeigyvFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 90 NLYQSFYENPLP-----LEEIIE---LTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTS 151
Cdd:pfam00005 81 RLGLLLKGLSKRekdarAEEALEklgLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-216 |
1.64e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 99.01 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLI------------DILIGNVNANSGEIfdKDKLLQSE 68
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrcinkleeitsgDLIVDGLKVNDPKV--DERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 69 NRSIMFQKTMFPdQLKVIEIInlyqSFyeNPLPL--------EEIIE--LTKFD-SSQLNQFVNKLSGGQQRLLDFVLSL 137
Cdd:PRK09493 79 AGMVFQQFYLFP-HLTALENV----MF--GPLRVrgaskeeaEKQARelLAKVGlAERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446537461 138 IGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQQSQ 216
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-203 |
2.21e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.98 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 4 ISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQS--ENRSIMFQKTMFPD 81
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEarEDTRLMFQDARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 82 QLKVIEIINLYQSFYENPLPLE--EIIELtkfdSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIRE 159
Cdd:PRK11247 95 WKKVIDNVGLGLKGQWRDAALQalAAVGL----ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446537461 160 YFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEIILN 203
Cdd:PRK11247 171 EMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-201 |
2.82e-24 |
|
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: 97.54 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSF----NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQ-SENRSIMFQ 75
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlVDGEPVTGpGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 76 K-TMFPdQLKVIEIINL--------YQSFYENPLPLEEIIELTKFdssqLNQFVNKLSGGQQRLLDFVLSLIGQPQLILL 146
Cdd:cd03293 81 QdALLP-WLTVLDNVALglelqgvpKAEARERAEELLELVGLSGF----ENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 147 DEPTSTMDIEIREYFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIILIEN--GEII 201
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-207 |
2.88e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.90 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRcvLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----DKDKLLQSEnR--SIMF 74
Cdd:COG3840 1 MLRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILwngqDLTALPPAE-RpvSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 75 QK-TMFPdQLKVIEiiNLYqsfyenpLPLEEIIELTKFDSSQLNQFVNK-------------LSGGQQ------RLLdfv 134
Cdd:COG3840 78 QEnNLFP-HLTVAQ--NIG-------LGLRPGLKLTAEQRAQVEQALERvglaglldrlpgqLSGGQRqrvalaRCL--- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446537461 135 lsLIGQPqLILLDEPTSTMDIEIREYFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTS 207
Cdd:COG3840 145 --VRKRP-ILLLDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTA 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-201 |
2.94e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 100.56 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF--DKDKL-LQSENRSI--MFQ 75
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILldGRDVTgLPPEKRNVgmVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 76 K-TMFPdqlkvieiiNLyqSFYEN---PL-----PLEEI----------IELTKFdssqLNQFVNKLSGGQQ------Rl 130
Cdd:COG3842 85 DyALFP---------HL--TVAENvafGLrmrgvPKAEIrarvaellelVGLEGL----ADRYPHQLSGGQQqrvalaR- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446537461 131 ldfvlSLIGQPQLILLDEPTSTMD--------IEIREYfwsiienLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:COG3842 149 -----ALAPEPRVLLLDEPLSALDaklreemrEELRRL-------QRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-200 |
3.86e-24 |
|
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: 97.69 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQS-----ENRSIMFQK 76
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpphkRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 -TMFPdqlkvieiinlYQSFYEN---PLPL------------EEIIELTKFDsSQLNQFVNKLSGGQQRLLDFVLSLIGQ 140
Cdd:cd03300 81 yALFP-----------HLTVFENiafGLRLkklpkaeikervAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446537461 141 PQLILLDEPTSTMDIEIREyfwSIIENLKEDNR----TILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRK---DMQLELKRLQKelgiTFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-202 |
4.25e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 4.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 4 ISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFdkdklLQSENR-SIMFQKTMFPDQ 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS-----IPKGLRiGYLPQEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 83 LKVIEII---------------NLYQSFYENPLPLEEIIELT----------------------KFDSSQLNQFVNKLSG 125
Cdd:COG0488 76 LTVLDTVldgdaelraleaeleELEAKLAEPDEDLERLAELQeefealggweaearaeeilsglGFPEEDLDRPVSELSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 126 GQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREyfWsiIEN-LKEDNRTILYTSH---YIEEVermSDKIILIENGEII 201
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--W--LEEfLKNYPGTVLVVSHdryFLDRV---ATRILELDRGKLT 228
|
.
gi 446537461 202 L 202
Cdd:COG0488 229 L 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-221 |
5.10e-24 |
|
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: 101.44 E-value: 5.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIG--NVNANSGEI-FDKDKLLQSENR------- 70
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIyWSGSPLKASNIRdteragi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 71 SIMFQKTMFPDQLKVIEIINL---------YQSFYENPLPLEEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQP 141
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLgneitlpggRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 142 QLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEiilndstsHIRTNQQSQITLSD 221
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ--------HVATKDMSTMSEDD 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-216 |
6.18e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.39 E-value: 6.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDIL------------IGNVNAN-SGEIFDKDKLLQSE 68
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprsgtlnIAGNHFDfSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 69 NRSIMFQKTMFPDQLKVIEiiNLYqsfyENPLpleEIIELTK----------FDSSQLNQFVNK----LSGGQQRLLDFV 134
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQ--NLI----EAPC---RVLGLSKdqalaraeklLERLRLKPYADRfplhLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 135 LSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQQ 214
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQPQT 233
|
..
gi 446537461 215 SQ 216
Cdd:PRK11124 234 EA 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-215 |
6.71e-24 |
|
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: 101.13 E-value: 6.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSF--NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNAN---SGEI-FDKDKLLQSENR---- 70
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVlLDGRDLLELSEAlrgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 71 --SIMFQKTMfpDQLkvieiinlyqsfyeNPLP----LEEIIELTKFDSSQ-----------------LNQFVNKLSGGQ 127
Cdd:COG1123 84 riGMVFQDPM--TQL--------------NPVTvgdqIAEALENLGLSRAEararvlelleavglerrLDRYPHQLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 128 -QRLLdFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDS 205
Cdd:COG1123 148 rQRVA-IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
250
....*....|
gi 446537461 206 TSHIRTNQQS 215
Cdd:COG1123 227 PEEILAAPQA 236
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-201 |
9.69e-24 |
|
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: 101.06 E-value: 9.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNInkSF----NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----DKDKLLQSENRSIM 73
Cdd:COG2274 474 IELENV--SFrypgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgiDLRQIDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 ---FQKTMFpdqlkvieiinLYQSFYEN------PLPLEEIIELTKFdsSQLNQFVNK---------------LSGGQ-Q 128
Cdd:COG2274 552 gvvLQDVFL-----------FSGTIRENitlgdpDATDEEIIEAARL--AGLHDFIEAlpmgydtvvgeggsnLSGGQrQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446537461 129 RLLdfvL--SLIGQPQLILLDEPTSTMDIEIREYfwsIIENLKE--DNRTILYTSHYIEEVeRMSDKIILIENGEII 201
Cdd:COG2274 619 RLA---IarALLRNPRILILDEATSALDAETEAI---ILENLRRllKGRTVIIIAHRLSTI-RLADRIIVLDKGRIV 688
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-199 |
1.02e-23 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 94.05 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIfdkdkllqsenrsimfqktmfpD 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------T 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 82 QLKVIEIinlyqsfyenplpleeiieltkfdssqlnQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREyf 161
Cdd:cd03221 59 WGSTVKI-----------------------------GYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIE-- 107
|
170 180 190
....*....|....*....|....*....|....*...
gi 446537461 162 wSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGE 199
Cdd:cd03221 108 -ALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-201 |
1.12e-23 |
|
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: 100.65 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIG--NVNANSGEI--------------------- 58
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 59 ----------------FDKDKLLQSENR---SIMFQKT--MFPDQLKVIEIIN-LYQSFYENPLPLE---EIIELTKFdS 113
Cdd:TIGR03269 81 pcpvcggtlepeevdfWNLSDKLRRRIRkriAIMLQRTfaLYGDDTVLDNVLEaLEEIGYEGKEAVGravDLIEMVQL-S 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 114 SQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWS-IIENLKEDNRTILYTSHYIEEVERMSDKI 192
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
....*....
gi 446537461 193 ILIENGEII 201
Cdd:TIGR03269 240 IWLENGEIK 248
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-213 |
1.34e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.49 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQSENRSIMFQK-TM 78
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIvFDGKDITDWQTAKIMREAvAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 79 FPDQLKVIEIINLYQS------FYENPLPLEEII---ELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEP 149
Cdd:PRK11614 85 VPEGRRVFSRMTVEENlamggfFAERDQFQERIKwvyELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446537461 150 TSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQ 213
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANE 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-213 |
1.35e-23 |
|
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: 96.60 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNK-RCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSEN-----RSI--M 73
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDpvelrRKIgyV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 FQKT-MFPdQLKVIEIINLYQSFYENPLP-----LEEIIELTKFDSSQL-NQFVNKLSGGQQRLLDFVLSLIGQPQLILL 146
Cdd:cd03295 81 IQQIgLFP-HMTVEENIALVPKLLKWPKEkirerADELLALVGLDPAEFaDRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 147 DEPTSTMDIEIREYFWSIIENLKED-NRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQ 213
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-200 |
1.41e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 98.62 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDK---LLQSENRSI--MFQK 76
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsRLHARDRKVgfVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 TMFPDQLKVIEIInlyqSFYENPLP----------------LEEIIELTKFdssqLNQFVNKLSGGQQRLLDFVLSLIGQ 140
Cdd:PRK10851 83 YALFRHMTVFDNI----AFGLTVLPrrerpnaaaikakvtqLLEMVQLAHL----ADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446537461 141 PQLILLDEPTSTMDIEIREYFWSIIENLKEDNR-TILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-214 |
2.51e-23 |
|
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: 95.43 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQS------------ 67
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIrFDGEDITGLpphriarlgigy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 68 --ENRSImfqktmFPDqLKVIEiiNL----YQSFYENPLP--LEEIIELtkFD--SSQLNQFVNKLSGGQQRLLDFVLSL 137
Cdd:COG0410 83 vpEGRRI------FPS-LTVEE--NLllgaYARRDRAEVRadLERVYEL--FPrlKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 138 IGQPQLILLDEPTstmdiE-----IREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTN 212
Cdd:COG0410 152 MSRPKLLLLDEPS-----LglaplIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLAD 226
|
..
gi 446537461 213 QQ 214
Cdd:COG0410 227 PE 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-294 |
2.53e-23 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 100.09 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 24 IEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSeNRSIMFQKTMFPDQLKVIEII-----NLYQSFYEN 98
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLltgreHLYLYARLR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 99 PLPLEEIIELTKF--DSSQLNQFVNKL----SGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDN 172
Cdd:TIGR01257 2041 GVPAEEIEKVANWsiQSLGLSLYADRLagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREG 2120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 173 RTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNqqsqitLSDEYI--RKLKLDKDDLV---------IQKNHN 241
Cdd:TIGR01257 2121 RAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSK------FGDGYIvtMKIKSPKDDLLpdlnpveqfFQGNFP 2194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446537461 242 GTIK------IITSNVNDTIL--YLQQLHINLDDIEIQKVSIVDS-----YFNNKKQRGSNYDTKL 294
Cdd:TIGR01257 2195 GSVQrerhynMLQFQVSSSSLarIFQLLISHKDSLLIEEYSVTQTtldqvFVNFAKQQTETYDLPL 2260
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-213 |
2.56e-23 |
|
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: 95.30 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENrsiMFQK----- 76
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP---MHKRarlgi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 -------TMFPDqLKVIEiiNLYQSFYENPLPLEEIIE-----LTKFDSSQL-NQFVNKLSGGQQRLLDFVLSLIGQPQL 143
Cdd:cd03218 78 gylpqeaSIFRK-LTVEE--NILAVLEIRGLSKKEREEkleelLEEFHITHLrKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446537461 144 ILLDEPTSTMD----IEIREyfwsIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQ 213
Cdd:cd03218 155 LLLDEPFAGVDpiavQDIQK----IIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-201 |
2.90e-23 |
|
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: 95.48 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFnKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF--DKD-KLLQSENRSIMF---Q 75
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlnGKDiTNLPPEKRDISYvpqN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 76 KTMFPdQLKVIEII--NLYQSFYENPLPLEEIIELTKF--DSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTS 151
Cdd:cd03299 80 YALFP-HMTVYKNIayGLKKRKVDKKEIERKVLEIAEMlgIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446537461 152 TMDIEIREyfwSIIENLK----EDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:cd03299 159 ALDVRTKE---KLREELKkirkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-200 |
6.05e-23 |
|
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: 96.64 E-value: 6.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLL-----QSENRSIMFQK 76
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDItrlppQKRDYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 -TMFPDqLKVIEII--NLYQSFY---ENPLPLEEIIELTKFDSSQlNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPT 150
Cdd:TIGR03265 85 yALFPN-LTVADNIayGLKNRGMgraEVAERVAELLDLVGLPGSE-RKYPGQLSGGQQQRVALARALATSPGLLLLDEPL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446537461 151 STMDIEIREYF-WSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:TIGR03265 163 SALDARVREHLrTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVI 213
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-221 |
6.41e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.08 E-value: 6.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIG--NVNANSGEIFDKDKLLQSENR-------- 70
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIFEGEELQASNIrdteragi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 71 SIMFQKTMFPDQLKVIEIINL-----------YQSFYenpLPLEEIIELTKFDSSqLNQFVNKLSGGQQRLLDFVLSLIG 139
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLgneitpggimdYDAMY---LRAQKLLAQLKLDIN-PATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 140 QPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEiilndstsHIRTNQQSQITL 219
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR--------HIGTRPAAGMTE 232
|
..
gi 446537461 220 SD 221
Cdd:PRK13549 233 DD 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-201 |
8.32e-23 |
|
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: 97.91 E-value: 8.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSF-NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQK---- 76
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQiawv 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 ----TMFPDQLKVieiiNLyqSFYENPLPLEEIIELTKfdSSQLNQFVNK---------------LSGGQ-QRLldfVL- 135
Cdd:COG4988 417 pqnpYLFAGTIRE----NL--RLGRPDASDEELEAALE--AAGLDEFVAAlpdgldtplgeggrgLSGGQaQRL---ALa 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446537461 136 -SLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDnRTILYTSHYIEEVERMsDKIILIENGEII 201
Cdd:COG4988 486 rALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG-RTVILITHRLALLAQA-DRILVLDDGRIV 550
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-201 |
1.22e-22 |
|
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: 93.13 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 19 NISFDIEQGKcIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSI-----------MFQK-TMFPdQLKVI 86
Cdd:cd03297 16 KIDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqqrkiglVFQQyALFP-HLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 87 EIINLYQSFYENP---LPLEEIIELTKFDSsQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWS 163
Cdd:cd03297 94 ENLAFGLKRKRNRedrISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 446537461 164 IIENLKED-NRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:cd03297 173 ELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-224 |
1.61e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 93.95 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLI-----------------DILIGNVNansgeIFDKDKL 64
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmndlipgarvegEILLDGED-----IYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 65 LQSENRSIM--FQK-TMFPdqlkvieiinlyQSFYEN---PLP---------LEEIIE--LTK---FD--SSQLNQFVNK 122
Cdd:COG1117 87 VVELRRRVGmvFQKpNPFP------------KSIYDNvayGLRlhgikskseLDEIVEesLRKaalWDevKDRLKKSALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 123 LSGGQQRLLDFVLSLIGQPQLILLDEPTS------TMDIEireyfwSIIENLKEDnRTILYTSHYIEEVERMSDKIILIE 196
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSaldpisTAKIE------ELILELKKD-YTIVIVTHNMQQAARVSDYTAFFY 227
|
250 260
....*....|....*....|....*...
gi 446537461 197 NGEIILNDSTSHIRTNQQSQITlsDEYI 224
Cdd:COG1117 228 LGELVEFGPTEQIFTNPKDKRT--EDYI 253
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-216 |
1.90e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 93.54 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILigNV--NANSGEI------FD-------KDKLLQ 66
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVL--NLleTPDSGQLniaghqFDfsqkpseKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 67 SENRSIMFQKTMFPDQLKVIEiiNLYqsfyENP-----LPLEEIIELTKFDSSQL------NQFVNKLSGGQQRLLDFVL 135
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVME--NLI----EAPckvlgLSKEQAREKAMKLLARLrltdkaDRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 136 SLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQQS 215
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQPQTE 234
|
.
gi 446537461 216 Q 216
Cdd:COG4161 235 A 235
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-214 |
2.75e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 92.78 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF--DKD--KL------------ 64
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFldGEDitHLpmhkrarlgigy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 65 LQSENrSImFQKtmfpdqLKVieiinlyqsfYENplpLEEIIELTKFDSSQLNQFVNKL-----------------SGGQ 127
Cdd:COG1137 83 LPQEA-SI-FRK------LTV----------EDN---ILAVLELRKLSKKEREERLEELleefgithlrkskayslSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 128 QRLLDFVLSLIGQPQLILLDEPTSTMD----IEIREyfwsIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILN 203
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDpiavADIQK----IIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAE 217
|
250
....*....|.
gi 446537461 204 DSTSHIRTNQQ 214
Cdd:COG1137 218 GTPEEILNNPL 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-201 |
3.31e-22 |
|
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: 92.21 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLlqsenRSIMFQKTMFPDQLKVIEIINLYQSF 95
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV-----SSLLGLGGGFNPELTGRENIYLNGRL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 96 Y-----ENPLPLEEIIELtkfdsSQLNQFVNK----LSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIE 166
Cdd:cd03220 112 LglsrkEIDEKIDEIIEF-----SELGDFIDLpvktYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLR 186
|
170 180 190
....*....|....*....|....*....|....*
gi 446537461 167 NLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:cd03220 187 ELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-155 |
3.49e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.91 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQS-------ENRSIM 73
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaelaRRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 FQKTM--FPdqLKVIEIINLYQS-FYENPLPLEEIIE--LTKFDSSQL-NQFVNKLSGG-QQRL-LDFVLSLI----GQP 141
Cdd:PRK13548 82 PQHSSlsFP--FTVEEVVAMGRApHGLSRAEDDALVAaaLAQVDLAHLaGRDYPQLSGGeQQRVqLARVLAQLwepdGPP 159
|
170
....*....|....
gi 446537461 142 QLILLDEPTSTMDI 155
Cdd:PRK13548 160 RWLLLDEPTSALDL 173
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-206 |
4.69e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.45 E-value: 4.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSF----------------------NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 59 ---------------FDKDkLLQSENrsIMFQKTMFpdQLKVIEIINLYqsfyenplplEEII---ELTKFdssqLNQFV 120
Cdd:COG1134 84 evngrvsallelgagFHPE-LTGREN--IYLNGRLL--GLSRKEIDEKF----------DEIVefaELGDF----IDQPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 121 NKLSGGQQ-RLLdFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGE 199
Cdd:COG1134 145 KTYSSGMRaRLA-FAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
....*..
gi 446537461 200 IILNDST 206
Cdd:COG1134 224 LVMDGDP 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-200 |
4.79e-22 |
|
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: 91.55 E-value: 4.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKL---LQSENRSI--MFQK 76
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtdLPPKDRDIamVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 -TMFPdqlkvieiinlYQSFYEN---PLPL------------EEIIELTKFDsSQLNQFVNKLSGGQQRLLDFVLSLIGQ 140
Cdd:cd03301 81 yALYP-----------HMTVYDNiafGLKLrkvpkdeidervREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446537461 141 PQLILLDEPTSTMDIEIREYFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-198 |
5.93e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 95.36 E-value: 5.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 6 NINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIfdkdkllQSENRSIMFQKTMfpDQLKV 85
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI-------LIDGQEMRFASTT--AALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 86 -IEIInlYQSFYENP-LPLEEIIELTKF-------DSSQLNQF-----------------VNKLSGGQQRLLDFVLSLIG 139
Cdd:PRK11288 80 gVAII--YQELHLVPeMTVAENLYLGQLphkggivNRRLLNYEareqlehlgvdidpdtpLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 140 QPQLILLDEPTSTMDI-EIREYFwSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENG 198
Cdd:PRK11288 158 NARVIAFDEPTSSLSArEIEQLF-RVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-198 |
6.88e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 95.24 E-value: 6.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI------FDK-DKLLQSENR-SI 72
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinninYNKlDHKLAAQLGiGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 73 MFQKTMFPDQLKVIEiiNLYQSfyenPLPLEEIIELTKFDSSQ-----------------LNQFVNKLSGGQQRLLDFVL 135
Cdd:PRK09700 85 IYQELSVIDELTVLE--NLYIG----RHLTKKVCGVNIIDWREmrvraammllrvglkvdLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446537461 136 SLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENG 198
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-213 |
7.70e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 91.74 E-value: 7.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLI------------DILIGNVNANSGEIFDKDKLLQSE 68
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLrcinlleqpeagTIRVGDITIDTARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 69 NRS---IMFQK-TMFPDQLKVIEIInlyqsfyENPL-----PLEEIIE-----LTKFD-SSQLNQFVNKLSGGQQRLLDF 133
Cdd:PRK11264 83 LRQhvgFVFQNfNLFPHRTVLENII-------EGPVivkgePKEEATArarelLAKVGlAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 134 VLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII-------LNDST 206
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVeqgpakaLFADP 235
|
....*..
gi 446537461 207 SHIRTNQ 213
Cdd:PRK11264 236 QQPRTRQ 242
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-201 |
8.67e-22 |
|
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: 91.13 E-value: 8.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFN-KRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----DKDKLLQSENRS---IM 73
Cdd:cd03254 3 IEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidgiDIRDISRKSLRSmigVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 FQKT-MFPDQlkVIEIInlyqSFYENPLPLEEIIELTKfdSSQLNQFVNK---------------LSGGQQRLLDFVLSL 137
Cdd:cd03254 83 LQDTfLFSGT--IMENI----RLGRPNATDEEVIEAAK--EAGAHDFIMKlpngydtvlgenggnLSQGERQLLAIARAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446537461 138 IGQPQLILLDEPTSTMDIEIREYFWSIIENLKEdNRTILYTSHYIEEVERmSDKIILIENGEII 201
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKN-ADKILVLDDGKII 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-201 |
9.63e-22 |
|
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: 90.39 E-value: 9.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 3 QISNINKSFNKRC-VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQSENRSIMFQKTMFP 80
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIlLNGKPIKAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 81 D-QL---KVIEiiNLYQSFYENPLPLEEIIE-LTKFDssqLNQFVNK----LSGGQQRLLDFVLSLIGQPQLILLDEPTS 151
Cdd:cd03226 81 DyQLftdSVRE--ELLLGLKELDAGNEQAETvLKDLD---LYALKERhplsLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446537461 152 TMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-201 |
1.13e-21 |
|
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: 91.79 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIM--FQKTM---FPD-------QL 83
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRraFRRDVqlvFQDspsavnpRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 84 KVIEII--------NLYQSfyENPLPLEEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDI 155
Cdd:TIGR02769 106 TVRQIIgeplrhltSLDES--EQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446537461 156 EIREYFWSIIENLKEDNRT-ILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:TIGR02769 184 VLQAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-200 |
2.55e-21 |
|
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: 88.43 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNInkSF----NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIfdkdkLLQSenrsimfqkt 77
Cdd:cd03246 1 LEVENV--SFrypgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-----RLDG---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 78 mfpdqlkvieiinlyqsfyenplpleeiIELTKFDSSQLNQFV----------------NKLSGGQ-QRLLdFVLSLIGQ 140
Cdd:cd03246 64 ----------------------------ADISQWDPNELGDHVgylpqddelfsgsiaeNILSGGQrQRLG-LARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 141 PQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMsDKIILIENGEI 200
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-209 |
2.58e-21 |
|
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: 92.47 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 19 NISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIM-----------FQKT-MFPdQLKVI 86
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFlpphrrrigyvFQEArLFP-HLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 87 EiiNLyqsFY--------ENPLPLEEIIELTKFdSSQLNQFVNKLSGGQ-QRlldfVL---SLIGQPQLILLDEPTSTMD 154
Cdd:COG4148 96 G--NL---LYgrkrapraERRISFDEVVELLGI-GHLLDRRPATLSGGErQR----VAigrALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 155 I----EIREYfwsiIENLKEDNRT-ILYTSHYIEEVERMSDKIILIENGEIILNDSTSHI 209
Cdd:COG4148 166 LarkaEILPY----LERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-155 |
2.78e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 90.56 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI--FDKD----KLLQ-SENRSIM 73
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVrlNGRPlaawSPWElARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 FQKTM--FPdqLKVIEIINL----YQSFYENPlplEEIIE--LTKFDSSQL-NQFVNKLSGG-QQRL-LDFVL-----SL 137
Cdd:COG4559 81 PQHSSlaFP--FTVEEVVALgrapHGSSAAQD---RQIVReaLALVGLAHLaGRSYQTLSGGeQQRVqLARVLaqlwePV 155
|
170
....*....|....*...
gi 446537461 138 IGQPQLILLDEPTSTMDI 155
Cdd:COG4559 156 DGGPRWLFLDEPTSALDL 173
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-200 |
3.80e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 91.67 E-value: 3.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKL---LQSENRSI-M-FQ 75
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdLPPKDRNIaMvFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 76 ktmfpdqlkvieiiN--LY--QSFYEN---PL-----PLEEI----------IELTKFdssqLNQFVNKLSGGQQ----- 128
Cdd:COG3839 83 --------------SyaLYphMTVYENiafPLklrkvPKAEIdrrvreaaelLGLEDL----LDRKPKQLSGGQRqrval 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 129 -RlldfvlSLIGQPQLILLDEPTS--------TMDIEIREYFwsiienlKEDNRTILYTSHYIEEVERMSDKIILIENGE 199
Cdd:COG3839 145 gR------ALVREPKVFLLDEPLSnldaklrvEMRAEIKRLH-------RRLGTTTIYVTHDQVEAMTLADRIAVMNDGR 211
|
.
gi 446537461 200 I 200
Cdd:COG3839 212 I 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-214 |
4.32e-21 |
|
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: 89.56 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSF----NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI----FDKDKLLQSENRSI 72
Cdd:cd03258 1 MIELKNVSKVFgdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 73 MFQKTMfpdqlkVIEIINLYQS--FYEN-PLPLE-------EIIEltkfDSSQLNQFVN----------KLSGGQQRLLD 132
Cdd:cd03258 81 RRRIGM------IFQHFNLLSSrtVFENvALPLEiagvpkaEIEE----RVLELLELVGledkadaypaQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 133 FVLSLIGQPQLILLDEPTSTMDIEIREyfwSIIENLKEDNR----TILYTSHYIEEVERMSDKIILIENGEIILNDSTSH 208
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQ---SILALLRDINRelglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
....*.
gi 446537461 209 IRTNQQ 214
Cdd:cd03258 228 VFANPQ 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-201 |
4.82e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.78 E-value: 4.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQ--SENRSI-----M 73
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirSPRDAIalgigM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 -FQKTMFPDQLKVIEIINLYQsfyENPLPL--------EEIIELTK-----FDssqLNQFVNKLSGGQQRLLDFVLSLIG 139
Cdd:COG3845 85 vHQHFMLVPNLTVAENIVLGL---EPTKGGrldrkaarARIRELSErygldVD---PDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446537461 140 QPQLILLDEPTS--TmDIEIREYFwSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:COG3845 159 GARILILDEPTAvlT-PQEADELF-EILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-200 |
6.65e-21 |
|
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: 91.33 E-value: 6.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 20 ISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQS---------ENR--SIMFQK-TMFPdQLKVIE 87
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgiflppEKRriGYVFQEaRLFP-HLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 88 IINLYQSFYENPLPL---EEIIELTKFDSsQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSI 164
Cdd:TIGR02142 95 NLRYGMKRARPSERRisfERVIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 446537461 165 IENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:TIGR02142 174 LERLhAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-227 |
8.83e-21 |
|
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: 88.35 E-value: 8.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 3 QISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQSE-----NRSIMF-- 74
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIrLDGEDITKLPpheraRAGIAYvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 75 QKTM-FPdQLKVIEiiNL-----YQSFYENPLPlEEIIELtkFDSsqLNQFVNK----LSGGQQRLLDFVLSLIGQPQLI 144
Cdd:TIGR03410 82 QGREiFP-RLTVEE--NLltglaALPRRSRKIP-DEIYEL--FPV--LKEMLGRrggdLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 145 LLDEPTSTM------DIEireyfwSIIENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTShirtnqqsqi 217
Cdd:TIGR03410 154 LLDEPTEGIqpsiikDIG------RVIRRLrAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGD---------- 217
|
250
....*....|
gi 446537461 218 TLSDEYIRKL 227
Cdd:TIGR03410 218 ELDEDKVRRY 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-201 |
1.11e-20 |
|
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: 88.03 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFN--KRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----DKDKLLQSENR---SI 72
Cdd:cd03245 3 IEFRNVSFSYPnqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLldgtDIRQLDPADLRrniGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 73 MFQK-TMFPDQLKviEIINLYQSFYENplplEEIIELTKFdsSQLNQFVNK---------------LSGGQQRLLDFVLS 136
Cdd:cd03245 83 VPQDvTLFYGTLR--DNITLGAPLADD----ERILRAAEL--AGVTDFVNKhpngldlqigergrgLSGGQRQAVALARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446537461 137 LIGQPQLILLDEPTSTMDIEIREYFwsiIENLKE--DNRTILYTSHyieeveRMS-----DKIILIENGEII 201
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERL---KERLRQllGDKTLIIITH------RPSlldlvDRIIVMDSGRIV 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-201 |
1.18e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.55 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF-DKDKLLQS--ENRSI--MFQK 76
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFiDGEDVTHRsiQQRDIcmVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 -TMFPdqlkvieiinlYQSFYEN--------PLPLEEI----------IELTKFDssqlNQFVNKLSGGQQRLLDFVLSL 137
Cdd:PRK11432 87 yALFP-----------HMSLGENvgyglkmlGVPKEERkqrvkealelVDLAGFE----DRYVDQISGGQQQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446537461 138 IGQPQLILLDEPTSTMDIEIREYFWSIIENLKED-NRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-201 |
2.11e-20 |
|
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: 87.78 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF--DKD---KLLQSENRSIMFQK 76
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILfgGEDatdVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 TMFPDQLKVIEIINL---YQSFYENPLPLE------EIIELTKFDSSQlNQFVNKLSGGQQRLLDFVLSLIGQPQLILLD 147
Cdd:cd03296 83 YALFRHMTVFDNVAFglrVKPRSERPPEAEirakvhELLKLVQLDWLA-DRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446537461 148 EPTSTMDIEIREYFWSIIENLKED-NRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIE 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-235 |
2.21e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.22 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNK-----RCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF--DKDKLLQSENR--- 70
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILidGKDVTKLPEYKrak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 71 --SIMFQKTM---FPDqLKVIEiiNL---YQ-------SFYENPLPLEEIIE-LTKFD---SSQLNQFVNKLSGGQQRLL 131
Cdd:COG1101 81 yiGRVFQDPMmgtAPS-MTIEE--NLalaYRrgkrrglRRGLTKKRRELFRElLATLGlglENRLDTKVGLLSGGQRQAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 132 DFVLSLIGQPQLILLDEPTSTMD-------IEIREYfwsIIEnlkEDNRTILYTSHYIEEVERMSDKIILIENGEIILnd 204
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDpktaalvLELTEK---IVE---ENNLTTLMVTHNMEQALDYGNRLIMMHEGRIIL-- 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 446537461 205 stsHIRTNQQSQITLSD-----EYIRKLKLDKDDLV 235
Cdd:COG1101 230 ---DVSGEEKKKLTVEDllelfEEIRGEELADDRLL 262
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
14-201 |
2.48e-20 |
|
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: 90.98 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 14 RCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----DKDKLLQSENRSIMfqkTMFPDQlkvIEII 89
Cdd:COG4987 348 RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvDLRDLDEDDLRRRI---AVVPQR---PHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 90 NlyQSFYENpLPL-------EEIIE-LTKfdsSQLNQFVN---------------KLSGGQQRLLDFVLSLIGQPQLILL 146
Cdd:COG4987 422 D--TTLREN-LRLarpdatdEELWAaLER---VGLGDWLAalpdgldtwlgeggrRLSGGERRRLALARALLRDAPILLL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446537461 147 DEPTSTMDIEIREyfwSIIENLKE--DNRTILYTSHYIEEVERMsDKIILIENGEII 201
Cdd:COG4987 496 DEPTEGLDAATEQ---ALLADLLEalAGRTVLLITHRLAGLERM-DRILVLEDGRIV 548
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-201 |
7.19e-20 |
|
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: 85.30 E-value: 7.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 13 KRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVN--ANSGEIF--DKDKLLQSENRSIMF--QKTMFPDQLKVI 86
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLinGRPLDKRSFRKIIGYvpQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 87 EiiNLYqsfyenplpleeiieltkFdSSQLNQfvnkLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIE 166
Cdd:cd03213 101 E--TLM------------------F-AAKLRG----LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLR 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 446537461 167 NLKEDNRTILYTSHYI-EEVERMSDKIILIENGEII 201
Cdd:cd03213 156 RLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-240 |
1.05e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 86.61 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 12 NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSEN-----RSI--MFQKtmfPDQLK 84
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdvrRQVgmVFQN---PDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 85 VIEIINLYQSF-YENP-LPLEEIIELTKFDSSQLN--QFVNK----LSGGQ-QRL-LDFVLSLigQPQLILLDEPTSTMD 154
Cdd:PRK13635 95 VGATVQDDVAFgLENIgVPREEMVERVDQALRQVGmeDFLNRephrLSGGQkQRVaIAGVLAL--QPDIIILDEATSMLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 155 IEIREYFWSIIENLKEDNR-TILYTSHYIEEVERmSDKIILIENGEIILNDSTSHI-RTNQQ-SQITLSDEYIRKLK--L 229
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIfKSGHMlQEIGLDVPFSVKLKelL 251
|
250
....*....|.
gi 446537461 230 DKDDLVIQKNH 240
Cdd:PRK13635 252 KRNGILLPNTY 262
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-201 |
1.82e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 88.30 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----DKDKLLQSENR---SIMFQKT-MFPDqlkvie 87
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidgvDIRDLTLESLRrqiGVVPQDTfLFSG------ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 88 iinlyqSFYEN------PLPLEEIIELTKfdSSQLNQFV---------------NKLSGGQ-QRlldfvLS----LIGQP 141
Cdd:COG1132 429 ------TIRENirygrpDATDEEVEEAAK--AAQAHEFIealpdgydtvvgergVNLSGGQrQR-----IAiaraLLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446537461 142 QLILLDEPTSTMDIEIrEYfwSIIENLKE--DNRTILYTSHyieeveRMS-----DKIILIENGEII 201
Cdd:COG1132 496 PILILDEATSALDTET-EA--LIQEALERlmKGRTTIVIAH------RLStirnaDRILVLDDGRIV 553
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-200 |
2.38e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 86.92 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKL---LQSENRSI--MFQK 76
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDithVPAENRHVntVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 -TMFPdqlkvieiinlYQSFYEN--------PLPLEEIIELTkFDS---SQLNQFVNK----LSGGQQRLLDFVLSLIGQ 140
Cdd:PRK09452 95 yALFP-----------HMTVFENvafglrmqKTPAAEITPRV-MEAlrmVQLEEFAQRkphqLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446537461 141 PQLILLDEPTSTMDIEIREYFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-201 |
2.68e-19 |
|
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: 84.59 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FD----KDKLLQSENRSI--MFQKT-MFPDQlkVIE 87
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIlIDghdvRDYTLASLRRQIglVSQDVfLFNDT--VAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 88 IINlyqsfYENP-LPLEEIIELTKfdSSQLNQFVN---------------KLSGGQQRLLDFVLSLIGQPQLILLDEPTS 151
Cdd:cd03251 95 NIA-----YGRPgATREEVEEAAR--AANAHEFIMelpegydtvigergvKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446537461 152 TMDIEIREYFWSIIENLKEdNRTILYTSHYIEEVERmSDKIILIENGEII 201
Cdd:cd03251 168 ALDTESERLVQAALERLMK-NRTTFVIAHRLSTIEN-ADRIVVLEDGKIV 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-202 |
4.62e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 85.10 E-value: 4.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNK-----RCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF-------DKDKLLQSEN 69
Cdd:PRK13637 3 IKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIidgvditDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 70 RSI----------MFQKTMFPD---------------QLKVIEIINLYQsfyenpLPLEEIIELTKFDssqlnqfvnkLS 124
Cdd:PRK13637 83 KKVglvfqypeyqLFEETIEKDiafgpinlglseeeiENRVKRAMNIVG------LDYEDYKDKSPFE----------LS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446537461 125 GGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEIIL 202
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCEL 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-200 |
6.70e-19 |
|
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: 86.99 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 19 NISFdiEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQKTMFPDQ------LKVIEIINLY 92
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHnilfhhLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 93 -----QSFYENPLPLEEIIELTKFDSSQlNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIEN 167
Cdd:TIGR01257 1028 aqlkgRSWEEAQLEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK 1106
|
170 180 190
....*....|....*....|....*....|...
gi 446537461 168 LKEdNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:TIGR01257 1107 YRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-193 |
8.60e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.62 E-value: 8.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQKTMFP 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 81 dqLKVIEIINLYQSFY-ENPLPLEEIIELTKFdssqLNQFVNKLSGGQ-QRLLdFVLSLIGQPQLILLDEPTSTMDIEIR 158
Cdd:PRK09544 84 --LTVNRFLRLRPGTKkEDILPALKRVQAGHL----IDAPMQKLSGGEtQRVL-LARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 446537461 159 EYFWSIIENLK-EDNRTILYTSHYIEEVERMSDKII 193
Cdd:PRK09544 157 VALYDLIDQLRrELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-218 |
1.68e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 84.08 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSF--NKRCV--LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----D----KDKLLQSE 68
Cdd:PRK11153 1 MIELKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLvdgqDltalSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 69 NRSI-M-FQKtmFpdqlkvieiiNLYQS--FYEN-PLPLE--------------EIIELTKFdSSQLNQFVNKLSGGQ-Q 128
Cdd:PRK11153 81 RRQIgMiFQH--F----------NLLSSrtVFDNvALPLElagtpkaeikarvtELLELVGL-SDKADRYPAQLSGGQkQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 129 RlldfV---LSLIGQPQLILLDEPTSTMDIEIREyfwSIIENLKEDNR----TILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:PRK11153 148 R----VaiaRALASNPKVLLCDEATSALDPATTR---SILELLKDINRelglTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
250
....*....|....*..
gi 446537461 202 LNDSTSHIRTNQQSQIT 218
Cdd:PRK11153 221 EQGTVSEVFSHPKHPLT 237
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-201 |
1.75e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.26 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKR--CVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQKTMF 79
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 80 PDQLkvIEIINlyQSFYENpLPL-------EEIIE------LTKF--DSSQLNQFV----NKLSGGQQRLLDFVLSLIGQ 140
Cdd:PRK11160 419 VSQR--VHLFS--ATLRDN-LLLaapnasdEALIEvlqqvgLEKLleDDKGLNAWLgeggRQLSGGEQRRLGIARALLHD 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446537461 141 PQLILLDEPTSTMDIEI-REyfwsIIENLKE--DNRTILYTSHYIEEVERMsDKIILIENGEII 201
Cdd:PRK11160 494 APLLLLDEPTEGLDAETeRQ----ILELLAEhaQNKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-195 |
2.04e-18 |
|
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: 85.03 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSF-NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQK---- 76
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQiawv 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 ----TMFPDQLKviEIINLYQSfYENPLPLEEIIELTKFDS--SQLNQFVNK--------LSGGQQRLLDFVLSLIGQPQ 142
Cdd:TIGR02857 402 pqhpFLFAGTIA--ENIRLARP-DASDAEIREALERAGLDEfvAALPQGLDTpigeggagLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446537461 143 LILLDEPTSTMDIEIREYFWSIIENLKEdNRTILYTSHYIEEVERMsDKIILI 195
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-218 |
2.33e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.59 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRC----VLKNISFDIEQGKCIALIGKNGAGKSTLI------------DILIGNVNANSgeiFDKDKL 64
Cdd:COG1135 1 MIELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIrcinllerptsgSVLVDGVDLTA---LSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 65 LQsENRSI-M-FQKtmFpdqlkvieiiNLYQS--FYEN-PLPLE--------------EIIELT----KFDS--SQLnqf 119
Cdd:COG1135 78 RA-ARRKIgMiFQH--F----------NLLSSrtVAENvALPLEiagvpkaeirkrvaELLELVglsdKADAypSQL--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 120 vnklSGGQ-QRlldfV---LSLIGQPQLILLDEPTSTMDIEIREyfwSIIENLKEDNR----TILYTSHYIEEVERMSDK 191
Cdd:COG1135 142 ----SGGQkQR----VgiaRALANNPKVLLCDEATSALDPETTR---SILDLLKDINRelglTIVLITHEMDVVRRICDR 210
|
250 260
....*....|....*....|....*..
gi 446537461 192 IILIENGEIILNDSTSHIRTNQQSQIT 218
Cdd:COG1135 211 VAVLENGRIVEQGPVLDVFANPQSELT 237
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-223 |
2.77e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.05 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF-DKDKLLQSENR------SIM 73
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLvDGLDVATTPSRelakrlAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 FQKTMFPDQLKVIEIInlyqSFYENP-----LPLE--EIIE--LTKFDSSQL-NQFVNKLSGGQ-QRLldFVLSLIGQ-P 141
Cdd:COG4604 81 RQENHINSRLTVRELV----AFGRFPyskgrLTAEdrEIIDeaIAYLDLEDLaDRYLDELSGGQrQRA--FIAMVLAQdT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 142 QLILLDEPTSTMDI----EIReyfwSIIENL-KEDNRTIL-------YTSHYieevermSDKIILIENGEIILNDSTSHI 209
Cdd:COG4604 155 DYVLLDEPLNNLDMkhsvQMM----KLLRRLaDELGKTVVivlhdinFASCY-------ADHIVAMKDGRVVAQGTPEEI 223
|
250
....*....|....
gi 446537461 210 RTNQqsqiTLSDEY 223
Cdd:COG4604 224 ITPE----VLSDIY 233
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-200 |
3.44e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 83.54 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQS---ENRSI--MFQK 76
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvppAERGVgmVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 TMFPDQLKVIEiiNLyqSFYenplpleeiIELTKFDSSQLNQFVNK-----------------LSGGQQRLLDFVLSLIG 139
Cdd:PRK11000 84 YALYPHLSVAE--NM--SFG---------LKLAGAKKEEINQRVNQvaevlqlahlldrkpkaLSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446537461 140 QPQLILLDEPTSTMDIEIREYFWSIIENL-KEDNRTILYTSHyiEEVERMS--DKIILIENGEI 200
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLhKRLGRTMIYVTH--DQVEAMTlaDKIVVLDAGRV 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-201 |
3.85e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.28 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI--------FDKDKLLQSENRSI 72
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlylgkevtFNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 73 MFQKTMFPDQLKVIEIINLYQSF------------YENPLPLEEIIELtKFDSSQLnqfVNKLSGGQQRLLDFVLSLIGQ 140
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGREFvnrfgridwkkmYAEADKLLARLNL-RFSSDKL---VGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446537461 141 PQLILLDEPTSTM-DIEIREYFwSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:PRK10762 160 SKVIIMDEPTDALtDTETESLF-RVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-201 |
7.06e-18 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 83.76 E-value: 7.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSF--NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI----FDKDKLLQSENRsimfQ 75
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVlldgVDIRQIDPADLR----R 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 76 KTMFPDQlkviEIINLYQSFYEN-----PLPLEEIIeLTKFDSSQLNQFVNK---------------LSGGQQRLLDFVL 135
Cdd:TIGR03375 540 NIGYVPQ----DPRLFYGTLRDNialgaPYADDEEI-LRAAELAGVTEFVRRhpdgldmqigergrsLSGGQRQAVALAR 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446537461 136 SLIGQPQLILLDEPTSTMDIEIREYFwsiIENLKE--DNRTILYTSHyieeveRMS-----DKIILIENGEII 201
Cdd:TIGR03375 615 ALLRDPPILLLDEPTSAMDNRSEERF---KDRLKRwlAGKTLVLVTH------RTSlldlvDRIIVMDNGRIV 678
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-198 |
1.00e-17 |
|
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: 80.17 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFN-------KRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDK-----LLQSE 68
Cdd:COG4778 4 LLEVENLSKTFTlhlqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 69 NRSIMF--QKTM-FPDQ-LKVI------EIInlYQSFYENPLPLEEIIELTKFDSSQLN-----------QFvnklSGG- 126
Cdd:COG4778 84 PREILAlrRRTIgYVSQfLRVIprvsalDVV--AEPLLERGVDREEARARARELLARLNlperlwdlppaTF----SGGe 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446537461 127 QQRlLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENG 198
Cdd:COG4778 158 QQR-VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-201 |
1.05e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.83 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSEN-----RSIMF- 74
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSsrqlaRRLALl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 75 -QKTMFPDQLKVIEIINLYQSFYenpLPL--------EEIIElTKFDSSQLNQFVNK----LSGGQQRLLDFVLSLIGQP 141
Cdd:PRK11231 82 pQHHLTPEGITVRELVAYGRSPW---LSLwgrlsaedNARVN-QAMEQTRINHLADRrltdLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 142 QLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-200 |
1.47e-17 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 79.52 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 21 SFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF--DKDKLLQSENR---SIMFQKTMFPDQLKVIEIINL--YQ 93
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKvnDQSHTGLAPYQrpvSMLFQENNLFAHLTVRQNIGLglHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 94 SFYENPLPLEEIIELTKFD--SSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENL-KE 170
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVgiADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLcSE 177
|
170 180 190
....*....|....*....|....*....|
gi 446537461 171 DNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-200 |
1.76e-17 |
|
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: 79.37 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSF-NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRS--------- 71
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipylrrki 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 72 -IMFQKTMFPDQLKVIEIINL-----YQSFYENPLPLEEIIELTKFdSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLIL 145
Cdd:cd03292 81 gVVFQDFRLLPDRNVYENVAFalevtGVPPREIRKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 146 LDEPTSTMDieiREYFWSIIENLKEDNR---TILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:cd03292 160 ADEPTGNLD---PDTTWEIMNLLKKINKagtTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
6-209 |
2.17e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 80.45 E-value: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 6 NINKSFNKRcVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRS-----------IMF 74
Cdd:PRK13634 13 QYKTPFERR-ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkplrkkvgIVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 75 QktmFPD-QL------KVIEI--INLYQSFYENPLPLEEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLIL 145
Cdd:PRK13634 92 Q---FPEhQLfeetveKDICFgpMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 146 LDEPTSTMD----IEIREYFWSIienLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHI 209
Cdd:PRK13634 169 LDEPTAGLDpkgrKEMMEMFYKL---HKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-223 |
2.71e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.17 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 6 NINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDK---LLQSENR------------ 70
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisLLPLHARarrgigylpqea 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 71 SIMFQKTMFPDQLKVIEI-INLYQSFYENplPLEEIIEltKFDSSQL-NQFVNKLSGGQQRLLDFVLSLIGQPQLILLDE 148
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIrDDLSAEQRED--RANELME--EFHIEHLrDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 149 PTSTMD----IEIREyfwsIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQQ-SQITLSDEY 223
Cdd:PRK10895 164 PFAGVDpisvIDIKR----IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHvKRVYLGEDF 239
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-201 |
5.59e-17 |
|
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: 78.30 E-value: 5.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIfdkdkLLQSENRSIMfQKTMFPDQLKVI--EIINLYQ 93
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-----LVDGHDLALA-DPAWLRRQVGVVlqENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 94 SFYEN------PLPLEEIIELTKFDSSQ---------LNQFVNK----LSGGQQRLLDFVLSLIGQPQLILLDEPTSTMD 154
Cdd:cd03252 91 SIRDNialadpGMSMERVIEAAKLAGAHdfiselpegYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446537461 155 IEIREyfwSIIENLKE--DNRTILYTSHYIEEVeRMSDKIILIENGEII 201
Cdd:cd03252 171 YESEH---AIMRNMHDicAGRTVIIIAHRLSTV-KNADRIIVMEKGRIV 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-241 |
6.37e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.07 E-value: 6.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 13 KRCVLKNISFDIEQGKCIALIGKNGAGKST---LID-ILIGNVNANSGEIFDKDKLLQS------ENRSIMFQKtmfPDQ 82
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINgLLLPDDNPNSKITVDGITLTAKtvwdirEKVGIVFQN---PDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 83 LKVIEIINLYQSF-YEN-PLPLEEIIELTKFDSSQLN--QFVNK----LSGGQQRLLDFVLSLIGQPQLILLDEPTSTMD 154
Cdd:PRK13640 96 QFVGATVGDDVAFgLENrAVPRPEMIKIVRDVLADVGmlDYIDSepanLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 155 IEIREYFWSIIENLKEDNR-TILYTSHYIEEVErMSDKIILIENGEIILNDSTSHIRTN----QQSQITLSDEYIRKLKL 229
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNlTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKvemlKEIGLDIPFVYKLKNKL 254
|
250
....*....|..
gi 446537461 230 DKDDLVIQKNHN 241
Cdd:PRK13640 255 KEKGISVPQEIN 266
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-201 |
6.86e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 80.71 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIfdkdKLlqSENRSI--MFQKT-- 77
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----KW--SENANIgyYAQDHay 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 78 MFPDQLKVIEIINLYQSFYENPLPLEEIIELTKFDSSQLNQFVNKLSGGQQ-RLLdFVLSLIGQPQLILLDEPTSTMDIE 156
Cdd:PRK15064 394 DFENDLTLFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKgRML-FGKLMMQKPNVLVMDEPTNHMDME 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446537461 157 IREYFWSIIENLKEdnrTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:PRK15064 473 SIESLNMALEKYEG---TLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-213 |
9.68e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 9.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLL------QSENRSIMF 74
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltpaKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 75 --QKTM-FPDqLKVIEiiNLYQSFYENPLPLEEIIELTKFDSSQLNQFVNK--LSGGQQRLLDFVLSLIGQPQLILLDEP 149
Cdd:PRK15439 91 vpQEPLlFPN-LSVKE--NILFGLPKRQASMQKMKQLLAALGCQLDLDSSAgsLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446537461 150 TSTMD-IEIREYFwSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQ 213
Cdd:PRK15439 168 TASLTpAETERLF-SRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDD 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-212 |
1.09e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 78.20 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRC-VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRS-------- 71
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllevrktv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 72 -IMFQKTmfPDQL---KVIEII-----NLyqsfyenPLPLEEIIELTK--FDSSQLNQFVNK----LSGGQQRLLDFVLS 136
Cdd:PRK13639 81 gIVFQNP--DDQLfapTVEEDVafgplNL-------GLSKEEVEKRVKeaLKAVGMEGFENKpphhLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446537461 137 LIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTN 212
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-200 |
1.09e-16 |
|
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: 76.32 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQKTMF--P-DQLKviEIINLY 92
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvPeDRKR--EGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 93 QSFYENplpleeiIELTKFdssqlnqfvnkLSGG-QQRLldfVLS--LIGQPQLILLDEPTSTMDIEIREYFWSIIENLK 169
Cdd:cd03215 93 LSVAEN-------IALSSL-----------LSGGnQQKV---VLArwLARDPRVLILDEPTRGVDVGAKAEIYRLIRELA 151
|
170 180 190
....*....|....*....|....*....|.
gi 446537461 170 EDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:cd03215 152 DAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-201 |
1.27e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.68 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF-D----KDKLLQS--ENRSIMFQKT-MFPDQlkvieI 88
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILlDghdlRDYTLASlrNQVALVSQNVhLFNDT-----I 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 89 INLYQSFYENPLPLEEIIELTKFdsSQLNQFVNK---------------LSGGQQRLLDFVLSLIGQPQLILLDEPTSTM 153
Cdd:PRK11176 434 ANNIAYARTEQYSREQIEEAARM--AYAMDFINKmdngldtvigengvlLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446537461 154 DIEIREYFWSIIENLKEdNRTILYTSHYIEEVERmSDKIILIENGEII 201
Cdd:PRK11176 512 DTESERAIQAALDELQK-NRTSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-218 |
1.28e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 77.65 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDIL------------IGNVNANSGEIFDKDKLLQSEN 69
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlielypearvSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 70 RSIMFQ-------KTMFPD---QLKVIEIINLYQSFYENPLPLEEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIG 139
Cdd:PRK14247 84 VQMVFQipnpipnLSIFENvalGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446537461 140 QPQLILLDEPTSTMDIEIREYFWSIIENLKEDnRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQQSQIT 218
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-201 |
1.46e-16 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 77.30 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGN--VNANSGEI-FDKDKLLQSE----NRSIMF 74
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsYEVTSGTIlFKGQDLLELEpderARAGLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 75 QKTMFPDQLKVIEIINLYQSFY--------ENPLP-------LEEIIELTKFDSSQLNQFVNK-LSGGQQRLLDFVLSLI 138
Cdd:TIGR01978 81 LAFQYPEEIPGVSNLEFLRSALnarrsargEEPLDlldfeklLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEILQMAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 139 GQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYieevERMSDKII-----LIENGEII 201
Cdd:TIGR01978 161 LEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHY----QRLLNYIKpdyvhVLLDGRIV 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
1.67e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 77.72 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFN--KRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRS------- 71
Cdd:PRK13632 7 MIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeirkkig 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 72 IMFQKtmfPDQLKVIEIINLYQSF-YEN----PLPLEEIIEltkfDSSQ-------LNQFVNKLSGGQ-QRL-LDFVLSL 137
Cdd:PRK13632 87 IIFQN---PDNQFIGATVEDDIAFgLENkkvpPKKMKDIID----DLAKkvgmedyLDKEPQNLSGGQkQRVaIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 138 igQPQLILLDEPTSTMDIEIREYFWSIIENLKED-NRTILYTSHYIEEVeRMSDKIILIENGEIILNDSTSHIRTNqqsq 216
Cdd:PRK13632 160 --NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNN---- 232
|
250
....*....|....
gi 446537461 217 itlsDEYIRKLKLD 230
Cdd:PRK13632 233 ----KEILEKAKID 242
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-201 |
1.83e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.90 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDIL-------IGNVNANSGEIFD--KDKLLQSENRSI--MFQ---KTMFPDQ 82
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNInallkptTGTVTVDDITITHktKDKYIRPVRKRIgmVFQfpeSQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 83 LKViEIINLYQSFyenPLPLEEI--------IELtKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMD 154
Cdd:PRK13646 103 VER-EIIFGPKNF---KMNLDEVknyahrllMDL-GFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446537461 155 IEIREYFWSIIENLK-EDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:PRK13646 178 PQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-201 |
2.13e-16 |
|
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: 79.38 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 14 RCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FD----KDKLLQSENRSI--------MFQKTMF- 79
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQIlLDghdlADYTLASLRRQValvsqdvvLFNDTIAn 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 80 ------PDQLKVIEIINLYQSFYenplpLEEIIE-LTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTST 152
Cdd:TIGR02203 425 niaygrTEQADRAEIERALAAAY-----AQDFVDkLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSA 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446537461 153 MDIEIREYFWSIIENLKEdNRTILYTSHYIEEVERmSDKIILIENGEII 201
Cdd:TIGR02203 500 LDNESERLVQAALERLMQ-GRTTLVIAHRLSTIEK-ADRIVVMDDGRIV 546
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-201 |
2.29e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 76.64 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 3 QISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGN--VNANSGEI-FDKDKLLQ--SENRSIM---- 73
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSIlLDGEDILElsPDERARAgifl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 -FQKTM-FPDqLKVIEIINL-YQSFYENPLP-------LEEIIELTKFDSSQLNQFVN-KLSGGQQRLLDFVLSLIGQPQ 142
Cdd:COG0396 82 aFQYPVeIPG-VSVSNFLRTaLNARRGEELSareflklLKEKMKELGLDEDFLDRYVNeGFSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 143 LILLDEPTSTMDIeireyfWSI------IENLKEDNRTILYTSHY---IEEVErmSDKIILIENGEII 201
Cdd:COG0396 161 LAILDETDSGLDI------DALrivaegVNKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDGRIV 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-237 |
2.47e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 78.34 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQSE--NRSI--MFQ 75
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImLDGVDLSHVPpyQRPInmMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 76 K-TMFPdQLKVIEiiNLYQSFYENPLPLEEI----------IELTKFDSSQLNQfvnkLSGGQQRLLDFVLSLIGQPQLI 144
Cdd:PRK11607 99 SyALFP-HMTVEQ--NIAFGLKQDKLPKAEIasrvnemlglVHMQEFAKRKPHQ----LSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 145 LLDEPTSTMDIEIREYF-WSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQQSQitLSDEY 223
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR--YSAEF 249
|
250 260
....*....|....*....|..
gi 446537461 224 IRK-------LKLDKDD-LVIQ 237
Cdd:PRK11607 250 IGSvnvfegvLKERQEDgLVID 271
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-207 |
3.01e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.08 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNK---RCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSEN-----RSI 72
Cdd:PRK13650 4 IIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwdirHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 73 --MFQKtmfPDQLKVIEIINLYQSF-YENP-LPLEEIIELTK--FDSSQLNQFVNK----LSGGQQRLLDFVLSLIGQPQ 142
Cdd:PRK13650 84 gmVFQN---PDNQFVGATVEDDVAFgLENKgIPHEEMKERVNeaLELVGMQDFKEReparLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446537461 143 LILLDEPTSTMDIEIREYFWSIIENLKEDNR-TILYTSHYIEEVErMSDKIILIENGEIilnDSTS 207
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQmTVISITHDLDEVA-LSDRVLVMKNGQV---ESTS 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-214 |
3.14e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.18 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSG--EIFDKDKLLQSENR---------SIMFQktmFPDQ--- 82
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGtiTIAGYHITPETGNKnlkklrkkvSLVFQ---FPEAqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 83 ----LKVIEIINLYQSFYENPLPLEEIIELTK--FDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIE 156
Cdd:PRK13641 100 entvLKDVEFGPKNFGFSEDEAKEKALKWLKKvgLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 157 IREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQQ 214
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-214 |
3.22e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.43 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRC-----VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF---------DKDKLLQS 67
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 68 ENRSIMFQKTMFPDQLKVIEI---------INLYQSFYEN--------PLPL-----------EEIIELTKFDSSQLNQF 119
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEIrrrvgvvfqFAEYQLFEQTiekdiifgPVSMgvskeeakkraAKYIELVGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 120 VNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGE 199
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
250
....*....|....*
gi 446537461 200 IILNDSTSHIRTNQQ 214
Cdd:PRK13651 243 IIKDGDTYDILSDNK 257
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-209 |
4.39e-16 |
|
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: 77.15 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 32 LIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQ--SENRSI--MFQK-TMFPdQLKVIEiiNLYQSFYENPLPLEEI 105
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSImLDGEDVTNvpPHLRHInmVFQSyALFP-HMTVEE--NVAFGLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 106 ----------IELTKFDSSQLNQfvnkLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKED-NRT 174
Cdd:TIGR01187 78 kprvlealrlVQLEEFADRKPHQ----LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGIT 153
|
170 180 190
....*....|....*....|....*....|....*
gi 446537461 175 ILYTSHYIEEVERMSDKIILIENGEIILNDSTSHI 209
Cdd:TIGR01187 154 FVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-200 |
4.73e-16 |
|
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: 75.59 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQsenrsiMFQKTMFPDQLKVI--EIINLYQ 93
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS------QYEHKYLHSKVSLVgqEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 94 SFYEN------PLPLEEIIELTkfDSSQLNQFV---------------NKLSGGQQRLLDFVLSLIGQPQLILLDEPTST 152
Cdd:cd03248 103 SLQDNiayglqSCSFECVKEAA--QKAHAHSFIselasgydtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446537461 153 MDIEIREYFWSIIENLKEdNRTILYTSHYIEEVERmSDKIILIENGEI 200
Cdd:cd03248 181 LDAESEQQVQQALYDWPE-RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-235 |
6.27e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.18 E-value: 6.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSF-NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF-------DKDKLLQSENR-S 71
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgidtgDFSKLQGIRKLvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 72 IMFQKtmfPDQLKVIEIINLYQSF-YEN-PLPLEEIIELTK--FDSSQLNQFVNK----LSGGQQRLLDFVLSLIGQPQL 143
Cdd:PRK13644 81 IVFQN---PETQFVGRTVEEDLAFgPENlCLPPIEIRKRVDraLAEIGLEKYRHRspktLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 144 ILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVErMSDKIILIENGEIILNDSTSHIrtnqqsqitLSDEY 223
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENV---------LSDVS 227
|
250
....*....|..
gi 446537461 224 IRKLKLDKDDLV 235
Cdd:PRK13644 228 LQTLGLTPPSLI 239
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-220 |
7.50e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.46 E-value: 7.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSF----NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI---------FDKDKL--L 65
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYrvagqdvatLDADALaqL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 66 QSENRSIMFQKTMFPDQLKV---IEIINLYQSFYENPLPLEEIIELTKFD-SSQLNQFVNKLSGGQQRLLDFVLSLIGQP 141
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAaqnVEVPAVYAGLERKQRLLRAQELLQRLGlEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446537461 142 QLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYiEEVERMSDKIILIENGEIILNDSTSHIRTNQQSQITLS 220
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTEPVV 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-227 |
7.76e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.81 E-value: 7.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQK---- 76
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRqqva 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 TMF--PDQLKVIEIINLYQSFYENPL--PLEEIIE-----LTKFDSSQL-NQFVNKLSGGQQRLLDFVLSLIGQPQLILL 146
Cdd:PRK13638 81 TVFqdPEQQIFYTDIDSDIAFSLRNLgvPEAEITRrvdeaLTLVDAQHFrHQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 147 DEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHI--RTNQQSQITLSDEYI 224
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVfaCTEAMEQAGLTQPWL 240
|
...
gi 446537461 225 RKL 227
Cdd:PRK13638 241 VKL 243
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
9-213 |
9.77e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 76.04 E-value: 9.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 9 KSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDklLQSENRSIMFQKTMFPDQLKVIEI 88
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGD--IYIGDKKNNHELITNPYSKKIKNF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 89 INL------------YQSFYEN--------PLPL----EEIIELTKF-------DSSQLNQFVNKLSGGQQRLLDFVLSL 137
Cdd:PRK13631 112 KELrrrvsmvfqfpeYQLFKDTiekdimfgPVALgvkkSEAKKLAKFylnkmglDDSYLERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446537461 138 IGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQ 213
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-200 |
1.15e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 75.01 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTL---IDILI----GNVNANSGEI------------FDKD 62
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFlrcINFLEkpseGSIVVNGQTInlvrdkdgqlkvADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 63 KLLQSENRSIM-FQKTMFPDQLKVIEiinlyqSFYENPLpleEIIELTK---------------FDSSQLNQFVNKLSGG 126
Cdd:PRK10619 86 QLRLLRTRLTMvFQHFNLWSHMTVLE------NVMEAPI---QVLGLSKqeareravkylakvgIDERAQGKYPVHLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446537461 127 QQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-218 |
1.26e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.21 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVL---------KNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQ----- 66
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdys 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 67 --SENRSIMFQ---KTMFPDQlKVIEIINLyqsfyenPLPL---------EEIIELTKFDSSQLNQFVN----KLSGGQQ 128
Cdd:PRK15112 84 yrSQRIRMIFQdpsTSLNPRQ-RISQILDF-------PLRLntdlepeqrEKQIIETLRQVGLLPDHASyyphMLAPGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 129 RLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNR-TILYTSHYIEEVERMSDKIILIENGEIILNDSTS 207
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGiSYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTA 235
|
250
....*....|.
gi 446537461 208 HIRTNQQSQIT 218
Cdd:PRK15112 236 DVLASPLHELT 246
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-201 |
1.27e-15 |
|
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: 74.57 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFN-KRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FD----KDKLLQSENRSIMF- 74
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlIDgqdiREVTLDSLRRAIGVv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 75 -QKT-MFPDQLkvieiinLYQSFYENP-LPLEEIIELTKfdSSQLNQFVN---------------KLSGGQQRLLDFVLS 136
Cdd:cd03253 81 pQDTvLFNDTI-------GYNIRYGRPdATDEEVIEAAK--AAQIHDKIMrfpdgydtivgerglKLSGGEKQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446537461 137 LIGQPQLILLDEPTSTMDIEI-REYFWSIIENLKedNRTILYTSHYIEEVERmSDKIILIENGEII 201
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTeREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-198 |
1.43e-15 |
|
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: 74.42 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSE--NRSIMFQK-TMFPdQLKVIEIINLYQ 93
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpDRMVVFQNySLLP-WLTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 94 SFYENPLP-------LEEIIELTKFDSSQlNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIE 166
Cdd:TIGR01184 80 DRVLPDLSkserraiVEEHIALVGLTEAA-DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190
....*....|....*....|....*....|...
gi 446537461 167 NLKEDNR-TILYTSHYIEEVERMSDKIILIENG 198
Cdd:TIGR01184 159 QIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-201 |
2.86e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.38 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRC-----VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRsimfQ 75
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSK----Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 76 KTMFPDQLKVIEIINLYQSFYENPLPLEEII-----------ELTKFDSSQL------NQFVNK----LSGGQQRLLDFV 134
Cdd:PRK13643 77 KEIKPVRKKVGVVFQFPESQLFEETVLKDVAfgpqnfgipkeKAEKIAAEKLemvglaDEFWEKspfeLSGGQMRRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446537461 135 LSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
122-211 |
2.87e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 75.16 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 122 KLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:NF000106 144 KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
90
....*....|
gi 446537461 202 LNDSTSHIRT 211
Cdd:NF000106 224 ADGKVDELKT 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-218 |
2.99e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.93 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVnansgEIFDKDklLQSENRSIMFQKTMFP 80
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLI-----EIYDSK--IKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 81 -DQLKVIEIINL---------YQSFYEN---PLP---------LEEIIE-------LTKFDSSQLNQFVNKLSGGQQRLL 131
Cdd:PRK14246 83 iDAIKLRKEVGMvfqqpnpfpHLSIYDNiayPLKshgikekreIKKIVEeclrkvgLWKEVYDRLNSPASQLSGGQQQRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 132 DFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDnRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRT 211
Cdd:PRK14246 163 TIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
....*..
gi 446537461 212 NQQSQIT 218
Cdd:PRK14246 242 SPKNELT 248
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-208 |
3.47e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.89 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANS---------GEIFDKDKLLQSENRS 71
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 72 ------IMFQKTMFPDQLKVIEIInLYQSFYENPL---------PLEE---IIELTKFDSSQL-NQFVNKLSGGQQRLLD 132
Cdd:PRK09984 84 srantgYIFQQFNLVNRLSVLENV-LIGALGSTPFwrtcfswftREQKqraLQALTRVGMVHFaHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446537461 133 FVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKE-DNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSH 208
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-200 |
4.69e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 73.63 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRS-------IMFQKtmfPDQLKVIEII 89
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEklrkhigIVFQN---PDNQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 90 NLYQSF-YENPL-PLEEIIELTKFDSSQLNQFV------NKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYF 161
Cdd:PRK13648 102 KYDVAFgLENHAvPYDEMHRRVSEALKQVDMLEradyepNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446537461 162 WSIIENLKED-NRTILYTSHYIEEVERmSDKIILIENGEI 200
Cdd:PRK13648 182 LDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-227 |
4.72e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.13 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNAnSGEIFDKDKLLQSENRSIMFQ-----KTMFPD-------QL 83
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPLHNLNRRQLLPvrhriQVVFQDpnsslnpRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 84 KVIEII----NLYQ---SFYENPLPLEEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIE 156
Cdd:PRK15134 380 NVLQIIeeglRVHQptlSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446537461 157 IREYFWSIIENLKEDNR-TILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQQSqitlsdEYIRKL 227
Cdd:PRK15134 460 VQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQ------EYTRQL 525
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-200 |
5.41e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.49 E-value: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQSENRSIMFQKTMF 79
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVlVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 80 PDQLKVieiinlyqSFyenPLPLEEIIE------LTKFDS---------------SQLNQFVNK----LSGG-QQRLLdF 133
Cdd:PRK09536 83 PQDTSL--------SF---EFDVRQVVEmgrtphRSRFDTwtetdraaveramerTGVAQFADRpvtsLSGGeRQRVL-L 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446537461 134 VLSLIGQPQLILLDEPTSTMDI--EIREYfwSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDInhQVRTL--ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-201 |
5.88e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.18 E-value: 5.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIM--FQKTM---FPDQL------- 83
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRkaFRRDIqmvFQDSIsavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 84 KVIEIIN------LYQSFYENPLPLEEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEI 157
Cdd:PRK10419 107 TVREIIReplrhlLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446537461 158 REYFWSIIENLKEDNRT-ILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:PRK10419 187 QAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-201 |
6.56e-15 |
|
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: 74.84 E-value: 6.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFN--KRCVLK---NISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF--------DKDKLlQS 67
Cdd:TIGR03269 279 IIKVRNVSKRYIsvDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewvDMTKP-GP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 68 ENRS-------IMFQK-TMFPDQlKVIEiiNLYQSF-YENPLPL---EEIIELTK--FDS----SQLNQFVNKLSGGQQR 129
Cdd:TIGR03269 358 DGRGrakryigILHQEyDLYPHR-TVLD--NLTEAIgLELPDELarmKAVITLKMvgFDEekaeEILDKYPDELSEGERH 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446537461 130 LLDFVLSLIGQPQLILLDEPTSTMD-IEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
8-201 |
9.68e-15 |
|
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: 71.92 E-value: 9.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 8 NKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNanSGEIFDKDKLLQSENRSI-MFQK-TMFPDQLKV 85
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQILFNGQPRKPdQFQKcVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 86 -IEIINLYQS-FYENPLPLEEiiELTKFDSSQL---------------NQFVNKLSGGQQRLLDFVLSLIGQPQLILLDE 148
Cdd:cd03234 92 lLPGLTVRETlTYTAILRLPR--KSSDAIRKKRvedvllrdlaltrigGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446537461 149 PTSTMDIEIREYFWSIIENLKEDNRTILYTSHYI-EEVERMSDKIILIENGEII 201
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPrSDLFRLFDRILLLSSGEIV 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-200 |
1.09e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.93 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 18 KNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----------DKDKLLQ-----SENRSimfQKTMF--- 79
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMlngkeinalsTAQRLARglvylPEDRQ---SSGLYlda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 80 PDQLKVIEIINLYQSFYENPLPLEEIIEL------TKFdsSQLNQFVNKLSGG-QQRLLdFVLSLIGQPQLILLDEPTST 152
Cdd:PRK15439 357 PLAWNVCALTHNRRGFWIKPARENAVLERyrralnIKF--NHAEQAARTLSGGnQQKVL-IAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446537461 153 MDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-209 |
1.35e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 72.47 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGE--IFDKDKLLQSENRSI---------MFQktmFPDQLKV 85
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSvrVDDTLITSTSKNKDIkqirkkvglVFQ---FPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 86 IEII---------NLYQSFYENPLPLEEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIE 156
Cdd:PRK13649 100 EETVlkdvafgpqNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446537461 157 IREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHI 209
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-209 |
1.61e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.19 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQK----TMFPDQLKVIEIINLY 92
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLResvgMVFQDPDNQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 93 QSFYENP----LPLEEIIE-----LTKFDSSQL-NQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMD-IEIREYF 161
Cdd:PRK13636 102 QDVSFGAvnlkLPEDEVRKrvdnaLKRTGIEHLkDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpMGVSEIM 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446537461 162 WSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHI 209
Cdd:PRK13636 182 KLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-202 |
3.85e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 70.89 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNI------NKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTL---IDILI----GNVNANSGEIFDKDKLLQS 67
Cdd:PRK13633 4 MIKCKNVsykyesNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLipseGKVYVDGLDTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 68 ENRSIM-FQKtmfPDQLKVIEIINLYQSF-YEN-PLPLEEIIELTKFDSSQLNQFVNK------LSGGQQRLLDFVLSLI 138
Cdd:PRK13633 84 RNKAGMvFQN---PDNQIVATIVEEDVAFgPENlGIPPEEIRERVDESLKKVGMYEYRrhaphlLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446537461 139 GQPQLILLDEPTSTMDIEIREYFWSIIENL-KEDNRTILYTSHYIEEVERmSDKIILIENGEIIL 202
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVM 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-190 |
4.07e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.84 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILiGNVNANSGEIfdkdkllQSENRSIMFQKTMFPD 81
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEV-------RVEGRVEFFNQNIYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 82 QLKV------IEII----NLY-QSFYEN------------PLPLEEIIELTKFDSSQLNQFVNK-------LSGGQQRLL 131
Cdd:PRK14258 80 RVNLnrlrrqVSMVhpkpNLFpMSVYDNvaygvkivgwrpKLEIDDIVESALKDADLWDEIKHKihksaldLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 132 DFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLK-EDNRTILYTSHYIEEVERMSD 190
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-209 |
4.32e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKR----CVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSI---- 72
Cdd:PRK10261 12 VLAVENLNIAFMQEqqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQViels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 73 -----------------MFQKTM------FPDQLKVIEIINLYQSF--YENPLPLEEIIELTKFDSSQ--LNQFVNKLSG 125
Cdd:PRK10261 92 eqsaaqmrhvrgadmamIFQEPMtslnpvFTVGEQIAESIRLHQGAsrEEAMVEAKRMLDQVRIPEAQtiLSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 126 GQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKED-NRTILYTSHYIEEVERMSDKIILIENGEIILND 204
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
....*
gi 446537461 205 STSHI 209
Cdd:PRK10261 252 SVEQI 256
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-219 |
4.51e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.00 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 21 SFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF--DKDKLLQSENR---SIMFQK-TMFPdQLKVIEIINL--- 91
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTlnGQDHTTTPPSRrpvSMLFQEnNLFS-HLTVAQNIGLgln 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 92 -------YQSfyenpLPLEEIIELTKFDsSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSI 164
Cdd:PRK10771 98 pglklnaAQR-----EKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446537461 165 IENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQQSQITL 219
Cdd:PRK10771 172 VSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-224 |
4.76e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.19 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLI-------DI-----LIGNVNANSGEIFDK--DKL-L 65
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLrsinrmnDLnpevtITGSIVYNGHNIYSPrtDTVdL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 66 QSENRSIMFQKTMFPdqlkvieiinlyQSFYENPL------------PLEEIIELTKFDSSQLNQFVNKL-------SGG 126
Cdd:PRK14239 85 RKEIGMVFQQPNPFP------------MSIYENVVyglrlkgikdkqVLDEAVEKSLKGASIWDEVKDRLhdsalglSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 127 QQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDnRTILYTSHYIEEVERMSDKIILIENGEIILNDST 206
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDT 231
|
250
....*....|....*...
gi 446537461 207 SHIRTNQQSQITlsDEYI 224
Cdd:PRK14239 232 KQMFMNPKHKET--EDYI 247
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-201 |
5.43e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.91 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKD----KLLQSENRSImfQ 75
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiYEQDlivaRLQQDPPRNV--E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 76 KTMF----------PDQLK--------------------------VIEIINLYQsfYENplPLEEIIELTKFDSSQLnqf 119
Cdd:PRK11147 81 GTVYdfvaegieeqAEYLKryhdishlvetdpseknlnelaklqeQLDHHNLWQ--LEN--RINEVLAQLGLDPDAA--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 120 VNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREyfWsiIEN-LKEDNRTILYTSHYIEEVERMSDKIILIENG 198
Cdd:PRK11147 154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIE--W--LEGfLKTFQGSIIFISHDRSFIRNMATRIVDLDRG 229
|
...
gi 446537461 199 EII 201
Cdd:PRK11147 230 KLV 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-212 |
7.03e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.02 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQ---SENRSIM---- 73
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpGHQIARMgvvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 -FQKTMFPDQLKVIEIINLYQSFYENPLPLEEIIELTKFDSSQ---------------LNQFVNK----LSGGQQRLLDF 133
Cdd:PRK11300 85 tFQHVRLFREMTVIENLLVAQHQQLKTGLFSGLLKTPAFRRAEsealdraatwlervgLLEHANRqagnLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 134 VLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKED-NRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTN 212
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 244
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-194 |
7.07e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 68.80 E-value: 7.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 10 SFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEifdkdkLLQSENRSIMF--QKTMFPDQLkvie 87
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT------VRRAGGARVAYvpQRSEVPDSL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 88 iinlyqsfyenPLPLEEIIELTKF---------------------DSSQLNQF----VNKLSGGQ-QRLLdFVLSLIGQP 141
Cdd:NF040873 71 -----------PLTVRDLVAMGRWarrglwrrltrddraavddalERVGLADLagrqLGELSGGQrQRAL-LAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446537461 142 QLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIIL 194
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-213 |
7.32e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 71.68 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQSENRSImFQKTMFPDQLKVieiinLY-Q 93
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlLDGVPLVQYDHHYL-HRQVALVGQEPV-----LFsG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 94 SFYENPL------PLEE-------------IIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMD 154
Cdd:TIGR00958 570 SVRENIAygltdtPDEEimaaakaanahdfIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446537461 155 IEIREYFWsiiENLKEDNRTILYTSHYIEEVERmSDKIILIENGEIILNDSTSHIRTNQ 213
Cdd:TIGR00958 650 AECEQLLQ---ESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
12-196 |
7.59e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.91 E-value: 7.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 12 NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIfdkdKLLQSENRSIMFQKTM------------F 79
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI----SILGQPTRQALQKNLVayvpqseevdwsF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 80 PDQLKVIEIINLY--QSFYENPLPLE-EIIE--LTKFDSSQL-NQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTM 153
Cdd:PRK15056 94 PVLVEDVVMMGRYghMGWLRRAKKRDrQIVTaaLARVDMVEFrHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446537461 154 DIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIE 196
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-193 |
8.23e-14 |
|
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: 70.47 E-value: 8.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKR----CVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNAN---SGEI-FD-KD--KLLQSEN 69
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEIlFDgEDllKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 70 R-------SIMFQKTM--FPDQLKVIEIInlyqsfyENPL----------PLEEIIELTK-----FDSSQLNQFVNKLSG 125
Cdd:COG0444 81 RkirgreiQMIFQDPMtsLNPVMTVGDQI-------AEPLrihgglskaeARERAIELLErvglpDPERRLDRYPHELSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 126 GQ-QRLLdFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKED-NRTILYTSHYIEEVERMSDKII 193
Cdd:COG0444 154 GMrQRVM-IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVA 222
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
17-200 |
1.09e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.16 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSI-------------MFQKTMFPDQL 83
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrklfsavftdfhLFDQLLGPEGK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 84 KVIEiiNLYQSFYENpLPLEEIIELtkfdssQLNQFVN-KLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFW 162
Cdd:PRK10522 419 PANP--ALVEKWLER-LKMAHKLEL------EDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFY 489
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446537461 163 SIIEN-LKEDNRTILYTSH---YIEeverMSDKIILIENGEI 200
Cdd:PRK10522 490 QVLLPlLQEMGKTIFAISHddhYFI----HADRLLEMRNGQL 527
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-180 |
1.09e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.44 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF------DKDKLLQSENRSIMF 74
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILferqsiKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 75 QKTMFPDQLKVIEIINLYQSFYENPLPLEEIIELTKFDsSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMD 154
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLE-HLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180
....*....|....*....|....*.
gi 446537461 155 IEIREYFWSIIENLKEDNRTILYTSH 180
Cdd:PRK13540 160 ELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-207 |
1.54e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.90 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGN--VNANSGEIFDKDKL---LQSENRS---- 71
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESildLEPEERAhlgi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 72 -IMFQktmFPdqlkvIEI------------INLYQSFYENPL--PLE------EIIELTKFDSSQLNQFVNK-LSGGQQR 129
Cdd:CHL00131 87 fLAFQ---YP-----IEIpgvsnadflrlaYNSKRKFQGLPEldPLEfleiinEKLKLVGMDPSFLSRNVNEgFSGGEKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 130 ---LLDFVLSligQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYieevERMSDKII-----LIENGEII 201
Cdd:CHL00131 159 rneILQMALL---DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHY----QRLLDYIKpdyvhVMQNGKII 231
|
....*.
gi 446537461 202 LNDSTS 207
Cdd:CHL00131 232 KTGDAE 237
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-236 |
1.86e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 20 ISFDIEQGKCIALIGKNGAGKSTLIDILIGnVNANSGEIFDKDKLL-------QSENRSIMFQKTMFPDQLKVIEIINLY 92
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLeawsaaeLARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 93 QS----FYENPLPLEEIIELTKFDsSQLNQFVNKLSGGQ-QR------LLDFVLSLIGQPQLILLDEPTSTMDIEIREYF 161
Cdd:PRK03695 94 QPdktrTEAVASALNEVAEALGLD-DKLGRSVNQLSGGEwQRvrlaavVLQVWPDINPAGQLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 162 WSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQqsqiTLSDEY---IRKLKLDKDDLVI 236
Cdd:PRK03695 173 DRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE----NLAQVFgvnFRRLDVEGHPMLI 246
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-207 |
2.01e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 68.33 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGnVNANSGEIFDKDKLL-------QSENRSIMFQKTMFPDQLKVIEII 89
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLsdwsaaeLARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 90 NLYQSfyeNPLPLEEIIELTKFDSSQLN------QFVNKLSGG-QQR-LLDFVL-----SLIGQPQLILLDEPTSTMDIE 156
Cdd:COG4138 91 ALHQP---AGASSEAVEQLLAQLAEALGledklsRPLTQLSGGeWQRvRLAAVLlqvwpTINPEGQLLLLDEPMNSLDVA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446537461 157 IREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTS 207
Cdd:COG4138 168 QQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-227 |
2.16e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.54 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDiLI--------GNVNANSGEIFDKdkllqSENRSI- 72
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLS-LIagarkiqqGRVEVLGGDMADA-----RHRRAVc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 73 -----MFQ---KtmfpdqlkvieiiNLYQ--SFYEN--------PLPLEE----IIELTKfdSSQLNQFVN----KLSGG 126
Cdd:NF033858 76 priayMPQglgK-------------NLYPtlSVFENldffgrlfGQDAAErrrrIDELLR--ATGLAPFADrpagKLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 127 QQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNR--TILYTSHYIEEVERMsDKIILIENGEIILND 204
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmSVLVATAYMEEAERF-DWLVAMDAGRVLATG 219
|
250 260
....*....|....*....|...
gi 446537461 205 STSHIRTNQQSQiTLSDEYIRKL 227
Cdd:NF033858 220 TPAELLARTGAD-TLEAAFIALL 241
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-201 |
2.43e-13 |
|
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: 67.55 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGN--VNANSGEIFDKDKL---LQSENRS----- 71
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDitdLPPEERArlgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 72 IMFQKTMFPDQLKVIEIInlyqsfyenplpleeiieltkfdssqlnQFVNK-LSGGQQRLLDFVLSLIGQPQLILLDEPT 150
Cdd:cd03217 81 LAFQYPPEIPGVKNADFL----------------------------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446537461 151 STMDIEIREYFWSIIENLKEDNRTILYTSHYieevERM-----SDKIILIENGEII 201
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREEGKSVLIITHY----QRLldyikPDRVHVLYDGRIV 184
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-205 |
2.47e-13 |
|
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: 67.44 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSG--EIFDKD----KLLQSENR-SIMFQK-TMFPDQLKV-I 86
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGkiEIDGIDistiPLEDLRSSlTIIPQDpTLFSGTIRSnL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 87 EIINLYQSfyenplplEEIIELTKFDSSQLNqfvnkLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIE--------IR 158
Cdd:cd03369 103 DPFDEYSD--------EEIYGALRVSEGGLN-----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYAtdaliqktIR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446537461 159 EYFwsiienlkeDNRTILYTSHYIEEVERMsDKIILIENGEIILNDS 205
Cdd:cd03369 170 EEF---------TNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-200 |
2.53e-13 |
|
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: 69.78 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 13 KRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF---------DKDKLLQS---------------- 67
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgadlsqwDREELGRHigylpqdvelfdgtia 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 68 ENrsI-MFQKtmfPDQLKVIE----------IINLYQSfYEnplpleeiielTKFDSSQLNqfvnkLSGGQ-QRLldfVL 135
Cdd:COG4618 424 EN--IaRFGD---ADPEKVVAaaklagvhemILRLPDG-YD-----------TRIGEGGAR-----LSGGQrQRI---GL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446537461 136 S--LIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHyieeveRMS-----DKIILIENGEI 200
Cdd:COG4618 479 AraLYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITH------RPSllaavDKLLVLRDGRV 544
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-200 |
3.19e-13 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 67.90 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTL---IDILignVNANSGEIF----------DKDKLLQS 67
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFlrcINLL---ETPDSGEIRvggeeirlkpDRDGELVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 68 ENR----------SIMFQKtmFpdqlkvieiiNLY------QSFYENP-----LPLEEIIE-----LTKFD-SSQLNQFV 120
Cdd:COG4598 85 ADRrqlqrirtrlGMVFQS--F----------NLWshmtvlENVIEAPvhvlgRPKAEAIEraealLAKVGlADKRDAYP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 121 NKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSH---YIEEVermSDKIILIEN 197
Cdd:COG4598 153 AHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHemgFARDV---SSHVVFLHQ 229
|
...
gi 446537461 198 GEI 200
Cdd:COG4598 230 GRI 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-180 |
4.14e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 12 NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQSENRSIMF---QKTMFPDQLKVIE 87
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkLDGGDIDDPDVAEACHylgHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 88 IINLYQSFY-ENPLPLEEIIELTKFDSSQLNQFvNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIE 166
Cdd:PRK13539 93 NLEFWAAFLgGEELDIAAALEAVGLAPLAHLPF-GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIR 171
|
170
....*....|....
gi 446537461 167 NLKEDNRTILYTSH 180
Cdd:PRK13539 172 AHLAQGGIVIAATH 185
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-207 |
4.25e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.35 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNK----RCVLKNISFDIEQGKCIALIGKNGAGKS-TLIDIL----IGNVNANSGEI-FDKDKLLQSENR 70
Cdd:PRK15134 5 LLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpSPPVVYPSGDIrFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 71 ----------SIMFQKTM--------FPDQLkvIEIINLYQSFYENPLPLEEIIELTKFDSSQ----LNQFVNKLSGGQQ 128
Cdd:PRK15134 85 tlrgvrgnkiAMIFQEPMvslnplhtLEKQL--YEVLSLHRGMRREAARGEILNCLDRVGIRQaakrLTDYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 129 RLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLK-EDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTS 207
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQqELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-224 |
5.09e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.50 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLI------DILI------GNVNANSGEIFDKDKLLQSEN 69
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIpgfrveGKVTFHGKNLYAPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 70 RSI--MFQK-TMFP----DQLKVIEIINLYQSfyenplPLEEIIE-------LTKFDSSQLNQFVNKLSGGQQRLLDFVL 135
Cdd:PRK14243 91 RRIgmVFQKpNPFPksiyDNIAYGARINGYKG------DMDELVErslrqaaLWDEVKDKLKQSGLSLSGGQQQRLCIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 136 SLIGQPQLILLDEPTSTMD----IEIREyfwsIIENLKEDnRTILYTSHYIEEVERMSDKIIL---------IENGEIIL 202
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDpistLRIEE----LMHELKEQ-YTIIIVTHNMQQAARVSDMTAFfnvelteggGRYGYLVE 239
|
250 260
....*....|....*....|..
gi 446537461 203 NDSTSHIRTNQQSQITlsDEYI 224
Cdd:PRK14243 240 FDRTEKIFNSPQQQAT--RDYV 259
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
13-200 |
5.22e-13 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 68.91 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 13 KRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIG-------NVNANSGEI--FDKDKLlqseNRSIMF---QKTMFP 80
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGiwpptsgSVRLDGADLkqWDRETF----GKHIGYlpqDVELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 81 DQLKviEIInlyQSFYENPLPlEEIIELTK--------------FDSSqLNQFVNKLSGGQQRLLDFVLSLIGQPQLILL 146
Cdd:TIGR01842 406 GTVA--ENI---ARFGENADP-EKIIEAAKlagvhelilrlpdgYDTV-IGPGGATLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446537461 147 DEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVErMSDKIILIENGEI 200
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLG-CVDKILVLQDGRI 531
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-154 |
5.28e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.98 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNK-RCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQKTMFP 80
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 81 DQLKVIeiinLYQSFYENPLPLEEIIE---LTKFDSSQLNQFV---------------NKLSGGQQRLLDFVLSLIGQPQ 142
Cdd:PRK10790 421 QQDPVV----LADTFLANVTLGRDISEeqvWQALETVQLAELArslpdglytplgeqgNNLSVGQKQLLALARVLVQTPQ 496
|
170
....*....|..
gi 446537461 143 LILLDEPTSTMD 154
Cdd:PRK10790 497 ILILDEATANID 508
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-217 |
7.84e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.10 E-value: 7.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKD--------KLLQSENR- 70
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlFDGEnipamsrsRLYTVRKRm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 71 SIMFQK-TMFPDqLKVIEiiNLYQSFYEN---PLPLEEIIELTKFDSSQL----NQFVNKLSGGQQRLLDFVLSLIGQPQ 142
Cdd:PRK11831 87 SMLFQSgALFTD-MNVFD--NVAYPLREHtqlPAPLLHSTVMMKLEAVGLrgaaKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 143 LILLDEP-----TSTMDIEIReyfwsIIENLKED-NRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQQSQ 216
Cdd:PRK11831 164 LIMFDEPfvgqdPITMGVLVK-----LISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR 238
|
.
gi 446537461 217 I 217
Cdd:PRK11831 239 V 239
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-230 |
1.12e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 66.75 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSEN-------RSIMFQKtmfPDQLKVIEI 88
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENirevrkfVGLVFQN---PDDQIFSPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 89 INLYQSFYENPLPLEEIIELTKFDSS--------QLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREY 160
Cdd:PRK13652 96 VEQDIAFGPINLGLDEETVAHRVSSAlhmlgleeLRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446537461 161 FWSIIENLKED-NRTILYTSHYIEEVERMSDKIILIENGEIILNDSTshirtnqqSQITLSDEYIRKLKLD 230
Cdd:PRK13652 176 LIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTV--------EEIFLQPDLLARVHLD 238
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-201 |
1.30e-12 |
|
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: 65.59 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI----FDKDKLLQSENRS---------IMFQKTM---- 78
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIlidgVDISKIGLHDLRSrisiipqdpVLFSGTIrsnl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 79 -----FPDQ--LKVIEIINLYQSFYENPLPLEEIIEltkfdSSQLNqfvnkLSGGQQRLLDFVLSLIGQPQLILLDEPTS 151
Cdd:cd03244 99 dpfgeYSDEelWQALERVGLKEFVESLPGGLDTVVE-----EGGEN-----LSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446537461 152 TMDIE--------IREYFwsiienlkeDNRTILYTSHYIEEVerM-SDKIILIENGEII 201
Cdd:cd03244 169 SVDPEtdaliqktIREAF---------KDCTVLTIAHRLDTI--IdSDRILVLDKGRVV 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-214 |
1.34e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.57 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRC-----VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQK 76
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 TM---------FPD-QL--KVIEI------INLYQSFYENPLPLEEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLI 138
Cdd:PRK13645 87 RLrkeiglvfqFPEyQLfqETIEKdiafgpVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446537461 139 GQPQLILLDEPTSTMDIEIREYFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQQ 214
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE 243
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-198 |
1.63e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.88 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQ--SENRSIMFQKTM 78
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 79 FPDQLKVIEiiNLYQSFYENPLPLEEIIE-----LTKFDSSQLNQ-FVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTST 152
Cdd:PRK11248 81 LLPWRNVQD--NVAFGLQLAGVEKMQRLEiahqmLKKVGLEGAEKrYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446537461 153 MDIEIREYFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIILIENG 198
Cdd:PRK11248 159 LDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-200 |
1.68e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 65.67 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSF-NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQSENRSIMFQK-- 76
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwFSGHDITRLKNREVPFLRrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 --TMFPDQLKVIEiinlyQSFYEN-PLPLeeII------ELTKFDSSQLNQ---------FVNKLSGGQQRLLDFVLSLI 138
Cdd:PRK10908 81 igMIFQDHHLLMD-----RTVYDNvAIPL--IIagasgdDIRRRVSAALDKvglldkaknFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446537461 139 GQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-180 |
2.02e-12 |
|
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: 64.57 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 13 KRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNAN--SGEIF-DKDKLLQSENRSIMF--QKTMFPDQLKVIE 87
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILiNGRPLDKNFQRSTGYveQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 88 IINLyqsfyenplpleeiieltkfdSSQLNQfvnkLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIEN 167
Cdd:cd03232 99 ALRF---------------------SALLRG----LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKK 153
|
170
....*....|...
gi 446537461 168 LKEDNRTILYTSH 180
Cdd:cd03232 154 LADSGQAILCTIH 166
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-180 |
2.33e-12 |
|
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: 63.71 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 14 RCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIfdkDKLLQSEnrsIMF--QKTMFPD-QLKviEIIn 90
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGED---LLFlpQRPYLPLgTLR--EQL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 91 LYqsfyenplPLEEIieltkfdssqlnqfvnkLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIienLKE 170
Cdd:cd03223 85 IY--------PWDDV-----------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL---LKE 136
|
170
....*....|
gi 446537461 171 DNRTILYTSH 180
Cdd:cd03223 137 LGITVISVGH 146
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-198 |
2.74e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 67.24 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRS----------IMFQKTMfpDQLKV 85
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSwimpgtikdnIIFGLSY--DEYRY 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 86 IEIINLYQsfyenplpLEEiiELTKF---DSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEI-REYF 161
Cdd:TIGR01271 519 TSVIKACQ--------LEE--DIALFpekDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTeKEIF 588
|
170 180 190
....*....|....*....|....*....|....*..
gi 446537461 162 WSIIENLKEDNRTILYTSHyIEEVERmSDKIILIENG 198
Cdd:TIGR01271 589 ESCLCKLMSNKTRILVTSK-LEHLKK-ADKILLLHEG 623
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-209 |
3.53e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.50 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 6 NINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDIL------------IGNVNANSGEIFDKDKLLQSENR-SI 72
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvsgyrySGDVLLGGRSIFNYRDVLEFRRRvGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 73 MFQKtmfPDQLKVIEIINLYQSFYENPL-PLEE--------IIELTKFDS--SQLNQFVNKLSGGQQRLLDFVLSLIGQP 141
Cdd:PRK14271 106 LFQR---PNPFPMSIMDNVLAGVRAHKLvPRKEfrgvaqarLTEVGLWDAvkDRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 142 QLILLDEPTSTMDIEIREYFWSIIENLKeDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHI 209
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-209 |
5.45e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.81 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 14 RCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQKTMF-PDQL------KVI 86
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYlPQQLpaaegmTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 87 EIINLYQSFYENPL---------PLEEIIELTKFdSSQLNQFVNKLSGGQ-QRLldFVLSLIGQ-PQLILLDEPTSTMDI 155
Cdd:PRK10575 104 ELVAIGRYPWHGALgrfgaadreKVEEAISLVGL-KPLAHRLVDSLSGGErQRA--WIAMLVAQdSRCLLLDEPTSALDI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446537461 156 EIREYFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHI 209
Cdd:PRK10575 181 AHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-201 |
8.19e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.14 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 4 ISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQK--TMFPD 81
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgiSMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 82 QLKVIEIINLYQSFYENPLPL-------EEIIELTK--FDSSQLN----QFVNKLSGGQQRLLDFVLSLIGQPQLILLDE 148
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTkgmfvdqDKMYRDTKaiFDELDIDidprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446537461 149 PTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-199 |
8.40e-12 |
|
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: 63.26 E-value: 8.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKL--------LQS----ENrsIMFQKTMFPDQL 83
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIayvsqepwIQNgtirEN--ILFGKPFDEERY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 84 -KVIEIINLYQSFyeNPLP---LEEIIEltkfdssqlnQFVNkLSGGQ-QRlldfvLSL----IGQPQLILLDEPTSTMD 154
Cdd:cd03250 98 eKVIKACALEPDL--EILPdgdLTEIGE----------KGIN-LSGGQkQR-----ISLaravYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446537461 155 IEIREYFWS--IIENLKeDNRTILYTSHYIEEVERmSDKIILIENGE 199
Cdd:cd03250 160 AHVGRHIFEncILGLLL-NNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-194 |
9.89e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 63.73 E-value: 9.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRC----VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQ--SENRSIMF 74
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpGADRGVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 75 QK-TMFPdQLKVIEIINLyqsfyenPLPL------------EEIIELTKFDSSQlNQFVNKLSGGQQRLLDFVLSLIGQP 141
Cdd:COG4525 83 QKdALLP-WLNVLDNVAF-------GLRLrgvpkaerraraEELLALVGLADFA-RRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446537461 142 QLILLDEPTSTMDIEIREYFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIIL 194
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVV 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-211 |
1.02e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.85 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 6 NINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF-DKDKLLQSENRSI------MFQKTM 78
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWlDGEHIQHYASKEVarriglLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 79 FPDQLKVIEIINL----YQSFY-----ENPLPLEEIIELTKFdSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEP 149
Cdd:PRK10253 92 TPGDITVQELVARgrypHQPLFtrwrkEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446537461 150 TSTMDIeirEYFWSIIENLKEDNRTILYT----SHYIEEVERMSDKIILIENGEIILNDSTSHIRT 211
Cdd:PRK10253 171 TTWLDI---SHQIDLLELLSELNREKGYTlaavLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-180 |
1.02e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 3 QISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI----------FDKDKLLQSENRSI 72
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklevayFDQHRAELDPEKTV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 73 M------FQKTMFPDQLKviEIINLYQSFYENPL----PleeiieltkfdssqlnqfVNKLSGGQQ-RLLDFVLSLigQP 141
Cdd:PRK11147 401 MdnlaegKQEVMVNGRPR--HVLGYLQDFLFHPKramtP------------------VKALSGGERnRLLLARLFL--KP 458
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446537461 142 -QLILLDEPTSTMDIEIREYFWSIIENLKEdnrTILYTSH 180
Cdd:PRK11147 459 sNLLILDEPTNDLDVETLELLEELLDSYQG---TVLLVSH 495
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-156 |
1.12e-11 |
|
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: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF--DKDKLL---QSENrSIMFQK 76
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEigETVKLAyvdQSRD-ALDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 TMF---PDQLKVIEIINlyqsfYEnpLPLEEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTM 153
Cdd:TIGR03719 402 TVWeeiSGGLDIIKLGK-----RE--IPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDL 474
|
...
gi 446537461 154 DIE 156
Cdd:TIGR03719 475 DVE 477
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-201 |
1.52e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 64.60 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSF-NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FD----KDKLLQSENRSI--M 73
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIlIDgtdiRTVTRASLRRNIavV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 FQKTMFpdqlkvieiinLYQSFYENpLPL-------EEIIELTKfdSSQLNQFV---------------NKLSGGQQRLL 131
Cdd:PRK13657 415 FQDAGL-----------FNRSIEDN-IRVgrpdatdEEMRAAAE--RAQAHDFIerkpdgydtvvgergRQLSGGERQRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 132 DFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEdNRTILYTSHYIEEVeRMSDKIILIENGEII 201
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTV-RNADRILVFDNGRVV 548
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-176 |
1.78e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.49 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF-----------DKDKLLQSENRSIMFQKTMFPDQLK 84
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlvgqplhqmdeEARAKLRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 85 VIEIINL---------YQSfYENPLPLEEIIELTKfdssQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDI 155
Cdd:PRK10584 105 ALENVELpallrgessRQS-RNGAKALLEQLGLGK----RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180
....*....|....*....|.
gi 446537461 156 EIREYFWSIIENLKEDNRTIL 176
Cdd:PRK10584 180 QTGDKIADLLFSLNREHGTTL 200
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-201 |
1.98e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 64.10 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVnansgeifdkdkllqsenrsimfqktmfPDQ--LKV--IEIINLY 92
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL----------------------------PYQgsLKIngIELRELD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 93 QSFY--------ENP-LP---LEEIIELTKFDSS-----------QLNQFVNK---------------LSGGQ-QRLldf 133
Cdd:PRK11174 418 PESWrkhlswvgQNPqLPhgtLRDNVLLGNPDASdeqlqqalenaWVSEFLPLlpqgldtpigdqaagLSVGQaQRL--- 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 134 VL--SLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTsHYIEEVERMsDKIILIENGEII 201
Cdd:PRK11174 495 ALarALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQLEDLAQW-DQIWVMQDGQIV 562
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-227 |
2.10e-11 |
|
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: 63.94 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSF----NKRCVLKNISFDIEQGKCIALIGKNGAGKS----TLIDILIGNVNANSGEI-FDKDKLLQ-SENR 70
Cdd:COG4172 6 LLSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSIlFDGQDLLGlSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 71 ---------SIMFQKTMF---P-----DQlkVIEIINLYQSFYENPLpLEEIIEL---TKFDS--SQLNQFVNKLSGGQ- 127
Cdd:COG4172 86 lrrirgnriAMIFQEPMTslnPlhtigKQ--IAEVLRLHRGLSGAAA-RARALELlerVGIPDpeRRLDAYPHQLSGGQr 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 128 QRlldfVL---SLIGQPQLILLDEPTSTMDIEIREyfwSIIENLK----EDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:COG4172 163 QR----VMiamALANEPDLLIADEPTTALDVTVQA---QILDLLKdlqrELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
250 260
....*....|....*....|....*..
gi 446537461 201 ILNDSTSHIRTNQQsqitlsDEYIRKL 227
Cdd:COG4172 236 VEQGPTAELFAAPQ------HPYTRKL 256
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
19-201 |
2.26e-11 |
|
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: 62.13 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 19 NISFD--IEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----DKDKLLQSENR-SIMFQKT-MFPdQLKVIEIIN 90
Cdd:cd03298 14 PMHFDltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLingvDVTAAPPADRPvSMLFQENnLFA-HLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 91 LYQS--FYENPLPLEEI------IELTKFDSSQLNQfvnkLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFW 162
Cdd:cd03298 93 LGLSpgLKLTAEDRQAIevalarVGLAGLEKRLPGE----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446537461 163 SIIENL-KEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:cd03298 169 DLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-218 |
3.73e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.17 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILignvnansGEIFDKDKLLQSENRSIMFQKTMFPD 81
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTF--------NRLLELNEEARVEGEVRLFGRNIYSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 82 QLKVIEIIN----LYQsfYENPLP-----------------------LEEIIE-------LTKFDSSQLNQFVNKLSGGQ 127
Cdd:PRK14267 77 DVDPIEVRRevgmVFQ--YPNPFPhltiydnvaigvklnglvkskkeLDERVEwalkkaaLWDEVKDRLNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 128 QRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDnRTILYTSHYIEEVERMSDKIILIENGEIILNDSTS 207
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR 233
|
250
....*....|.
gi 446537461 208 HIRTNQQSQIT 218
Cdd:PRK14267 234 KVFENPEHELT 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-193 |
3.86e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.80 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 20 ISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI--FDKDKLLQSEN--RSIMFQKTM-FPDQL-------KVIE 87
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVawLGKDLLGMKDDewRAVRSDIQMiFQDPLaslnprmTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 88 IINLYQSFYENPLPLEEIIELTK-------FDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREY 160
Cdd:PRK15079 120 IIAEPLRTYHPKLSRQEVKDRVKammlkvgLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 199
|
170 180 190
....*....|....*....|....*....|....
gi 446537461 161 FWSIIENL-KEDNRTILYTSHYIEEVERMSDKII 193
Cdd:PRK15079 200 VVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVL 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-201 |
3.93e-11 |
|
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: 61.79 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKllqsENRSIMFQKtmFPDQLKVI--EIINLYQ 93
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGV----DIRDLNLRW--LRSQIGLVsqEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 94 SFYEN------PLPLEEIIELTKFdsSQLNQFVNK---------------LSGGQQRLLDFVLSLIGQPQLILLDEPTST 152
Cdd:cd03249 92 TIAENirygkpDATDEEVEEAAKK--ANIHDFIMSlpdgydtlvgergsqLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446537461 153 MDIEIREYFWSIIENLKEdNRTILYTSHYIEEVeRMSDKIILIENGEII 201
Cdd:cd03249 170 LDAESEKLVQEALDRAMK-GRTTIVIAHRLSTI-RNADLIAVLQNGQVV 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
31-209 |
4.05e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.97 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 31 ALIGKNGAGKSTLIDILIGNVNANSGEI-------FDKDK--LLQSENRSI--MFQKT-MFPdQLKVIEiiNL-YQSFYE 97
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvlFDAEKgiCLPPEKRRIgyVFQDArLFP-HYKVRG--NLrYGMAKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 98 NPLPLEEIIELTKFDSsQLNQFVNKLSGGQ-QRLLdfvlslIG-----QPQLILLDEPTSTMDI----EIREYfwsiIEN 167
Cdd:PRK11144 105 MVAQFDKIVALLGIEP-LLDRYPGSLSGGEkQRVA------IGralltAPELLLMDEPLASLDLprkrELLPY----LER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446537461 168 L-KEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHI 209
Cdd:PRK11144 174 LaREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-198 |
4.65e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.36 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 3 QISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANS--GEIFDKD-KLLQSENRSIMF--QKT 77
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNrKPTKQILKRTGFvtQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 78 MFPDQLKVIE------IINLYQSFY--ENPLPLEEIIE---LTKFDSSQL-NQFVNKLSGGQQRLLDFVLSLIGQPQLIL 145
Cdd:PLN03211 150 ILYPHLTVREtlvfcsLLRLPKSLTkqEKILVAESVISelgLTKCENTIIgNSFIRGISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446537461 146 LDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHY-IEEVERMSDKIILIENG 198
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-201 |
6.15e-11 |
|
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: 62.83 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFN-KRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQKTMFP 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 81 DQLKVI---EII-NLYQSFYENpLPLEEIIELTKFDS-------------SQLNQFVNKLSGGQQRLLDFVLSLIGQPQL 143
Cdd:TIGR01193 554 PQEPYIfsgSILeNLLLGAKEN-VSQDEIWAACEIAEikddienmplgyqTELSEEGSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446537461 144 ILLDEPTSTMDIeIREYfwSIIENL-KEDNRTILYTSHYIeEVERMSDKIILIENGEII 201
Cdd:TIGR01193 633 LILDESTSNLDT-ITEK--KIVNNLlNLQDKTIIFVAHRL-SVAKQSDKIIVLDHGKII 687
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-199 |
7.18e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 61.41 E-value: 7.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQKTMFP--------DQLKVIE 87
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKEniifgvsyDEYRYKS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 88 IINLYQsfyenplpLEEiiELTKF---DSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEI-REYFWS 163
Cdd:cd03291 132 VVKACQ--------LEE--DITKFpekDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTeKEIFES 201
|
170 180 190
....*....|....*....|....*....|....*.
gi 446537461 164 IIENLKEDNRTILYTSHyIEEVERmSDKIILIENGE 199
Cdd:cd03291 202 CVCKLMANKTRILVTSK-MEHLKK-ADKILILHEGS 235
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-200 |
8.85e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 60.99 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQSENRSIMFQKTmfpdQLKVIEIINLYQSF 95
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSVIAISAGLSGQLT----GIENIEFKMLCMGF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 96 YENPLP--LEEIIELtkfdsSQLNQF----VNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLK 169
Cdd:PRK13546 116 KRKEIKamTPKIIEF-----SELGEFiyqpVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK 190
|
170 180 190
....*....|....*....|....*....|.
gi 446537461 170 EDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:PRK13546 191 EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-208 |
1.01e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.99 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILI----------GNVNANsGEIFDKDKllQSENRSIMFQKTMFPDQLKVI 86
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspkgvkgsGSVLLN-GMPIDAKE--MRAISAYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 87 EIINlYQSFYENP---------LPLEEIIELTKFDSSQ-----LNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTST 152
Cdd:TIGR00955 118 EHLM-FQAHLRMPrrvtkkekrERVDEVLQALGLRKCAntrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446537461 153 MDIEIREYFWSIIENLKEDNRTILYTSHY-IEEVERMSDKIILIENGEIILNDSTSH 208
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-189 |
1.13e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.21 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGE-IFDKDKL--LQSENRSimfqktmfpdQLKVIEIINLY 92
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDvIFNGQPMskLSSAAKA----------ELRNQKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 93 Q--------SFYEN-PLPL-------EEIIE--LTKFDSSQLNQFVN----KLSGGQQRLLDFVLSLIGQPQLILLDEPT 150
Cdd:PRK11629 94 QfhhllpdfTALENvAMPLligkkkpAEINSraLEMLAAVGLEHRANhrpsELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446537461 151 STMDIEIREyfwSIIENLKEDNR----TILYTSHYIEEVERMS 189
Cdd:PRK11629 174 GNLDARNAD---SIFQLLGELNRlqgtAFLVVTHDLQLAKRMS 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-225 |
1.17e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.59 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----DKDKLLQSENRSI-------MFQKTMFPDQLKV 85
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLidgvDIAKISDAELREVrrkkiamVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 86 IEIINLYQSFYENPLPLEEIIELTKFDSSQLNQFV----NKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYF 161
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAhsypDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446537461 162 WSIIENLK-EDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQqsqitlSDEYIR 225
Cdd:PRK10070 204 QDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP------ANDYVR 262
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-196 |
1.28e-10 |
|
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: 60.50 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 23 DIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIfdkdkllQSENRSIMFQ-KTMFPDQ-------LKVIEIINLYQS 94
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-------EIELDTVSYKpQYIKADYegtvrdlLSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 95 FYE----NPLPLEEIIEltkfdssqlnQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKE 170
Cdd:cd03237 94 YFKteiaKPLQIEQILD----------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170 180
....*....|....*....|....*..
gi 446537461 171 DN-RTILYTSHYIEEVERMSDKIILIE 196
Cdd:cd03237 164 NNeKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-200 |
1.35e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.72 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKD-KLLQSENRSIMFQKtm 78
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGiKLGYFAQHQLEFLR-- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 79 fPDQLKVIEIINLYQSFYENplPLEEIIELTKFDSSQLNQFVNKLSGGQQRLLdfVLSLI--GQPQLILLDEPTSTMDIE 156
Cdd:PRK10636 390 -ADESPLQHLARLAPQELEQ--KLRDYLGGFGFQGDKVTEETRRFSGGEKARL--VLALIvwQRPNLLLLDEPTNHLDLD 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446537461 157 IREyfwSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:PRK10636 465 MRQ---ALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-198 |
1.45e-10 |
|
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: 60.04 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQKTMFPD----------QLKVI 86
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVayaaqkpwllNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 87 EIINLYQSFYE-------NPLPLEEIIELTKF-DSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIR 158
Cdd:cd03290 97 ENITFGSPFNKqrykavtDACSLQPDIDLLPFgDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446537461 159 EYFWS--IIENLKEDNRTILYTSHYIEEVERmSDKIILIENG 198
Cdd:cd03290 177 DHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-201 |
1.81e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.19 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQ---------------SENR---------S 71
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdairagiayvPEDRkgeglvldlS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 72 IM----------FQKTMFPDQLKVIEIInlyqsfyenplplEEIIEL--TKFDSsqLNQFVNKLSGG-QQRLldfVLS-- 136
Cdd:COG1129 347 IRenitlasldrLSRGGLLDRRRERALA-------------EEYIKRlrIKTPS--PEQPVGNLSGGnQQKV---VLAkw 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446537461 137 LIGQPQLILLDEPTSTMDI----EIreYfwSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:COG1129 409 LATDPKVLILDEPTRGIDVgakaEI--Y--RLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-180 |
2.16e-10 |
|
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: 58.91 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 12 NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----DKDKLLQSENRSIMF---QKTMFPDqLK 84
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRwngtPLAEQRDEPHENILYlghLPGLKPE-LS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 85 VIEIINLYQSF--YENPLPLE--EIIELTKFDssqlNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREY 160
Cdd:TIGR01189 90 ALENLHFWAAIhgGAQRTIEDalAAVGLTGFE----DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|
gi 446537461 161 FWSIIENLKEDNRTILYTSH 180
Cdd:TIGR01189 166 LAGLLRAHLARGGIVLLTTH 185
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-219 |
2.62e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 59.72 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSEN-----RSI--MFQKtmfPDQLKVIEII 89
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrRKIgmVFQN---PDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 90 NLYQSF-YENP-LPLEEIIELTKFDSSQLNQFVNK------LSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYF 161
Cdd:PRK13642 100 EDDVAFgMENQgIPREEMIKRVDEALLAVNMLDFKtreparLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446537461 162 WSIIENLKED-NRTILYTSHYIEEVERmSDKIILIENGEIILNDSTSHIRTNQQSQITL 219
Cdd:PRK13642 180 MRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
14-201 |
2.75e-10 |
|
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: 60.99 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 14 RCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----DKDKLLQSENRS---IMFQKT-MFPDQLkv 85
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILidgqDIRDVTQASLRAaigIVPQDTvLFNDTI-- 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 86 ieiinLYQSFYENP-LPLEEIIELTKfdSSQLNQFVN---------------KLSGGQ-QR------LLDfvlsligQPQ 142
Cdd:COG5265 449 -----AYNIAYGRPdASEEEVEAAAR--AAQIHDFIEslpdgydtrvgerglKLSGGEkQRvaiartLLK-------NPP 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446537461 143 LILLDEPTSTMDIEIREyfwSIIENLKE--DNRTILYTSHyieeveRMS-----DKIILIENGEII 201
Cdd:COG5265 515 ILIFDEATSALDSRTER---AIQAALREvaRGRTTLVIAH------RLStivdaDEILVLEAGRIV 571
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-201 |
3.64e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.36 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSEN----RS---IMFQKTmfPDQLKVIEI- 88
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENekwvRSkvgLVFQDP--DDQVFSSTVw 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 89 -------INLyqsfyenPLPLEEIIELTK--FDSSQLNQFVNK----LSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDI 155
Cdd:PRK13647 99 ddvafgpVNM-------GLDKDEVERRVEeaLKAVRMWDFRDKppyhLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446537461 156 EIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:PRK13647 172 RGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-209 |
3.88e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.76 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 19 NISFDIEQGKCIALIGKNGAGKST-------LIDiLIGNVNANSGEIFDKD--KLLQSENR-------SIMFQKTM---- 78
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVsslaimgLID-YPGRVMAEKLEFNGQDlqRISEKERRnlvgaevAMIFQDPMtsln 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 79 --FPDQLKVIEIINLYQSFYENPLPlEEIIELTKF-----DSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTS 151
Cdd:PRK11022 104 pcYTVGFQIMEAIKVHQGGNKKTRR-QRAIDLLNQvgipdPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446537461 152 TMDIEIREyfwSIIENL----KEDNRTILYTSHYIEEVERMSDKIILIENGEIILNDSTSHI 209
Cdd:PRK11022 183 ALDVTIQA---QIIELLlelqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-194 |
4.14e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.57 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQKTMFP 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 81 DQLKVI-------EIINLYQSFYENPLPLEEIIELTKF--DSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTS 151
Cdd:PRK10247 87 AQTPTLfgdtvydNLIFPWQIRNQQPDPAIFLDDLERFalPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446537461 152 TMDIEIREYFWSIIENL-KEDNRTILYTSHYIEEVERMSDKIIL 194
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-201 |
5.91e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.87 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKL-------LQSENRSIMF-----QKTMFPDQ- 82
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIiFNGQRIdtlspgkLQALRRDIQFifqdpYASLDPRQt 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 83 -----LKVIEIINLYQSfYENPLPLEEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEI 157
Cdd:PRK10261 420 vgdsiMEPLRVHGLLPG-KAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446537461 158 REYFWSIIENLKED-NRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:PRK10261 499 RGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-193 |
7.08e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 58.97 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 19 NISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----DKDKLLQSENRS------IMFQktmfpD------- 81
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqDITGLSGRELRPlrrrmqMVFQ-----Dpyaslnp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 82 QLKVIEIInlyqsfyENPLPL-------------EEIIELTKFDSSQLNQFVNKLSGGQ-QRlldfvlslIG-------Q 140
Cdd:COG4608 111 RMTVGDII-------AEPLRIhglaskaerrervAELLELVGLRPEHADRYPHEFSGGQrQR--------IGiaralalN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 141 PQLILLDEPTSTMDIEIReyfwSIIENLKED-----NRTILYTSHYIEEVERMSDKII 193
Cdd:COG4608 176 PKLIVCDEPVSALDVSIQ----AQVLNLLEDlqdelGLTYLFISHDLSVVRHISDRVA 229
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
12-154 |
1.11e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.28 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 12 NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQ-SENRSIMFQKTMFPDQLKVIEIIN 90
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQfGREASLIDAIGRKGDFKDAVELLN 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446537461 91 --------LYqsfyenplpleeiieLTKFDssqlnqfvnKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMD 154
Cdd:COG2401 121 avglsdavLW---------------LRRFK---------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-181 |
1.58e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIG--NVNANSGEIFDKDK---LLQSENRS--IM 73
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKdllELSPEDRAgeGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 FQKTMFPdqlkvIEIINLYQSFY-------------ENPLP-------LEEIIELTKFDSSQLNQFVN-KLSGGQQRLLD 132
Cdd:PRK09580 81 FMAFQYP-----VEIPGVSNQFFlqtalnavrsyrgQEPLDrfdfqdlMEEKIALLKMPEDLLTRSVNvGFSGGEKKRND 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446537461 133 FVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHY 181
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHY 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-201 |
1.90e-09 |
|
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: 58.16 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTL---IDILIgnvnANSGEIF----DKDKLLQSENRS------IMFQktmfpdql 83
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglaLLRLI----PSEGEIRfdgqDLDGLSRRALRPlrrrmqVVFQ-------- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 84 kvieiiNLYQSFyeNP-LPLEEII---------ELTK---------------FDSSQLNQFVNKLSGGQ-QRLldfvlS- 136
Cdd:COG4172 370 ------DPFGSL--SPrMTVGQIIaeglrvhgpGLSAaerrarvaealeevgLDPAARHRYPHEFSGGQrQRI-----Ai 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446537461 137 ---LIGQPQLILLDEPTSTMDIEIREyfwSIIENLKEDNR----TILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:COG4172 437 araLILEPKLLVLDEPTSALDVSVQA---QILDLLRDLQRehglAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-229 |
2.21e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 3 QISNINKSFNKRcvLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQSENRSIMFQKTM---- 78
Cdd:PRK09700 267 EVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMayit 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 79 --------FPD-----------QLKVIEI---INLYQSFYENPLPlEEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLS 136
Cdd:PRK09700 345 esrrdngfFPNfsiaqnmaisrSLKDGGYkgaMGLFHEVDEQRTA-ENQRELLALKCHSVNQNITELSGGNQQKVLISKW 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 137 LIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEIilndstSHIRTNQQsq 216
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL------TQILTNRD-- 495
|
250
....*....|...
gi 446537461 217 iTLSDEYIRKLKL 229
Cdd:PRK09700 496 -DMSEEEIMAWAL 507
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-156 |
3.09e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIfdkdKLLQSenrsimfQKTMFPD 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI----KIGET-------VKLAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 82 QLKviEIINLYQSFYENPLPLEEIIELTKFDS------SQLN-------QFVNKLSGGQQRLLDFVLSLIGQPQLILLDE 148
Cdd:PRK11819 394 QSR--DALDPNKTVWEEISGGLDIIKVGNREIpsrayvGRFNfkggdqqKKVGVLSGGERNRLHLAKTLKQGGNVLLLDE 471
|
....*...
gi 446537461 149 PTSTMDIE 156
Cdd:PRK11819 472 PTNDLDVE 479
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-192 |
3.57e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.22 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 27 GKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKD-------------------KLLQSENRSIMfqKTMFPDQL---- 83
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdeildefrgselqnyftKLLEGDVKVIV--KPQYVDLIpkav 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 84 --KVIEIINLYQSFYEnplpLEEIIELTKFDSSqLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYF 161
Cdd:cd03236 104 kgKVGELLKKKDERGK----LDELVDQLELRHV-LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180 190
....*....|....*....|....*....|.
gi 446537461 162 WSIIENLKEDNRTILYTSHYIEEVERMSDKI 192
Cdd:cd03236 179 ARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-200 |
4.45e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGN---VNAN----------SGE-IFDKDKLLQS 67
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqGYSNdltlfgrrrgSGEtIWDIKKHIGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 68 ENRSIMFQKTMFPDQLKVI-----EIINLYQSFYENPLPL-EEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQP 141
Cdd:PRK10938 341 VSSSLHLDYRVSTSVRNVIlsgffDSIGIYQAVSDRQQKLaQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHP 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446537461 142 QLILLDEPTSTMDIEIREYFWSIIENLKEDNRT-ILYTSHYIEEVER-MSDKIILIENGEI 200
Cdd:PRK10938 421 TLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHHAEDAPAcITHRLEFVPDGDI 481
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-154 |
5.46e-09 |
|
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: 55.19 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 14 RCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF----DKDKLLQSENRSIMF------QKTMfpdqL 83
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlnggPLDFQRDSIARGLLYlghapgIKTT----L 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446537461 84 KVIEIINLYQSFYENplpleEIIElTKFDSSQLNQF----VNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMD 154
Cdd:cd03231 89 SVLENLRFWHADHSD-----EQVE-EALARVGLNGFedrpVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
12-156 |
9.39e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 55.97 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 12 NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIfdkdklLQSENRSIMF--QKTMFP-----DQLk 84
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI------ARPAGARVLFlpQRPYLPlgtlrEAL- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 85 vieiinLY-QSfyENPLPLEEIIE------LTKFdSSQLNQFVN---KLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMD 154
Cdd:COG4178 447 ------LYpAT--AEAFSDAELREaleavgLGHL-AERLDEEADwdqVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
..
gi 446537461 155 IE 156
Cdd:COG4178 518 EE 519
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-180 |
1.77e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 13 KRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNanSGEIFDKDKLL------QSENRSIMF--QKTMFPDQLK 84
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT--TGVITGGDRLVngrpldSSFQRSIGYvqQQDLHLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 85 VIEIIN----LYQ----SFYENPLPLEEIIELTkfdssQLNQFVNKLSG--------GQQRLLDFVLSLIGQPQLIL-LD 147
Cdd:TIGR00956 853 VRESLRfsayLRQpksvSKSEKMEYVEEVIKLL-----EMESYADAVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190
....*....|....*....|....*....|....*.
gi 446537461 148 EPTSTMDIEIReyfWSI---IENLKEDNRTILYTSH 180
Cdd:TIGR00956 928 EPTSGLDSQTA---WSIcklMRKLADHGQAILCTIH 960
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
14-201 |
2.23e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.06 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 14 RCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNAN--------SGEI-FDKDKLLQSENRSIMFQKTMFPDQ-- 82
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVtLNGEPLAAIDAPRLARLRAVLPQAaq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 83 ----LKVIEIINLYQSFY-----ENPLPLEEIIE--LTKFDSSQL-NQFVNKLSGGQQRLLDFVLSL---------IGQP 141
Cdd:PRK13547 94 pafaFSAREIVLLGRYPHarragALTHRDGEIAWqaLALAGATALvGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446537461 142 QLILLDEPTSTMDIEIREYFWSIIENLKED-NRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-197 |
2.54e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRC---VLKNISFDIEQGKCIALIGKNGAGKSTLIDIL-----------IGNVNANSGEIFDKDKLLQS 67
Cdd:PTZ00265 1166 IEIMDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhIVFKNEHTNDMTNEQDYQGD 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 68 ENRSIMFQK----------------TMFPDQLKVI------------EIINLYQ-----------SFYEN------PLPL 102
Cdd:PTZ00265 1246 EEQNVGMKNvnefsltkeggsgedsTVFKNSGKILldgvdicdynlkDLRNLFSivsqepmlfnmSIYENikfgkeDATR 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 103 EEIIELTKFdsSQLNQFV----NK-----------LSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIEN 167
Cdd:PTZ00265 1326 EDVKRACKF--AAIDEFIeslpNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1403
|
250 260 270
....*....|....*....|....*....|.
gi 446537461 168 LKED-NRTILYTSHYIEEVERmSDKIILIEN 197
Cdd:PTZ00265 1404 IKDKaDKTIITIAHRIASIKR-SDKIVVFNN 1433
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
20-198 |
2.57e-08 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 53.04 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 20 ISFDIEQGKCIALI-GKNGAGKSTLIDI----LIGNVNANSGEIFDKDKLLQSENR-SIMFQKTMFPDQLKVIEIINL-Y 92
Cdd:cd03279 20 IDFTGLDNNGLFLIcGPTGAGKSTILDAityaLYGKTPRYGRQENLRSVFAPGEDTaEVSFTFQLGGKKYRVERSRGLdY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 93 QSFYENP-LPLEEIIELTKFDssqlnqfVNKLSGGQQRLLDFVLSLI----------GQPQLILLDEPTSTMDIEIREYF 161
Cdd:cd03279 100 DQFTRIVlLPQGEFDRFLARP-------VSTLSGGETFLASLSLALAlsevlqnrggARLEALFIDEGFGTLDPEALEAV 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 446537461 162 WSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENG 198
Cdd:cd03279 173 ATALELIRTENRMVGVISHVEELKERIPQRLEVIKTP 209
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-200 |
3.68e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDkllqseNRSIMFQKTMFPDQLKVIEIINL----- 91
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAISSGLNGQLTGIENIELkglmm 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 92 ---YQSFYENPLPLEEIIELTKFdssqLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENL 168
Cdd:PRK13545 114 gltKEKIKEIIPEIIEFADIGKF----IYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF 189
|
170 180 190
....*....|....*....|....*....|..
gi 446537461 169 KEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:PRK13545 190 KEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-180 |
3.72e-08 |
|
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: 54.29 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI----FDKDKLLQSENRSI---------MFQKTMF--- 79
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgVPVSSLDQDEVRRRvsvcaqdahLFDTTVRenl 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 80 -------PDQ--LKVIEIINLyqsfyenplpLEEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPT 150
Cdd:TIGR02868 430 rlarpdaTDEelWAALERVGL----------ADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|..
gi 446537461 151 STMDIEIREyfwSIIENL--KEDNRTILYTSH 180
Cdd:TIGR02868 500 EHLDAETAD---ELLEDLlaALSGRTVVLITH 528
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-197 |
4.56e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.02 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQSENrsimfQKTMF 79
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtFPGNWQLAWVN-----QETPA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 80 PDQLKVIEIINLYQSFYENPLPLEEIIELTK-------------------------------FDSSQLNQFVNKLSGGQQ 128
Cdd:PRK10636 76 LPQPALEYVIDGDREYRQLEAQLHDANERNDghaiatihgkldaidawtirsraasllhglgFSNEQLERPVSDFSGGWR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 129 RLLDFVLSLIGQPQLILLDEPTSTMDIEirEYFWsiIEN-LKEDNRTILYTSHYIEEVERMSDKIILIEN 197
Cdd:PRK10636 156 MRLNLAQALICRSDLLLLDEPTNHLDLD--AVIW--LEKwLKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-199 |
5.79e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 24 IEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLlqsenrSIMFQKtMFPDQ-LKVIEII-----NLYQSFYE 97
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKI------SYKPQY-IKPDYdGTVEDLLrsitdDLGSSYYK 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 98 ----NPLPLEEIieltkfdssqLNQFVNKLSGGQ-QRLLdFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDN 172
Cdd:PRK13409 435 seiiKPLQLERL----------LDKNVKDLSGGElQRVA-IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEER 503
|
170 180
....*....|....*....|....*...
gi 446537461 173 R-TILYTSHYIEEVERMSDKIILIEnGE 199
Cdd:PRK13409 504 EaTALVVDHDIYMIDYISDRLMVFE-GE 530
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
16-180 |
6.17e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLlqsenRSIMFQKTMFpDQLKVIEIINLYQSF 95
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV-----RMAVFSQHHV-DGLDLSSNPLLYMMR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 96 YENPLPLEEI-IELTKFD-SSQLN-QFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREyfwSIIENLKEDN 172
Cdd:PLN03073 598 CFPGVPEQKLrAHLGSFGvTGNLAlQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVE---ALIQGLVLFQ 674
|
....*...
gi 446537461 173 RTILYTSH 180
Cdd:PLN03073 675 GGVLMVSH 682
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-180 |
7.65e-08 |
|
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: 53.25 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 25 EQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF---DKDKLLQSENRSIM---FQKT---------------MFPDQL 83
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepSWDEVLKRFRGTELqdyFKKLangeikvahkpqyvdLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 84 K--VIEIINLYQSFYEnplpLEEIIELTKFDSSqLNQFVNKLSGGQ-QRLLdFVLSLIGQPQLILLDEPTSTMDIEIREY 160
Cdd:COG1245 177 KgtVRELLEKVDERGK----LDELAEKLGLENI-LDRDISELSGGElQRVA-IAAALLRDADFYFFDEPSSYLDIYQRLN 250
|
170 180
....*....|....*....|
gi 446537461 161 FWSIIENLKEDNRTILYTSH 180
Cdd:COG1245 251 VARLIRELAEEGKYVLVVEH 270
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-228 |
8.22e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 19 NISFDIEQGKCIALIGKNGAGKSTLIDILIGnvnansgeifdkdkLLQ-SENRSIMFQKTMFPDQLKVIEIINlY--QSF 95
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTG--------------LLPaSEGEAWLFGQPVDAGDIATRRRVG-YmsQAF 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 96 --------YEN--------PLPLEEI---IE--LTKFD-SSQLNQFVNKLSGGQ-QRLldfvlSL----IGQPQLILLDE 148
Cdd:NF033858 349 slygeltvRQNlelharlfHLPAAEIaarVAemLERFDlADVADALPDSLPLGIrQRL-----SLavavIHKPELLILDE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 149 PTSTMDIEIREYFWSIIENL-KEDNRTILYTSHYIEEVERmSDKIILIENGEIILNDSTSHIRTNQQSQiTLSDEYIRKL 227
Cdd:NF033858 424 PTSGVDPVARDMFWRLLIELsREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAARGAA-TLEEAFIAYL 501
|
.
gi 446537461 228 K 228
Cdd:NF033858 502 E 502
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-198 |
1.10e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.42 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 19 NISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANsGEI-----FDKDKLL----------QSENRSIMFQKTM----- 78
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIggsatFNGREILnlpekelnklRAEQISMIFQDPMtslnp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 79 ---FPDQLkvIEIINLY------QSFYENPLPLE--EIIELTKfdssQLNQFVNKLSGG-QQRLLdFVLSLIGQPQLILL 146
Cdd:PRK09473 113 ymrVGEQL--MEVLMLHkgmskaEAFEESVRMLDavKMPEARK----RMKMYPHEFSGGmRQRVM-IAMALLCRPKLLIA 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446537461 147 DEPTSTMDIEIREYFWSIIENLKED-NRTILYTSHYIEEVERMSDKIILIENG 198
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-200 |
1.20e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQS----------------------------- 67
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspqdglangivyisedrkrdglvlgmsv 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 68 -ENRSIM----FQKTMFpdQLKvieiinlyqsFYENPLPLEEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQ 142
Cdd:PRK10762 348 kENMSLTalryFSRAGG--SLK----------HADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 143 LILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-156 |
1.72e-07 |
|
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: 52.24 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 3 QISNINKSFN-KRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGnvnansgeiFDKD---KLLQSENRSIMF--QK 76
Cdd:TIGR03719 6 TMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---------VDKDfngEARPQPGIKVGYlpQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 77 TMFPDQLKVIEII---------------NLYQSFYE-----NPL-----PLEEIIELTK---FDsSQL------------ 116
Cdd:TIGR03719 77 PQLDPTKTVRENVeegvaeikdaldrfnEISAKYAEpdadfDKLaaeqaELQEIIDAADawdLD-SQLeiamdalrcppw 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446537461 117 NQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIE 156
Cdd:TIGR03719 156 DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE 195
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-215 |
1.88e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI----FDKDKLLQSENR---SIMFQKTMF--------- 79
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRImiddCDVAKFGLTDLRrvlSIIPQSPVLfsgtvrfni 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 80 --------PDQLKVIEIINLYQSFYENPLPLEeiieltkfdsSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTS 151
Cdd:PLN03232 1331 dpfsehndADLWEALERAHIKDVIDRNPFGLD----------AEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446537461 152 TMDIEIREYfwsIIENLKEDNR--TILYTSHYIEEVERmSDKIILIENGEIILNDSTSHIRTNQQS 215
Cdd:PLN03232 1401 SVDVRTDSL---IQRTIREEFKscTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTS 1462
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-209 |
2.37e-07 |
|
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: 52.26 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQSENRSIMFQKTMFPDQLKVIE---IINL 91
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIiIDGLNIAKIGLHDLRFKITIIPQDPVLFSgslRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 92 --YQSFYENPLPLE-EIIELTKFDSSQLNQFVNK-------LSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYF 161
Cdd:TIGR00957 1381 dpFSQYSDEEVWWAlELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446537461 162 WSIIENLKEDNrTILYTSHYIEEVERMSdKIILIENGEIILNDSTSHI 209
Cdd:TIGR00957 1461 QSTIRTQFEDC-TVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
12-193 |
4.62e-07 |
|
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: 48.90 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 12 NKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDilignvnansgeifdkdkllqsenrsimfqktmfpdQLKVIEiinL 91
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILD------------------------------------AIGLAL---G 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 92 YQSFYENPLPLEEIIELTKFDSSQLNQFVNKLSGGQQRL--LDFVLSL--IGQPQLILLDEPTSTMDI-EIREYFWSIIE 166
Cdd:cd03227 47 GAQSATRRRSGVKAGCIVAAVSAELIFTRLQLSGGEKELsaLALILALasLKPRPLYILDEIDRGLDPrDGQALAEAILE 126
|
170 180
....*....|....*....|....*..
gi 446537461 167 NLKEDNRTILyTSHYiEEVERMSDKII 193
Cdd:cd03227 127 HLVKGAQVIV-ITHL-PELAELADKLI 151
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
23-196 |
5.39e-07 |
|
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: 48.72 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 23 DIEQGKCIALIGKNGAGKSTLIDILIGnvnansgeifdkdkllqsenrsimfqktmfpdQLKvieiinlyqsfyenplPL 102
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAG--------------------------------QLI----------------PN 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 103 EEIIELTKFDSSQLNQFVnKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDN-RTILYTSHY 181
Cdd:cd03222 53 GDNDEWDGITPVYKPQYI-DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHD 131
|
170
....*....|....*
gi 446537461 182 IEEVERMSDKIILIE 196
Cdd:cd03222 132 LAVLDYLSDRIHVFE 146
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-200 |
7.35e-07 |
|
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: 50.71 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKL--------LQSEN--RSIMFQKTMFPdqlkvi 86
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVayvpqqawIQNDSlrENILFGKALNE------ 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 87 eiiNLYQSFYENPLPLEEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYfwsIIE 166
Cdd:TIGR00957 728 ---KYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH---IFE 801
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446537461 167 N-------LKedNRTILYTSHYIEEVERMsDKIILIENGEI 200
Cdd:TIGR00957 802 HvigpegvLK--NKTRILVTHGISYLPQV-DVIIVMSGGKI 839
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-201 |
9.46e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.23 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNAN--SGEI----FDKDKLLQSENRSIMFQKTMFPDQLKVIEII 89
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIrisgFPKKQETFARISGYCEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 90 nLYQSF---------YENPLPLEEIIELTKFDSSQLNQF----VNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIE 156
Cdd:PLN03140 975 -IYSAFlrlpkevskEEKMMFVDEVMELVELDNLKDAIVglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446537461 157 IREYFWSIIENLKEDNRTILYTSHY--IEEVERMSDKIILIENGEII 201
Cdd:PLN03140 1054 AAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELLLMKRGGQVI 1100
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-183 |
1.04e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.29 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 14 RCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANsGEIfDKDKLlqSENrSIMFQKtmFPDQLKVI--EIINL 91
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEI-QIDGV--SWN-SVTLQT--WRKAFGVIpqKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 92 YQSFYENPLPL-----EEIIELTKFDS--SQLNQFVNK-----------LSGGQQRLLDFVLSLIGQPQLILLDEPTSTM 153
Cdd:TIGR01271 1305 SGTFRKNLDPYeqwsdEEIWKVAEEVGlkSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180 190
....*....|....*....|....*....|..
gi 446537461 154 DIEIreyFWSIIENLKE--DNRTILYTSHYIE 183
Cdd:TIGR01271 1385 DPVT---LQIIRKTLKQsfSNCTVILSEHRVE 1413
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-199 |
1.09e-06 |
|
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: 49.78 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 23 DIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKL------LQSEN----RSIMFQ--KTMFPDQLKVIEIIN 90
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKIsykpqyISPDYdgtvEEFLRSanTDDFGSSYYKTEIIK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 91 lyqsfyenPLPLEEIieltkfdssqLNQFVNKLSGGQ-QRLLdFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLK 169
Cdd:COG1245 442 --------PLGLEKL----------LDKNVKDLSGGElQRVA-IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFA 502
|
170 180 190
....*....|....*....|....*....|.
gi 446537461 170 EDN-RTILYTSHYIEEVERMSDKIILIEnGE 199
Cdd:COG1245 503 ENRgKTAMVVDHDIYLIDYISDRLMVFE-GE 532
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-201 |
1.24e-06 |
|
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: 48.03 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 4 ISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNAN---SGEI----FDKDKLLQSENRSIMF-- 74
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIhyngIPYKEFAEKYPGEIIYvs 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 75 QKTMFPDQLKVIEIInlyqsfyenplpleeiieltKFDSS-QLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTM 153
Cdd:cd03233 90 EEDVHFPTLTVRETL--------------------DFALRcKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446537461 154 DIEIREYFWSIIENLKEDNRTILYTSHY--IEEVERMSDKIILIENGEII 201
Cdd:cd03233 150 DSSTALEILKCIRTMADVLKTTTFVSLYqaSDEIYDLFDKVLVLYEGRQI 199
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-200 |
1.38e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.44 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 19 NISFDIEQGKCIALIGKNGAGKSTLIDILIGNV-NANSGEIFDKDKLLQSEN--RSIMFQKTMFPD---------QLKVI 86
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPVDIRNpaQAIRAGIAMVPEdrkrhgivpILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 87 EIINL--YQSF---------YENPLPLEEIIELtKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDI 155
Cdd:TIGR02633 358 KNITLsvLKSFcfkmridaaAELQIIGSAIQRL-KVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446537461 156 EIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-200 |
1.67e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 10 SFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGE----------------IFDKdkllqSENRSIM 73
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDAsvvirgtvayvpqvswIFNA-----TVRDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 74 FQKTMFPDQL-KVIEIINLYQSFyeNPLP---LEEIIEltkfdssqlnQFVNkLSGGQQRLLDFVLSLIGQPQLILLDEP 149
Cdd:PLN03130 701 FGSPFDPERYeRAIDVTALQHDL--DLLPggdLTEIGE----------RGVN-ISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446537461 150 TSTMDIEI-REYFWSII-ENLKEDNRtILYTS--HYIEEVermsDKIILIENGEI 200
Cdd:PLN03130 768 LSALDAHVgRQVFDKCIkDELRGKTR-VLVTNqlHFLSQV----DRIILVHEGMI 817
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
10-156 |
2.16e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.54 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 10 SFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI-FDKDKLLQSENRSIMFQKTMFP------DQ 82
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqIDGKTATRGDRSRFMAYLGHLPglkadlST 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446537461 83 LKVIEIINLYQSFYENPLPLE--EIIELTKFDSSqlnqFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIE 156
Cdd:PRK13543 100 LENLHFLCGLHGRRAKQMPGSalAIVGLAGYEDT----LVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-193 |
3.90e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.65 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF-------DKDKLLQSENRS---IMFQK---TMFPDQl 83
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYyqgqdllKADPEAQKLLRQkiqIVFQNpygSLNPRK- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 84 KVIEI------INLYQSFYENPLPLEEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEI 157
Cdd:PRK11308 110 KVGQIleepllINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 446537461 158 REYFWSIIENLKEDNRT-ILYTSHYIEEVERMSDKII 193
Cdd:PRK11308 190 QAQVLNLMMDLQQELGLsYVFISHDLSVVEHIADEVM 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-200 |
9.41e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 20 ISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGE--IFDKDKLLQSENRSIMFQKTMFPDQLKVIEII-------N 90
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQvyLDGKPIDIRSPRDAIRAGIMLCPEDRKAEGIIpvhsvadN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 91 LYQSFYENPLPLEEII------ELTKFDSSQLN-------QFVNKLSGG-QQRLldfVLS--LIGQPQLILLDEPTSTMD 154
Cdd:PRK11288 352 INISARRHHLRAGCLInnrweaENADRFIRSLNiktpsreQLIMNLSGGnQQKA---ILGrwLSEDMKVILLDEPTRGID 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446537461 155 IEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:PRK11288 429 VGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-201 |
1.39e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 6 NINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANS--GEIFDKDKLLQ------SENRSIMF--Q 75
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRfkdirdSEALGIVIihQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 76 KTMFPDQLKVIEIInlyqsFYENPLPLEEII--ELTKFDSSQL----------NQFVNKLSGGQQRLLDFVLSLIGQPQL 143
Cdd:NF040905 86 ELALIPYLSIAENI-----FLGNERAKRGVIdwNETNRRARELlakvgldespDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 144 ILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEII 201
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-156 |
1.66e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 13 KRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFdkdkllQSENRSIMF---------QKTMFPD-Q 82
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR------PAPGIKVGYlpqepqldpEKTVRENvE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 83 LKVIEIINLYQSF------YENPLP-----------LEEIIE---LTKFDsSQLNQF------------VNKLSGGQQR- 129
Cdd:PRK11819 93 EGVAEVKAALDRFneiyaaYAEPDAdfdalaaeqgeLQEIIDaadAWDLD-SQLEIAmdalrcppwdakVTKLSGGERRr 171
|
170 180 190
....*....|....*....|....*....|..
gi 446537461 130 -----LLdfvLSligQPQLILLDEPTSTMDIE 156
Cdd:PRK11819 172 valcrLL---LE---KPDMLLLDEPTNHLDAE 197
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
2-197 |
1.87e-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: 44.52 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNInKSFNKRCVlknISFDieqGKCIALIGKNGAGKSTLID----ILIGNVNANSGEIFDKDKLLqSENRSIMFQKT 77
Cdd:cd03240 4 LSIRNI-RSFHERSE---IEFF---SPLTLIVGQNGAGKTTIIEalkyALTGELPPNSKGGAHDPKLI-REGEVRAQVKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 78 MFPDQLKVIEIINLYQSFYENPL--PLEEIIELtkfdssqLNQFVNKLSGGQQRLLDFVL------SLIGQPQLILLDEP 149
Cdd:cd03240 76 AFENANGKKYTITRSLAILENVIfcHQGESNWP-------LLDMRGRCSGGEKVLASLIIrlalaeTFGSNCGILALDEP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446537461 150 TSTMDIE-IREYFWSIIENLKED-NRTILYTSHYiEEVERMSDKIILIEN 197
Cdd:cd03240 149 TTNLDEEnIEESLAEIIEERKSQkNFQLIVITHD-EELVDAADHIYRVEK 197
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
103-201 |
2.41e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.40 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 103 EEIIEltKFD--SSQLNQFVNKLSGG-QQRlldFVLS--LIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILY 177
Cdd:COG3845 383 EELIE--EFDvrTPGPDTPARSLSGGnQQK---VILAreLSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL 457
|
90 100
....*....|....*....|....
gi 446537461 178 TSHYIEEVERMSDKIILIENGEII 201
Cdd:COG3845 458 ISEDLDEILALSDRIAVMYEGRIV 481
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-218 |
3.28e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 44.31 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 14 RCVLKNISFDIEQGKCIALIGKNGAGKS----TLIDILIGNVNANSGEI-FDKDKLLQSENRSIMFQKTMfpdQlkviei 88
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVlLDGKPVAPCALRGRKIATIM---Q------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 89 iNLYQSFyeNPL---------------------PLEEIIELTKFDSSQ--LNQFVNKLSGGQ-QRLLdFVLSLIGQPQLI 144
Cdd:PRK10418 87 -NPRSAF--NPLhtmhtharetclalgkpaddaTLTAALEAVGLENAArvLKLYPFEMSGGMlQRMM-IALALLCEAPFI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446537461 145 LLDEPTSTMDIEIREYFWSIIENLKEDNRT-ILYTSHYIEEVERMSDKIILIENGEIILNDSTSHIRTNQQSQIT 218
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQKRALgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-158 |
3.75e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 24 IEQGKCIALIGKNGAGKSTLIDILIGNVNANSG---------EIFDK----------DKLLQSENRSImfQKTMFPDQL- 83
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeepswdEVLKRfrgtelqnyfKKLYNGEIKVV--HKPQYVDLIp 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 84 -----KVIEIINLYQsfyENPLpLEEIIELTKFDSSqLNQFVNKLSGGQ-QRLLdFVLSLIGQPQLILLDEPTSTMDIEI 157
Cdd:PRK13409 174 kvfkgKVRELLKKVD---ERGK-LDEVVERLGLENI-LDRDISELSGGElQRVA-IAAALLRDADFYFFDEPTSYLDIRQ 247
|
.
gi 446537461 158 R 158
Cdd:PRK13409 248 R 248
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-201 |
4.48e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 44.70 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 2 IQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKD------KLLQSENRSIMFQ 75
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDipltklQLDSWRSRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 76 KTMFPDQLKVIEIINL-----YQSFYENPLPL----EEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILL 146
Cdd:PRK10789 396 QTPFLFSDTVANNIALgrpdaTQQEIEHVARLasvhDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446537461 147 DEPTSTMDIEIrEYfwSIIENLKE--DNRTILYTSHyieeveRMS-----DKIILIENGEII 201
Cdd:PRK10789 476 DDALSAVDGRT-EH--QILHNLRQwgEGRTVIISAH------RLSalteaSEILVMQHGHIA 528
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-155 |
4.57e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.15 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIF--DKDKLL-------QSENRS 71
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrMRDGQLrdlyalsEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 72 IMFQKTMFPDQ-------LKVIEIINL-----------YQSFYENPLPLEEIIELtkfDSSQLNQFVNKLSGGQQRLLDF 133
Cdd:PRK11701 86 LLRTEWGFVHQhprdglrMQVSAGGNIgerlmavgarhYGDIRATAGDWLERVEI---DAARIDDLPTTFSGGMQQRLQI 162
|
170 180
....*....|....*....|..
gi 446537461 134 VLSLIGQPQLILLDEPTSTMDI 155
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDV 184
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-199 |
5.14e-05 |
|
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: 42.75 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 26 QGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFdkdkllqsenrsimfqktmfpdqlkvieIINlyqsfyenplpLEEI 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI----------------------------YID-----------GEDI 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 106 IELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLI--GQPQLILLDEPTS------TMDIEIREYFWSIIENLKEDNRTILY 177
Cdd:smart00382 42 LEEVLDQLLLIIVGGKKASGSGELRLRLALALArkLKPDVLILDEITSlldaeqEALLLLLEELRLLLLLKSEKNLTVIL 121
|
170 180
....*....|....*....|....*..
gi 446537461 178 TSHYIE-----EVERMSDKIILIENGE 199
Cdd:smart00382 122 TTNDEKdlgpaLLRRRFDRRIVLLLIL 148
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-200 |
6.77e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.15 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 13 KRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGN-VNANSGEIFDKDKLLQSEN--RSIMFQKTMFPD-------- 81
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNpqQAIAQGIAMVPEdrkrdgiv 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 82 -QLKVIEIINL--YQSFY---------ENPLPLEEIIELtKFDSSQLNQFVNKLSGG-QQRLldfVLS--LIGQPQLILL 146
Cdd:PRK13549 354 pVMGVGKNITLaaLDRFTggsriddaaELKTILESIQRL-KVKTASPELAIARLSGGnQQKA---VLAkcLLLNPKILIL 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446537461 147 DEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEI 200
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
113-201 |
7.96e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 113 SSQLNQFVNKLSGG-QQRLldfVLS--LIGQPQLILLDEPTSTMDI----EIreyfWSIIENLKEDNRTILYTSHYIEEV 185
Cdd:NF040905 395 TPSVFQKVGNLSGGnQQKV---VLSkwLFTDPDVLILDEPTRGIDVgakyEI----YTIINELAAEGKGVIVISSELPEL 467
|
90
....*....|....*.
gi 446537461 186 ERMSDKIILIENGEII 201
Cdd:NF040905 468 LGMCDRIYVMNEGRIT 483
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-149 |
1.02e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.48 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDKLLQsENRSIMFQKTMF- 79
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR-RQRDEYHQDLLYl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 80 ------PDQLKVIEiiNLyqSFY---ENPLPLEEIIELtkfdssqLNQF---------VNKLSGGQQR---LLDFVLSli 138
Cdd:PRK13538 80 ghqpgiKTELTALE--NL--RFYqrlHGPGDDEALWEA-------LAQVglagfedvpVRQLSAGQQRrvaLARLWLT-- 146
|
170
....*....|.
gi 446537461 139 gQPQLILLDEP 149
Cdd:PRK13538 147 -RAPLWILDEP 156
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
121-284 |
1.03e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 121 NKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLK-EDNRTILYTSHYIEEVeRMSDKIILIENGE 199
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTI-RYANTIFVLSNRE 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 200 iilNDSTSHIRTNQQSQITLSDEyiRKLKLDKDDLViQKNHNGTIKIitSNVNDTILYlQQLHinlDDIEIQKVSIVDSY 279
Cdd:PTZ00265 657 ---RGSTVDVDIIGEDPTKDNKE--NNNKNNKDDNN-NNNNNNNNKI--NNAGSYIIE-QGTH---DALMKNKNGIYYTM 724
|
....*
gi 446537461 280 FNNKK 284
Cdd:PTZ00265 725 INNQK 729
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-193 |
1.63e-04 |
|
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: 41.54 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGKCIALIGKNGAGKSTLIDilignvnansgEIFDKDKLLQSENRSIMF--QKTMFPDQLKVIEIINLyqs 94
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------EGLYASGKARLISFLPKFsrNKLIFIDQLQFLIDVGL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 95 fyeNPLPLeeiieltkfdssqlNQFVNKLSGG-QQRL-LDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDN 172
Cdd:cd03238 77 ---GYLTL--------------GQKLSTLSGGeLQRVkLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLG 139
|
170 180
....*....|....*....|.
gi 446537461 173 RTILYTSHYiEEVERMSDKII 193
Cdd:cd03238 140 NTVILIEHN-LDVLSSADWII 159
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
93-180 |
2.31e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.99 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 93 QSFYENPLPLEEIIELTKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQ---LILLDEPTSTMDIEIREYFWSIIENLK 169
Cdd:pfam13304 207 EKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELS 286
|
90
....*....|.
gi 446537461 170 EDNRTILYTSH 180
Cdd:pfam13304 287 RNGAQLILTTH 297
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
16-154 |
2.35e-04 |
|
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: 41.76 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLI-----------DILIGNVNANS----------GEIFDKDKLLQSENRSIMF 74
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLsaflrllntegDIQIDGVSWNSvplqkwrkafGVIPQKVFIFSGTFRKNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 75 QKTMFPDQ--LKVIEIINLYQSFYENPLPLEEIIEltkfDSSQLnqfvnkLSGGQQRLLDFVLSLIGQPQLILLDEPTST 152
Cdd:cd03289 99 PYGKWSDEeiWKVAEEVGLKSVIEQFPGQLDFVLV----DGGCV------LSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
..
gi 446537461 153 MD 154
Cdd:cd03289 169 LD 170
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-159 |
2.97e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.46 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 16 VLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKdkllqsenRSIMFqktmFPDQLKVIEII---NLY 92
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--------RSIAY----VPQQAWIMNATvrgNIL 742
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 93 QSFYENPLPLEEIIELTKF--DSSQL---------NQFVNkLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIRE 159
Cdd:PTZ00243 743 FFDEEDAARLADAVRVSQLeaDLAQLgggleteigEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
123-224 |
3.05e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 123 LSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYFWSIIENLKEDNRTILYTSHYIEEVERMSDKIILIENGEI-- 200
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVag 471
|
90 100
....*....|....*....|....
gi 446537461 201 ILNDSTshirTNQQSQITLSDEYI 224
Cdd:PRK10982 472 IVDTKT----TTQNEILRLASLHL 491
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-58 |
3.72e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 3.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446537461 1 MIQISNINKSFNKRCVLKNISFDIEQGKCIALIGKNGAGKSTLIDILIGNVNANSGEI 58
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV 58
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
26-63 |
2.94e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.91 E-value: 2.94e-03
10 20 30
....*....|....*....|....*....|....*...
gi 446537461 26 QGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDK 63
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEISEKLG 142
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
17-180 |
3.05e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 37.93 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 17 LKNISFDIEQGK----CIALI--------GKNGAGKSTLIDILIGNVNANSGEIFDKD---KLLQSENRSIMFQKTMFPD 81
Cdd:PRK13541 4 LHQLQFNIEQKNlfdlSITFLpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYYKNcniNNIAKPYCTYIGHNLGLKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 82 QLKVIEIINLYQSFYENPLPLEEIIELTKFDsSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLILLDEPTSTMDIEIREYF 161
Cdd:PRK13541 84 EMTVFENLKFWSEIYNSAETLYAAIHYFKLH-DLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170
....*....|....*....
gi 446537461 162 WSIIENLKEDNRTILYTSH 180
Cdd:PRK13541 163 NNLIVMKANSGGIVLLSSH 181
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-192 |
3.07e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 38.63 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 20 ISFDIEQGKCIALIGKNGAGKStLIDILIGNVNANSGEI------FDKDKLLQSENR----------SIMFQK---TMFP 80
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKS-LIAKAICGVTKDNWRVtadrmrFDDIDLLRLSPRerrklvghnvSMIFQEpqsCLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446537461 81 DQ---LKVIEII-------NLYQSFYENplpLEEIIEL-----TKFDSSQLNQFVNKLSGGQQRLLDFVLSLIGQPQLIL 145
Cdd:PRK15093 105 SErvgRQLMQNIpgwtykgRWWQRFGWR---KRRAIELlhrvgIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446537461 146 LDEPTSTMDIEIREYFWSIIENLKEDNR-TILYTSHYIEEVERMSDKI 192
Cdd:PRK15093 182 ADEPTNAMEPTTQAQIFRLLTRLNQNNNtTILLISHDLQMLSQWADKI 229
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
26-63 |
3.60e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.76 E-value: 3.60e-03
10 20 30
....*....|....*....|....*....|....*...
gi 446537461 26 QGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKDK 63
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEISEKLG 121
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
26-62 |
4.04e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.38 E-value: 4.04e-03
10 20 30
....*....|....*....|....*....|....*..
gi 446537461 26 QGKCIALIGKNGAGKSTLIDILIGNVNANSGEIFDKD 62
Cdd:PRK01889 194 GGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVREDD 230
|
|
| |
