|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-220 |
2.35e-67 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 207.22 E-value: 2.35e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP---GDEAVLKKLTYASH 79
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDvarDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 TPYLFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTA 158
Cdd:COG1131 81 EPALYPdLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 159 NIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKAS 220
Cdd:COG1131 161 GLDPEARREL-WELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-217 |
2.37e-59 |
|
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: 186.77 E-value: 2.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLsLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKL------ 74
Cdd:COG1122 1 IELENLSFSYPGGTPA-LDdvSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELrrkvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 75 --TYASHtpYLFAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLL 152
Cdd:COG1122 80 vfQNPDD--QLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 153 LDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAF 217
Cdd:COG1122 158 LDEPTAGLDPRGRREL-LELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-208 |
2.86e-59 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 185.79 E-value: 2.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDE----AVLKKLTYAS 78
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmpppEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 79 HTPYLFAMSVYDNIAYPLKIRKygKAAAAPIVEGLLQEFKI-EEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPT 157
Cdd:COG4619 81 QEPALWGGTVRDNLPFPFQLRE--RKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 158 ANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-219 |
5.38e-59 |
|
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: 186.22 E-value: 5.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDE---AVLKKLTYASH 79
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKeprEARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 TPYLFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTA 158
Cdd:COG4555 82 ERGLYDrLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 159 NIDPQSLKIIEaALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKA 219
Cdd:COG4555 162 GLDVMARRLLR-EILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-229 |
5.88e-59 |
|
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: 185.95 E-value: 5.88e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSlD-SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDE--AVLKKL 74
Cdd:COG1127 6 IEVRNLTKSFGDRVVLD-GvSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditgLSEKElyELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 75 TYashtpyLF-------AMSVYDNIAYPLKIR-KYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSF 146
Cdd:COG1127 85 GM------LFqggalfdSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 147 SPDTLLLDEPTANIDPQSLKIIeAALIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKASDNPVI 225
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVI-DELIRElRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDDPWV 237
|
....
gi 1172643631 226 QDFI 229
Cdd:COG1127 238 RQFL 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-228 |
8.25e-56 |
|
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: 177.69 E-value: 8.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP---GDEAVLKKLTYasH 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRR--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 TPYLF-------AMSVYDNIAYPLK---------IRKygkaaaapIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARA 143
Cdd:cd03261 79 MGMLFqsgalfdSLTVFENVAFPLRehtrlseeeIRE--------IVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 144 LSFSPDTLLLDEPTANIDPQSLKIIEaALIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKASDN 222
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVID-DLIRSlKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
|
....*.
gi 1172643631 223 PVIQDF 228
Cdd:cd03261 230 PLVRQF 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-215 |
4.45e-55 |
|
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: 176.39 E-value: 4.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKLTYAS 78
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 79 -HTPYLFAMSVYDNIA---YPLK--IRKYGKAAAApIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLL 152
Cdd:COG1120 82 qEPPAPFGLTVRELVAlgrYPHLglFGRPSAEDRE-AVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 153 LDEPTANIDPQS-LKIIEaaLIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVE 215
Cdd:COG1120 161 LDEPTSHLDLAHqLEVLE--LLRRlARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-209 |
6.98e-55 |
|
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: 174.63 E-value: 6.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgdEAVLKKLTYASHTPYLF 84
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG----RDVTGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 85 A-------MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPT 157
Cdd:cd03259 79 QdyalfphLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 158 ANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLL 209
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-209 |
1.01e-53 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 176.06 E-value: 1.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSlD-SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgdeavlKKLT------ 75
Cdd:COG3842 6 LELENVSKRYGDVTALD-DvSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG--------RDVTglppek 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 76 ---------YAshtpyLFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALS 145
Cdd:COG3842 77 rnvgmvfqdYA-----LFPhLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 146 FSPDTLLLDEPTANIDPQsLKIIEAALIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRLL 209
Cdd:COG3842 152 PEPRVLLLDEPLSALDAK-LREEMREELRRlQRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-217 |
4.12e-53 |
|
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: 170.82 E-value: 4.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLL-----APTSGAITYNGLP---GDEAVL--- 71
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDiydLDVDVLelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 72 KKLTYASHTPYLFAMSVYDNIAYPLKIRKY-GKAAAAPIVE------GLLQEFKieeiAKQNAKKLSGGESQKTALARAL 144
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGIkLKEELDERVEealrkaALWDEVK----DRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172643631 145 SFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREagLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAF 217
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-222 |
1.06e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 167.57 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAvLKKLTY---ASH 79
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-RRRIGYvpqRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 TPYLFAMSVYDNIA---YPLK--IRKYGKAAAApIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLD 154
Cdd:COG1121 86 VDWDFPITVRDVVLmgrYGRRglFRRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1172643631 155 EPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDsGRLLFNGSVEAFKASDN 222
Cdd:COG1121 165 EPFAGVDAATEEAL-YELLRELRREGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPEEVLTPEN 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-216 |
2.41e-50 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 167.25 E-value: 2.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKTVL---SLDslcLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLpgdeavlkklTYA 77
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLddvSLE---IASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR----------DLF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 SHTP-------YLFA-------MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARA 143
Cdd:COG1118 68 TNLPprerrvgFVFQhyalfphMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172643631 144 LSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEA 216
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDE 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-207 |
5.24e-50 |
|
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: 162.25 E-value: 5.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTYHGKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLtyASHTPY 82
Cdd:cd03225 2 LKNLSFSYPDGARPALDdiSLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL--RRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 --------LFAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLD 154
Cdd:cd03225 80 vfqnpddqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1172643631 155 EPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGR 207
Cdd:cd03225 160 EPTAGLDPAGRREL-LELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-208 |
6.21e-50 |
|
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: 162.27 E-value: 6.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYH--GKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLT--Y 76
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKgvSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTPYLF-------AMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPD 149
Cdd:cd03255 81 RRHIGFVFqsfnllpDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 150 TLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAyRICDTLSFMDSGRL 208
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-220 |
1.35e-49 |
|
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: 161.94 E-value: 1.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDEAVLKKLTYA 77
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditkLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 SHTPYLF-AMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEP 156
Cdd:cd03218 81 PQEASIFrKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1172643631 157 TANIDPQSLKIIEaALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKAS 220
Cdd:cd03218 161 FAGVDPIAVQDIQ-KIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-215 |
7.00e-49 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 160.19 E-value: 7.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG----------------- 63
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedithlpmhkrarlgig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 64 -LPGDEAVLKKLTyashtpylfamsVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALAR 142
Cdd:COG1137 82 yLPQEASIFRKLT------------VEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1172643631 143 ALSFSPDTLLLDEPTANIDPQSlkIIEA-ALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVE 215
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIA--VADIqKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPE 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-217 |
1.67e-47 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 155.77 E-value: 1.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGdEAVLKKLTYASHTPYL- 83
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-EKERKRIGYVPQRRSId 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 84 --FAMSVYDNIA---YPLK--IRKYGKAAAApIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEP 156
Cdd:cd03235 81 rdFPISVRDVVLmglYGHKglFRRLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 157 TANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLsfmdsgrLLFNGSVEAF 217
Cdd:cd03235 160 FAGVDPKTQEDI-YELLRELRREGMTILVVTHDLGLVLEYFDRV-------LLLNRTVVAS 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-207 |
3.04e-47 |
|
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: 153.88 E-value: 3.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLTYASHTPY 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 LFA-------MSVYDNIAYPLkirkygkaaaapivegllqefkieeiakqnakklSGGESQKTALARALSFSPDTLLLDE 155
Cdd:cd03229 81 VFQdfalfphLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 156 PTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGR 207
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-208 |
3.08e-47 |
|
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: 153.71 E-value: 3.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP---GDEAVLKKLTYASH 79
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDikkEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 TPYLFA-MSVYDNIayplkirkygkaaaapivegllqefkieeiakqnakKLSGGESQKTALARALSFSPDTLLLDEPTA 158
Cdd:cd03230 81 EPSLYEnLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1172643631 159 NIDPQSLKIIEAALIKRNREaGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-212 |
4.81e-47 |
|
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: 153.75 E-value: 4.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 4 AIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPgdeavlkkltYASHTPYL 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKD----------LASLSPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 84 FAmsvyDNIAYplkirkygkaaaapiVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDP- 162
Cdd:cd03214 71 LA----RKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIa 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 163 QSLKIIEaaLIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNG 212
Cdd:cd03214 132 HQIELLE--LLRRlARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-208 |
4.93e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 155.20 E-value: 4.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYH-GK---TVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDE-AVL- 71
Cdd:COG1136 5 LELRNLTKSYGtGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdissLSERElARLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 72 -KKLTYASHTPYLFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPD 149
Cdd:COG1136 85 rRHIGFVFQFFNLLPeLTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 150 TLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAyRICDTLSFMDSGRL 208
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRI 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-190 |
3.19e-46 |
|
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: 152.25 E-value: 3.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP---GDEAVLKKLTYA 77
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPirdAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 SHTPYLF-AMSVYDNIAYPLKIrkYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEP 156
Cdd:COG4133 81 GHADGLKpELTVRENLRFWAAL--YGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|....
gi 1172643631 157 TANIDPQSLKIIeAALIKRNREAGLTVIIITHNP 190
Cdd:COG4133 159 FTALDAAGVALL-AELIAAHLARGGAVLLTTHQP 191
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-209 |
3.19e-45 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 154.08 E-value: 3.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 2 QIAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYnglpGDEAVLKKLT------ 75
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI----GGRDVTDLPPkdrnia 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 76 -----YAshtpyLF-AMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPD 149
Cdd:COG3839 79 mvfqsYA-----LYpHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 150 TLLLDEPTANIDPQsLKIIEAALIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRLL 209
Cdd:COG3839 154 VFLLDEPLSNLDAK-LRVEMRAEIKRlHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-200 |
3.87e-45 |
|
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: 149.93 E-value: 3.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGK----TVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEaVLKKLTYAS 78
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-PGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 79 HTPYLFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPT 157
Cdd:cd03293 80 QQDALLPwLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1172643631 158 ANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTL 200
Cdd:cd03293 160 SALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRV 202
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-215 |
5.30e-45 |
|
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: 150.04 E-value: 5.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTY--HGKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDE--AVL 71
Cdd:cd03258 2 IELKNVSKVFgdTGGKVTALKdvSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltlLSGKElrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 72 KKLTYAS-HTPYLFAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDT 150
Cdd:cd03258 82 RRIGMIFqHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 151 LLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVE 215
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVE 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
11-219 |
1.62e-44 |
|
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: 148.35 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 11 TYHGKT-VLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDEAVLKKLTYASHTPYLF 84
Cdd:cd03224 8 AGYGKSqILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditgLPPHERARAGIGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 85 A-MSVYDNI---AYPLKirkygKAAAAPIVEGLLQEF-KIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTAN 159
Cdd:cd03224 88 PeLTVEENLllgAYARR-----RAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 160 IDPqslKIIE--AALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKA 219
Cdd:cd03224 163 LAP---KIVEeiFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-191 |
2.98e-44 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 147.89 E-value: 2.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTY-HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPgdeavLKKLTyASHTP 81
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD-----LSRLK-RREIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 82 Y--------------LFAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFS 147
Cdd:COG2884 76 YlrrrigvvfqdfrlLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1172643631 148 PDTLLLDEPTANIDPQ-SLKIIEaaLIKRNREAGLTVIIITHNPS 191
Cdd:COG2884 156 PELLLADEPTGNLDPEtSWEIME--LLEEINRRGTTVLIATHDLE 198
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-229 |
3.27e-44 |
|
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: 148.41 E-value: 3.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTY----HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLT--- 75
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRrrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 76 -------YASHTPYlfaMSVYDNIAYPLKIrkYGKAAAAPIVEGLLQEFKI-EEIAKQNAKKLSGGESQKTALARALSFS 147
Cdd:COG1124 82 qmvfqdpYASLHPR---HTVDRILAEPLRI--HGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 148 PDTLLLDEPTANIDPQSLKIIeAALIKRNR-EAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKAS-DNPVI 225
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEI-LNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGpKHPYT 235
|
....
gi 1172643631 226 QDFI 229
Cdd:COG1124 236 RELL 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-229 |
3.86e-44 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 151.00 E-value: 3.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGK--TVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDEavLKK 73
Cdd:COG1135 2 IELENLSKTFPTKggPVTALDdvSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltaLSERE--LRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 74 LT------------YASHTpylfamsVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALA 141
Cdd:COG1135 80 ARrkigmifqhfnlLSSRT-------VAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 142 RALSFSPDTLLLDEPTANIDPQSLKIIeAALIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSV-EAFKA 219
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSI-LDLLKDiNRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVlDVFAN 231
|
250
....*....|
gi 1172643631 220 SDNPVIQDFI 229
Cdd:COG1135 232 PQSELTRRFL 241
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-207 |
6.50e-43 |
|
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: 142.38 E-value: 6.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLTyashtpylf 84
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 85 amsvyDNIAYplkirkygkaaaapivegLLQefkieeiakqnakkLSGGESQKTALARALSFSPDTLLLDEPTANIDPQS 164
Cdd:cd00267 73 -----RRIGY------------------VPQ--------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1172643631 165 LKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGR 207
Cdd:cd00267 116 RERL-LELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-198 |
7.92e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 145.23 E-value: 7.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGK----TVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAvLKKLTY 76
Cdd:COG1116 6 PALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-GPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTPYLFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDE 155
Cdd:COG1116 85 VFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1172643631 156 PTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICD 198
Cdd:COG1116 165 PFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLAD 207
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-215 |
8.16e-43 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 144.72 E-value: 8.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDEAVLKKLTYASH 79
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGqdithLPMHERARLGIGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 TPYLF-AMSVYDNIAYPLKIRK-YGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPT 157
Cdd:TIGR04406 84 EASIFrKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1172643631 158 ANIDPQSLKIIEaALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVE 215
Cdd:TIGR04406 164 AGVDPIAVGDIK-KIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPA 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-216 |
2.26e-42 |
|
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: 143.35 E-value: 2.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDEAVLKKLTYA 77
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditgLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 SHTPYLFA-MSVYDNI----------AYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSF 146
Cdd:cd03219 81 FQIPRLFPeLTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 147 SPDTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEA 216
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEEL-AELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-229 |
2.87e-42 |
|
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: 143.15 E-value: 2.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDE----AVLKK 73
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditnLPPHKrpvnTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 74 ltYAshtpyLFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLL 152
Cdd:cd03300 81 --YA-----LFPhLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1172643631 153 LDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGS-VEAFKASDNPVIQDFI 229
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTpEEIYEEPANRFVADFI 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-217 |
4.61e-42 |
|
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: 142.71 E-value: 4.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTY-HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKL-TYASHT 80
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 81 PYLFA-------MSVYDNIAYplkirkyGKAAAAPIVEGLLQEFKIEEIAK---------------QNAKKLSGGESQKT 138
Cdd:cd03256 81 GMIFQqfnlierLSVLENVLS-------GRLGRRSTWRSLFGLFPKEEKQRalaalervglldkayQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 139 ALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAF 217
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-220 |
9.35e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 143.71 E-value: 9.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLTYASHTPY 82
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYLPEERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 LFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANID 161
Cdd:COG4152 82 LYPkMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 162 PQSLKIIEAALIKRnREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKAS 220
Cdd:COG4152 162 PVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
33-229 |
1.31e-41 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 144.45 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 33 ILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDEavlKKLTYASHTPYLFA-MSVYDNIAYPLKIRKYGKAAA 106
Cdd:NF040840 31 ILGPSGAGKTVLLELIAGIWPPDSGKIYLDGkditnLPPEK---RGIAYVYQNYMLFPhKTVFENIAFGLKLRKVPKEEI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 107 APIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQslkiIEAALI---KR-NREAGLT 182
Cdd:NF040840 108 ERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQ----TRDELIremKRwHREFGFT 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1172643631 183 VIIITHNPSQAYRICDTLSFMDSGRLLFNGSV-EAFKASDNPVIQDFI 229
Cdd:NF040840 184 AIHVTHNFEEALSLADRVGIMLNGRLSQVGDVrEVFRRPKNEFVARFV 231
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-207 |
1.67e-41 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 139.06 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKLTY 76
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKdvSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlrdlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTPYLFAMSVYDNIayplkirkygkaaaapivegllqefkieeiakqnakkLSGGESQKTALARALSFSPDTLLLDEP 156
Cdd:cd03228 81 VPQDPFLFSGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 157 TANIDPQSLKIIEAALikRNREAGLTVIIITHNPSQAyRICDTLSFMDSGR 207
Cdd:cd03228 124 TSALDPETEALILEAL--RALAKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-216 |
4.82e-41 |
|
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: 146.20 E-value: 4.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGK---TVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLTYA 77
Cdd:COG1123 261 LEVRNLSKRYPVRgkgGVRAVDdvSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 SHT-------PY--LFA-MSVYDNIAYPLKIRKYG-KAAAAPIVEGLLQEFKI-EEIAKQNAKKLSGGESQKTALARALS 145
Cdd:COG1123 341 RRRvqmvfqdPYssLNPrMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1172643631 146 FSPDTLLLDEPTANIDP--QSlKIIEaaLIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEA 216
Cdd:COG1123 421 LEPKLLILDEPTSALDVsvQA-QILN--LLRDlQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-229 |
6.38e-41 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 139.74 E-value: 6.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG--LPGDEAVLKKL------ 74
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedLTDSKKDINKLrrkvgm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 75 ---TYAshtpyLFA-MSVYDNIAY-PLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPD 149
Cdd:COG1126 82 vfqQFN-----LFPhLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 150 TLLLDEPTANIDPQSLKIIEaALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEA-FKASDNPVIQDF 228
Cdd:COG1126 157 VMLFDEPTSALDPELVGEVL-DVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEfFENPQHERTRAF 235
|
.
gi 1172643631 229 I 229
Cdd:COG1126 236 L 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-212 |
1.52e-40 |
|
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: 138.27 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYH--GKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDE---AVLKKLT 75
Cdd:cd03266 2 ITADALTKRFRdvKKTVQAVDgvSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepaEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 76 YASHTPYLFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLD 154
Cdd:cd03266 82 FVSDSTGLYDrLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1172643631 155 EPTANIDPQSLKIIEAAlIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNG 212
Cdd:cd03266 162 EPTTGLDVMATRALREF-IRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-217 |
2.80e-40 |
|
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: 144.28 E-value: 2.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQ--IAIDKLTKTYHGKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPT---SGAITYNG---LPGDEAV 70
Cdd:COG1123 1 MTplLEVRDLSVRYPGGDVPAVDgvSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGrdlLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 71 L-KKLTYASHTPY--LFAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFS 147
Cdd:COG1123 81 RgRRIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 148 PDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAF 217
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
3.17e-40 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 144.90 E-value: 3.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 2 QIAIDKLTKTYH-GKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKLTY 76
Cdd:COG4988 336 SIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDlsdlDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTPYLFAMSVYDNI--AYP----------LKirkygKAAAAPIVEGLLQ--EFKIEEiakqNAKKLSGGESQKTALAR 142
Cdd:COG4988 416 VPQNPYLFAGTIRENLrlGRPdasdeeleaaLE-----AAGLDEFVAALPDglDTPLGE----GGRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 143 ALSFSPDTLLLDEPTANIDPQSLKIIEAALikRNREAGLTVIIITHNPSQAyRICDTLSFMDSGRLLFNGSVEAFKASD 221
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQAL--RRLAKGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-214 |
4.38e-40 |
|
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: 136.87 E-value: 4.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTYHGKTVLSLDSLCLES--GKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG---LPGDEAVLKKLTYASH 79
Cdd:cd03263 3 IRNLTKTYKKGTKPAVDDLSLNVykGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysiRTDRKAARQSLGYCPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 TPYLF-AMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTA 158
Cdd:cd03263 83 FDALFdELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1172643631 159 NIDPQSLKIIEAAL--IKRNReaglTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSV 214
Cdd:cd03263 163 GLDPASRRAIWDLIleVRKGR----SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-208 |
4.48e-40 |
|
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: 137.25 E-value: 4.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGK--TVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG---LPGDEAVLKKLT 75
Cdd:cd03257 2 LEVKNLSVSFPTGggSVKALDdvSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 76 ----------YASHTPYlfaMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKI---EEIAKQNAKKLSGGESQKTALAR 142
Cdd:cd03257 82 keiqmvfqdpMSSLNPR---MTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 143 ALSFSPDTLLLDEPTANIDPqSLK--IIEaaLIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:cd03257 159 ALALNPKLLIADEPTSALDV-SVQaqILD--LLKKlQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
22-221 |
1.04e-39 |
|
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: 136.65 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDEAVLKKLTYASHTPYLFA-MSVYDNI--- 92
Cdd:COG0410 23 SLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGeditgLPPHRIARLGIGYVPEGRRIFPsLTVEENLllg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 93 AYPLKirkyGKAAAAPIVEGLLQEF-KIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPqslKIIE-- 169
Cdd:COG0410 103 AYARR----DRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAP---LIVEei 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 170 AALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKASD 221
Cdd:COG0410 176 FEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-208 |
1.80e-39 |
|
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: 135.46 E-value: 1.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDE----AVLKK 73
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdLPPKDrdiaMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 74 LTYASHtpylfaMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLL 153
Cdd:cd03301 81 YALYPH------MTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 154 DEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-207 |
3.14e-39 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 134.72 E-value: 3.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLTYASHTPY 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 LF-AMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANID 161
Cdd:cd03269 81 LYpKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1172643631 162 PQSLKIIEAAlIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGR 207
Cdd:cd03269 161 PVNVELLKDV-IRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-212 |
8.48e-39 |
|
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: 133.57 E-value: 8.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 32 GILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKkltyaSHTP-------YLFA-------MSVYDNIAYPLK 97
Cdd:cd03297 27 GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKK-----INLPpqqrkigLVFQqyalfphLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 98 IRKYGKAAAApiVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNR 177
Cdd:cd03297 102 RKRNREDRIS--VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 1172643631 178 EAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNG 212
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-226 |
1.15e-38 |
|
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: 134.40 E-value: 1.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDEAVLKKLTYASH 79
Cdd:COG0411 7 VRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrditgLPPHRIARLGIARTFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 TPYLFA-MSVYDNIA----------------YPLKIRKYGKAAAApIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALAR 142
Cdd:COG0411 87 NPRLFPeLTVLENVLvaaharlgrgllaallRLPRARREEREARE-RAEELLERVGLADRADEPAGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 143 ALSFSPDTLLLDEPTANIDPQSLKIIeAALIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKAsd 221
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEEL-AELIRRlRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRA-- 242
|
....*.
gi 1172643631 222 NP-VIQ 226
Cdd:COG0411 243 DPrVIE 248
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-232 |
1.45e-38 |
|
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: 133.62 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYhGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDEavlKKLTYA 77
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnLPPEK---RDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 SHTPYLFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEP 156
Cdd:cd03299 77 PQNYALFPhMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172643631 157 TANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEA-FKASDNPVIQDFITLN 232
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEvFKKPKNEFVAEFLGFN 233
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-206 |
3.42e-38 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 131.61 E-value: 3.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTYHGKT-VLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAV-LKKLTYASHTP- 81
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKErRKSIGYVMQDVd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 82 -YLFAMSVYDNIAYPLKIrkygKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANI 160
Cdd:cd03226 82 yQLFTDSVREELLLGLKE----LDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1172643631 161 DPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSG 206
Cdd:cd03226 158 DYKNMERV-GELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-223 |
3.99e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 132.19 E-value: 3.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTvLSLDsLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgdeavlkkltyASHTPY 82
Cdd:COG3840 2 LRLDDLTYRYGDFP-LRFD-LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG-------------QDLTAL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 ---------------LFA-MSVYDNIAypLKIRKYGKAAAAPI--VEGLLQEFKIEEIAKQNAKKLSGGESQKTALARAL 144
Cdd:COG3840 67 ppaerpvsmlfqennLFPhLTVAQNIG--LGLRPGLKLTAEQRaqVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 145 SFSPDTLLLDEPTANIDPqSLKIIEAALIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKASDNP 223
Cdd:COG3840 145 VRKRPILLLDEPFSALDP-ALRQEMLDLVDElCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPP 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-230 |
5.21e-38 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 132.85 E-value: 5.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKS-------VAGllAPTSGAITYNGL----PGDEAVL 71
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPG--ARVEGEILLDGEdiydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 72 --KKLTYASHTPYLFAMSVYDNIAYPLKIRKY-GKAAAAPIVE------GLLQEFKieEIAKQNAKKLSGGESQKTALAR 142
Cdd:COG1117 90 lrRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIkSKSELDEIVEeslrkaALWDEVK--DRLKKSALGLSGGQQQRLCIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 143 ALSFSPDTLLLDEPTANIDPQS-LKIIEaaLIKRNREAgLTVIIITHNPSQAYRICDTLSFMDSGRLL-FNGSVEAFKAS 220
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPIStAKIEE--LILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVeFGPTEQIFTNP 244
|
250
....*....|
gi 1172643631 221 DNPVIQDFIT 230
Cdd:COG1117 245 KDKRTEDYIT 254
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-212 |
6.12e-38 |
|
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: 131.19 E-value: 6.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG--LPGDEAVLKK----LTY 76
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksYQKNIEALRRigalIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTPYLFAMsvyDNIAYPLKIRKYGKAaaapIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEP 156
Cdd:cd03268 81 PGFYPNLTAR---ENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 157 TANIDPQSLKIIEaALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNG 212
Cdd:cd03268 154 TNGLDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-213 |
2.15e-37 |
|
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: 138.04 E-value: 2.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKLTY 76
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDniSLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlrqiDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTPYLFAMSVYDNIAY--P----------LKIrkygkAAAAPIVEGLLQ--EFKIEEiakqNAKKLSGGESQKTALAR 142
Cdd:COG2274 554 VLQDVFLFSGTIRENITLgdPdatdeeiieaARL-----AGLHDFIEALPMgyDTVVGE----GGSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 143 ALSFSPDTLLLDEPTANIDPQSLKIIEAALikRNREAGLTVIIITHNPSQAyRICDTLSFMDSGRLLFNGS 213
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENL--RRLLKGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGT 692
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-229 |
5.83e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 132.23 E-value: 5.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYH--GKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLpgDEAVL--KKLTY 76
Cdd:PRK11153 2 IELKNISKVFPqgGRTIHALNnvSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQ--DLTALseKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 A--------SHTPYLFAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSP 148
Cdd:PRK11153 80 ArrqigmifQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 149 DTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSV-EAFKASDNPVIQD 227
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVsEVFSHPKHPLTRE 239
|
..
gi 1172643631 228 FI 229
Cdd:PRK11153 240 FI 241
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-229 |
1.02e-36 |
|
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: 129.00 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgDEAVLKKLT----- 75
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVPVQernvg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 76 -----YAshtpyLFA-MSVYDNIAYPLKIRKYG----KAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALS 145
Cdd:cd03296 78 fvfqhYA-----LFRhMTVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 146 FSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSV-EAFKASDNPV 224
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPdEVYDHPASPF 232
|
....*
gi 1172643631 225 IQDFI 229
Cdd:cd03296 233 VYSFL 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-212 |
1.19e-36 |
|
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: 128.08 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGkIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP---GDEAVLKKLTYASH 79
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDvlkQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 TPYLFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTA 158
Cdd:cd03264 80 EFGVYPnFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 159 NIDPQSlkiieaalikRNR--------EAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNG 212
Cdd:cd03264 160 GLDPEE----------RIRfrnllselGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-208 |
1.27e-36 |
|
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: 126.39 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgdeavlkkltyashTPY 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG----------------KEV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 LFAmSVYDniayplkirkygkAAAAPIvegllqefkieEIAKQnakkLSGGESQKTALARALSFSPDTLLLDEPTANIDP 162
Cdd:cd03216 65 SFA-SPRD-------------ARRAGI-----------AMVYQ----LSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1172643631 163 QslkiiEA----ALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:cd03216 116 A-----EVerlfKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-215 |
1.69e-36 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 128.74 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDE-----AV 70
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladWSPAElarrrAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 71 LkkltyASHTPYLFAMSVYDNIA---YPLKIrkyGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARAL--- 144
Cdd:PRK13548 81 L-----PQHSSLSFPFTVEEVVAmgrAPHGL---SRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaql 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172643631 145 ---SFSPDTLLLDEPTANIDP-QSLKIIEAAlikRN--REAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVE 215
Cdd:PRK13548 153 wepDGPPRWLLLDEPTSALDLaHQHHVLRLA---RQlaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-221 |
2.31e-36 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 128.09 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 6 DKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDEAVLKKLTYASHT 80
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedislLPLHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 81 PYLFA-MSVYDNIAYPLKIRK-YGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTA 158
Cdd:PRK10895 87 ASIFRrLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172643631 159 NIDPQSLKIIEaALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKASD 221
Cdd:PRK10895 167 GVDPISVIDIK-RIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-208 |
2.73e-36 |
|
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: 126.88 E-value: 2.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG--LPGDEAVLKKLTyaSHT 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELR--QKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 81 P------YLFA-MSVYDNIAY-PLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLL 152
Cdd:cd03262 79 GmvfqqfNLFPhLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 153 LDEPTANIDPQSLKIIEaALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:cd03262 159 FDEPTSALDPELVGEVL-DVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-208 |
4.93e-36 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 126.78 E-value: 4.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGK----TVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGL---PGDE---AVLK 72
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlfALDEdarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 73 kltyASHTPYLF-------AMSVYDNIAYPLKIRkyGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALS 145
Cdd:COG4181 89 ----ARHVGFVFqsfqllpTLTALENVMLPLELA--GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172643631 146 FSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRiCDTLSFMDSGRL 208
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRL 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-158 |
6.46e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 124.30 E-value: 6.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKLTYASHTPYLF-AMSVYDNIAYPL 96
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltddERKSLRKEIGYVFQDPQLFpRLTVRENLRLGL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 97 KIRKYGKAAAAPIVEGLLQEFKIEEIAKQ----NAKKLSGGESQKTALARALSFSPDTLLLDEPTA 158
Cdd:pfam00005 85 LLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-218 |
3.31e-35 |
|
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: 3.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGL-----PGDeaVLKKLTYA 77
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHdvvrePRE--VRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 SHTPYL-FAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEP 156
Cdd:cd03265 79 FQDLSVdDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 157 TANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFK 218
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-229 |
5.35e-35 |
|
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: 124.72 E-value: 5.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTY-HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDE----AVLKKLTYA 77
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqdpvELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 SHTPYLFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIE--EIAKQNAKKLSGGESQKTALARALSFSPDTLLLD 154
Cdd:cd03295 81 IQQIGLFPhMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 155 EPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKASD-NPVIQDFI 229
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPaNDFVAEFV 236
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
3-229 |
3.01e-34 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 125.38 E-value: 3.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYH--GKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLTYA- 77
Cdd:TIGR02314 2 IKLSNITKVFHqgTKTIQALNnvSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 -------SHTPYLFAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDT 150
Cdd:TIGR02314 82 rqigmifQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 151 LLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSV-EAFKASDNPVIQDFI 229
Cdd:TIGR02314 162 LLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVsEIFSHPKTPLAQKFI 241
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-212 |
4.31e-34 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 121.54 E-value: 4.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCL--ESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPG---DEAVLKK-LTY 76
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLtiRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrqlDPADLRRnIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTPYLFAMSVYDNIAYplkirkygkaaAAPIV--EGLLQEFKI---EEIAKQNAK-----------KLSGGESQKTAL 140
Cdd:cd03245 83 VPQDVTLFYGTLRDNITL-----------GAPLAddERILRAAELagvTDFVNKHPNgldlqigergrGLSGGQRQAVAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1172643631 141 ARALSFSPDTLLLDEPTANIDPQSlkiiEAALIKRNRE--AGLTVIIITHNPSqAYRICDTLSFMDSGRLLFNG 212
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNS----EERLKERLRQllGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-189 |
7.66e-34 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 120.97 E-value: 7.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 14 GKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKLTYASHTPYLFAMSVY 89
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDistlKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 90 DNIAYPLKIRKygKAAAAPIVEGLLQEFKI-EEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKII 168
Cdd:PRK10247 99 DNLIFPWQIRN--QQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176
|
170 180
....*....|....*....|.
gi 1172643631 169 EAALIKRNREAGLTVIIITHN 189
Cdd:PRK10247 177 NEIIHRYVREQNIAVLWVTHD 197
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-207 |
1.93e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 123.52 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDE----AVLKk 73
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdithVPAENrhvnTVFQ- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 74 lTYAshtpyLFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLL 152
Cdd:PRK09452 94 -SYA-----LFPhMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 153 LDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGR 207
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-215 |
2.06e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 120.99 E-value: 2.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDE-----AVLk 72
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaaWSPWElarrrAVL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 73 kltyASHTPYLFAMSVYDNIA---YPlkiRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARAL----- 144
Cdd:COG4559 81 ----PQHSSLAFPFTVEEVVAlgrAP---HGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwe 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172643631 145 --SFSPDTLLLDEPTANIDP----QSLKiieaaLIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVE 215
Cdd:COG4559 154 pvDGGPRWLFLDEPTSALDLahqhAVLR-----LARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPE 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-208 |
3.02e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 125.66 E-value: 3.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKLTYASHTPYLFAMSVYDNIAyplk 97
Cdd:COG1132 360 SLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDirdlTLESLRRQIGVVPQDTFLFSGTIRENIR---- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 98 irkYGK--------------AAAAPIVEGLlqEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQ 163
Cdd:COG1132 436 ---YGRpdatdeeveeaakaAQAHEFIEAL--PDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTE 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1172643631 164 SLKIIEAALikRNREAGLTVIIITHNPSQAyRICDTLSFMDSGRL 208
Cdd:COG1132 511 TEALIQEAL--ERLMKGRTTIVIAHRLSTI-RNADRILVLDDGRI 552
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-189 |
4.75e-33 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 117.91 E-value: 4.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 14 GKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGD------EAVLKKLTYASHTP--YLFA 85
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysrkglLERRQRVGLVFQDPddQLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 86 MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSL 165
Cdd:TIGR01166 84 ADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163
|
170 180
....*....|....*....|....
gi 1172643631 166 KIIeAALIKRNREAGLTVIIITHN 189
Cdd:TIGR01166 164 EQM-LAILRRLRAEGMTVVISTHD 186
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3-212 |
5.59e-33 |
|
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: 118.36 E-value: 5.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYhGKTVLSLDsLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGL------PGDEAVlkKLTY 76
Cdd:cd03298 1 VRLDKIRFSY-GEQPMHFD-LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaapPADRPV--SMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTpyLFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDE 155
Cdd:cd03298 77 QENN--LFAhLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1172643631 156 PTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNG 212
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-206 |
5.75e-33 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 122.11 E-value: 5.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG--LPGDEAVLKKLTYAS 78
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdVSRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 79 HTPYLFA-MSVYDNIAYPLKI----RKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLL 153
Cdd:PRK10851 81 QHYALFRhMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1172643631 154 DEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSG 206
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-213 |
6.30e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 124.88 E-value: 6.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKLTY 76
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDglSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDlrdlDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTPYLFAMSVYDN--IAYP----------LKirkygKAAAAPIVEGL-------LQEfkieeiakqNAKKLSGGESQK 137
Cdd:COG4987 414 VPQRPHLFDTTLRENlrLARPdatdeelwaaLE-----RVGLGDWLAALpdgldtwLGE---------GGRRLSGGERRR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1172643631 138 TALARALSFSPDTLLLDEPTANIDPQSlkiiEAALIKRNREA--GLTVIIITHNPSQAyRICDTLSFMDSGRLLFNGS 213
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAAT----EQALLADLLEAlaGRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGT 552
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-195 |
7.09e-33 |
|
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: 124.32 E-value: 7.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 2 QIAIDKLTKTYHGKT-VLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP---GDEAVLKK-LTY 76
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladADADSWRDqIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTPYLFAMSVYDNIAYPLK-------IRKYGKAAAAPIVEGLLQ--EFKIEEiakqNAKKLSGGESQKTALARALSFS 147
Cdd:TIGR02857 401 VPQHPFLFAGTIAENIRLARPdasdaeiREALERAGLDEFVAALPQglDTPIGE----GGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1172643631 148 PDTLLLDEPTANIDPQSlkiiEAALIKRNREA--GLTVIIITHNPSQAYR 195
Cdd:TIGR02857 477 APLLLLDEPTAHLDAET----EAEVLEALRALaqGRTVLLVTHRLALAAL 522
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-188 |
1.15e-32 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 119.20 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHG----KTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP-----GDEAVL 71
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 72 kkltYASHT--PYLfamSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPD 149
Cdd:COG4525 82 ----FQKDAllPWL---NVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1172643631 150 TLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITH 188
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-223 |
2.50e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 117.93 E-value: 2.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAI--------TYNGLPGDEAVLKKL 74
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidTARSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 75 TyaSHTPYLFA-------MSVYDN-IAYPLKIRKYGKAAAAPIVEGLLQefKIEEIAKQNA--KKLSGGESQKTALARAL 144
Cdd:PRK11264 84 R--QHVGFVFQnfnlfphRTVLENiIEGPVIVKGEPKEEATARARELLA--KVGLAGKETSypRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 145 SFSPDTLLLDEPTANIDP----QSLKIIEaALIKRNReaglTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKAs 220
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPelvgEVLNTIR-QLAQEKR----TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA- 233
|
...
gi 1172643631 221 dNP 223
Cdd:PRK11264 234 -DP 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-212 |
4.99e-32 |
|
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: 116.66 E-value: 4.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTY-----------------HGK--TVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITY 61
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfKRKyrEVEALKgiSFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 62 NGL-PGDE--AVLKKLT--YASHTPYLFAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQ 136
Cdd:cd03267 81 AGLvPWKRrkKFLRRIGvvFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 137 KTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNG 212
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-215 |
5.10e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 117.04 E-value: 5.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKLTY 76
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 -ASHTPYLFAMSVYDNIAY---PLkIRKYGKAAAA--PIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDT 150
Cdd:PRK11231 81 lPQHHLTPEGITVRELVAYgrsPW-LSLWGRLSAEdnARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 151 LLLDEPTANIDpQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVE 215
Cdd:PRK11231 160 VLLDEPTTYLD-INHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-230 |
1.54e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 116.03 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSV--AGLLAP---TSGAITYNG----LPGDEAV--L 71
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGhniySPRTDTVdlR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 72 KKLTYASHTPYLFAMSVYDNIAYPLKIRK-YGKAAAAPIVEGLLQEFKIEEIAK----QNAKKLSGGESQKTALARALSF 146
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENVVYGLRLKGiKDKQVLDEAVEKSLKGASIWDEVKdrlhDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 147 SPDTLLLDEPTANIDPQSLKIIEAALIKRNREagLTVIIITHNPSQAYRICDTLSFMDSGRLL-FNGSVEAFKASDNPVI 225
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIeYNDTKQMFMNPKHKET 243
|
....*
gi 1172643631 226 QDFIT 230
Cdd:PRK14239 244 EDYIS 248
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-229 |
1.30e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 113.26 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 7 KLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP-GDEAVLKKLTYAS-----HT 80
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvNDPKVDERLIRQEagmvfQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 81 PYLFA-MSVYDNIAY-PLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTA 158
Cdd:PRK09493 86 FYLFPhLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 159 NIDPQ----SLKIIEAAlikrnREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGS-VEAFKASDNPVIQDFI 229
Cdd:PRK09493 166 ALDPElrheVLKVMQDL-----AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDpQVLIKNPPSQRLQEFL 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-208 |
1.62e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.44 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGktVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgdeavlKKLTYAS 78
Cdd:COG3845 4 PALELRGITKRFGG--VVANDdvSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG--------KPVRIRS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 79 --------------HtPYLF-AMSVYDNIAYPLKIRKYG----KAAAApivegllqefKIEEIAKQ-------NAK--KL 130
Cdd:COG3845 74 prdaialgigmvhqH-FMLVpNLTVAENIVLGLEPTKGGrldrKAARA----------RIRELSERygldvdpDAKveDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 131 SGGESQKTALARALSFSPDTLLLDEPTANIDPQslkiiEA----ALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSG 206
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVLTPQ-----EAdelfEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
..
gi 1172643631 207 RL 208
Cdd:COG3845 218 KV 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-208 |
5.46e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.89 E-value: 5.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 8 LTKTYHGktVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPgdeavlkkltYASHTP---- 81
Cdd:COG1129 10 ISKSFGG--VKALDgvSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEP----------VRFRSPrdaq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 82 -------Y----LFA-MSVYDNIAYPLKIRKYG---KAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSF 146
Cdd:COG1129 78 aagiaiiHqelnLVPnLSVAENIFLGREPRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 147 SPDTLLLDEPTANIDPQslkiiEA----ALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:COG1129 158 DARVLILDEPTASLTER-----EVerlfRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-221 |
6.42e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 112.98 E-value: 6.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLTYASHTPY 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 lfamsvYDNIAYPLKIRK----YGK------AAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLL 152
Cdd:PRK13537 88 ------FDNLDPDFTVREnllvFGRyfglsaAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 153 LDEPTANIDPQSLKIIEAALiKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKASD 221
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERL-RSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-190 |
1.18e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 109.25 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 12 YHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYnglpGDEAVLKKLTYASHTPYLFAMSVYDN 91
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR----AGGARVAYVPQRSEVPDSLPLTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 92 IAYPL-----KIRKYGKAAAApIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLK 166
Cdd:NF040873 78 VAMGRwarrgLWRRLTRDDRA-AVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180
....*....|....*....|....
gi 1172643631 167 IIeAALIKRNREAGLTVIIITHNP 190
Cdd:NF040873 157 RI-IALLAEEHARGATVVVVTHDL 179
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-215 |
1.37e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.39 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPgdeavlkkltyASHTP--- 81
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-----------LSHVPpyq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 82 ----------YLFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDT 150
Cdd:PRK11607 91 rpinmmfqsyALFPhMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 151 LLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVE 215
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-198 |
2.21e-29 |
|
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: 111.68 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTYH--GKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAP---TSGAITYNG---LPGDEAVLKKL 74
Cdd:COG0444 4 VRNLKVYFPtrRGVVKAVDgvSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGedlLKLSEKELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 75 T-----------YASHTPYlfaMSVYDNIAYPLKI-RKYGKAAAAPIVEGLLQEFKI---EEIAKQNAKKLSGGESQKTA 139
Cdd:COG0444 84 RgreiqmifqdpMTSLNPV---MTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 140 LARALSFSPDTLLLDEPTANIDP--QSlKIIEaaLIKR-NREAGLTVIIITHNPSQAYRICD 198
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVtiQA-QILN--LLKDlQRELGLAILFITHDLGVVAEIAD 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-208 |
2.34e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 108.07 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHG--KTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEavLKKLTYASHT 80
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ--WDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 81 PY------LFAMSVYDNIayplkirkygkaaaapivegllqefkieeiakqnakkLSGGESQKTALARALSFSPDTLLLD 154
Cdd:cd03246 79 GYlpqddeLFSGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1172643631 155 EPTANIDPQSLKIIEAAlIKRNREAGLTVIIITHNPSqAYRICDTLSFMDSGRL 208
Cdd:cd03246 122 EPNSHLDVEGERALNQA-IAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-216 |
5.22e-29 |
|
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: 111.35 E-value: 5.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDkLTKTYHGktvLSLD-SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgdeAVL----KKLT 75
Cdd:COG4148 1 MMLEVD-FRLRRGG---FTLDvDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-----EVLqdsaRGIF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 76 YASH---------TPYLFA-MSVYDNIAYPLKIRKYGKAAAAP--IVEgLLQefkIEEIAKQNAKKLSGGESQKTALARA 143
Cdd:COG4148 72 LPPHrrrigyvfqEARLFPhLSVRGNLLYGRKRAPRAERRISFdeVVE-LLG---IGHLLDRRPATLSGGERQRVAIGRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 144 LSFSPDTLLLDEPTANIDPQS-LKIIEaaLIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEA 216
Cdd:COG4148 148 LLSSPRLLLMDEPLAALDLARkAEILP--YLERlRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAE 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-189 |
7.38e-29 |
|
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: 107.88 E-value: 7.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYhGKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLpgDEAVLKKltyaSHT 80
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDgiNISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQ--DVSDLRG----RAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 81 PY--------------LFAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSF 146
Cdd:cd03292 74 PYlrrkigvvfqdfrlLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1172643631 147 SPDTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHN 189
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEI-MNLLKKINKAGTTVVVATHA 195
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-218 |
1.15e-28 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 108.18 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAIT-------YNGLPGDEAVL-- 71
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqfdFSQKPSEKAIRll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 72 -KKLTYASHTPYLFA-MSVYDN-IAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSP 148
Cdd:COG4161 81 rQKVGMVFQQYNLWPhLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 149 DTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFK 218
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQV-VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFT 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-213 |
1.85e-28 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 107.31 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 13 HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDE----AVLKKLTYASHTPYLFAMSV 88
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDisrkSLRSMIGVVLQDTFLFSGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 89 YDNIAY-------PLKIRKYGKAAAAPIVEGLLQEFkiEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANID 161
Cdd:cd03254 94 MENIRLgrpnatdEEVIEAAKEAGAHDFIMKLPNGY--DTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 162 PQSLKIIEAALIKRNReaGLTVIIITHNPSqAYRICDTLSFMDSGRLLFNGS 213
Cdd:cd03254 172 TETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGT 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
8-213 |
2.26e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 109.81 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 8 LTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgdEAVLKK--------LTYASH 79
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG----EDVTHRsiqqrdicMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 TpyLFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTA 158
Cdd:PRK11432 88 A--LFPhMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172643631 159 NIDpqslkiieAALIKRNREA--------GLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGS 213
Cdd:PRK11432 166 NLD--------ANLRRSMREKirelqqqfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGS 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-229 |
9.21e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 106.28 E-value: 9.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLA------PTSGAITYNG---LPGDEAVLKK-- 73
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGkdiFQIDAIKLRKev 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 74 -LTYASHTPYLFaMSVYDNIAYPLKIRKYG-KAAAAPIVEGLLQEF----KIEEIAKQNAKKLSGGESQKTALARALSFS 147
Cdd:PRK14246 93 gMVFQQPNPFPH-LSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 148 PDTLLLDEPTANIDPQSLKIIEAALIKRNREagLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSV-EAFKASDNPVIQ 226
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSnEIFTSPKNELTE 249
|
...
gi 1172643631 227 DFI 229
Cdd:PRK14246 250 KYV 252
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-193 |
1.11e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 105.94 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLTYASHTPYLF 84
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 85 AMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQS 164
Cdd:PRK11248 84 WRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180
....*....|....*....|....*....
gi 1172643631 165 LKIIEAALIKRNREAGLTVIIITHNPSQA 193
Cdd:PRK11248 164 REQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-209 |
1.97e-27 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 105.42 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP---GDEAVLKKL--TYASHTPYLFA----MSVYDNI 92
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaaMSRKELRELrrKKISMVFQSFAllphRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 93 AYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAAL 172
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDEL 203
|
170 180 190
....*....|....*....|....*....|....*..
gi 1172643631 173 IKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLL 209
Cdd:cd03294 204 LRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-230 |
2.09e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 104.99 E-value: 2.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 2 QIAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLL-----APTSGAITYNG---LPGDEAVLKK 73
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGqdiFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 74 ---LTYASHTPyLFAMSVYDNIAYPLKIRKYGKAAAA--PIVEGLLQEFKIEEIAKQN----AKKLSGGESQKTALARAL 144
Cdd:PRK14247 83 rvqMVFQIPNP-IPNLSIFENVALGLKLNRLVKSKKElqERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 145 SFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREagLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSV-EAFKASDNP 223
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTrEVFTNPRHE 239
|
....*..
gi 1172643631 224 VIQDFIT 230
Cdd:PRK14247 240 LTEKYVT 246
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-229 |
2.16e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 105.23 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG--LPGDE-----AVLKKLTYASHTPYLFA-MSVYDNIA 93
Cdd:PRK11831 27 SLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenIPAMSrsrlyTVRKRMSMLFQSGALFTdMNVFDNVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 94 YPLkiRKYGKAAAAPIVEGLLqeFKIEEIAKQNAKKL-----SGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKII 168
Cdd:PRK11831 107 YPL--REHTQLPAPLLHSTVM--MKLEAVGLRGAAKLmpselSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 169 EAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKASDNPVIQDFI 229
Cdd:PRK11831 183 VKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQFL 243
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-221 |
2.69e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.48 E-value: 2.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEA----VLKKLTY 76
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKdvSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtvwdVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTP--YLFAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLD 154
Cdd:PRK13635 86 VFQNPdnQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1172643631 155 EPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRiCDTLSFMDSGRLLFNGS-VEAFKASD 221
Cdd:PRK13635 166 EATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTpEEIFKSGH 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-217 |
3.09e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 104.71 E-value: 3.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQ--IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGD----EAVLKKL 74
Cdd:PRK09984 1 MQtiIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRtvqrEGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 75 TYAS--HTPYLFA-------MSVYDNIAYplkirkyGKAAAAPIVEGLLQEFKIEE---------------IAKQNAKKL 130
Cdd:PRK09984 81 IRKSraNTGYIFQqfnlvnrLSVLENVLI-------GALGSTPFWRTCFSWFTREQkqralqaltrvgmvhFAHQRVSTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 131 SGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLF 210
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFY 233
|
....*..
gi 1172643631 211 NGSVEAF 217
Cdd:PRK09984 234 DGSSQQF 240
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-212 |
1.05e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 104.91 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAID--KLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP-GDEAVLKKLTYAsh 79
Cdd:PRK13536 40 VAIDlaGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPvPARARLARARIG-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 tpylfAMSVYDNIAYPLKIRK----YGK------AAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPD 149
Cdd:PRK13536 118 -----VVPQFDNLDLEFTVREnllvFGRyfgmstREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 150 TLLLDEPTANIDPQSLKIIEA---ALIKRnreaGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNG 212
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWErlrSLLAR----GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-212 |
1.45e-26 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 101.96 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLL---APTSGAITYNGLPgdeavLKKLTYASHTPYL-----FA--MSVYDN 91
Cdd:cd03234 27 SLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQP-----RKPDQFQKCVAYVrqddiLLpgLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 92 IAYPLKIR---KYGKAAAAPIVE-GLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQS-LK 166
Cdd:cd03234 102 LTYTAILRlprKSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTaLN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1172643631 167 IIE--AALIKRNReaglTVIIITHNP-SQAYRICDTLSFMDSGRLLFNG 212
Cdd:cd03234 182 LVStlSQLARRNR----IVILTIHQPrSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-223 |
3.21e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 101.84 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLT-KTYHGKT-VLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLL-----APTSGAI------TYNGLPGD 67
Cdd:PRK14267 1 MKFAIETVNlRVYYGSNhVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVrlfgrnIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 68 EAVLKKLTYASHTPYLFA-MSVYDNIAYPLKIRKY--GKAAAAPIVEGLLQEFKIEEIAKQNAK----KLSGGESQKTAL 140
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPhLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 141 ARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREagLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEafKAS 220
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR--KVF 236
|
...
gi 1172643631 221 DNP 223
Cdd:PRK14267 237 ENP 239
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
25-217 |
3.30e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.62 E-value: 3.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 25 LESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAV-----LKK---LTYASHTPYLFAMSVYDNIAYPL 96
Cdd:PRK13636 29 IKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkglmkLREsvgMVFQDPDNQLFSASVYQDVSFGA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 97 KIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRN 176
Cdd:PRK13636 109 VNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQ 188
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1172643631 177 REAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSV-EAF 217
Cdd:PRK13636 189 KELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPkEVF 230
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-205 |
3.58e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 102.04 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTS-----GAITYNGLPGDEA------VL 71
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERrvnlnrLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 72 KKLTYASHTPYLFAMSVYDNIAYPLKIRKY-GKAAAAPIVEGLLQEFKIEEIAK----QNAKKLSGGESQKTALARALSF 146
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKhkihKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 147 SPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDS 205
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-220 |
4.65e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 102.10 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGaITYNG--LPGDEAVL--------- 71
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGdvLLGGRSIFnyrdvlefr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 72 KKLTYASHTPYLFAMSVYDNI-----AYPLKIRK-YGKAAAAPIVEGLLQEfKIEEIAKQNAKKLSGGESQKTALARALS 145
Cdd:PRK14271 101 RRVGMLFQRPNPFPMSIMDNVlagvrAHKLVPRKeFRGVAQARLTEVGLWD-AVKDRLSDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 146 FSPDTLLLDEPTANIDPQSLKIIEAALikRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKAS 220
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFI--RSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-209 |
4.95e-26 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 101.81 E-value: 4.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTY-HG--------KTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP-------G 66
Cdd:TIGR02769 3 LEVRDVTHTYrTGglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDlyqldrkQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 67 DEAVLKKL------TYASHTPylfAMSVYDNIAYPLK-IRKYGKAAAAPIVEGLLQEFKIE-EIAKQNAKKLSGGESQKT 138
Cdd:TIGR02769 83 RRAFRRDVqlvfqdSPSAVNP---RMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 139 ALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLL 209
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-222 |
5.72e-26 |
|
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: 103.27 E-value: 5.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 19 SLD-SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----------LPGDEavlKKLTYASHTPYLFA- 85
Cdd:TIGR02142 13 SLDaDFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgifLPPEK---RRIGYVFQEARLFPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 86 MSVYDNIAYPLK--IRKYGKAAAAPIVEGLlqefKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQ 163
Cdd:TIGR02142 90 LSVRGNLRYGMKraRPSERRISFERVIELL----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 164 SLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKASDN 222
Cdd:TIGR02142 166 RKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-228 |
7.14e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 100.86 E-value: 7.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGL-------PGDEAVL-- 71
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktPSDKAIRel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 72 -KKLTYASHTPYLFA-MSVYDN-IAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSP 148
Cdd:PRK11124 81 rRNVGMVFQQYNLWPhLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 149 DTLLLDEPTANIDP----QSLKIieaalIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKasdNPV 224
Cdd:PRK11124 161 QVLLFDEPTAALDPeitaQIVSI-----IRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFT---QPQ 232
|
....
gi 1172643631 225 IQDF 228
Cdd:PRK11124 233 TEAF 236
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-221 |
1.91e-25 |
|
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: 103.67 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 2 QIAIDKLTKTYHGKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP---GDEAVLkklty 76
Cdd:COG4618 330 RLSVENLTVVPPGSKRPILRgvSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADlsqWDREEL----- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTPY------LFAMSVYDNIAyplkirKYGKAAAAPIVE------------GLLQ--EFKIEEiakqNAKKLSGGESQ 136
Cdd:COG4618 405 GRHIGYlpqdveLFDGTIAENIA------RFGDADPEKVVAaaklagvhemilRLPDgyDTRIGE----GGARLSGGQRQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 137 KTALARALSFSPDTLLLDEPTANIDPQSlkiiEAAL---IKRNREAGLTVIIITHNPSqAYRICDTLSFMDsgrllfNGS 213
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDDEG----EAALaaaIRALKARGATVVVITHRPS-LLAAVDKLLVLR------DGR 543
|
....*...
gi 1172643631 214 VEAFKASD 221
Cdd:COG4618 544 VQAFGPRD 551
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-190 |
2.77e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 98.41 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP-GDEAVLKKLTYASH 79
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDiDDPDVAEACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 ----TPylfAMSVYDNIAYPLKIRkygkAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDE 155
Cdd:PRK13539 81 rnamKP---ALTVAENLEFWAAFL----GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1172643631 156 PTANIDPQSLKIIeAALIKRNREAGLTVIIITHNP 190
Cdd:PRK13539 154 PTAALDAAAVALF-AELIRAHLAQGGIVIAATHIP 187
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-221 |
3.79e-25 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 98.46 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCL--ESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKL----TY 76
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLdiPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLrrqiGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTPYLFAMSVYDNIAY------PLKIRKYGKAAAApivegllQEFkIEEIAK-------QNAKKLSGGESQKTALARA 143
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYgrpgatREEVEEAARAANA-------HEF-IMELPEgydtvigERGVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 144 LSFSPDTLLLDEPTANIDPQSLKIIEAALIK--RNReaglTVIIITHNPS---QAYRICdtlsFMDSGRLLFNGSVEAFK 218
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERlmKNR----TTFVIAHRLStieNADRIV----VLEDGKIVERGTHEELL 224
|
...
gi 1172643631 219 ASD 221
Cdd:cd03251 225 AQG 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-221 |
4.91e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 99.35 E-value: 4.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKTVL---SLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGL-PGDEAVlkKL 74
Cdd:PRK13637 1 MSIKIENLTHIYMEGTPFekkALDnvNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVdITDKKV--KL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 75 T-----------YASHTpyLFAMSVYDNIAYPLK--------IRKYGKAAAApIVeGLlqefKIEEIAKQNAKKLSGGES 135
Cdd:PRK13637 79 SdirkkvglvfqYPEYQ--LFEETIEKDIAFGPInlglseeeIENRVKRAMN-IV-GL----DYEDYKDKSPFELSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 136 QKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSV- 214
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPr 230
|
....*..
gi 1172643631 215 EAFKASD 221
Cdd:PRK13637 231 EVFKEVE 237
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-208 |
5.64e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 98.35 E-value: 5.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 6 DKLTKTYH-GKT---VLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPgdeavLKKLTYASHTP 81
Cdd:PRK11629 9 DNLCKRYQeGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP-----MSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 82 ---------YLFA-----MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFS 147
Cdd:PRK11629 84 lrnqklgfiYQFHhllpdFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 148 PDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSfMDSGRL 208
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-213 |
6.22e-25 |
|
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: 98.00 E-value: 6.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKL----TYASHTPYLFAMSVYDNIAYPLK 97
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLrsqiGLVSQEPVLFDGTIAENIRYGKP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 98 -------IRKYGKAAAAPIVEGLLQefKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEA 170
Cdd:cd03249 103 datdeevEEAAKKANIHDFIMSLPD--GYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1172643631 171 AL--IKRNReaglTVIIITHNPSqAYRICDTLSFMDSGRLLFNGS 213
Cdd:cd03249 181 ALdrAMKGR----TTIVIAHRLS-TIRNADLIAVLQNGQVVEQGT 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-221 |
7.07e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.07 E-value: 7.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKL-----T 75
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAsrrvaS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 76 YASHTPYLFAMSVYDNIA---YPLKIRkYGKAAAA--PIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDT 150
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEmgrTPHRSR-FDTWTETdrAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 151 LLLDEPTANIDPQSlKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKASD 221
Cdd:PRK09536 161 LLLDEPTASLDINH-QVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-215 |
7.13e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.91 E-value: 7.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTY-HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGL-PGDEAVLKK------L 74
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdTGDFSKLQGirklvgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 75 TYASHTPYLFAMSVYDNIAY--------PLKIRKygkaaaapIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSF 146
Cdd:PRK13644 82 VFQNPETQFVGRTVEEDLAFgpenlclpPIEIRK--------RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 147 SPDTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYrICDTLSFMDSGRLLFNGSVE 215
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAV-LERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPE 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-212 |
1.05e-24 |
|
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: 96.47 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 13 HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAP--TSGAITYNGLPGDEAVLKKLTyashtpylfAMSVYD 90
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKII---------GYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 91 NIAYP-LKIRKYGKAAAapivegllqefkieeiakqNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDP-QSLKII 168
Cdd:cd03213 91 DILHPtLTVRETLMFAA-------------------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSsSALQVM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1172643631 169 EaaLIKRNREAGLTVIIITHNPS-QAYRICDTLSFMDSGRLLFNG 212
Cdd:cd03213 152 S--LLRRLADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-215 |
1.06e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.85 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGL-----PGDE-----AVLK 72
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattPSRElakrlAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 73 -------KLTyashtpylfamsVYDNIA---YPlkirkYGK----AAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKT 138
Cdd:COG4604 82 qenhinsRLT------------VRELVAfgrFP-----YSKgrltAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 139 ALARALSFSPDTLLLDEPTANIDPQ-SLKIIeaALIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVE 215
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKhSVQMM--KLLRRlADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPE 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-219 |
1.11e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESG-KIhGILGPNGSGKTTLMKSVAGLLAPTSGAITYNglpgdeavlKKLT---YAS 78
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGdRI-GLIGPNGAGKSTLLKLLAGELEPDSGTVKLG---------ETVKigyFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 79 HTPYLFA-MSVYDNI------AYPLKIRKYgkaaaapiVEGLLqeFKIEEiAKQNAKKLSGGEsqKT--ALARALSFSPD 149
Cdd:COG0488 386 HQEELDPdKTVLDELrdgapgGTEQEVRGY--------LGRFL--FSGDD-AFKPVGVLSGGE--KArlALAKLLLSPPN 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1172643631 150 TLLLDEPTANIDPQSLKIIEAALikrNREAGlTVIIITHNPsqaY---RICD-TLSFMDSGRLLFNGSVEAFKA 219
Cdd:COG0488 453 VLLLDEPTNHLDIETLEALEEAL---DDFPG-TVLLVSHDR---YfldRVATrILEFEDGGVREYPGGYDDYLE 519
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-202 |
1.11e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 98.32 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 12 YHGKTvLSLDSLCLE--SGKIHGILGPNGSGKTTLMKSVAGL--LAPT---SGAITYNG--LPGDE----AVLKKLTYAS 78
Cdd:PRK14243 19 YYGSF-LAVKNVWLDipKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGknLYAPDvdpvEVRRRIGMVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 79 HTPYLFAMSVYDNIAYPLKIRKYgKAAAAPIVEGLLQEF----KIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLD 154
Cdd:PRK14243 98 QKPNPFPKSIYDNIAYGARINGY-KGDMDELVERSLRQAalwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1172643631 155 EPTANIDPQS-LKIIEaaLIKRNREAgLTVIIITHNPSQAYRICDTLSF 202
Cdd:PRK14243 177 EPCSALDPIStLRIEE--LMHELKEQ-YTIIIVTHNMQQAARVSDMTAF 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-206 |
1.21e-24 |
|
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: 97.15 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLTYASHTPYLFAMSVYDNIAYPLK--IR 99
Cdd:TIGR01184 5 NLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVDrvLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 100 KYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREA 179
Cdd:TIGR01184 85 DLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEH 164
|
170 180
....*....|....*....|....*..
gi 1172643631 180 GLTVIIITHNPSQAYRICDTLSFMDSG 206
Cdd:TIGR01184 165 RVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
33-215 |
1.22e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 98.34 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 33 ILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKK------LTYASHTPYLFAMSVYDNIAYPLKIRKYGKAAA 106
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrkfvgLVFQNPDDQIFSPTVEQDIAFGPINLGLDEETV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 107 APIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIII 186
Cdd:PRK13652 115 AHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFS 194
|
170 180
....*....|....*....|....*....
gi 1172643631 187 THNPSQAYRICDTLSFMDSGRLLFNGSVE 215
Cdd:PRK13652 195 THQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-213 |
1.54e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 101.03 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGL--LAPTSGAITYN----------GLPG---- 66
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyvERPSkvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 67 -------------------DEAVLKKLT--YASHTPYLFAM----SVYDNIAYPLKIRKY-GKAAAAPIVEgLLQEFKIE 120
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlSDKLRRRIRkrIAIMLQRTFALygddTVLDNVLEALEEIGYeGKEAVGRAVD-LIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 121 EIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTL 200
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|...
gi 1172643631 201 SFMDSGRLLFNGS 213
Cdd:TIGR03269 240 IWLENGEIKEEGT 252
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-190 |
1.82e-24 |
|
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: 100.90 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 17 VLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDE----AVLKKLTYASHTPYLFAMSVYDNi 92
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSldqdEVRRRVSVCAQDAHLFDTTVREN- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 93 aypLKIRK-------YGKAAAAPIVEGLLQEFK--IEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQ 163
Cdd:TIGR02868 429 ---LRLARpdatdeeLWAALERVGLADWLRALPdgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
170 180
....*....|....*....|....*....
gi 1172643631 164 SlkiiEAALIK--RNREAGLTVIIITHNP 190
Cdd:TIGR02868 506 T----ADELLEdlLAALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
2.12e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 97.78 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKTVLSLDSL-----CLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYnglpGDEAV----- 70
Cdd:PRK13634 1 MDITFQKVEHRYQYKTPFERRALydvnvSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI----GERVItagkk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 71 ---LKKL--------TYASHTpyLFAMSVYDNIAY-PLKI---RKYGKAAAAPIVE--GLlqefkIEEIAKQNAKKLSGG 133
Cdd:PRK13634 77 nkkLKPLrkkvgivfQFPEHQ--LFEETVEKDICFgPMNFgvsEEDAKQKAREMIElvGL-----PEELLARSPFELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 134 ESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGS 213
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT 229
|
..
gi 1172643631 214 VE 215
Cdd:PRK13634 230 PR 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-208 |
2.31e-24 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 96.39 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 17 VLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKLTYASHTPYLFAMSVYDNI 92
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPisqyEHKYLHSKVSLVGQEPVLFARSLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 93 AYPLKIRKYGK---AAAAPIVEGLLQEFK--IEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKI 167
Cdd:cd03248 109 AYGLQSCSFECvkeAAQKAHAHSFISELAsgYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQ 188
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1172643631 168 IEAALIKRNREAglTVIIITHNPSQAYRiCDTLSFMDSGRL 208
Cdd:cd03248 189 VQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-191 |
5.84e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 99.50 E-value: 5.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 2 QIAIDKLT-KTYHGKTVLSLDSLCLESGkiHGIL--GPNGSGKTTLMKSVAGLLAPTSGAITyngLPGDEAVLkkltYAS 78
Cdd:COG4178 362 ALALEDLTlRTPDGRPLLEDLSLSLKPG--ERLLitGPSGSGKSTLLRAIAGLWPYGSGRIA---RPAGARVL----FLP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 79 HTPYLFAMSVYDNIAYPLKIRKYGKAAaapiVEGLLQEFKIEEIA-----KQN-AKKLSGGESQKTALARALSFSPDTLL 152
Cdd:COG4178 433 QRPYLPLGTLREALLYPATAEAFSDAE----LREALEAVGLGHLAerldeEADwDQVLSLGEQQRLAFARLLLHKPDWLF 508
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1172643631 153 LDEPTANIDPQSlkiiEAALIK--RNREAGLTVIIITHNPS 191
Cdd:COG4178 509 LDEATSALDEEN----EAALYQllREELPGTTVISVGHRST 545
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-188 |
8.95e-24 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 92.51 E-value: 8.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITynglpgdeaVLKKLTyashtpy 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT---------WGSTVK------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 lfamsvydnIAYplkirkygkaaaapivegLLQefkieeiakqnakkLSGGESQKTALARALSFSPDTLLLDEPTANIDP 162
Cdd:cd03221 65 ---------IGY------------------FEQ--------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180
....*....|....*....|....*.
gi 1172643631 163 QSLKIIEAALIKRNReaglTVIIITH 188
Cdd:cd03221 104 ESIEALEEALKEYPG----TVILVSH 125
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-208 |
1.21e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 95.13 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAvlkkltyASHTPY 82
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-------REDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 LFA-------MSVYDNIAYPLKIRKYGKAAAApiveglLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDE 155
Cdd:PRK11247 86 MFQdarllpwKKVIDNVGLGLKGQWRDAALQA------LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 156 PTANIDpqSLKIIE-AALIKRN-REAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:PRK11247 160 PLGALD--ALTRIEmQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-213 |
1.36e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 95.44 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLTyaSHT 80
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKnvSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIR--KKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 81 PYLF--------AMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLL 152
Cdd:PRK13632 86 GIIFqnpdnqfiGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 153 LDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYrICDTLSFMDSGRLLFNGS 213
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGK 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-212 |
1.63e-23 |
|
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: 92.76 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP---GDEAVLKKLTYA 77
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKnlSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPvsdLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 SHTPYLFAMSVYDNIayplkirkygkaaaapivegllqefkieeiakqnAKKLSGGESQKTALARALSFSPDTLLLDEPT 157
Cdd:cd03247 81 NQRPYLFDTTLRNNL----------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 158 ANIDPqslkIIEAALIKRNREA--GLTVIIITHN---PSQAYRICdtlsFMDSGRLLFNG 212
Cdd:cd03247 127 VGLDP----ITERQLLSLIFEVlkDKTLIWITHHltgIEHMDKIL----FLENGKIIMQG 178
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-208 |
1.78e-23 |
|
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: 92.88 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 14 GKTVLSLDSLCLES-----------GKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPgdeavlkkltyashtpy 82
Cdd:cd03215 1 GEPVLEVRGLSVKGavrdvsfevraGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 lfamsvydniaypLKIRKYGKAAAAPIV--------EGLLQEFKIEE---IAKQnakkLSGGESQKTALARALSFSPDTL 151
Cdd:cd03215 64 -------------VTRRSPRDAIRAGIAyvpedrkrEGLVLDLSVAEniaLSSL----LSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 152 LLDEPTANIDpqslkiIEA-----ALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:cd03215 127 ILDEPTRGVD------VGAkaeiyRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
3-191 |
2.17e-23 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 92.22 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLT-KTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAItynGLPGDEAVLkkltYASHTP 81
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGEDLL----FLPQRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 82 YLFAMSVYDNIAYPLKirkygkaaaapivegllqefkieeiakqnaKKLSGGESQKTALARALSFSPDTLLLDEPTANID 161
Cdd:cd03223 74 YLPLGTLREQLIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180 190
....*....|....*....|....*....|
gi 1172643631 162 PQSlkiiEAALIKRNREAGLTVIIITHNPS 191
Cdd:cd03223 124 EES----EDRLYQLLKELGITVISVGHRPS 149
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-207 |
3.85e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 95.68 E-value: 3.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 2 QIAIDKLTKTYHGKT-VLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYnglpgDEAVLKKL------ 74
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWI-----GGRVVNELepadrd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 75 ------TYA--SHtpylfaMSVYDNIAYPLKIRKYGKA-------AAAPIVEgllqefkIEEIAKQNAKKLSGGESQKTA 139
Cdd:PRK11650 78 iamvfqNYAlyPH------MSVRENMAYGLKIRGMPKAeieervaEAARILE-------LEPLLDRKPRELSGGQRQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 140 LARALSFSPDTLLLDEPTANIDpqslkiieAAL-------IKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGR 207
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLD--------AKLrvqmrleIQRlHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-223 |
4.16e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 97.12 E-value: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP---GDEAVLKKLTYASHTPYLFA-MSVYDNIAypLK 97
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPvdaGDIATRRRVGYMSQAFSLYGeLTVRQNLE--LH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 98 IRKYG--KAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPqslkiieAA---- 171
Cdd:NF033858 364 ARLFHlpAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP-------VArdmf 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 172 ---LIKRNREAGLTVIIITHNPSQAYRiCDTLSFMDSGRLLfngsveafkASDNP 223
Cdd:NF033858 437 wrlLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVL---------ASDTP 481
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-193 |
5.06e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 92.54 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAP---TSGAITYNG-----LPgdeAVLKKLTY 76
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGrrltaLP---AEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTPYLFA-MSVYDNIAYPLKiRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDE 155
Cdd:COG4136 81 LFQDDLLFPhLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1172643631 156 PTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQA 193
Cdd:COG4136 160 PFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA 197
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-221 |
7.25e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 93.31 E-value: 7.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 4 AIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKLTY-AS 78
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswSSKAFARKVAYlPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 79 HTPYLFAMSVYDNIA---YPL--KIRKYGkAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLL 153
Cdd:PRK10575 93 QLPAAEGMTVRELVAigrYPWhgALGRFG-AADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 154 DEPTANID-PQSLKIIeaALIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKASD 221
Cdd:PRK10575 172 DEPTSALDiAHQVDVL--ALVHRlSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-188 |
7.92e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 7.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTYHGKTVLSLDSLCLESG-KIhGILGPNGSGKTTLMKSVAGLLAPTSGAITyngLPGDEavlkKLTYASHTPYL 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGdRI-GLVGRNGAGKSTLLKILAGELEPDSGEVS---IPKGL----RIGYLPQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 84 FA-MSVYDNIAYPLK-----IRKYGKAAAAPI---------------------------VEGLLQEFKI-EEIAKQNAKK 129
Cdd:COG0488 73 DDdLTVLDTVLDGDAelralEAELEELEAKLAepdedlerlaelqeefealggweaearAEEILSGLGFpEEDLDRPVSE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 130 LSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNreaGlTVIIITH 188
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP---G-TVLVVSH 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-207 |
9.93e-23 |
|
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: 91.38 E-value: 9.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 17 VLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgdeavlkKLTYASHTPYLFAMSVYDNI--AY 94
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG---------SIAYVSQEPWIQNGTIRENIlfGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 95 PLKIRKYGKA--AAApivegLLQEFKI------EEIAkQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQ-SL 165
Cdd:cd03250 91 PFDEERYEKVikACA-----LEPDLEIlpdgdlTEIG-EKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1172643631 166 KIIEAALI---KRNReaglTVIIITHNPsQAYRICDTLSFMDSGR 207
Cdd:cd03250 165 HIFENCILgllLNNK----TRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-219 |
2.36e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 92.84 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYH------G-------------KTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITY 61
Cdd:COG4586 2 IEVENLSKTYRvyekepGlkgalkglfrreyREVEAVDdiSFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 62 NGL-PgdeaVLKKLTYASHTPYLFA--------MSVYDNiaypLKIRK--YG--KAAAAPIVEGLLQEFKIEEIAKQNAK 128
Cdd:COG4586 82 LGYvP----FKRRKEFARRIGVVFGqrsqlwwdLPAIDS----FRLLKaiYRipDAEYKKRLDELVELLDLGELLDTPVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 129 KLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
250
....*....|.
gi 1172643631 209 LFNGSVEAFKA 219
Cdd:COG4586 234 IYDGSLEELKE 244
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-212 |
2.79e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 92.46 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKT-----VLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLpgDEAVLKKlt 75
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFK--DEKNKKK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 76 yashtPYLFAMSVYDNIAYPLKIRKYGKAAA----APIV----EGLLQEFKIEE----------IAKQNAKK-------- 129
Cdd:PRK13651 77 -----TKEKEKVLEKLVIQKTRFKKIKKIKEirrrVGVVfqfaEYQLFEQTIEKdiifgpvsmgVSKEEAKKraakyiel 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 130 --------------LSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREaGLTVIIITHNPSQAYR 195
Cdd:PRK13651 152 vgldesylqrspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLE 230
|
250
....*....|....*..
gi 1172643631 196 ICDTLSFMDSGRLLFNG 212
Cdd:PRK13651 231 WTKRTIFFKDGKIIKDG 247
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-213 |
3.25e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.99 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKT-----VLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAItyngLPGDEAV---LKK- 73
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT----IVGDYAIpanLKKi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 74 -----------LTYASHTPYLFAMSVYDNIAY-PLKIRKYGKAAAAPIVEgLLQEFKI-EEIAKQNAKKLSGGESQKTAL 140
Cdd:PRK13645 83 kevkrlrkeigLVFQFPEYQLFQETIEKDIAFgPVNLGENKQEAYKKVPE-LLKLVQLpEDYVKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172643631 141 ARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGS 213
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-231 |
3.41e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.76 E-value: 3.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKT-----VLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP-----GDE-- 68
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTpyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktKDKyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 69 -AVLKKLTYASHTP--YLFAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIE-EIAKQNAKKLSGGESQKTALARAL 144
Cdd:PRK13646 81 rPVRKRIGMVFQFPesQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 145 SFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKASDNPV 224
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
....*..
gi 1172643631 225 IQDFITL 231
Cdd:PRK13646 241 ADWHIGL 247
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3-222 |
4.19e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 91.48 E-value: 4.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTY-HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLT----YA 77
Cdd:PRK15056 7 IVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVayvpQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 SHTPYLFAMSVYDNIAyplkIRKYG--------KAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPD 149
Cdd:PRK15056 87 EEVDWSFPVLVEDVVM----MGRYGhmgwlrraKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1172643631 150 TLLLDEPTANIDPQS-LKIIeaALIKRNREAGLTVIIITHNPSQAYRICDtLSFMDSGRLLFNGSVEAFKASDN 222
Cdd:PRK15056 163 VILLDEPFTGVDVKTeARII--SLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFTAEN 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-213 |
4.40e-22 |
|
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: 90.62 E-value: 4.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG----LPGDEAVLKKLTY 76
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDniSLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaLADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTPYLFAMSVYDNIAYP---LKIRKYGKAAAAPIVEGLLQEFKI--EEIAKQNAKKLSGGESQKTALARALSFSPDTL 151
Cdd:cd03252 81 VLQENVLFNRSIRDNIALAdpgMSMERVIEAAKLAGAHDFISELPEgyDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 152 LLDEPTANIDPQSLKIIEAALikRNREAGLTVIIITHNPSqAYRICDTLSFMDSGRLLFNGS 213
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNM--HDICAGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGS 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-218 |
9.54e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.53 E-value: 9.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 15 KTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEA-----VLKKLTYASHTP--YLFAMS 87
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEenlwdIRNKAGMVFQNPdnQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 88 VYDNIAY--------PLKIRKYgkaaaapiVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTAN 159
Cdd:PRK13633 103 VEEDVAFgpenlgipPEEIRER--------VDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 160 IDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRiCDTLSFMDSGRLLFNGSV-EAFK 218
Cdd:PRK13633 175 LDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPkEIFK 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-212 |
1.25e-21 |
|
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: 92.54 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGktvLSLDSlclESGKIH-----GILGPNGSGKTTLMKSVAGLLAPTSGAItynglpgDEAVlkKLTYa 77
Cdd:COG1245 342 VEYPDLTKSYGG---FSLEV---EGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEV-------DEDL--KISY- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 shTP-YL---FAMSVYDNIayplkirkygKAAAAPIVEG------LLQEFKIEEIAKQNAKKLSGGESQKTALARALSFS 147
Cdd:COG1245 406 --KPqYIspdYDGTVEEFL----------RSANTDDFGSsyykteIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRD 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 148 PDTLLLDEPTANIDPQSlKIIEAALIKR---NREAglTVIIITHNpsqayricdtLSFMD--SGRLL-FNG 212
Cdd:COG1245 474 ADLYLLDEPSAHLDVEQ-RLAVAKAIRRfaeNRGK--TAMVVDHD----------IYLIDyiSDRLMvFEG 531
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-209 |
1.44e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 90.27 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKTVLS---LD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGL--------PGD 67
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMEkkgLDniSFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpetgnKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 68 EAVLKKLTYASHTP--YLFAMSVYDNIAY-PLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARAL 144
Cdd:PRK13641 81 KKLRKKVSLVFQFPeaQLFENTVLKDVEFgPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 145 SFSPDTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLL 209
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-230 |
1.66e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 89.64 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 2 QIAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDEAVLK---- 72
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlVRDKDGQLKvadk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 73 --------KLTYASHTPYLFA-MSVYDNI-AYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQN-AKKLSGGESQKTALA 141
Cdd:PRK10619 85 nqlrllrtRLTMVFQHFNLWShMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 142 RALSFSPDTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEA-FKAS 220
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEV-LRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQlFGNP 243
|
250
....*....|
gi 1172643631 221 DNPVIQDFIT 230
Cdd:PRK10619 244 QSPRLQQFLK 253
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
10-226 |
1.98e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.04 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 10 KTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPgdeavLKKLTYA-SHT-------- 80
Cdd:PRK15439 19 KQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNP-----CARLTPAkAHQlgiylvpq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 81 -PYLFA-MSVYDNIAYPLKirkyGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTA 158
Cdd:PRK15439 94 ePLLFPnLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 159 NIDPqslkiIEA-ALIKRNRE---AGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFkaSDNPVIQ 226
Cdd:PRK15439 170 SLTP-----AETeRLFSRIREllaQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL--STDDIIQ 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-213 |
2.38e-21 |
|
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: 88.44 E-value: 2.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYH-GKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLTYA---- 77
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAigvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 -SHTPyLFAMSVYDNIAY------PLKIRKYGKAAA-APIVEGLlqEFKIEEIAKQNAKKLSGGESQKTALARALSFSPD 149
Cdd:cd03253 81 pQDTV-LFNDTIGYNIRYgrpdatDEEVIEAAKAAQiHDKIMRF--PDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 150 TLLLDEPTANIDPQSLKIIEAALIK--RNReaglTVIIITHNPSQAYRiCDTLSFMDSGRLLFNGS 213
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDvsKGR----TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-208 |
2.54e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.09 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDE----AVLKKLTYASHTPYLFAMSVYDNIAYPL- 96
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhhYLHRQVALVGQEPVLFSGSVRENIAYGLt 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 97 -----KIRKYGKAAAA-PIVEGLLQEFKIEEIAKQNakKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSlkiiEA 170
Cdd:TIGR00958 581 dtpdeEIMAAAKAANAhDFIMEFPNGYDTEVGEKGS--QLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC----EQ 654
|
170 180 190
....*....|....*....|....*....|....*...
gi 1172643631 171 ALIKRNREAGLTVIIITHNPSQAYRiCDTLSFMDSGRL 208
Cdd:TIGR00958 655 LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-213 |
3.01e-21 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 91.70 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 8 LTKTYHGKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKL----TYASHTP 81
Cdd:TIGR02203 336 VTFRYPGRDRPALDsiSLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLrrqvALVSQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 82 YLFAMSVYDNIAYPlKIRKYGKA-AAAPIVEGLLQEF------KIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLD 154
Cdd:TIGR02203 416 VLFNDTIANNIAYG-RTEQADRAeIERALAAAYAQDFvdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 155 EPTANIDPQSLKIIEAAL--IKRNReaglTVIIITHNPSQAYRiCDTLSFMDSGRLLFNGS 213
Cdd:TIGR02203 495 EATSALDNESERLVQAALerLMQGR----TTLVIAHRLSTIEK-ADRIVVMDDGRIVERGT 550
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-212 |
4.18e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 91.02 E-value: 4.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 7 KLTKTYHGktvLSLDSlclESGKIH-----GILGPNGSGKTTLMKSVAGLLAPTSGAitynglpgdeaVLKKLTYASHTP 81
Cdd:PRK13409 345 DLTKKLGD---FSLEV---EGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGE-----------VDPELKISYKPQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 82 YL---FAMSVYDNIAyplKIRKygKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTA 158
Cdd:PRK13409 408 YIkpdYDGTVEDLLR---SITD--DLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 159 NIDPQSlKIIEAALIKR---NREAglTVIIITHNpsqayricdtLSFMD--SGRLL-FNG 212
Cdd:PRK13409 483 HLDVEQ-RLAVAKAIRRiaeEREA--TALVVDHD----------IYMIDyiSDRLMvFEG 529
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
13-198 |
4.69e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 87.53 E-value: 4.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 13 HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP---GDEAVLKKLTyASHTPYLF----- 84
Cdd:PRK10584 21 HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlhqMDEEARAKLR-AKHVGFVFqsfml 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 85 --AMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDP 162
Cdd:PRK10584 100 ipTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 1172643631 163 QSLKIIEAALIKRNREAGLTVIIITHNPSQAYRiCD 198
Cdd:PRK10584 180 QTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CD 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-215 |
4.78e-21 |
|
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: 91.02 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 17 VLSLDSLCLE--SGKIHGILGPNGSGKTTLMKSVAGLLAPTSGaiTYNGLPGDEAV----LKKLTYASHTPYLFAM---- 86
Cdd:TIGR03269 297 VKAVDNVSLEvkEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSG--EVNVRVGDEWVdmtkPGPDGRGRAKRYIGILhqey 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 87 ------SVYDN------IAYPLKIRKYgKAAAAPIVEGLLQEfKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLD 154
Cdd:TIGR03269 375 dlyphrTVLDNlteaigLELPDELARM-KAVITLKMVGFDEE-KAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 155 EPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVE 215
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
14-215 |
6.20e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 88.21 E-value: 6.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 14 GKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDE------AVLKKLTYASHTP--YLFA 85
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdkksllEVRKTVGIVFQNPddQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 86 MSVYDNIAY-PLKIrKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQS 164
Cdd:PRK13639 94 PTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 165 LKIIEAALIKRNREaGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVE 215
Cdd:PRK13639 173 ASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-223 |
6.94e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.67 E-value: 6.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 16 TVLSLD--------SLCLESGKIHGILGPNGSGKTTLMKSVAGLLaPTSGAITYNGLPGDEAVL----KKLTYASHTPYL 83
Cdd:PRK11174 356 EILSPDgktlagplNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPeswrKHLSWVGQNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 84 FAMSVYDNIAYplkirkyGKAAAAPI-VEGLLQEFKIEE------------IAKQNAKkLSGGESQKTALARALSFSPDT 150
Cdd:PRK11174 435 PHGTLRDNVLL-------GNPDASDEqLQQALENAWVSEflpllpqgldtpIGDQAAG-LSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172643631 151 LLLDEPTANIDPQSLKIIEAALIKRNReaGLTVIIITHNPSQAYRiCDTLSFMDSGRLLFNGSVEAFKASDNP 223
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAGGL 576
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
15-213 |
1.05e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 89.32 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 15 KTVLSLD----SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGL--------PGDEAVLKKLTYASHTPY 82
Cdd:PRK10070 37 KTGLSLGvkdaSLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiakisdaELREVRRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 LFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANID 161
Cdd:PRK10070 117 LMPhMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 162 PQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGS 213
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-207 |
1.22e-20 |
|
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: 86.33 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTY-----HGKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpGDEAV----- 70
Cdd:COG4778 5 LEVENLSKTFtlhlqGGKRLPVLDgvSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRH--DGGWVdlaqa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 71 -------LKKLT--YASHtpYLFAM---SVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEiakqnakKL-------- 130
Cdd:COG4778 83 spreilaLRRRTigYVSQ--FLRVIprvSALDVVAEPLLERGVDREEARARARELLARLNLPE-------RLwdlppatf 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172643631 131 SGGESQKTALARALSFSPDTLLLDEPTANIDPQSlKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGR 207
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAAN-RAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-190 |
2.06e-20 |
|
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: 85.24 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDE---AVLKKLTYASH 79
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFqrdSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 TPYL-FAMSVYDNiayplkIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTA 158
Cdd:cd03231 81 APGIkTTLSVLEN------LRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|..
gi 1172643631 159 NIDPQSLKIIEAALiKRNREAGLTVIIITHNP 190
Cdd:cd03231 155 ALDKAGVARFAEAM-AGHCARGGMVVLTTHQD 185
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-215 |
2.17e-20 |
|
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: 85.27 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 14 GKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLA--PTSGAITYNG-----LPGDEAVLKKLTYASHTPylfam 86
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGeditdLPPEERARLGIFLAFQYP----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 87 svydniayplkirkygkaaaaPIVEGLlqefKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLK 166
Cdd:cd03217 87 ---------------------PEIPGV----KNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1172643631 167 IIeAALIKRNREAGLTVIIITHNPSQA-YRICDTLSFMDSGRLLFNGSVE 215
Cdd:cd03217 142 LV-AEVINKLREEGKSVLIITHYQRLLdYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-213 |
2.18e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.98 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDE------AVLKKLTY 76
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYskrgllALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTP--YLFAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLD 154
Cdd:PRK13638 82 VFQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 155 EPTANIDPQSlKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGS 213
Cdd:PRK13638 162 EPTAGLDPAG-RTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-218 |
3.41e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.39 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHG--KTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGA---ITYNGLPGDEA----VLKK 73
Cdd:PRK13640 6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKtvwdIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 74 LTYASHTP--YLFAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTL 151
Cdd:PRK13640 86 VGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1172643631 152 LLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAyRICDTLSFMDSGRLLFNGS-VEAFK 218
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSpVEIFS 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-195 |
3.99e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.47 E-value: 3.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP---GDEAVLKKLTYASHTPYLFA-MSVYDNIAYPLK 97
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPirrQRDEYHQDLLYLGHQPGIKTeLTALENLRFYQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 98 IRkyGKAAAAPIVEGL----LQEFkiEEIAkqnAKKLSGGESQKTALARaLSFSPDTL-LLDEP-TAnIDPQSLKIIEaA 171
Cdd:PRK13538 101 LH--GPGDDEALWEALaqvgLAGF--EDVP---VRQLSAGQQRRVALAR-LWLTRAPLwILDEPfTA-IDKQGVARLE-A 170
|
170 180
....*....|....*....|....*...
gi 1172643631 172 LIKRNREAGLTVIIITHNP----SQAYR 195
Cdd:PRK13538 171 LLAQHAEQGGMVILTTHQDlpvaSDKVR 198
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-190 |
4.54e-20 |
|
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: 84.33 E-value: 4.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVL---KKLTYASH 79
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDephENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 TPYL-FAMSVYDNIAYPLKIRKYgkaaAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTA 158
Cdd:TIGR01189 81 LPGLkPELSALENLHFWAAIHGG----AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|..
gi 1172643631 159 NIDPQSLKIIeAALIKRNREAGLTVIIITHNP 190
Cdd:TIGR01189 157 ALDKAGVALL-AGLLRAHLARGGIVLLTTHQD 187
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-215 |
5.27e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.94 E-value: 5.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYH-GKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKK------LT 75
Cdd:PRK13647 5 IEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrskvgLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 76 YASHTPYLFAMSVYDNIAY-PLKIRkYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLD 154
Cdd:PRK13647 85 FQDPDDQVFSSTVWDDVAFgPVNMG-LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 155 EPTANIDPQSLKIIEAALIKRNREaGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVE 215
Cdd:PRK13647 164 EPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-161 |
8.76e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.78 E-value: 8.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYN-GLpgdeavlkKLTYASHTP 81
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNgKL--------RIGYVPQKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 82 YLfamsvydNIAYPLKIRKY-------GKAAAAPIveglLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLD 154
Cdd:PRK09544 77 YL-------DTTLPLTVNRFlrlrpgtKKEDILPA----LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
....*..
gi 1172643631 155 EPTANID 161
Cdd:PRK09544 146 EPTQGVD 152
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-216 |
8.80e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 84.25 E-value: 8.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTvLSLDsLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpGDEAvlkkLTYASHTPY 82
Cdd:PRK10771 2 LKLTDITWLYHHLP-MRFD-LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG--QDHT----TTPPSRRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 --------LFA-MSVYDNIA---YP-LKIRKYGKAAaapiVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPD 149
Cdd:PRK10771 74 smlfqennLFShLTVAQNIGlglNPgLKLNAAQREK----LHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 150 TLLLDEPTANIDP----QSLKIIEAALIKRNreagLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEA 216
Cdd:PRK10771 150 ILLLDEPFSALDPalrqEMLTLVSQVCQERQ----LTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
15-208 |
9.87e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.12 E-value: 9.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 15 KTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPgdeavLKKLTYASHTPY------LFA--- 85
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEP-----LAKLNRAQRKAFrrdiqmVFQdsi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 86 ------MSVYDNIAYPLK-IRKYGKAAAAPIVEGLLQEFKI-EEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPT 157
Cdd:PRK10419 100 savnprKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 158 ANIDpQSLKIIEAALIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:PRK10419 180 SNLD-LVLQAGVIRLLKKlQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-208 |
1.31e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.61 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 14 GKTVLSLDSLCLES-----------GKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGD-----EAVLKKLTYA 77
Cdd:COG1129 253 GEVVLEVEGLSVGGvvrdvsfsvraGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprDAIRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 S---HTPYLFA-MSVYDNIAYPL--KIRKYG---KAAAAPIVEGLLQEFKIeeiaK-----QNAKKLSGGESQKTALARA 143
Cdd:COG1129 333 PedrKGEGLVLdLSIRENITLASldRLSRGGlldRRRERALAEEYIKRLRI----KtpspeQPVGNLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 144 LSFSPDTLLLDEPTANIDpqslkiIEA-----ALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:COG1129 409 LATDPKVLILDEPTRGID------VGAkaeiyRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-208 |
1.38e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.85 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 9 TKTYhGKTVLSLD-SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGL------PGDEAVlkKLTYASHTP 81
Cdd:PRK11000 10 TKAY-GDVVISKDiNLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvpPAERGV--GMVFQSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 82 YLFaMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANID 161
Cdd:PRK11000 87 YPH-LSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1172643631 162 pQSLKI---IEAAliKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:PRK11000 166 -AALRVqmrIEIS--RLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-213 |
2.73e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.03 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKT-----VLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSG-------AITYNGLPGD- 67
Cdd:PRK13649 1 MGINLQNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGsvrvddtLITSTSKNKDi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 68 EAVLKKLTYASHTP--YLFAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKI-EEIAKQNAKKLSGGESQKTALARAL 144
Cdd:PRK13649 81 KQIRKKVGLVFQFPesQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 145 SFSPDTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGS 213
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKEL-MTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
7-189 |
3.00e-19 |
|
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: 83.23 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 7 KLTKTYHGKTvLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAItynglpgdEAVLKKLTYASHtpYL--- 83
Cdd:cd03237 5 TMKKTLGEFT-LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--------EIELDTVSYKPQ--YIkad 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 84 FAMSVYDNIAYplKIRKYGKAAAApIVEgLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQ 163
Cdd:cd03237 74 YEGTVRDLLSS--ITKDFYTHPYF-KTE-IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180
....*....|....*....|....*....
gi 1172643631 164 SlKIIEAALIKR---NREAglTVIIITHN 189
Cdd:cd03237 150 Q-RLMASKVIRRfaeNNEK--TAFVVEHD 175
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-190 |
3.21e-19 |
|
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: 83.21 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKiH-GILGPNGSGKTTLMKSVAGLLAPTSGA-ITYNGLP-GDEAVL---KKLTY 76
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGE-HwAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERrGGEDVWelrKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 AS---HTPYLFAMSV--------YDNIAYPlkiRKYGKAAAApIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALS 145
Cdd:COG1119 83 VSpalQLRFPRDETVldvvlsgfFDSIGLY---REPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1172643631 146 FSPDTLLLDEPTANIDPQS----LKIIEaALIkrnREAGLTVIIITHNP 190
Cdd:COG1119 159 KDPELLILDEPTAGLDLGArellLALLD-KLA---AEGAPTLVLVTHHV 203
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-213 |
3.36e-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: 86.22 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 4 AIDKLTKTYHgktvlsldslcleSGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGD---EAVLKKLTYASHT 80
Cdd:TIGR01257 945 AVDRLNITFY-------------ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtnlDAVRQSLGMCPQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 81 PYLFA-MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTAN 159
Cdd:TIGR01257 1012 NILFHhLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1172643631 160 IDPQSLKIIEAALIKrnREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGS 213
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLK--YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
14-190 |
4.51e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.81 E-value: 4.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 14 GKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLA--PTSGAITYNG-----LPGDEAVLKKLTYAshtpylFam 86
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGedileLSPDERARAGIFLA------F-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 87 svydniAYP-----LKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKL---------------SGGESQKTALARALSF 146
Cdd:COG0396 84 ------QYPveipgVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELgldedfldryvnegfSGGEKKRNEILQMLLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1172643631 147 SPDTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNP 190
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIV-AEGVNKLRSPDRGILIITHYQ 200
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-213 |
4.75e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 82.67 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLaPTSGAITYNGLPGDEAVLKKLtyASHTPYL-------FAMSVYDNIAY 94
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAEL--ARHRAYLsqqqtppFAMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 95 --PLKIRKYGKAAAapiVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARA-LSFSPDT------LLLDEPTANID-PQs 164
Cdd:PRK03695 93 hqPDKTRTEAVASA---LNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPMNSLDvAQ- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 165 lkiiEAAL---IKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGS 213
Cdd:PRK03695 169 ----QAALdrlLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGR 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-212 |
5.34e-19 |
|
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: 82.20 E-value: 5.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 15 KTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgdeavlkKLTyashtpYLFA------- 85
Cdd:cd03220 33 GEFWALKdvSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---------RVS------SLLGlgggfnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 86 -MSVYDNIAYPLKI----RKYGKAAAAPIVegllqEF-KIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTAN 159
Cdd:cd03220 98 eLTGRENIYLNGRLlglsRKEIDEKIDEII-----EFsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1172643631 160 IDPQ-SLKIIEAalIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNG 212
Cdd:cd03220 173 GDAAfQEKCQRR--LRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-226 |
5.67e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.73 E-value: 5.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYN-----GLPGDEAVLKKLTYASHTPYLF-AMSVYDN---- 91
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRgqhieGLPGHQIARMGVVRTFQHVRLFrEMTVIENllva 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 92 ---------IAYPLKIRKYGKAAAAPIVEGL--LQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANI 160
Cdd:PRK11300 105 qhqqlktglFSGLLKTPAFRRAESEALDRAAtwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGL 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172643631 161 DPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKasDNP-VIQ 226
Cdd:PRK11300 185 NPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR--NNPdVIK 249
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-219 |
6.85e-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: 85.07 E-value: 6.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCL--ESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG----------------L 64
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVgvRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksiltnisdvhqnmgyC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 65 PGDEAVLKKLTYASHTpYLFAmsvydniayplKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARAL 144
Cdd:TIGR01257 2018 PQFDAIDDLLTGREHL-YLYA-----------RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2085
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 145 SFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREaGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKA 219
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKS 2159
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-210 |
7.66e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.44 E-value: 7.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVL---SLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgdEAVLKKLTY- 76
Cdd:COG1101 2 LELKNLSKTFNPGTVNekrALDglNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG----KDVTKLPEYk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 -ASHTPYLF---------AMSVYDN--IAYpLKIRKYGKAAAapIVEGLLQEFKiEEIA----------KQNAKKLSGGE 134
Cdd:COG1101 78 rAKYIGRVFqdpmmgtapSMTIEENlaLAY-RRGKRRGLRRG--LTKKRRELFR-ELLAtlglglenrlDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 135 SQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLF 210
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIIL 229
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-213 |
1.32e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.96 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 6 DKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKK-------LTYAS 78
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvarriglLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 79 HTP------YLFAMSVYDNIAYPLKIRKYGKAAaapiVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLL 152
Cdd:PRK10253 91 TTPgditvqELVARGRYPHQPLFTRWRKEDEEA----VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 153 LDEPTANID-PQSLKIIEaALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGS 213
Cdd:PRK10253 167 LDEPTTWLDiSHQIDLLE-LLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-208 |
1.44e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.07 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTY-HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpGDEAVLKK-------- 73
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSG--HDITRLKNrevpflrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 74 ---LTYASHTpYLFAMSVYDNIAYPL--------KIRKYGKAAAAPIveGLLQEfkieeiAKQNAKKLSGGESQKTALAR 142
Cdd:PRK10908 80 qigMIFQDHH-LLMDRTVYDNVAIPLiiagasgdDIRRRVSAALDKV--GLLDK------AKNFPIQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 143 ALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNReAGLTVIIITHN----PSQAYRICdTLSfmdSGRL 208
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDigliSRRSYRML-TLS---DGHL 215
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-191 |
2.66e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 83.14 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLD--SLCLESGKIHGILGPNGSGKTTlmksVAGLLAP----TSGAITYNGLPGDEAVLKKL-- 74
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRniNFKIPAGKTVALVGRSGSGKST----IANLLTRfydiDEGEILLDGHDLRDYTLASLrn 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 75 --TYASHTPYLFAMSVYDNIAYPLK-------IRKYGKAA-AAPIVEGLLQEFkiEEIAKQNAKKLSGGESQKTALARAL 144
Cdd:PRK11176 418 qvALVSQNVHLFNDTIANNIAYARTeqysreqIEEAARMAyAMDFINKMDNGL--DTVIGENGVLLSGGQRQRIAIARAL 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1172643631 145 SFSPDTLLLDEPTANIDPQSLKIIEAAL--IKRNReaglTVIIITHNPS 191
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALdeLQKNR----TSLVIAHRLS 540
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-209 |
3.51e-18 |
|
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: 79.85 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 2 QIAIDKLTKTY--HGKTVLSLDSLCLESG-KIhGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKL 74
Cdd:cd03244 2 DIEFKNVSLRYrpNLPPVLKNISFSIKPGeKV-GIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskiGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 75 TYASHTPYLFAMSVYDNIAyPLKI-----------RKYGKAAAAPIVEGLlqEFKIEEiakqNAKKLSGGESQKTALARA 143
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLD-PFGEysdeelwqaleRVGLKEFVESLPGGL--DTVVEE----GGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 144 LSFSPDTLLLDEPTANIDPQSLKIIEAALikRNREAGLTVIIITHnpsqayRI-----CDTLSFMDSGRLL 209
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTI--REAFKDCTVLTIAH------RLdtiidSDRILVLDKGRVV 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-215 |
4.28e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYH--------------------GKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAIT 60
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtrREEFWALKdvSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 61 YNGlpgdeavlkkltyasHTPYLFA--------MSVYDNI-----AYPLKiRKYGKAAAAPIVegllqEF-KIEEIAKQN 126
Cdd:COG1134 85 VNG---------------RVSALLElgagfhpeLTGRENIylngrLLGLS-RKEIDEKFDEIV-----EFaELGDFIDQP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 127 AKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQ----SLKIIEaALIKRNReaglTVIIITHNPSQAYRICDTLSF 202
Cdd:COG1134 144 VKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIR-ELRESGR----TVIFVSHSMGAVRRLCDRAIW 218
|
250
....*....|...
gi 1172643631 203 MDSGRLLFNGSVE 215
Cdd:COG1134 219 LEKGRLVMDGDPE 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-196 |
4.96e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 82.46 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 17 VLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDE-AVLKKltyaSHTPYLFA----- 85
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdvatLDADAlAQLRR----EHFGFIFQryhll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 86 --MSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQ 163
Cdd:PRK10535 99 shLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1172643631 164 SLKIIEAALiKRNREAGLTVIIITHNP---SQAYRI 196
Cdd:PRK10535 179 SGEEVMAIL-HQLRDRGHTVIIVTHDPqvaAQAERV 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
8-189 |
5.68e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 80.93 E-value: 5.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 8 LTKTY---------HGKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP---GDEAVLKK 73
Cdd:COG4608 13 LKKHFpvrgglfgrTVGVVKAVDgvSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSGRELRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 74 L----------TYASHTPylfAMSVYDNIAYPLKIRKYGKAAA--APIVE-----GLLQEFkieeiAKQNAKKLSGGESQ 136
Cdd:COG4608 93 LrrrmqmvfqdPYASLNP---RMTVGDIIAEPLRIHGLASKAErrERVAEllelvGLRPEH-----ADRYPHEFSGGQRQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 137 KTALARALSFSPDTLLLDEPTANIDpqslKIIEAALIkrN------REAGLTVIIITHN 189
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALD----VSIQAQVL--NlledlqDELGLTYLFISHD 217
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-221 |
5.81e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.54 E-value: 5.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDEAVLKKLTYA 77
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdWQTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 SHTPYLFA-MSVYDNIA----------YPLKIRKygkaaaapiVEGLLQefKIEEIAKQNAKKLSGGESQKTALARALSF 146
Cdd:PRK11614 86 PEGRRVFSrMTVEENLAmggffaerdqFQERIKW---------VYELFP--RLHERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 147 SPDTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKASD 221
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQI-FDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANE 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-219 |
8.87e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.71 E-value: 8.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYhGKTVlSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYngLPGD-------EAVLKK 73
Cdd:NF033858 2 ARLEGVSHRY-GKTV-ALDdvSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEV--LGGDmadarhrRAVCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 74 LTYashtpylfaM------------SVYDNIAYplKIRKYGKAAA---APIVEgLLQEFKIEEIAKQNAKKLSGGESQKT 138
Cdd:NF033858 78 IAY---------MpqglgknlyptlSVFENLDF--FGRLFGQDAAerrRRIDE-LLRATGLAPFADRPAGKLSGGMKQKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 139 ALARALSFSPDTLLLDEPTANIDP----QSLKIIEAalIKRNReAGLTVIIIThnpsqAY-----RiCDTLSFMDSGRLL 209
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDPlsrrQFWELIDR--IRAER-PGMSVLVAT-----AYmeeaeR-FDWLVAMDAGRVL 216
|
250
....*....|
gi 1172643631 210 FNGSVEAFKA 219
Cdd:NF033858 217 ATGTPAELLA 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-193 |
1.62e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.02 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLTyaSHT 80
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKdvSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLR--KHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 81 PYLF---------AMSVYDnIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTL 151
Cdd:PRK13648 86 GIVFqnpdnqfvgSIVKYD-VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1172643631 152 LLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQA 193
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA 206
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
14-215 |
1.73e-17 |
|
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: 78.46 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 14 GKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGllAP----TSGAITYNG-----LPGDEAVLKKLTYASHTP--- 81
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPsyevTSGTILFKGqdlleLEPDERARAGLFLAFQYPeei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 82 -----YLFAMSVYDniayplKIRKYGKaaaapivEGLLQEFKIEEIAKQNAKKL---------------SGGESQKTALA 141
Cdd:TIGR01978 90 pgvsnLEFLRSALN------ARRSARG-------EEPLDLLDFEKLLKEKLALLdmdeeflnrsvnegfSGGEKKRNEIL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 142 RALSFSPDTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQA-YRICDTLSFMDSGRLLFNGSVE 215
Cdd:TIGR01978 157 QMALLEPKLAILDEIDSGLDIDALKIV-AEGINRLREPDRSFLIITHYQRLLnYIKPDYVHVLLDGRIVKSGDVE 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
10-213 |
3.22e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.74 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 10 KTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLTYASHTP-------- 81
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSkkiknfke 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 82 --------------YLFAMSVYDNIAY---PLKIRKY-GKAAAAPIVEGL-LQEFKIEeiakQNAKKLSGGESQKTALAR 142
Cdd:PRK13631 114 lrrrvsmvfqfpeyQLFKDTIEKDIMFgpvALGVKKSeAKKLAKFYLNKMgLDDSYLE----RSPFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 143 ALSFSPDTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGS 213
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-213 |
6.94e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.47 E-value: 6.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYH------GKTVLSLDsLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYnglpGD--------- 67
Cdd:PRK13643 2 IKFEKVNYTYQpnspfaSRALFDID-LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV----GDivvsstskq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 68 ---EAVLKKLTYASHTP--YLFAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKI-EEIAKQNAKKLSGGESQKTALA 141
Cdd:PRK13643 77 keiKPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 142 RALSFSPDTLLLDEPTANIDPQSlKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGS 213
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKA-RIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-213 |
8.36e-17 |
|
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: 78.63 E-value: 8.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTY-HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDE----AVLKKLTYA 77
Cdd:TIGR01193 474 IVINDVSYSYgYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDidrhTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 SHTPYLFAMSVYDNIAYplkirkygKAAAAPIVEGLLQEFKIEEIAK--------------QNAKKLSGGESQKTALARA 143
Cdd:TIGR01193 554 PQEPYIFSGSILENLLL--------GAKENVSQDEIWAACEIAEIKDdienmplgyqtelsEEGSSISGGQKQRIALARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 144 LSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREaglTVIIITHNPSQAYRIcDTLSFMDSGRLLFNGS 213
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGS 691
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-225 |
1.18e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 76.31 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 4 AIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgdeavlKKLTYAS----- 78
Cdd:COG4674 12 YVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGG--------TDLTGLDeheia 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 79 --------HTPYLF-AMSVYDNIAYPLKiRKYG---------KAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTAL 140
Cdd:COG4674 84 rlgigrkfQKPTVFeELTVFENLELALK-GDRGvfaslfarlTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 141 ARALSFSPDTLLLDEPTANIDPQslkiiE----AALIKRNREaGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEA 216
Cdd:COG4674 163 GMLLAQDPKLLLLDEPVAGMTDA-----EtertAELLKSLAG-KHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDE 236
|
250
....*....|
gi 1172643631 217 FKAsdNP-VI 225
Cdd:COG4674 237 VQA--DPrVI 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-214 |
1.71e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgdeavlkkLTYASHTPY 82
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN----------INYNKLDHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 LFA----------------MSVYDNI---AYPLKirkygKAAAAPIVEGLLQEFKIEEIAKQNAKK---------LSGGE 134
Cdd:PRK09700 76 LAAqlgigiiyqelsvideLTVLENLyigRHLTK-----KVCGVNIIDWREMRVRAAMMLLRVGLKvdldekvanLSISH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 135 SQKTALARALSFSPDTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSV 214
Cdd:PRK09700 151 KQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL-FLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMV 229
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-215 |
2.33e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.39 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 15 KTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAP---TSGAITYNGLPGDEAVLKKLT-YASHTPYLF-AMSVY 89
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAISaYVQQDDLFIpTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 90 DNIAYP--LKI-RKYGKAAAAPIVEGLLQEFKIEEIAK------QNAKKLSGGESQKTALARALSFSPDTLLLDEPTANI 160
Cdd:TIGR00955 118 EHLMFQahLRMpRRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 161 DPQSLKIIEAALiKRNREAGLTVIIITHNPS-QAYRICDTLSFMDSGRLLFNGSVE 215
Cdd:TIGR00955 198 DSFMAYSVVQVL-KGLAQKGKTIICTIHQPSsELFELFDKIILMAEGRVAYLGSPD 252
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
33-213 |
3.17e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.92 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 33 ILGPNGSGKTTLMksvaGLLA----PTSGAITYNGLPGDEAVLKKLTYASHT----PYLFAMSVYDNI------AYPLKI 98
Cdd:PRK13657 366 IVGPTGAGKSTLI----NLLQrvfdPQSGRILIDGTDIRTVTRASLRRNIAVvfqdAGLFNRSIEDNIrvgrpdATDEEM 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 99 RKYGKAAAA-PIVEGllQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAAL--IKR 175
Cdd:PRK13657 442 RAAAERAQAhDFIER--KPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALdeLMK 519
|
170 180 190
....*....|....*....|....*....|....*...
gi 1172643631 176 NReaglTVIIITHNPSqAYRICDTLSFMDSGRLLFNGS 213
Cdd:PRK13657 520 GR----TTFIIAHRLS-TVRNADRILVFDNGRVVESGS 552
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-188 |
3.27e-16 |
|
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: 77.13 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 25 LESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAitYNGLPGDEAVLKKLTYASHTPYLfaMSVYDN-------IAYPLK 97
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLGD--YDEEPSWDEVLKRFRGTELQDYF--KKLANGeikvahkPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 98 IRKY---------GKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANID-PQSLKI 167
Cdd:COG1245 172 IPKVfkgtvrellEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiYQRLNV 251
|
170 180
....*....|....*....|.
gi 1172643631 168 ieAALIKRNREAGLTVIIITH 188
Cdd:COG1245 252 --ARLIRELAEEGKYVLVVEH 270
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-213 |
3.79e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.79 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKT--VLSLDSLCLESGKIHGILGPNGSGKTTLMksvaGLLA----PTSGAITYNGLP---GDEAVLKK 73
Cdd:PRK11160 339 LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLL----QLLTrawdPQQGEILLNGQPiadYSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 74 -LTYASHTPYLFAMSVYDN--IAYPLK--------IRKYGkaaaapiVEGLLQEFK-----IEEIAKQnakkLSGGESQK 137
Cdd:PRK11160 415 aISVVSQRVHLFSATLRDNllLAAPNAsdealievLQQVG-------LEKLLEDDKglnawLGEGGRQ----LSGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 138 TALARALSFSPDTLLLDEPTANIDPQSLKIIEAALikRNREAGLTVIIITHNPS---QAYRICdtlsFMDSGRLLFNGS 213
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELL--AEHAQNKTVLMITHRLTgleQFDRIC----VMDNGQIIEQGT 556
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-188 |
5.05e-16 |
|
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: 76.51 E-value: 5.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTY-HGKTVLSLDSLCLESG-KIhGILGPNGSGKTTLMKSVAGLLAPTSGaitynglpgdEAVLK---KLTYASH 79
Cdd:TIGR03719 7 MNRVSKVVpPKKEILKDISLSFFPGaKI-GVLGLNGAGKSTLLRIMAGVDKDFNG----------EARPQpgiKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 TPYL------------------FAMSVYDNI--AYPLKIRKYGKAAAApivEGLLQEfKIE-----------EIA----- 123
Cdd:TIGR03719 76 EPQLdptktvrenveegvaeikDALDRFNEIsaKYAEPDADFDKLAAE---QAELQE-IIDaadawdldsqlEIAmdalr 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 124 ----KQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIkrnREAGlTVIIITH 188
Cdd:TIGR03719 152 cppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ---EYPG-TVVAVTH 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-208 |
5.23e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.10 E-value: 5.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 6 DKLTKTYHGktVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPgdeavlkkLTYASHTPYL 83
Cdd:PRK11288 8 DGIGKTFPG--VKALDdiSFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE--------MRFASTTAAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 84 FA--------------MSVYDNI---AYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSF 146
Cdd:PRK11288 78 AAgvaiiyqelhlvpeMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 147 SPDTLLLDEPTAnidpqSLKIIEA----ALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:PRK11288 158 NARVIAFDEPTS-----SLSAREIeqlfRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1-191 |
5.74e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.29 E-value: 5.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQIAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVL----KKLTY 76
Cdd:PRK10789 314 LDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLdswrSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTPYLFAMSVYDNIAyplkirkYGKAAAApivegllQEfKIEEIAK--------------------QNAKKLSGGESQ 136
Cdd:PRK10789 394 VSQTPFLFSDTVANNIA-------LGRPDAT-------QQ-EIEHVARlasvhddilrlpqgydtevgERGVMLSGGQKQ 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 137 KTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALikRNREAGLTVIIITHNPS 191
Cdd:PRK10789 459 RISIARALLLNAEILILDDALSAVDGRTEHQILHNL--RQWGEGRTVIISAHRLS 511
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
6-214 |
6.72e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.48 E-value: 6.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 6 DKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLL--------APTSGAITYNGLPgdEAVLKKLTYA 77
Cdd:PRK13547 5 DHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEP--LAAIDAPRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 SHTPYL-------FAMSVYDNIA---YPlKIRKYGKAAAAP--IVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALS 145
Cdd:PRK13547 83 RLRAVLpqaaqpaFAFSAREIVLlgrYP-HARRAGALTHRDgeIAWQALALAGATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1172643631 146 ---------FSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSV 214
Cdd:PRK13547 162 qlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-188 |
8.59e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.62 E-value: 8.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 25 LESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGaiTYNGLPGDEAVLKK------LTYashtpylFAMsVYDN------- 91
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLG--DYEEEPSWDEVLKRfrgtelQNY-------FKK-LYNGeikvvhk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 92 IAYPLKIRKYGKAAAAPIVEG---------LLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDp 162
Cdd:PRK13409 166 PQYVDLIPKVFKGKVRELLKKvdergkldeVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD- 244
|
170 180
....*....|....*....|....*....
gi 1172643631 163 qslkI---IEAALIKRNREAGLTVIIITH 188
Cdd:PRK13409 245 ----IrqrLNVARLIRELAEGKYVLVVEH 269
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
12-188 |
3.04e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.52 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 12 YHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDE---AVLKKLTYASH----TPYLf 84
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlcTYQKQLCFVGHrsgiNPYL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 85 amSVYDNIAYPLkirkYGKAAAAPIVEgLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQS 164
Cdd:PRK13540 90 --TLRENCLYDI----HFSPGAVGITE-LCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|....
gi 1172643631 165 LKIIEAAlIKRNREAGLTVIIITH 188
Cdd:PRK13540 163 LLTIITK-IQEHRAKGGAVLLTSH 185
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-190 |
3.92e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.53 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLL--APTSGAIT------YNGLPGDEAVLKKLTYASHTPYLFAMSVYDNIA 93
Cdd:COG2401 50 NLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDvpdnqfGREASLIDAIGRKGDFKDAVELLNAVGLSDAVL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 94 YplkIRKYgkaaaapivegllqefkieeiakqnaKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALI 173
Cdd:COG2401 130 W---LRRF--------------------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
170
....*....|....*..
gi 1172643631 174 KRNREAGLTVIIITHNP 190
Cdd:COG2401 181 KLARRAGITLVVATHHY 197
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
13-208 |
4.69e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 13 HGKTVLSLDSLC----------LESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP-----GDEAVLKKLTYA 77
Cdd:PRK10762 253 PGEVRLKVDNLSgpgvndvsftLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEvvtrsPQDGLANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 S----HTPYLFAMSVYDNI---AYPLKIRKYGK---AAAAPIVEGLLQEFKIEEIAK-QNAKKLSGGESQKTALARALSF 146
Cdd:PRK10762 333 SedrkRDGLVLGMSVKENMsltALRYFSRAGGSlkhADEQQAVSDFIRLFNIKTPSMeQAIGLLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 147 SPDTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEI-YQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
9-212 |
4.82e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.76 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 9 TKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTS--GAITYNGLPGDEAVLKKLTYASHTPYLFA- 85
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRTGFVTQDDILYPh 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 86 MSVYDNIAY------PLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNA--KKLSGGESQKTALARALSFSPDTLLLDEPT 157
Cdd:PLN03211 155 LTVRETLVFcsllrlPKSLTKQEKILVAESVISELGLTKCENTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 158 ANIDPQSLKIIEAALIKRNREaGLTVIIITHNP-SQAYRICDTLSFMDSGRLLFNG 212
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPsSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-188 |
6.03e-15 |
|
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: 73.05 E-value: 6.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNglpgdEAVlkKLTYA--SHT 80
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG-----ETV--KLAYVdqSRD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 81 PYLFAMSVYDNIAYPLKIRKYGKA---AAAPI----VEGLLQEFKIeeiakqnaKKLSGGESQKTALARALSFSPDTLLL 153
Cdd:TIGR03719 396 ALDPNKTVWEEISGGLDIIKLGKReipSRAYVgrfnFKGSDQQKKV--------GQLSGGERNRVHLAKTLKSGGNVLLL 467
|
170 180 190
....*....|....*....|....*....|....*
gi 1172643631 154 DEPTANIDPQSLKIIEAALIKRnreAGlTVIIITH 188
Cdd:TIGR03719 468 DEPTNDLDVETLRALEEALLNF---AG-CAVVISH 498
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
33-216 |
8.05e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 71.69 E-value: 8.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 33 ILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-LPGDEAVLKK-----LTYASHTPYLFAMSVYDNIAY-------PLKIR 99
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdLLTEENVWDIrhkigMVFQNPDNQFVGATVEDDVAFglenkgiPHEEM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 100 KYGKAAAAPIVEglLQEFKIEEIAKqnakkLSGGESQKTALARALSFSPDTLLLDEPTANIDPQS-LKIIEAalIKRNRE 178
Cdd:PRK13650 118 KERVNEALELVG--MQDFKEREPAR-----LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGrLELIKT--IKGIRD 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 1172643631 179 A-GLTVIIITHNpsqayriCDTLSFMDSGRLLFNGSVEA 216
Cdd:PRK13650 189 DyQMTVISITHD-------LDEVALSDRVLVMKNGQVES 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-188 |
1.55e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.37 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 56 SGAITYNGLPGDEAVLKKL----TYASHTPYLFAMSVYDNIAYPLK------IRKYGKAAAapiveglLQEFkIEEIAKQ 125
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDLrnlfSIVSQEPMLFNMSIYENIKFGKEdatredVKRACKFAA-------IDEF-IESLPNK 1347
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 126 N-------AKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITH 188
Cdd:PTZ00265 1348 YdtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-231 |
1.99e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 71.78 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 8 LTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLL--APTSGAITYNGLP------------GDEAVLKK 73
Cdd:TIGR02633 7 IVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPlkasnirdteraGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 74 LTYASHtpylfaMSVYDNIAYPLKIRKYGKAAAAPIV----EGLLQEFKIEEI-AKQNAKKLSGGESQKTALARALSFSP 148
Cdd:TIGR02633 87 LTLVPE------LSVAENIFLGNEITLPGGRMAYNAMylraKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 149 DTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLfngsveAFKASDNPVIQDF 228
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEIL-LDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV------ATKDMSTMSEDDI 233
|
...
gi 1172643631 229 ITL 231
Cdd:TIGR02633 234 ITM 236
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
4-216 |
2.10e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 70.76 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 4 AIDkLTKTYHGK--------TVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG---LPGDEAV 70
Cdd:PRK11308 8 AID-LKKHYPVKrglfkperLVKALDgvSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdlLKADPEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 71 LKKL----------TYASHTPylfAMSVYDNIAYPLKI-----RKYGKAAAAPIVE--GLLQEFkieeiAKQNAKKLSGG 133
Cdd:PRK11308 87 QKLLrqkiqivfqnPYGSLNP---RKKVGQILEEPLLIntslsAAERREKALAMMAkvGLRPEH-----YDRYPHMFSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 134 ESQKTALARALSFSPDTLLLDEPTANID----PQSLKIieaaLIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLL 209
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDvsvqAQVLNL----MMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
....*..
gi 1172643631 210 FNGSVEA 216
Cdd:PRK11308 235 EKGTKEQ 241
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-191 |
2.17e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.67 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 2 QIAIDKLTKTY-HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDE---AVLKK-LTY 76
Cdd:PRK10790 340 RIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlshSVLRQgVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ASHTPYLFAMSVYDNIAYPLKIRKYGKAAA------APIVEGLLQefKIEEIAKQNAKKLSGGESQKTALARALSFSPDT 150
Cdd:PRK10790 420 VQQDPVVLADTFLANVTLGRDISEEQVWQAletvqlAELARSLPD--GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1172643631 151 LLLDEPTANIDPQSLKIIEAAL--IKRNReaglTVIIITHNPS 191
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQALaaVREHT----TLVVIAHRLS 536
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-208 |
5.57e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.44 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLT-KTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPgdeavLKKLTYA------ 77
Cdd:COG3845 260 VENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED-----ITGLSPRerrrlg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 -SHTPY------LFA-MSVYDNIAyplkIRKYGKAAAAPivEGLLQEFKIEEIAKQ--------------NAKKLSGGES 135
Cdd:COG3845 335 vAYIPEdrlgrgLVPdMSVAENLI----LGRYRRPPFSR--GGFLDRKAIRAFAEElieefdvrtpgpdtPARSLSGGNQ 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172643631 136 QKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRnREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-207 |
6.02e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 8 LTKTYHGktVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLaPT---SGAITYNGLP------------GDEAV 70
Cdd:PRK13549 11 ITKTFGG--VKALDnvSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEElqasnirdteraGIAII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 71 LKKLTYASHtpylfaMSVYDNIAYPLKIRKYGKAAAAPIV---EGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFS 147
Cdd:PRK13549 88 HQELALVKE------LSVLENIFLGNEITPGGIMDYDAMYlraQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 148 PDTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGR 207
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVL-LDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-188 |
9.79e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.76 E-value: 9.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 7 KLTKTY-HGKTVLSLDSLCLESG-KIhGILGPNGSGKTTLMKSVAGLLAPtsgaitYNGlpgdEAVLK---KLTYASHTP 81
Cdd:PRK11819 11 RVSKVVpPKKQILKDISLSFFPGaKI-GVLGLNGAGKSTLLRIMAGVDKE------FEG----EARPApgiKVGYLPQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 82 YL-FAMSVYDNIAYPL-----KIRKYGKAAAA---PIVE--------GLLQEfKIE-----------EIA---------K 124
Cdd:PRK11819 80 QLdPEKTVRENVEEGVaevkaALDRFNEIYAAyaePDADfdalaaeqGELQE-IIDaadawdldsqlEIAmdalrcppwD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1172643631 125 QNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIkrnREAGlTVIIITH 188
Cdd:PRK11819 159 AKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLH---DYPG-TVVAVTH 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
32-208 |
1.04e-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: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 32 GILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKLTYASHTPYLFAMSVYDNIayplkiRKYGKAAAA 107
Cdd:cd03369 38 GIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDistiPLEDLRSSLTIIPQDPTLFSGTIRSNL------DPFDEYSDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 108 PIVEGLlqefKIEEiakqNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSlkiiEAALIKRNRE--AGLTVII 185
Cdd:cd03369 112 EIYGAL----RVSE----GGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT----DALIQKTIREefTNSTILT 179
|
170 180
....*....|....*....|....*...
gi 1172643631 186 ITHnpsqayRI-----CDTLSFMDSGRL 208
Cdd:cd03369 180 IAH------RLrtiidYDKILVMDAGEV 201
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-188 |
1.06e-13 |
|
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: 69.46 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPgdeavLKKLTYAS---------HTPYLFAMSVYDNI 92
Cdd:COG5265 378 SFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD-----IRDVTQASlraaigivpQDTVLFNDTIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 93 AYplkirkyGKAAAAPivegllqefkiEEI--AKQNAK---------------------KLSGGESQKTALARALSFSPD 149
Cdd:COG5265 453 AY-------GRPDASE-----------EEVeaAARAAQihdfieslpdgydtrvgerglKLSGGEKQRVAIARTLLKNPP 514
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1172643631 150 TLLLDEPTANIDPQSLKIIEAAL--IKRNReaglTVIIITH 188
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALreVARGR----TTLVIAH 551
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
25-215 |
1.24e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.98 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 25 LESGKIHGILGPNGSGKTTLMKSVAGLLAP---TSGAITYNG-----LPgdEAVLKKL-----------TYASHTPYlfa 85
Cdd:PRK09473 39 LRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGreilnLP--EKELNKLraeqismifqdPMTSLNPY--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 86 MSVYDNIAYPLKIRK-YGKAAAAPIVEGLLQEFKIEEiAKQNAK----KLSGGESQKTALARALSFSPDTLLLDEPTANI 160
Cdd:PRK09473 114 MRVGEQLMEVLMLHKgMSKAEAFEESVRMLDAVKMPE-ARKRMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 161 DPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVE 215
Cdd:PRK09473 193 DVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
25-191 |
1.27e-13 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 69.39 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 25 LESGKIHGILGPNGSGKTTLMKSVAGLLaPTSGAITYNGLPGdeavlkKLTYASHTPYLFAMSVYDNIAYP-----LKIR 99
Cdd:TIGR00954 475 VPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAKG------KLFYVPQRPYMTLGTLRDQIIYPdssedMKRR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 100 KYGKAaaapIVEGLLQEFKIEEIAKQNA---------KKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQslkiIEA 170
Cdd:TIGR00954 548 GLSDK----DLEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD----VEG 619
|
170 180
....*....|....*....|.
gi 1172643631 171 ALIKRNREAGLTVIIITHNPS 191
Cdd:TIGR00954 620 YMYRLCREFGITLFSVSHRKS 640
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-208 |
1.55e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.23 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVL---KKLTYASHTP-YLFamsvyDNIayplk 97
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPedyRKLFSAVFTDfHLF-----DQL----- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 98 IRKYGKAAAAPIVEGLLQEFKIEE-IAKQNAK----KLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAAL 172
Cdd:PRK10522 413 LGPEGKPANPALVEKWLERLKMAHkLELEDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVL 492
|
170 180 190
....*....|....*....|....*....|....*..
gi 1172643631 173 IKRNREAGLTVIIITHNpsQAYRI-CDTLSFMDSGRL 208
Cdd:PRK10522 493 LPLLQEMGKTIFAISHD--DHYFIhADRLLEMRNGQL 527
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-220 |
1.56e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.15 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITY--NGLPGdeavlkklTYASHTPY 82
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWseNANIG--------YYAQDHAY 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 LFA--MSVYDNIAyplKIRKYGKAAAApiVEGLLQE--FKIEEIAKQnAKKLSGGESQKTALARALSFSPDTLLLDEPTA 158
Cdd:PRK15064 394 DFEndLTLFDWMS---QWRQEGDDEQA--VRGTLGRllFSQDDIKKS-VKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTN 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 159 NIDPQSLKIIEAALIKRNreaGlTVIIITHN----PSQAYRIcdtLSFMDSGRLLFNGSVEAFKAS 220
Cdd:PRK15064 468 HMDMESIESLNMALEKYE---G-TLIFVSHDrefvSSLATRI---IEITPDGVVDFSGTYEEYLRS 526
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-207 |
1.79e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.64 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 8 LTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLTYA-----SHTPY 82
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAerrrlLRTEW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 LF-----------AMSVYDNIAYPLK---IRKYGK--AAAApiveGLLQEFKIEEIAKQNA-KKLSGGESQKTALARALS 145
Cdd:PRK11701 92 GFvhqhprdglrmQVSAGGNIGERLMavgARHYGDirATAG----DWLERVEIDAARIDDLpTTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 146 FSPDTLLLDEPTANIDPQslkiIEAALIK--RN--REAGLTVIIITHNPSQAYRICDTLSFMDSGR 207
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVS----VQARLLDllRGlvRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-201 |
2.65e-13 |
|
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: 67.01 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 26 ESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAIT-----------YNG----------LPGDEAVLKKLTYASHTPYLF 84
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGselqnyftklLEGDVKVIVKPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 85 AMSVYDNIAyplKIRKYGKaaaapiVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANID-PQ 163
Cdd:cd03236 104 KGKVGELLK---KKDERGK------LDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDiKQ 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1172643631 164 SLKIieAALIKRNREAGLTVIIITHNPSqayrICDTLS 201
Cdd:cd03236 175 RLNA--ARLIRELAEDDNYVLVVEHDLA----VLDYLS 206
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-217 |
5.43e-13 |
|
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: 67.40 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAP----TSGAITYNG---LPGDEAVLKKL-------------TyaSHTP 81
Cdd:COG4172 30 SFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGqdlLGLSERELRRIrgnriamifqepmT--SLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 82 YlfaMSVYDNIAYPLKI-RKYGKAAAAPIVEGLLQEFKIEEIAK-------QnakkLSGGESQKTALARALSFSPDTLLL 153
Cdd:COG4172 108 L---HTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERrldayphQ----LSGGQRQRVMIAMALANEPDLLIA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172643631 154 DEPTANIDP--QSlKIIEaaLIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAF 217
Cdd:COG4172 181 DEPTTALDVtvQA-QILD--LLKDlQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
35-188 |
5.96e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.64 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 35 GPNGSGKTTLMKSVAGLLAPTSGAITYNGLP---GDEAvlKKLTYASHTPYLFA-MSVYDNIAYPLKIRKYgKAAAAPiv 110
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTatrGDRS--RFMAYLGHLPGLKAdLSTLENLHFLCGLHGR-RAKQMP-- 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 111 EGLLQEFKIEEIAKQNAKKLSGGESQKTALARaLSFSPDTL-LLDEPTANIDPQSLKIIEAALIKRNREAGLTvIIITH 188
Cdd:PRK13543 119 GSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDLEGITLVNRMISAHLRGGGAA-LVTTH 195
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-216 |
6.49e-13 |
|
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: 67.40 E-value: 6.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLaPTSGAITYNGLP---GDEAVLKKLT----------YASHTPylfAMSV 88
Cdd:COG4172 306 SLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDldgLSRRALRPLRrrmqvvfqdpFGSLSP---RMTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 89 YDNIAYPLKIRKYGKAAAAP--IVEGLLQ--------------EFkieeiakqnakklSGGESQKTALARALSFSPDTLL 152
Cdd:COG4172 382 GQIIAEGLRVHGPGLSAAERraRVAEALEevgldpaarhryphEF-------------SGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 153 LDEPTANID----PQslkIIEaaLIKR-NREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEA 216
Cdd:COG4172 449 LDEPTSALDvsvqAQ---ILD--LLRDlQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQ 512
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-174 |
9.11e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 67.24 E-value: 9.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 13 HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgdeavlkKLTYASHTPYLFAMSVYDNI 92
Cdd:TIGR01271 437 YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG---------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 93 AYPLKIR--KYGKAAAAPIVEGLLQEF--KIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLK-I 167
Cdd:TIGR01271 508 IFGLSYDeyRYTSVIKACQLEEDIALFpeKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKeI 587
|
....*..
gi 1172643631 168 IEAALIK 174
Cdd:TIGR01271 588 FESCLCK 594
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
14-221 |
1.13e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.05 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 14 GKTVLSLDsLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----------LPGDEavlKKLTYASHTPY 82
Cdd:PRK11144 11 GDLCLTVN-LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaekgicLPPEK---RRIGYVFQDAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 LFA-MSVYDNIAYPLKirKYGKAAAAPIVEgLLqefKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANID 161
Cdd:PRK11144 87 LFPhYKVRGNLRYGMA--KSMVAQFDKIVA-LL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 162 -PQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKASD 221
Cdd:PRK11144 161 lPRKRELL-PYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
33-191 |
1.21e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 64.12 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 33 ILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLTYASHTPYL-FAMSVYDNIAYPLKIRKygkaaAAPIVE 111
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLkLEMTVFENLKFWSEIYN-----SAETLY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 112 GLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLtVIIITHNPS 191
Cdd:PRK13541 106 AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGI-VLLSSHLES 184
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-207 |
2.18e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNglpgDEAVLK---------KLTYASHTPYLFAMSVYDNI 92
Cdd:PTZ00265 405 NFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN----DSHNLKdinlkwwrsKIGVVSQDPLLFSNSIKNNI 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 93 AYPL---------------------------------------------------KIRK-YGKAAAAPIV----EGLLQE 116
Cdd:PTZ00265 481 KYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliEMRKnYQTIKDSEVVdvskKVLIHD 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 117 F------KIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNP 190
Cdd:PTZ00265 561 FvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
250
....*....|....*..
gi 1172643631 191 SqAYRICDTLsFMDSGR 207
Cdd:PTZ00265 641 S-TIRYANTI-FVLSNR 655
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-209 |
2.27e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.65 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLTKTYHGKTVLSLDslcLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLT--------- 75
Cdd:PRK10261 330 LNRVTREVHAVEKVSFD---LWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQalrrdiqfi 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 76 ----YASHTPYLfamSVYDNIAYPLKIRKY--GKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPD 149
Cdd:PRK10261 407 fqdpYASLDPRQ---TVGDSIMEPLRVHGLlpGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 150 TLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLL 209
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
6-208 |
2.66e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 64.45 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 6 DKLTKTYHGKTVLSLDSLCLES--GKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgDEAVLkkltyASHTPYL 83
Cdd:PRK13546 26 DALIPKHKNKTFFALDDISLKAyeGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---EVSVI-----AISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 84 FAMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDpQ 163
Cdd:PRK13546 98 GQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD-Q 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1172643631 164 SLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:PRK13546 177 TFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-229 |
3.54e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.20 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 9 TKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLaPT---SGAITYNglpGDEAVLKKLTYASH------ 79
Cdd:NF040905 8 TKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFD---GEVCRFKDIRDSEAlgivii 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 ------TPYLfamSVYDNIAYPLKIRKYG---------KAAAapivegLLQEFKIEEIAKQNAKKLSGGESQKTALARAL 144
Cdd:NF040905 84 hqelalIPYL---SIAENIFLGNERAKRGvidwnetnrRARE------LLAKVGLDESPDTLVTDIGVGKQQLVEIAKAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 145 SFSPDTLLLDEPTANI-DPQSLKIIEaaLIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRllfngSVEAFKASDNP 223
Cdd:NF040905 155 SKDVKLLILDEPTAALnEEDSAALLD--LLLELKAQGITSIIISHKLNEIRRVADSITVLRDGR-----TIETLDCRADE 227
|
....*.
gi 1172643631 224 VIQDFI 229
Cdd:NF040905 228 VTEDRI 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-207 |
4.33e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.73 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTY----HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLL-AP----TSGAITYNG---LPGDEAV 70
Cdd:PRK15134 6 LAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpSPpvvyPSGDIRFHGeslLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 71 LKKL-----------TYASHTP-YLFAMSVYDNIAYPLKIRKygKAAAAPIVEGLlqefkiEEIAKQNAKK--------L 130
Cdd:PRK15134 86 LRGVrgnkiamifqePMVSLNPlHTLEKQLYEVLSLHRGMRR--EAARGEILNCL------DRVGIRQAAKrltdyphqL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172643631 131 SGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGR 207
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-224 |
5.53e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.57 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG--LPGDEA--VLKKLTYASHTP--YLFAMSVYDNIAYP 95
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelLTAENVwnLRRKIGMVFQNPdnQFVGATVEDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 96 LKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKR 175
Cdd:PRK13642 107 MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEI 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1172643631 176 NREAGLTVIIITHNPSQAYRiCDTLSFMDSGRLLFNGS-VEAFKASDNPV 224
Cdd:PRK13642 187 KEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAApSELFATSEDMV 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-207 |
6.78e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 8 LTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGD-----EAVLKKLTYASHTPY 82
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksskEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 83 LFAM-SVYDNI---AYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTA 158
Cdd:PRK10982 84 LVLQrSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1172643631 159 NIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGR 207
Cdd:PRK10982 164 SLTEKEVNHL-FTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-212 |
7.45e-12 |
|
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: 62.28 E-value: 7.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 10 KTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPT---SGAITYNGLPGDEAVLK---KLTYAS----H 79
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKypgEIIYVSeedvH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 80 TPYLfamsvydniayplkirkygkaaaapIVEGLLqEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTAN 159
Cdd:cd03233 95 FPTL-------------------------TVRETL-DFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 160 IDPQS-LKIIEaALIKRNREAGLTVIIITHNPSQ-AYRICDTLSFMDSGRLLFNG 212
Cdd:cd03233 149 LDSSTaLEILK-CIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-188 |
9.45e-12 |
|
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: 62.35 E-value: 9.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 14 GKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKK--------LTYASHTPYLFA 85
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtrsrnrysVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 86 MSVYDNIAY--PLKIRKYGKAAAA----PIVEgLLQEFKIEEIAKQNAKkLSGGESQKTALARALSFSPDTLLLDEPTAN 159
Cdd:cd03290 93 ATVEENITFgsPFNKQRYKAVTDAcslqPDID-LLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190
....*....|....*....|....*....|
gi 1172643631 160 IDPQ-SLKIIEAALIKRNREAGLTVIIITH 188
Cdd:cd03290 171 LDIHlSDHLMQEGILKFLQDDKRTLVLVTH 200
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-188 |
1.63e-11 |
|
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: 62.18 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 2 QIAIDKLTKTY--HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLApTSGAITYNGLPGDEAVLKKLTYA-- 77
Cdd:cd03289 2 QMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAfg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 --SHTPYLFAMSVYDNiayplkIRKYGKAAAAPIVEgLLQEFKIEEIAKQNAKK-----------LSGGESQKTALARAL 144
Cdd:cd03289 81 viPQKVFIFSGTFRKN------LDPYGKWSDEEIWK-VAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1172643631 145 SFSPDTLLLDEPTANIDPQSLKIIEAALikRNREAGLTVIIITH 188
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTL--KQAFADCTVILSEH 195
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-226 |
1.99e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 61.64 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 2 QIAIDKLTKTYHGKTVLSLdSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAP----TSGAITYNGLPGDEAVLKKLTYA 77
Cdd:PRK10418 4 QIELRNIALQAAQPLVHGV-SLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 S--HTPylfaMSVYDniayPLK---------IRKYGKAAAAPIVEGLLQEFKIEE---IAKQNAKKLSGGESQKTALARA 143
Cdd:PRK10418 83 TimQNP----RSAFN----PLHtmhtharetCLALGKPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 144 LSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEA-FKASDN 222
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETlFNAPKH 234
|
....
gi 1172643631 223 PVIQ 226
Cdd:PRK10418 235 AVTR 238
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-203 |
2.15e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.42 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG--LPGDEAVLKKLT-----------YASHTPylfAMSV 88
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdLLGMKDDEWRAVrsdiqmifqdpLASLNP---RMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 89 YDNIAYPLKIRkYGKAAAAPIVE---------GLLqefkiEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTAN 159
Cdd:PRK15079 118 GEIIAEPLRTY-HPKLSRQEVKDrvkammlkvGLL-----PNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1172643631 160 IDPQslkiIEAALI----KRNREAGLTVIIITHNPSQAYRICDTLSFM 203
Cdd:PRK15079 192 LDVS----IQAQVVnllqQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
23-215 |
2.92e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.20 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 23 LCLESGKIHGILGPNGSGKTTLMKSVAGLLA--PTSGAITYNG-----LPGDEAVLKKLTYASHTPylFAMSVYDN---- 91
Cdd:CHL00131 28 LSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGesildLEPEERAHLGIFLAFQYP--IEIPGVSNadfl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 92 -IAYPLKIRKYGKAAAAPIvegllqEF-----KIEEIAKQNAKKL--------SGGESQKTALARALSFSPDTLLLDEPT 157
Cdd:CHL00131 106 rLAYNSKRKFQGLPELDPL------EFleiinEKLKLVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELAILDETD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 158 ANIDPQSLKIIeAALIKRNREAGLTVIIITHNPS-QAYRICDTLSFMDSGRLLFNGSVE 215
Cdd:CHL00131 180 SGLDIDALKII-AEGINKLMTSENSIILITHYQRlLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-188 |
3.69e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.24 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 2 QIAIDKLTKTY--HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLApTSGAITYNGLPGDEAVLKKLTYA-- 77
Cdd:TIGR01271 1217 QMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAfg 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 --SHTPYLFAMSVYDNIAyPLKI---RKYGKAAAAPIVEGLLQEF--KIEEIAKQNAKKLSGGESQKTALARALSFSPDT 150
Cdd:TIGR01271 1296 viPQKVFIFSGTFRKNLD-PYEQwsdEEIWKVAEEVGLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKI 1374
|
170 180 190
....*....|....*....|....*....|....*...
gi 1172643631 151 LLLDEPTANIDPQSLKIIEAALikRNREAGLTVIIITH 188
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQIIRKTL--KQSFSNCTVILSEH 1410
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-206 |
3.78e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 1 MQ--IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGD--------EA- 69
Cdd:PRK10762 1 MQalLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqEAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 70 ---------VLKKLTYASHtpyLFAMSVYDNIAYPLKIRK-YGKAAAapivegLLQEFKIEEIAKQNAKKLSGGESQKTA 139
Cdd:PRK10762 81 igiihqelnLIPQLTIAEN---IFLGREFVNRFGRIDWKKmYAEADK------LLARLNLRFSSDKLVGELSIGEQQMVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 140 LARALSFSPDTLLLDEPT---ANIDPQSLkiieAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSG 206
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTdalTDTETESL----FRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-186 |
3.93e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.95 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 18 LSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGaitynglpgdeavlkKLTYASHTPYLFAMSVYDNIAYPLK 97
Cdd:PRK10938 19 LQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG---------------ERQSQFSHITRLSFEQLQKLVSDEW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 98 IRK-----------YGKAAAAPIVEG---------LLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPT 157
Cdd:PRK10938 84 QRNntdmlspgeddTGRTTAEIIQDEvkdparceqLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180
....*....|....*....|....*....
gi 1172643631 158 ANIDPQSLKIIeAALIKRNREAGLTVIII 186
Cdd:PRK10938 164 DGLDVASRQQL-AELLASLHQSGITLVLV 191
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
13-218 |
5.46e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 61.29 E-value: 5.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 13 HGKTVLSLDSLCLE--SGKIHGILGPNGSG--KTTLMKSVAGllaPTSG--AITYNGLPGDEAVLKKlTYASHTPYLF-- 84
Cdd:NF000106 22 HFGEVKAVDGVDLDvrEGTVLGVLGP*GAA**RGALPAHV*G---PDAGrrPWRF*TWCANRRALRR-TIG*HRPVR*gr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 85 --AMSVYDNIAYPLKIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDP 162
Cdd:NF000106 98 reSFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 163 QSLKIIEAALIKRNREaGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFK 218
Cdd:NF000106 178 RTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-213 |
5.59e-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: 60.64 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 13 HGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgdeavlkKLTYASHTPYLFAMSVYDNI 92
Cdd:cd03291 48 VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG---------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 93 AYPLKIRKYGKAAaapIVEGLLQEFKIEEIAKQNAK-------KLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSL 165
Cdd:cd03291 119 IFGVSYDEYRYKS---VVKACQLEEDITKFPEKDNTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1172643631 166 K-IIEAALIKrnREAGLTVIIIThNPSQAYRICDTLSFMDSGRLLFNGS 213
Cdd:cd03291 196 KeIFESCVCK--LMANKTRILVT-SKMEHLKKADKILILHEGSSYFYGT 241
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-206 |
6.00e-11 |
|
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: 59.56 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 25 LESGKIHGILGPNGSGKTTLMKSVAG--LLAPTSGAITYNGLPGDEAVLKKLTYASHTPYLFAMS-VYDNIAYPLKIRky 101
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQRSTGYVEQQDVHSPNLtVREALRFSALLR-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 102 gkaaaapiveGLLQEFKieeiakqnaKKLSggesqktaLARALSFSPDTLLLDEPTANIDPQS-LKIIEaaLIKRNREAG 180
Cdd:cd03232 108 ----------GLSVEQR---------KRLT--------IGVELAAKPSILFLDEPTSGLDSQAaYNIVR--FLKKLADSG 158
|
170 180
....*....|....*....|....*..
gi 1172643631 181 LTVIIITHNPSQA-YRICDTLSFMDSG 206
Cdd:cd03232 159 QAILCTIHQPSASiFEKFDRLLLLKRG 185
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-188 |
7.37e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.29 E-value: 7.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNglpgdEAVlkKLTY------ 76
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG-----ETV--KLAYvdqsrd 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ---ASHTpylfamsVYDNIAYPLKIRKYGKaaaapivegllQE-----------FKIEEIAKQnAKKLSGGESQKTALAR 142
Cdd:PRK11819 398 aldPNKT-------VWEEISGGLDIIKVGN-----------REipsrayvgrfnFKGGDQQKK-VGVLSGGERNRLHLAK 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1172643631 143 ALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRnreAGlTVIIITH 188
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDVETLRALEEALLEF---PG-CAVVISH 500
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
5-190 |
1.06e-10 |
|
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: 59.16 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLT----KTYHGKTVLSLDSLclesgkIHGILGPNGSGKTTLMKSVA----GLLAPTSgaityNGLPGDEAVLKK--- 73
Cdd:cd03240 1 IDKLSirniRSFHERSEIEFFSP------LTLIVGQNGAGKTTIIEALKyaltGELPPNS-----KGGAHDPKLIREgev 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 74 -------LTYASHTPYLF--AMSVYDNIAYplkIRKygkaaaapivegllqefkiEEIAK---QNAKKLSGGE------S 135
Cdd:cd03240 70 raqvklaFENANGKKYTItrSLAILENVIF---CHQ-------------------GESNWpllDMRGRCSGGEkvlaslI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 136 QKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIK-RNREAGLTVIIITHNP 190
Cdd:cd03240 128 IRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEeRKSQKNFQLIVITHDE 183
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-230 |
1.38e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 4 AIDKLTKTYHGKTVLSLDSL--CLESGKIHGILGPNGSGKTTLMKSVA----GLLAPTSGAITYNGLPGDEAVLKK---L 74
Cdd:TIGR00956 61 GFRKLKKFRDTKTFDILKPMdgLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYrgdV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 75 TYAS----HTPYLfamSVYDNIAYPLKIRKYGKAaaapiVEGLLQEFKIEEIAK-----------QNAK-------KLSG 132
Cdd:TIGR00956 141 VYNAetdvHFPHL---TVGETLDFAARCKTPQNR-----PDGVSREEYAKHIADvymatyglshtRNTKvgndfvrGVSG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 133 GESQKTALARALSFSPDTLLLDEPTANIDPQS-LKIIEaALIKRNREAGLTVIIITHNPSQ-AYRICDTLSFMDSGRLLF 210
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDSATaLEFIR-ALKTSANILDTTPLVAIYQCSQdAYELFDKVIVLYEGYQIY 291
|
250 260
....*....|....*....|....*....
gi 1172643631 211 NGSVE---------AFKASDNPVIQDFIT 230
Cdd:TIGR00956 292 FGPADkakqyfekmGFKCPDRQTTADFLT 320
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-191 |
2.07e-10 |
|
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: 57.38 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 32 GILGPNGSGKTTLMKSVAGLLAPTSGAItynglpgdeavlkkltyashtpylfamsvydniayplkirkygKAAAAPIVE 111
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGV-------------------------------------------IYIDGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 112 GLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKII-----EAALIKRNREAGLTVIII 186
Cdd:smart00382 43 EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRLLLLLKSEKNLTVILT 122
|
....*
gi 1172643631 187 THNPS 191
Cdd:smart00382 123 TNDEK 127
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
13-208 |
2.65e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 13 HGKTVLSLD----------SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNG-----LPGDEAVLKKLTY- 76
Cdd:PRK15439 264 AGAPVLTVEdltgegfrniSLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGkeinaLSTAQRLARGLVYl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 ----ASHTPYLFAmSVYDNIA------YPLKIRKygkAAAAPIVEGLLQEFKIE-EIAKQNAKKLSGGESQKTALARALS 145
Cdd:PRK15439 344 pedrQSSGLYLDA-PLAWNVCalthnrRGFWIKP---ARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLE 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172643631 146 FSPDTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:PRK15439 420 ASPQLLIVDEPTRGVDVSARNDI-YQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-208 |
2.68e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGL------PGDeAVLKKLTYASH----TPYLFAMSVYDN 91
Cdd:PRK09700 283 SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprsPLD-AVKKGMAYITEsrrdNGFFPNFSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 92 IAYP--LKIRKYGKAAaapiveGLLQEFKIEEIAK--------------QNAKKLSGGESQKTALARALSFSPDTLLLDE 155
Cdd:PRK09700 362 MAISrsLKDGGYKGAM------GLFHEVDEQRTAEnqrellalkchsvnQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1172643631 156 PTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:PRK09700 436 PTRGIDVGAKAEI-YKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-231 |
3.04e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.33 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 15 KTVLSLDSLCLESGKIHGILGPNGSGKTTlmksvAGL----LAPTSGAITYNGLPGDEAVLKKL-------------TYA 77
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKST-----TGLallrLINSQGEIWFDGQPLHNLNRRQLlpvrhriqvvfqdPNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 SHTPYLfamSVYDNIAYPLKIRKYGKAAAA--PIVEGLLQEFKIEEIAKQN-AKKLSGGESQKTALARALSFSPDTLLLD 154
Cdd:PRK15134 374 SLNPRL---NVLQIIEEGLRVHQPTLSAAQreQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1172643631 155 EPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEA-FKASDNPVIQDFITL 231
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERvFAAPQQEYTRQLLAL 528
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-208 |
4.62e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 33 ILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgdEAVLKKLTyaSHTPYLFAMSVYDNIAYPLK--------------- 97
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ----DLIVARLQ--QDPPRNVEGTVYDFVAEGIEeqaeylkryhdishl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 98 ---------IRKYGKAAAAPIVEGLLQ-EFKIEEIAKQ---NAKK----LSGGESQKTALARALSFSPDTLLLDEPTANI 160
Cdd:PRK11147 108 vetdpseknLNELAKLQEQLDHHNLWQlENRINEVLAQlglDPDAalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 161 DPQSLKIIEAALikrnREAGLTVIIITHNPS----QAYRICDtlsfMDSGRL 208
Cdd:PRK11147 188 DIETIEWLEGFL----KTFQGSIIFISHDRSfirnMATRIVD----LDRGKL 231
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
8-220 |
4.98e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.88 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 8 LTKTY----------HGKTVLSLdSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP---GDEA----- 69
Cdd:PRK15112 10 LSKTFryrtgwfrrqTVEAVKPL-SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlhfGDYSyrsqr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 70 --VLKKLTYASHTPYLFAMSVYDniaYPLKIRK--YGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALS 145
Cdd:PRK15112 89 irMIFQDPSTSLNPRQRISQILD---FPLRLNTdlEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 146 FSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEAFKAS 220
Cdd:PRK15112 166 LRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
33-190 |
9.77e-10 |
|
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: 55.44 E-value: 9.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 33 ILGPNGSGKTTLMKSVAgllaptsgaitynglpgdeavlkkltyashtpYLFAM-SVYDNIAYPLKIRKYGKAAAAPIVE 111
Cdd:cd03227 26 ITGPNGSGKSTILDAIG--------------------------------LALGGaQSATRRRSGVKAGCIVAAVSAELIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 112 GLLQefkieeiakqnakkLSGGESQKTALARAL---SFSPDTL-LLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIIT 187
Cdd:cd03227 74 TRLQ--------------LSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDGQAL-AEAILEHLVKGAQVIVIT 138
|
...
gi 1172643631 188 HNP 190
Cdd:cd03227 139 HLP 141
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
7-189 |
1.14e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 55.66 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 7 KLTKTYhGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLpgdeavlkkltyashtpylfam 86
Cdd:cd03222 5 DCVKRY-GVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI---------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 87 svydNIAY-PLKIrkygkaaaapivegllqefkieeiakqnakKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSl 165
Cdd:cd03222 62 ----TPVYkPQYI------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQ- 106
|
170 180
....*....|....*....|....*
gi 1172643631 166 KIIEAALIKR-NREAGLTVIIITHN 189
Cdd:cd03222 107 RLNAARAIRRlSEEGKKTALVVEHD 131
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
12-196 |
1.67e-09 |
|
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: 55.74 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 12 YHGKTVLSLDSLclESGKIHGILGPNGSGKTTLMKSVA-GLLAPTSGAITYNGLPGDEAVLKKLTYASHTpylFAMSvyd 90
Cdd:cd03279 14 FREEQVIDFTGL--DNNGLFLICGPTGAGKSTILDAITyALYGKTPRYGRQENLRSVFAPGEDTAEVSFT---FQLG--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 91 NIAYPLkIRKYGKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSP----------DTLLLDEPTANI 160
Cdd:cd03279 86 GKKYRV-ERSRGLDYDQFTRIVLLPQGEFDRFLARPVSTLSGGETFLASLSLALALSEvlqnrggarlEALFIDEGFGTL 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 1172643631 161 DPQSLKIIEAALIKRNREaGLTVIIITHNPSQAYRI 196
Cdd:cd03279 165 DPEALEAVATALELIRTE-NRMVGVISHVEELKERI 199
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-208 |
1.93e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 57.12 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLkkLTYASHT------PYLFAmsvydniayp 95
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNR--EAYRQLFsavfsdFHLFD---------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 96 lkiRKYG--KAAAAPIVEGLLQEFKIEEIAK-QNAK----KLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKII 168
Cdd:COG4615 420 ---RLLGldGEADPARARELLERLELDHKVSvEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVF 496
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1172643631 169 EAALIKRNREAGLTVIIITHNpSQAYRICDTLSFMDSGRL 208
Cdd:COG4615 497 YTELLPELKARGKTVIAISHD-DRYFDLADRVLKMDYGKL 535
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-188 |
2.16e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.79 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVA--------------------------GLLAPTS 56
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqilhveqevvgddttALQCVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 57 GAITYNGLPGDEAVLKKLTYASHTPYLFAMSVYDNIAYPLK----------------IRKY-GKAAAAPIVEGLlqEFKi 119
Cdd:PLN03073 258 TDIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKdavsqrleeiykrlelIDAYtAEARAASILAGL--SFT- 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 120 EEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNReaglTVIIITH 188
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSH 399
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-218 |
2.47e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAItynGLpgdeAVLKKLTY-ASHT- 80
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---GL----AKGIKLGYfAQHQl 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 81 PYLFA-------MSVYDNIAYPLKIRKYgkaaaapiVEGL-LQEFKIEEIAKQnakkLSGGESQKTALARALSFSPDTLL 152
Cdd:PRK10636 386 EFLRAdesplqhLARLAPQELEQKLRDY--------LGGFgFQGDKVTEETRR----FSGGEKARLVLALIVWQRPNLLL 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172643631 153 LDEPTANIDPQSLKIIEAALIkrNREAGLTViiITHNPSQAYRICDTLSFMDSGRL-LFNGSVEAFK 218
Cdd:PRK10636 454 LDEPTNHLDLDMRQALTEALI--DFEGALVV--VSHDRHLLRSTTDDLYLVHDGKVePFDGDLEDYQ 516
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-188 |
2.57e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.57 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 3 IAIDKLTKTYHGKTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGL--LAPTSGAITYNGL------PGD---EAVL 71
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKdllelsPEDragEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 72 KKLTYASHTPYL---FAMSVYDNiayplKIRKYgkAAAAPIVEGLLQEFKIEEIAKQNAKK----------LSGGESQKT 138
Cdd:PRK09580 82 MAFQYPVEIPGVsnqFFLQTALN-----AVRSY--RGQEPLDRFDFQDLMEEKIALLKMPEdlltrsvnvgFSGGEKKRN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1172643631 139 ALARALSFSPDTLLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITH 188
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKIV-ADGVNSLRDGKRSFIIVTH 203
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
35-188 |
3.18e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 35 GPNGSGKTTLMKSVAGLLAPTSGAITynglpgdeaVLKKLTYASHTPYLFAM----SVYDNIAyplkirkYGKAAaapiV 110
Cdd:PRK11147 352 GPNGCGKTTLLKLMLGQLQADSGRIH---------CGTKLEVAYFDQHRAELdpekTVMDNLA-------EGKQE----V 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 111 E---------GLLQEFKIEEI-AKQNAKKLSGGESQKTALARaLSFSPDTLL-LDEPTANIDPQSLKIIEAALikrnreA 179
Cdd:PRK11147 412 MvngrprhvlGYLQDFLFHPKrAMTPVKALSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLDVETLELLEELL------D 484
|
170
....*....|.
gi 1172643631 180 GL--TVIIITH 188
Cdd:PRK11147 485 SYqgTVLLVSH 495
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-226 |
3.26e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGL------------------------PGDEAVLKKLTYA 77
Cdd:PRK10261 36 SFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqvielseqsaaqmrhvrGADMAMIFQEPMT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 78 SHTPylfAMSVYDNIAYPLKIRK-YGKAAAAPIVEGLLQEFKI---EEIAKQNAKKLSGGESQKTALARALSFSPDTLLL 153
Cdd:PRK10261 116 SLNP---VFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1172643631 154 DEPTANID----PQSLKIIEAAlikrNREAGLTVIIITHNPSQAYRICDTLSFMDSGRLLFNGSVEA-FKASDNPVIQ 226
Cdd:PRK10261 193 DEPTTALDvtiqAQILQLIKVL----QKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQiFHAPQHPYTR 266
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-188 |
4.35e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 15 KTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITynglpgdeAVLKKLTYASHTPYLFAMSVYDNIAY 94
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSV--------VIRGSVAYVPQVSWIFNATVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 95 PLKIR--KYGKAAAAPIVEGLLQEF---KIEEIAKQNAKkLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIE 169
Cdd:PLN03232 702 GSDFEseRYWRAIDVTALQHDLDLLpgrDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
170
....*....|....*....
gi 1172643631 170 AALIKRNREaGLTVIIITH 188
Cdd:PLN03232 781 DSCMKDELK-GKTRVLVTN 798
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-208 |
9.28e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGL------PGD--EA--VL-----KKLTyashtpyLFAM 86
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpidirsPRDaiRAgiMLcpedrKAEG-------IIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 87 -SVYDNIAYPLKiRKYGKAaaapiveGLLQEFKIEE------IAKQNAK---------KLSGGESQKTALARALSFSPDT 150
Cdd:PRK11288 346 hSVADNINISAR-RHHLRA-------GCLINNRWEAenadrfIRSLNIKtpsreqlimNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1172643631 151 LLLDEPTANIDPQSLKIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEI-YNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
28-208 |
1.25e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 28 GKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNglPGDE-AVLKKLTYA------------SHTPYLFAMSVYDNIaY 94
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD--PNERlGKLRQDQFAfeeftvldtvimGHTELWEVKQERDRI-Y 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 95 PL----------------KIRKY-GKAAAAPIVEGLL-------QEF-KIEEIAKqnAKKLsggesqKTALARALsFS-P 148
Cdd:PRK15064 104 ALpemseedgmkvadlevKFAEMdGYTAEARAGELLLgvgipeeQHYgLMSEVAP--GWKL------RVLLAQAL-FSnP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 149 DTLLLDEPTANIDPQSLKIIEAALIKRNReaglTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:PRK15064 175 DILLLDEPTNNLDINTIRWLEDVLNERNS----TMIIISHDRHFLNSVCTHMADLDYGEL 230
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
125-212 |
1.93e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.33 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 125 QNAKKLSGGESQKTALARAL--SFSPDTLLLDEPTANIDPQSL-KIIEAalIKRNREAGLTVIIITHNPSqAYRICDTLS 201
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELfsEPPGTLFILDEPSTGLHQQDInQLLEV--IKGLIDLGNTVILIEHNLD-VLSSADWII 159
|
90
....*....|....*..
gi 1172643631 202 FM------DSGRLLFNG 212
Cdd:cd03238 160 DFgpgsgkSGGKVVFSG 176
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-161 |
2.02e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 15 KTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAitynglpgdEAVLK-KLTYASHTPYLFAMSVYDNIA 93
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA---------SVVIRgTVAYVPQVSWIFNATVRDNIL 700
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 94 Y--PLKIRKYGKAAAapiVEGLLQEFKI------EEIAKQNAKkLSGGESQKTALARALSFSPDTLLLDEPTANID 161
Cdd:PLN03130 701 FgsPFDPERYERAID---VTALQHDLDLlpggdlTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-218 |
2.80e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 33 ILGPNGSGKTTLMKSVAGLLAPTSGAITYNglpgdeAVLKKLTYASH---------TPYLFAMSVYDNIAyPLKIRKYgk 103
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVFRS------AKVRMAVFSQHhvdgldlssNPLLYMMRCFPGVP-EQKLRAH-- 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 104 aaaapiveglLQEFKIE-EIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDpqsLKIIEaALIKrnreaGLT 182
Cdd:PLN03073 611 ----------LGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD---LDAVE-ALIQ-----GLV 671
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1172643631 183 -----VIIITHNPSQAYRICDTLSFMDSGRLL-FNGSVEAFK 218
Cdd:PLN03073 672 lfqggVLMVSHDEHLISGSVDELWVVSEGKVTpFHGTFHDYK 713
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-221 |
4.80e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.03 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 28 GKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGlpgdeavlkKLTYASHTPYLFAMSVYDNIAY--PLKIRKYGKAA 105
Cdd:TIGR00957 664 GALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG---------SVAYVPQQAWIQNDSLRENILFgkALNEKYYQQVL 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 106 AAPiveGLLQEFKI------EEIAKQNAKkLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLK-IIEAALIKRNRE 178
Cdd:TIGR00957 735 EAC---ALLPDLEIlpsgdrTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKhIFEHVIGPEGVL 810
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1172643631 179 AGLTVIIITHNPSQAYRIcDTLSFMDSGRLLFNGSVEAFKASD 221
Cdd:TIGR00957 811 KNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRD 852
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-222 |
1.06e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.14 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 130 LSGGESQKTALARAL--SFSPDTLLLDEPTANIDPQ-SLKIIEaaLIKRNREAGLTVIIITHNP---SQAYRICDT--LS 201
Cdd:PRK00635 477 LSGGEQERTALAKHLgaELIGITYILDEPSIGLHPQdTHKLIN--VIKKLRDQGNTVLLVEHDEqmiSLADRIIDIgpGA 554
|
90 100
....*....|....*....|.
gi 1172643631 202 FMDSGRLLFNGSVEAFKASDN 222
Cdd:PRK00635 555 GIFGGEVLFNGSPREFLAKSD 575
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-226 |
2.90e-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: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 17 VLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKLTYASHTPYLFAMSVYDNI 92
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNiakiGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 93 ayplkiRKYGKAAAAPIVEGL----LQEF------KIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDP 162
Cdd:TIGR00957 1381 ------DPFSQYSDEEVWWALelahLKTFvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172643631 163 QSLKIIEAALikRNREAGLTVIIITHNPSqayricdtlSFMDSGRLLF--NGSVEAFKASDNPVIQ 226
Cdd:TIGR00957 1455 ETDNLIQSTI--RTQFEDCTVLTIAHRLN---------TIMDYTRVIVldKGEVAEFGAPSNLLQQ 1509
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
10-192 |
3.37e-07 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 48.84 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 10 KTYHGKTVLSLdslcleSGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAItyngLPGDEAVLKKLTYASHTPYLFAMSVY 89
Cdd:cd03239 10 KSYRDETVVGG------SNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKL----RRGSLLFLAGGGVKAGINSASVEITF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 90 DNIAYPLkirkygkaaaapiveglLQEfKIEEIakqnakkLSGGESQKTALARALS---FSPDTL-LLDEPTANIDPQSL 165
Cdd:cd03239 80 DKSYFLV-----------------LQG-KVEQI-------LSGGEKSLSALALIFAlqeIKPSPFyVLDEIDAALDPTNR 134
|
170 180
....*....|....*....|....*..
gi 1172643631 166 KIIeAALIKRNREAGLTVIIITHNPSQ 192
Cdd:cd03239 135 RRV-SDMIKEMAKHTSQFIVITLKKEM 160
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-220 |
6.15e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.78 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNglpgdeavlKKLTYASHTPYLFAMSVYDNIAY--PLKIR 99
Cdd:PTZ00243 680 SVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE---------RSIAYVPQQAWIMNATVRGNILFfdEEDAA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 100 KYGKAAAAPIVEGLLQEFK--IE-EIAKQNAKkLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIkRN 176
Cdd:PTZ00243 751 RLADAVRVSQLEADLAQLGggLEtEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF-LG 828
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1172643631 177 REAGLTVIIITHNPSQAYRiCDTLSFMDSGRLLFNGSVEAFKAS 220
Cdd:PTZ00243 829 ALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRT 871
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
125-189 |
7.10e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 48.76 E-value: 7.10e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 125 QNAKKLSGGESQKTALARALSF--SPDTL-LLDEPTANIDPQSL-KIIEAalIKRNREAGLTVIIITHN 189
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKELSKrsTGKTLyILDEPTTGLHFHDVkKLLEV--LQRLVDKGNTVVVIEHN 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-208 |
1.03e-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: 48.67 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLL-APTSGAITYNGLPGD-----EAVLKKLTYA----SHTPYLFAMSVYDN 91
Cdd:TIGR02633 280 SFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPVDirnpaQAIRAGIAMVpedrKRHGIVPILGVGKN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 92 IAYPL-----KIRKYGKAAAAPIVEGLLQEFKIEEIAKQNA-KKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSL 165
Cdd:TIGR02633 360 ITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAK 439
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1172643631 166 KIIeAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:TIGR02633 440 YEI-YKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-221 |
1.37e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 32 GILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKLTYASHTPYLFAMSVYDNIayplkiRKYGKAAAA 107
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDvakfGLTDLRRVLSIIPQSPVLFSGTVRFNI------DPFSEHNDA 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 108 PIVEGLlQEFKIEEIAKQN-----AKKLSGGES------QKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALikRN 176
Cdd:PLN03232 1340 DLWEAL-ERAHIKDVIDRNpfgldAEVSEGGENfsvgqrQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTI--RE 1416
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1172643631 177 REAGLTVIIITHNPSQAYRiCDTLSFMDSGRLLFNGSVEAFKASD 221
Cdd:PLN03232 1417 EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
126-212 |
1.48e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.64 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 126 NAKKLSGGESQKTALARALSFSPDTLL--LDEPTANIDPQ-SLKIIEAalIKRNREAGLTVIIITHNPsQAYRICDTLSF 202
Cdd:cd03270 134 SAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRdNDRLIET--LKRLRDLGNTVLVVEHDE-DTIRAADHVID 210
|
90
....*....|....*.
gi 1172643631 203 M------DSGRLLFNG 212
Cdd:cd03270 211 IgpgagvHGGEIVAQG 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-208 |
2.17e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLL-APTSGAITYNGLPGD-----EAVLKKLTYASH-------TPylfAMSV 88
Cdd:PRK13549 282 SFSLRRGEILGIAGLVGAGRTELVQCLFGAYpGRWEGEIFIDGKPVKirnpqQAIAQGIAMVPEdrkrdgiVP---VMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 89 YDNIAYPLKIRKYG-----KAAAAPIVEGLLQEFKIE------EIAKqnakkLSGGESQKTALARALSFSPDTLLLDEPT 157
Cdd:PRK13549 359 GKNITLAALDRFTGgsridDAAELKTILESIQRLKVKtaspelAIAR-----LSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 158 ANIDPQS----LKIIeAALIKRnreaGLTVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:PRK13549 434 RGIDVGAkyeiYKLI-NQLVQQ----GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
125-189 |
2.59e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.71 E-value: 2.59e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172643631 125 QNAKKLSGGESQKTALARALS--FSPDTL-LLDEPT-----ANIDpqslKIIEAalIKRNREAGLTVIIITHN 189
Cdd:COG0178 822 QPATTLSGGEAQRVKLASELSkrSTGKTLyILDEPTtglhfHDIR----KLLEV--LHRLVDKGNTVVVIEHN 888
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-206 |
2.79e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 32 GILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKLTYASHTPYLFAMSVYDNIAYPLKIRKYGKAAAA 107
Cdd:PTZ00243 1340 GIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREigayGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAAL 1419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 108 PIVeGLLQEFK-----IEEIAKQNAKKLSGGESQKTALARAL-----SFspdtLLLDEPTANIDPQSLKIIEAALikRNR 177
Cdd:PTZ00243 1420 ELV-GLRERVAsesegIDSRVLEGGSNYSVGQRQLMCMARALlkkgsGF----ILMDEATANIDPALDRQIQATV--MSA 1492
|
170 180
....*....|....*....|....*....
gi 1172643631 178 EAGLTVIIITHNPSQAYRiCDTLSFMDSG 206
Cdd:PTZ00243 1493 FSAYTVITIAHRLHTVAQ-YDKIIVMDHG 1520
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-209 |
3.97e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 32 GILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLP----GDEAVLKKLTYASHTPYLFAMSVYDNIayplkiRKYGKAAAA 107
Cdd:PLN03130 1269 GIVGRTGAGKSSMLNALFRIVELERGRILIDGCDiskfGLMDLRKVLGIIPQAPVLFSGTVRFNL------DPFNEHNDA 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 108 PIVEGLlQEFKIEEIAKQNAKKL-----------SGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEaaliKRN 176
Cdd:PLN03130 1343 DLWESL-ERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQ----KTI 1417
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1172643631 177 REA--GLTVIIITHnpsqayRI-----CDTLSFMDSGRLL 209
Cdd:PLN03130 1418 REEfkSCTMLIIAH------RLntiidCDRILVLDAGRVV 1451
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
125-189 |
5.17e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.93 E-value: 5.17e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 125 QNAKKLSGGESQKTALARALSfSPDT----LLLDEPTANI---DPQslKIIEaaLIKRNREAGLTVIIITHN 189
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELS-KRSTgrtlYILDEPTTGLhfdDIK--KLLE--VLQRLVDKGNTVVVIEHN 891
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-197 |
6.64e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.42 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 22 SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLKKLTYashtpylfAMSVYDNIAYPLKIRKY 101
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNG--------QLTGIENIELKGLMMGL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 102 GKAAAAPIVEGLLQEFKIEEIAKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKiieAALIKRN--REA 179
Cdd:PRK13545 116 TKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK---KCLDKMNefKEQ 192
|
170
....*....|....*...
gi 1172643631 180 GLTVIIITHNPSQAYRIC 197
Cdd:PRK13545 193 GKTIFFISHSLSQVKSFC 210
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
125-189 |
1.23e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.83 E-value: 1.23e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172643631 125 QNAKKLSGGESQKTALARALSFSPD--TL-LLDEPT-----ANIDpqslKIIEaaLIKRNREAGLTVIIITHN 189
Cdd:PRK00349 826 QPATTLSGGEAQRVKLAKELSKRSTgkTLyILDEPTtglhfEDIR----KLLE--VLHRLVDKGNTVVVIEHN 892
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
129-226 |
1.33e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.12 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 129 KLSGGESQKTALARALSFSPDTLLLDEPTANIDPQ-SLKIIEaALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGR 207
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTiQAQIIE-LLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQ 231
|
90 100
....*....|....*....|
gi 1172643631 208 LLFNG-SVEAFKASDNPVIQ 226
Cdd:PRK11022 232 VVETGkAHDIFRAPRHPYTQ 251
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
127-222 |
1.52e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 127 AKKLSGGESQKTALARALSFSPDTLL--LDEPTANIDPQ-SLKIIEAalIKRNREAGLTVIIITHNPsqayricDTLSFM 203
Cdd:TIGR00630 486 AGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRdNRRLINT--LKRLRDLGNTLIVVEHDE-------DTIRAA 556
|
90 100 110
....*....|....*....|....*....|.
gi 1172643631 204 D------------SGRLLFNGSVEAFKASDN 222
Cdd:TIGR00630 557 DyvidigpgagehGGEVVASGTPEEILANPD 587
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
125-161 |
2.30e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 2.30e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1172643631 125 QNAKKLSGGESQKTALARALSFSPDTLLLDEPTANID 161
Cdd:NF040905 400 QKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-73 |
2.33e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 2.33e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172643631 16 TVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPT---SGAITYNGLPGDEAVLKK 73
Cdd:PLN03140 179 TILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRK 239
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
130-226 |
4.07e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 130 LSGGESQKTALARALSFSPDTLLLDEPTANIDPQS-LKIIEAALIKRNREAGltVIIITHNPSQAYRICDTLSFMDSGRL 208
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAkFEIYQLIAELAKKDKG--IIIISSEMPELLGITDRILVMSNGLV 469
|
90
....*....|....*...
gi 1172643631 209 lfNGSVEAFKASDNPVIQ 226
Cdd:PRK10982 470 --AGIVDTKTTTQNEILR 485
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-215 |
4.31e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 43.74 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLT---KTYHGKtVLSLD--SLCLESGKIHGILGPNGSGKTTLMKSVAGLLAP----TSGAITYNGLPgdeavLKKLT 75
Cdd:COG4170 6 IRNLTieiDTPQGR-VKAVDrvSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGID-----LLKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 76 YASHTPYL---FAMSVYDNIAY--PlkirkygkaaAAPIVEGLLQ-----EFK--------------IEEIAK---QNAK 128
Cdd:COG4170 80 PRERRKIIgreIAMIFQEPSSCldP----------SAKIGDQLIEaipswTFKgkwwqrfkwrkkraIELLHRvgiKDHK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 129 K--------LSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTL 200
Cdd:COG4170 150 DimnsypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTI 229
|
250
....*....|....*
gi 1172643631 201 SFMDSGRLLFNGSVE 215
Cdd:COG4170 230 TVLYCGQTVESGPTE 244
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
138-191 |
4.36e-05 |
|
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: 43.53 E-value: 4.36e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 138 TALARALSfSPDTLLLDEPTANIDPQSL-KIIEaaLIKRNREAGLTVIIITHNPS 191
Cdd:pfam13304 249 AALLSALP-KGGLLLIDEPESGLHPKLLrRLLE--LLKELSRNGAQLILTTHSPL 300
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
129-207 |
6.60e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.25 E-value: 6.60e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 129 KLSGGESQKTALARALSFSPDTLLLDEPTANIDPQSLKIIEAALIKRNREAGLTVIIITHNPSQAYRICDTLSFMDSGR 207
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
116-166 |
6.93e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.60 E-value: 6.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172643631 116 EFKIEEIAKQNAKK--------LSGGESQK---TALARALSF----------SPDTLLLDEPTANIDPQSLK 166
Cdd:pfam13558 11 SFEVEVRDEDGSEVetyrrsggLSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIR 82
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-229 |
7.57e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 39.51 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 2 QIAIDKLTKTYHG--KTVLSLDSLCLESGKIHGILGPNGSGKTTLMKSVAGLLAPTSGAITYNGLPGDEAVLK----KLT 75
Cdd:cd03288 19 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHtlrsRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 76 YASHTPYLFAMSVYDNIAYPLKIRKYGKAAAAPIVEgLLQEFK-----IEEIAKQNAKKLSGGESQKTALARALSFSPDT 150
Cdd:cd03288 99 IILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQ-LKNMVKslpggLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172643631 151 LLLDEPTANIDPQSLKIIEAALIkrNREAGLTVIIITHNPSQAYRiCDTLSFMDSGRLLFNGSVEAFKASDNPVIQDFI 229
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVM--TAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
11-62 |
9.41e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.42 E-value: 9.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1172643631 11 TYHGKTV-LSLDSLCLesgkihgILGPNGSGKTTLMKSVAGLLAPtSGAITYN 62
Cdd:pfam13555 11 TFDGHTIpIDPRGNTL-------LTGPSGSGKSTLLDAIQTLLVP-AKRARFN 55
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
32-189 |
2.03e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 32 GILGPNGSGKTTLMKSVAGLLAPTSGAITYnglPGDEAV--LKKLTYASHTPYLFAM----SVYDNIAYPLKIRK----- 100
Cdd:PRK10636 31 GLVGKNGCGKSTLLALLKNEISADGGSYTF---PGNWQLawVNQETPALPQPALEYVidgdREYRQLEAQLHDANerndg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 101 ------YGK----------AAAAPIVEGLlqEFKIEEIaKQNAKKLSGGESQKTALARALSFSPDTLLLDEPTANIDPQS 164
Cdd:PRK10636 108 haiatiHGKldaidawtirSRAASLLHGL--GFSNEQL-ERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA 184
|
170 180
....*....|....*....|....*
gi 1172643631 165 LKIIEAALikRNREAglTVIIITHN 189
Cdd:PRK10636 185 VIWLEKWL--KSYQG--TLILISHD 205
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
5-189 |
2.41e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 37.68 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 5 IDKLT----KTYHGKTVLSLDslclesGKIHGILGPNGSGKTTLMKSVA-GLLAPTSGAITYNG---LPGDEAVLKKLTY 76
Cdd:COG0419 2 LLRLRlenfRSYRDTETIDFD------DGLNLIVGPNGAGKSTILEAIRyALYGKARSRSKLRSdliNVGSEEASVELEF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172643631 77 AS-HTPY--------------------------LFAMSVYDNIAYPLKIRK---YGKAAAAPIVEGLLQEFKIEEIAKQN 126
Cdd:COG0419 76 EHgGKRYrierrqgefaefleakpserkealkrLLGLEIYEELKERLKELEealESALEELAELQKLKQEILAQLSGLDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172643631 127 AKKLSGGESQKTALARALSfspdtLLLDepTANIDPQSLKIIEAALIKrnreagltVIIITHN 189
Cdd:COG0419 156 IETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEE--------LAIITHV 203
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
33-60 |
3.47e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 37.67 E-value: 3.47e-03
10 20
....*....|....*....|....*...
gi 1172643631 33 ILGPNGSGKTTLMKSVAGLLAPTSGAIT 60
Cdd:COG3950 30 LVGENGSGKTTLLEAIALALSGLLSRLD 57
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
25-49 |
9.26e-03 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 36.07 E-value: 9.26e-03
10 20
....*....|....*....|....*
gi 1172643631 25 LESGKIHGILGPNGSGKTTLMKSVA 49
Cdd:cd03243 26 LGSGRLLLITGPNMGGKSTYLRSIG 50
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-198 |
9.85e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.12 E-value: 9.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172643631 130 LSGGESQKTALARALSFS---PDTLLLDEPTANI---DPQSLKIIEAALIKRnreaGLTVIIITHNpSQAYRICD 198
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLhthDIKALIYVLQSLTHQ----GHTVVIIEHN-MHVVKVAD 879
|
|
| |
