|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-224 |
1.76e-100 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 294.66 E-value: 1.76e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVVPQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 83 DVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491378809 163 AVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKDMV 224
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
10-305 |
5.38e-79 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 242.30 E-value: 5.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 10 KRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVVPQDVAVFEE 89
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 90 LSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSR 169
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 170 NKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKDMV---------RTADRLTIDIPLLP-- 238
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLgkdtlesrpRDIQSLKVEVSMLIae 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491378809 239 --DHVLATIQTTITADGIVYKEGQLQVTTTElntvllpILTLLQAEKISYGKIATKEATLNDVFLEITG 305
Cdd:TIGR01188 241 lgETGLGLLAVTVDSDRIKILVPDGDETVPE-------IVEAAIRNGIRIRSISTERPSLDDVFLKLTG 302
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-211 |
6.55e-75 |
|
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: 227.28 E-value: 6.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVVPQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 83 DVAVFEELSVQENIDYfcglyvadkekrqalieeviqlvglenfvtfhpgelSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:cd03230 81 EPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491378809 163 AVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQV 211
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-221 |
3.92e-73 |
|
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: 224.56 E-value: 3.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVVPQ 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 83 DVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 163 AVDPQSRNKILESIKELNR-QGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLK 221
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-247 |
1.06e-71 |
|
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: 221.66 E-value: 1.06e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVVPQ 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 83 DVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 163 AVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKDMVRTADrltidiplLPDHVL 242
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEN--------LEDAFV 233
|
....*
gi 491378809 243 ATIQT 247
Cdd:COG4555 234 ALIGS 238
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-221 |
5.21e-70 |
|
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: 216.60 E-value: 5.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGD--FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVV 80
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEP 160
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491378809 161 TVAVDPQSRNKILESIKELnRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLK 221
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-222 |
5.94e-58 |
|
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: 186.34 E-value: 5.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTP-ENYAVKAMI 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdiTGLSEkELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEELSVQENI----DYFCGLyvaDKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPR 153
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVafplREHTDL---SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 154 LIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKD 222
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-220 |
4.80e-55 |
|
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: 178.29 E-value: 4.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRY-GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPEN-YAVKAMIGVV 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQ--DVAVFEElSVQENIDYfcGL--YVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIF 156
Cdd:COG1122 81 FQnpDDQLFAP-TVEEDVAF--GPenLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491378809 157 LDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-215 |
6.91e-55 |
|
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: 177.39 E-value: 6.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGeVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVVPQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 83 DVAVFEELSVQENIDYFCGLY-VADKEKRQAlIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPT 161
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKgIPSKEVKAR-VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491378809 162 VAVDPQSRNKILESIKELNrQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG 215
Cdd:cd03264 159 AGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2-215 |
1.08e-54 |
|
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: 177.17 E-value: 1.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGD----FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMI 77
Cdd:cd03266 1 MITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFL 157
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 158 DEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG 215
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-222 |
1.16e-54 |
|
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: 1.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTP-ENYAVKAMIG 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGediSGLSEaELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 VVPQDVAVFEELSVQENIDYFCGLYVADKEKR-QALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFL 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 158 DEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKD 222
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-307 |
2.13e-54 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 179.15 E-value: 2.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAvkaMIGVVP 81
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRR---RIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 82 qdvavfEE------LSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLI 155
Cdd:COG4152 78 ------EErglypkMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 156 FLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKDMVRTaDRLTIDip 235
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGR-NTLRLE-- 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491378809 236 llPDHVLATIQTTITADGIVYKEGQLQVTTTElNTVLLPIL-TLLQAEKISygKIATKEATLNDVFLEITGKE 307
Cdd:COG4152 229 --ADGDAGWLRALPGVTVVEEDGDGAELKLED-GADAQELLrALLARGPVR--EFEEVRPSLNEIFIEVVGEK 296
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-310 |
3.46e-54 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 178.85 E-value: 3.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVVP 81
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 82 QDVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPT 161
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 162 VAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKDMVRTADRLTI---DIPLLP 238
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDVIEIygpDPVALR 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491378809 239 DHVLATIQTTITADGIVYkegqLQVTTTElntvllPILTLLQAEK-ISYgkiATKEATLNDVFLEITGKELRD 310
Cdd:PRK13537 247 DELAPLAERTEISGETLF----CYVRDPE------PLHARLKGRAgLRY---LHRPANLEDVFLRLTGREMQD 306
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-216 |
5.16e-53 |
|
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: 173.39 E-value: 5.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT--PENYAVKAMIGVV 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITglPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEELSVQENI----------DYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAH 150
Cdd:cd03219 81 FQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 151 KPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGT 216
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-215 |
1.05e-51 |
|
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: 169.24 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPEnyavKAMIGV 79
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvTGVPPE----RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDE 159
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491378809 160 PTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG 215
Cdd:cd03259 157 PLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-220 |
3.42e-51 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 172.20 E-value: 3.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT---PEnyavKAMIG 78
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglpPE----KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 VVPQDVAVFEELSVQENIDYfcGLYV--ADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIF 156
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAF--GLRMrgVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491378809 157 LDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-230 |
5.04e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 166.03 E-value: 5.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTpenyAVKAMIGVV 80
Cdd:COG1121 5 PAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR----RARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEE--LSVQE----NIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRL 154
Cdd:COG1121 81 PQRAEVDWDfpITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 155 IFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGqVIAKGTKESlkdmVRTADRL 230
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEE----VLTPENL 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-210 |
6.44e-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: 164.56 E-value: 6.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 4 EIDKLVKRYGDF--VALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPEN-YAVKAMIGVV 80
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVA-------VFEELS-VQENIdyfcGLyvaDKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKP 152
Cdd:cd03225 81 FQNPDdqffgptVEEEVAfGLENL----GL---PEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 153 RLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQ 210
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-216 |
2.75e-49 |
|
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: 164.44 E-value: 2.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPenYAVkAMI 77
Cdd:COG0411 3 PLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrdiTGLPP--HRI-ARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVP--QDVAVFEELSVQENI-------------DYFCGLYVADKEKRQAL--IEEVIQLVGLENFVTFHPGELSGGLKR 140
Cdd:COG0411 80 GIARtfQNPRLFPELTVLENVlvaaharlgrgllAALLRLPRARREEREARerAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491378809 141 RLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNR-QGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGT 216
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-220 |
4.75e-49 |
|
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: 163.14 E-value: 4.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGD----FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT----PENYAV 73
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 74 KAMIGVVPQDVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPR 153
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 154 LIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-222 |
6.59e-49 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 166.16 E-value: 6.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVV 80
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEP 160
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491378809 161 TVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKD 222
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-213 |
5.42e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 160.21 E-value: 5.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGD----FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPENYAV- 73
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdiSSLSERELARl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 74 -KAMIGVVPQDVAVFEELSVQENID---YFCGLyvaDKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIA 149
Cdd:COG1136 84 rRRHIGFVFQFFNLLPELTALENVAlplLLAGV---SRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491378809 150 HKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHymeEVEIL--CDQIVIMDQGQVIA 213
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTH---DPELAarADRVIRLRDGRIVS 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-213 |
6.59e-48 |
|
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: 159.94 E-value: 6.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGD----FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENyavkAMIG 78
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG----PDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 VVPQDVAVFEELSVQENIDYfcGLYVA--DKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIF 156
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVAL--GLELQgvPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 157 LDEPTVAVDPQSRNKILESIKEL-NRQGATIVYTTHYMEEVEILCDQIVIMDQ--GQVIA 213
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-223 |
1.09e-47 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 160.67 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRY--GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG-STMTPEN-YAVKAMIG 78
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENlWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 VVPQ-------------DVAvF--EELSVqenidyfcglyvaDKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLN 143
Cdd:TIGR04520 81 MVFQnpdnqfvgatvedDVA-FglENLGV-------------PREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 144 IACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNR-QGATIVYTTHYMEEVeILCDQIVIMDQGQVIAKGT------ 216
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTpreifs 225
|
....*...
gi 491378809 217 -KESLKDM 223
Cdd:TIGR04520 226 qVELLKEI 233
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-213 |
1.33e-47 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 160.26 E-value: 1.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRY----GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTpenyAVKAM 76
Cdd:COG1116 6 PALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----GPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 77 IGVVPQDVAVFEELSVQENIDYfcGLYVA--DKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRL 154
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVAL--GLELRgvPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491378809 155 IFLDEPTVAVDPQSRNKI---LESIkeLNRQGATIVYTTHYMEEVEILCDQIVIMDQ--GQVIA 213
Cdd:COG1116 160 LLMDEPFGALDALTRERLqdeLLRL--WQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-215 |
1.34e-47 |
|
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: 158.60 E-value: 1.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGStmtPENYAVKAMIGVVPQ 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK---PLDIAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 83 DVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491378809 163 AVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG 215
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-220 |
2.42e-47 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 159.00 E-value: 2.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAM---IG 78
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLrrkVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 VVPQDVAVFEELSVQENIDYfcGLYVADKEKRQALIEEVIQL---VGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLI 155
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTL--APIKVKKMSKAEAEERAMELlerVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 156 FLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYME---EVeilCDQIVIMDQGQVIAKGTKESL 220
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGfarEV---ADRVVFMDGGRIVEEGPPEEF 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-220 |
2.48e-47 |
|
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: 165.85 E-value: 2.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRY-----GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENY-AVKA 75
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 76 M---IGVVPQD--VAVFEELSVQENIDYFCGLY-VADKEKRQALIEEVIQLVGL-ENFVTFHPGELSGGLKRRLNIACGI 148
Cdd:COG1123 340 LrrrVQMVFQDpySSLNPRMTVGDIIAEPLRLHgLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491378809 149 AHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-215 |
1.88e-46 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 155.77 E-value: 1.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 4 EIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENyavkAMIGVVPQd 83
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER----KRIGYVPQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 84 vavFEE------LSVQE----NIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPR 153
Cdd:cd03235 76 ---RRSidrdfpISVRDvvlmGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491378809 154 LIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGqVIAKG 215
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT-VVASG 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-215 |
2.09e-46 |
|
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: 155.45 E-value: 2.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTpENYAVKAMIGVVPQ 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-KNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 83 DVAVFEELSVQENIDYFCGLYVADKEKrqalIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491378809 163 AVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG 215
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-230 |
3.03e-45 |
|
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: 154.05 E-value: 3.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPENYAvkAMIG 78
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlASLSRRELA--RRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 VVPQDVAVFEELSVQENIDY----FCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRL 154
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491378809 155 IFLDEPTVAVDPQSRNKILESIKELNR-QGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESlkdmVRTADRL 230
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE----VLTPELL 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-220 |
5.86e-45 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 156.08 E-value: 5.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTpENYAVKAM-IGV 79
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPRERrVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEELSVQENIDYfcGLYVA--DKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFL 157
Cdd:COG1118 80 VFQHYALFPHMTVAENIAF--GLRVRppSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491378809 158 DEPTVAVDPQSRNKILESIKEL-NRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:COG1118 158 DEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-211 |
1.62e-44 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 150.76 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAM---IGV 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELrqkVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEELSVQENIDYfcGLYVADKEKRQALIEEVIQL---VGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIF 156
Cdd:cd03262 81 VFQQFNLFPHLTVLENITL--APIKVKGMSKAEAEERALELlekVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491378809 157 LDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQV 211
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-220 |
2.00e-44 |
|
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: 158.14 E-value: 2.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRY--GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYD---KGTIKLFGSTMTPENYAVKA- 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 76 MIGVVPQDVAV-FEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRL 154
Cdd:COG1123 84 RIGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491378809 155 IFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-211 |
2.57e-44 |
|
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: 150.33 E-value: 2.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGD----FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTpeNYAVKAM-- 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS--KLSEKELaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 77 -----IGVVPQDVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHK 151
Cdd:cd03255 79 frrrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491378809 152 PRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEiLCDQIVIMDQGQV 211
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-208 |
3.91e-44 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 149.55 E-value: 3.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVV 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEELSVQENIDYFCGLYvaDKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEP 160
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALY--GLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491378809 161 TVAVDPQSRNKILESIKELNRQGATIVYTTHymEEVEILCDQIVIMDQ 208
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTH--QPLELAAARVLDLGD 204
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
2-255 |
3.92e-44 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 153.69 E-value: 3.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRY----GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCmLSLL-NYDKGTIKLFGSTMT----PENYA 72
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRC-INLLeRPTSGSVLVDGVDLTalseRELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 73 VKAMIGVVPQDVAVFEELSVQENIDYfcGLYVA--DKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAH 150
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENVAL--PLEIAgvPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 151 KPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTkesLKDMV----- 224
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGP---VLDVFanpqs 234
|
250 260 270
....*....|....*....|....*....|...
gi 491378809 225 RTADRL--TIDIPLLPDHVLATIQTTITADGIV 255
Cdd:COG1135 235 ELTRRFlpTVLNDELPEELLARLREAAGGGRLV 267
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-210 |
7.13e-44 |
|
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: 148.10 E-value: 7.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAM---IGV 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrrIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEELSVQENIDYfcglyvadkekrqalieeviqlvglenfvtfhpgELSGGLKRRLNIACGIAHKPRLIFLDE 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491378809 160 PTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQ 210
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-216 |
9.90e-44 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 152.92 E-value: 9.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT---PEnyavKAMIGV 79
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTdlpPK----DRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEELSVQENIDYfcGLYVA--DKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFL 157
Cdd:COG3839 80 VFQSYALYPHMTVYENIAF--PLKLRkvPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 158 DEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGT 216
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-210 |
1.80e-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: 146.24 E-value: 1.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 4 EIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG-STMTPENYAVKAMIGVVPQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 83 dvavfeelsvqenidyfcglyvadkekrqalieeviqlvglenfvtfhpgeLSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491378809 163 AVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQ 210
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-220 |
2.10e-43 |
|
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: 148.99 E-value: 2.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGD-FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG-STMTPENYAVKAMIGVV 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGeDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLE--NFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLD 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491378809 159 EPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-219 |
2.25e-43 |
|
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: 148.64 E-value: 2.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNhFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT---PEnyavKAMIGV 79
Cdd:cd03299 1 LKVENLSKDWKEFKLKN-VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITnlpPE----KRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDE 159
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491378809 160 PTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKES 219
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-216 |
3.74e-43 |
|
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: 151.41 E-value: 3.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDkLVKRYGDFvALNhFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGST---------MTPEny 71
Cdd:COG4148 1 MMLEVD-FRLRRGGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargifLPPH-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 72 avKAMIGVVPQDVAVFEELSVQENIDYfcGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHK 151
Cdd:COG4148 76 --RRRIGYVFQEARLFPHLSVRGNLLY--GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 152 PRLIFLDEPTVAVDPQSRNKILESIKELNRQGAT-IVYTTHYMEEVEILCDQIVIMDQGQVIAKGT 216
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-227 |
1.03e-42 |
|
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: 147.10 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENyAVKAMIGVV 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP-VQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEELSVQENIDYfcGLYVADKEKR------QALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRL 154
Cdd:cd03296 80 FQHYALFRHMTVFDNVAF--GLRVKPRSERppeaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491378809 155 IFLDEPTVAVDPQSRNKILESIKEL-NRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKDMVRTA 227
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASP 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-220 |
2.45e-42 |
|
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: 154.99 E-value: 2.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFV--ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPENYAvkAMI 77
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlRQIDPASLR--RQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEElSVQENIDYFCGLyvADKEKrqalIEEVIQLVGLENFVTFHP-------GE----LSGGLKRRLNIAC 146
Cdd:COG2274 552 GVVLQDVFLFSG-TIRENITLGDPD--ATDEE----IIEAARLAGLHDFIEALPmgydtvvGEggsnLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491378809 147 GIAHKPRLIFLDEPTVAVDPQSRNKILESIKELnRQGATIVYTTHYMEEVEiLCDQIVIMDQGQVIAKGTKESL 220
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-220 |
3.35e-42 |
|
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: 145.38 E-value: 3.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT--PENYAVKAMIGVV 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITklPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEP 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 161 TVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-223 |
1.56e-41 |
|
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: 143.53 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT--PENyavKAMIGVV 80
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITnlPPH---KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEELSVQENIDYfcGLYVA--DKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLD 158
Cdd:cd03300 78 FQNYALFPHLTVFENIAF--GLRLKklPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 159 EPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKDM 223
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
10-220 |
4.21e-41 |
|
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: 146.03 E-value: 4.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 10 KRYGDFvALNhFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGST---------MTPEnyavKAMIGVV 80
Cdd:TIGR02142 7 KRLGDF-SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgifLPPE----KRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEELSVQENIDYfcGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEP 160
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRY--GMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491378809 161 TVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-220 |
4.41e-41 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 152.20 E-value: 4.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINcMLS-LLNYDKGTIKLFGSTMTPENYAVKAMIGVVP 81
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMK-MLTgLLPASEGEAWLFGQPVDAGDIATRRRVGYMS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 82 QDVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPT 161
Cdd:NF033858 346 QAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 162 VAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEiLCDQIVIMDQGQVIAKGTKESL 220
Cdd:NF033858 426 SGVDPVARDMFWRLLIELSREdGVTIFISTHFMNEAE-RCDRISLMHAGRVLASDTPAAL 484
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-220 |
7.52e-41 |
|
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: 141.93 E-value: 7.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKST---AINCMLSLLNY--DKGTIKLFGSTMTPENYAVKAM- 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIPGapDEGEVLLDGKDIYDLDVDVLELr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 77 --IGVVPQDVAVFEeLSVQENIDYfcGLY---VADKEKRQALIEEVIQLVGLENFV--TFHPGELSGGLKRRLNIACGIA 149
Cdd:cd03260 81 rrVGMVFQKPNPFP-GSIYDNVAY--GLRlhgIKLKEELDERVEEALRKAALWDEVkdRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491378809 150 HKPRLIFLDEPTVAVDPQSRNKILESIKELNRQgATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
2-217 |
9.52e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 141.34 E-value: 9.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRY-GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPEnyAVKAM- 76
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlSRLKRR--EIPYLr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 77 --IGVVPQDVAVFEELSVQENIDYfcGLYVADKEKR--QALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKP 152
Cdd:COG2884 79 rrIGVVFQDFRLLPDRTVYENVAL--PLRVTGKSRKeiRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491378809 153 RLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTK 217
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-215 |
1.21e-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: 141.10 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRY----GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKA-- 75
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 76 --MIGVVPQD------------VAVFEELSVQENIDyfcglyvaDKEKRQALIEEVIQLVGL-ENFVTFHPGELSGGLKR 140
Cdd:cd03257 81 rkEIQMVFQDpmsslnprmtigEQIAEPLRIHGKLS--------KKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 141 RLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG 215
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-233 |
1.38e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 143.69 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 8 LVKR-YGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGstMTP--ENYAVKAMIGVV-PQD 83
Cdd:COG4586 27 LFRReYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG--YVPfkRRKEFARRIGVVfGQR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 84 VAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVA 163
Cdd:COG4586 105 SQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIG 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491378809 164 VDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKDMVRTADRLTID 233
Cdd:COG4586 185 LDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLE 255
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-220 |
2.30e-40 |
|
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: 147.99 E-value: 2.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRY--GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPEnyAVKAMI 77
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlRDLDED--DLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEElSVQENidyfcgLYVADKEKRQALIEEVIQLVGLENFVTFHP-------GE----LSGGLKRRLNIAC 146
Cdd:COG4987 412 AVVPQRPHLFDT-TLREN------LRLARPDATDEELWAALERVGLGDWLAALPdgldtwlGEggrrLSGGERRRLALAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491378809 147 GIAHKPRLIFLDEPTVAVDPQSRNKILESIKELnRQGATIVYTTHYMEEVEiLCDQIVIMDQGQVIAKGTKESL 220
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHEEL 556
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-220 |
2.68e-40 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 140.55 E-value: 2.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPenyavKAM---- 76
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH-----LPMhkra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 77 ---IGVVPQDVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENfVTFHPG-ELSGGLKRRLNIACGIAHKP 152
Cdd:COG1137 77 rlgIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITH-LRKSKAySLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 153 RLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-224 |
6.34e-40 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 145.55 E-value: 6.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENY--AVKAMIG 78
Cdd:COG1129 3 PLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 VVPQDVAVFEELSVQENIdyFCGLYVA-----DKEKRQALIEEVIQLVGLEnfvtFHP----GELSGGLKRRLNIACGIA 149
Cdd:COG1129 83 IIHQELNLVPNLSVAENI--FLGREPRrggliDWRAMRRRARELLARLGLD----IDPdtpvGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 150 HKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG-----TKESL-KDM 223
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGpvaelTEDELvRLM 236
|
.
gi 491378809 224 V 224
Cdd:COG1129 237 V 237
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-222 |
9.79e-40 |
|
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: 138.72 E-value: 9.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT--PENYAVKAMIGVV 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEELSVQENIDyfCGLYVADKEKRQALIEEVIQLV-GLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDE 159
Cdd:cd03224 81 PEGRRIFPELTVEENLL--LGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491378809 160 PTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKD 222
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-227 |
1.61e-39 |
|
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: 138.78 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYG----DFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPEnyAVKAM-- 76
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRR--RRKAFrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 77 -IGVVPQDV------------AVFEELSVQenidyfcglYVADKEKRqalIEEVIQLVGL-ENFVTFHPGELSGGLKRRL 142
Cdd:COG1124 80 rVQMVFQDPyaslhprhtvdrILAEPLRIH---------GLPDREER---IAELLEQVGLpPSFLDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 143 NIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLK 221
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
....*.
gi 491378809 222 DMVRTA 227
Cdd:COG1124 228 AGPKHP 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-235 |
3.40e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 138.99 E-value: 3.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDF--VALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPEN-YAVKAMIG 78
Cdd:PRK13635 5 IIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 VVPQdvavfeelsvqeNID-YFCGLYVAD------------KEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIA 145
Cdd:PRK13635 85 MVFQ------------NPDnQFVGATVQDdvafglenigvpREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 146 CGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVeILCDQIVIMDQGQVIAKGTKE---SLK 221
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEeifKSG 231
|
250
....*....|....
gi 491378809 222 DMVRtadRLTIDIP 235
Cdd:PRK13635 232 HMLQ---EIGLDVP 242
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-215 |
4.01e-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: 137.04 E-value: 4.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 21 FDLQVQ---EGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGST---------MTPEnyavKAMIGVVPQDVAVFE 88
Cdd:cd03297 13 FTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinLPPQ----QRKIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 89 ELSVQENIDYfcGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQS 168
Cdd:cd03297 89 HLNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491378809 169 RNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG 215
Cdd:cd03297 167 RLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-215 |
7.42e-39 |
|
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: 135.26 E-value: 7.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 4 EIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPENYAVKamIGVV 80
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGkdlASLSPKELARK--IAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQdvavfeelsvqenidyfcglyvadkekrqalieeVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEP 160
Cdd:cd03214 79 PQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 161 TVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG 215
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
6-220 |
2.57e-38 |
|
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: 136.62 E-value: 2.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 6 DKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENY-AVKAM----IGVV 80
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkELRELrrkkISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEELSVQENIDYfcGLYVA--DKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLD 158
Cdd:cd03294 108 FQSFALLPHRTVLENVAF--GLEVQgvPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491378809 159 EPTVAVDPQSRNKILESIKELNR-QGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAeLQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-220 |
3.33e-38 |
|
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: 135.09 E-value: 3.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT--PENYAVKAMIGV 79
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDIThlPMHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEELSVQENIDYFCGL-YVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLD 158
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIrKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491378809 159 EPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2-222 |
5.44e-38 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 134.84 E-value: 5.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAM---IG 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 VVPQDVAVFEELSVQENIdYFCGLYV--ADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIF 156
Cdd:PRK09493 81 MVFQQFYLFPHLTALENV-MFGPLRVrgASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 157 LDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKD 222
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-162 |
7.10e-37 |
|
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: 128.92 E-value: 7.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENY-AVKAMIGVVPQDVAVFEELSVQENI 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERkSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 97 DYFCGLYVADKEKRQALIEEVIQLVGLENF----VTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-235 |
1.05e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 132.52 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGD------FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG-STMTPEN-YAV 73
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENlWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 74 KAMIGVVPQD-----VAVFEELSVQ---ENidyfcgLYVADKEKRQAlIEEVIQLVGLENFVTFHPGELSGGLKRRLNIA 145
Cdd:PRK13633 84 RNKAGMVFQNpdnqiVATIVEEDVAfgpEN------LGIPPEEIRER-VDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 146 CGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVeILCDQIVIMDQGQVIAKGTKESLKDMV 224
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFKEV 235
|
250
....*....|.
gi 491378809 225 RTADRLTIDIP 235
Cdd:PRK13633 236 EMMKKIGLDVP 246
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-222 |
1.08e-36 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 131.54 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGD-FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT----PENYAVKAMI 77
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkgKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEELSVQENI------------DYFCGLYVADKEKRQALIEEViqlvGLENFVTFHPGELSGGLKRRLNIA 145
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgrrstwrSLFGLFPKEEKQRALAALERV----GLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 146 CGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKD 222
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-220 |
2.48e-36 |
|
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: 136.81 E-value: 2.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGD-FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPEnyAVKAMIG 78
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlSDLDPA--SWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 VVPQDVAVFEElSVQENIDyfcglyVADKEKRQALIEEVIQLVGLENFVTFHP-------GE----LSGGLKRRLNIACG 147
Cdd:COG4988 415 WVPQNPYLFAG-TIRENLR------LGRPDASDEELEAALEAAGLDEFVAALPdgldtplGEggrgLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491378809 148 IAHKPRLIFLDEPTVAVDPQSRNKILESIKELnRQGATIVYTTHYMEEVEiLCDQIVIMDQGQVIAKGTKESL 220
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLA-QADRILVLDDGRIVEQGTHEEL 558
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-213 |
3.03e-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: 127.54 E-value: 3.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENY--AVKAMIGVV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPrdARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQdvavfeelsvqenidyfcglyvadkekrqalieeviqlvglenfvtfhpgeLSGGLKRRLNIACGIAHKPRLIFLDEP 160
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491378809 161 TVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIA 213
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-222 |
3.14e-36 |
|
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: 130.10 E-value: 3.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPENyAVKAMI 77
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGediTGLPPHR-IARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEELSVQENIDyfCGLYVA-DKEKRQALIEEViqlvgLENFvtfhP----------GELSGGLKRRLNIAC 146
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLL--LGAYARrDRAEVRADLERV-----YELF----PrlkerrrqraGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 147 GIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKD 222
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-213 |
3.54e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 135.54 E-value: 3.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPEN--YAVKAMIG 78
Cdd:COG3845 4 PALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSprDAIALGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 VVPQDVAVFEELSVQENIdyFCGL-----YVADKEKRQALIEEVIQLVGLEnfvtFHP----GELSGGLKRRLNIACGIA 149
Cdd:COG3845 84 MVHQHFMLVPNLTVAENI--VLGLeptkgGRLDRKAARARIRELSERYGLD----VDPdakvEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491378809 150 HKPRLIFLDEPTvAV-DPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIA 213
Cdd:COG3845 158 RGARILILDEPT-AVlTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVG 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-211 |
6.21e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.40 E-value: 6.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPENYavKAMIGV 79
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplSAMPPPEW--RRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEElSVQENIDYfcGLYVADKEKRQALIEEVIQLVGL-ENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLD 158
Cdd:COG4619 79 VPQEPALWGG-TVRDNLPF--PFQLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491378809 159 EPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQV 211
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-235 |
9.32e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 129.73 E-value: 9.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFV--ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYA-VKAMIGV 79
Cdd:PRK13632 8 IKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDV-AVFEELSVQENIDYfcGL--YVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIF 156
Cdd:PRK13632 88 IFQNPdNQFIGATVEDDIAF--GLenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 157 LDEPTVAVDPQSRNKILESIKELNRQGA-TIVYTTHYMEEVeILCDQIVIMDQGQVIAKGT-KESLKD--MVRTADrltI 232
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKLIAQGKpKEILNNkeILEKAK---I 241
|
...
gi 491378809 233 DIP 235
Cdd:PRK13632 242 DSP 244
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-211 |
1.22e-35 |
|
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: 127.76 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTpENYAVKAMIGVVPQ 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-DLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 83 DVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491378809 163 AVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQV 211
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-215 |
1.31e-35 |
|
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: 128.22 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 8 LVKR-YGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVV-PQDVA 85
Cdd:cd03267 26 LFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 86 VFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVD 165
Cdd:cd03267 106 LWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491378809 166 PQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG 215
Cdd:cd03267 186 VVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-210 |
4.28e-35 |
|
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: 124.80 E-value: 4.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDF--VALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPENYAvkAMI 77
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlRDLDLESLR--KNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEElSVQENIdyfcglyvadkekrqalieeviqlvglenfvtfhpgeLSGGLKRRLNIACGIAHKPRLIFL 157
Cdd:cd03228 79 AYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491378809 158 DEPTVAVDPQSRNKILESIKELnRQGATIVYTTHYMEEVEiLCDQIVIMDQGQ 210
Cdd:cd03228 121 DEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-220 |
1.12e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 126.40 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKL------FGSTMTPENYAVKAM 76
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 77 ---IGVVPQDVAVFEELSVQENIdyFCGLYVADKEKRQALIE---EVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAH 150
Cdd:PRK11264 84 rqhVGFVFQNFNLFPHRTVLENI--IEGPVIVKGEPKEEATArarELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 151 KPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
1.27e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 127.44 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYG-----DFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPE--NYAV 73
Cdd:PRK13634 1 MDITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkkNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 74 KAM---IGVVPQ--DVAVFEElSVQENIDYFCGLYVADKEKRQALIEEVIQLVGL-ENFVTFHPGELSGGLKRRLNIACG 147
Cdd:PRK13634 81 KPLrkkVGIVFQfpEHQLFEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 148 IAHKPRLIFLDEPTVAVDPQSRNKILESIKELNR-QGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKEslkDMVRT 226
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPR---EIFAD 236
|
250
....*....|..
gi 491378809 227 ADRLT---IDIP 235
Cdd:PRK13634 237 PDELEaigLDLP 248
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-239 |
1.55e-34 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 132.94 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTaincMLSLLNYDK----GTIKLFGSTMTPENY--AVKA 75
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIAGARkiqqGRVEVLGGDMADARHrrAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 76 MIGVVPQDVA--VFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPR 153
Cdd:NF033858 77 RIAYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 154 LIFLDEPTVAVDPQSRNKILESIKEL--NRQGATIVYTTHYMEEVEiLCDQIVIMDQGQVIAKGTKESLKDMVRTAdrlT 231
Cdd:NF033858 157 LLILDEPTTGVDPLSRRQFWELIDRIraERPGMSVLVATAYMEEAE-RFDWLVAMDAGRVLATGTPAELLARTGAD---T 232
|
250
....*....|.
gi 491378809 232 ID---IPLLPD 239
Cdd:NF033858 233 LEaafIALLPE 243
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-222 |
1.59e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 125.25 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVAlnHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVK--AMIGvv 80
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERpvSMLF-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 pQDVAVFEELSVQENIdyfcGLYVADK----EKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIA-CGIAHKPRLI 155
Cdd:COG3840 78 -QENNLFPHLTVAQNI----GLGLRPGlkltAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALArCLVRKRPILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 156 fLDEPTVAVDPQSRNKILESIKELNR-QGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKD 222
Cdd:COG3840 153 -LDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
17-220 |
2.21e-34 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 131.44 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPEnyAVKAMIGVVPQDVAVFEElSVQ 93
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRDLTLE--SLRRQIGVVPQDTFLFSG-TIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 94 ENIDYfcGLYVADKEKrqalIEEVIQLVGLENFVTFHP-------GE----LSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:COG1132 432 ENIRY--GRPDATDEE----VEEAAKAAQAHEFIEALPdgydtvvGErgvnLSGGQRQRIAIARALLKDPPILILDEATS 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 163 AVDPQSRNKILESIKELnRQGATIVYTTHYMEEVEiLCDQIVIMDQGQVIAKGTKESL 220
Cdd:COG1132 506 ALDTETEALIQEALERL-MKGRTTIVIAHRLSTIR-NADRILVLDDGRIVEQGTHEEL 561
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
2-228 |
2.29e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 126.35 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGD-FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYA---VKAMI 77
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSlleVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQ--DVAVFEElSVQENIDY---FCGLYVADKEKRqalIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKP 152
Cdd:PRK13639 81 GIVFQnpDDQLFAP-TVEEDVAFgplNLGLSKEEVEKR---VKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491378809 153 RLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGT-KE--SLKDMVRTAD 228
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTpKEvfSDIETIRKAN 235
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-307 |
2.26e-33 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 125.62 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAInCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGV-VP 81
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*hRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 82 QDVAVFEELSVQENIdYFCG--LYVADKEKRqALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDE 159
Cdd:NF000106 93 VR*GRRESFSGRENL-YMIGr*LDLSRKDAR-ARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 160 PTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKDMV--RTADRLTIDIPLL 237
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVggRTLQIRPAHAAEL 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491378809 238 PDHVLATIQTTItaDGIV-----YKEGQLQVTTTElNTVLLPILTLLQAEKISYGKIATKEATLNDVFLEITGKE 307
Cdd:NF000106 251 DRMVGAIAQAGL--DGIAgatadHEDGVVNVPIVS-DEQLSAVVGMLGERGFTISGHQHPSAQL*EVFLAITGQK 322
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-231 |
2.59e-33 |
|
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: 122.89 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTaincMLSLLNYD-----KGTIKLFGSTMTPEN-YAVK 74
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKST----LLSLITGDlpptyGNDVRLFGERRGGEDvWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 75 AMIGVVPQDVA--VFEELSVQE--------NIdyfcGLY--VADKEKRQAliEEVIQLVGLENFVTFHPGELSGGLKRRL 142
Cdd:COG1119 78 KRIGLVSPALQlrFPRDETVLDvvlsgffdSI----GLYrePTDEQRERA--RELLELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 143 NIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGA-TIVYTTHYMEEV--EIlcDQIVIMDQGQVIAKGTKES 219
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHVEEIppGI--THVLLLKDGRVVAAGPKEE 229
|
250
....*....|..
gi 491378809 220 lkdmVRTADRLT 231
Cdd:COG1119 230 ----VLTSENLS 237
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-249 |
5.86e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 122.54 E-value: 5.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFV-ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPEN-YAVKAMIGV 79
Cdd:PRK13647 4 IIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENeKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDV--AVFEElSVQENIDY---FCGLYVADKEKRqalIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRL 154
Cdd:PRK13647 84 VFQDPddQVFSS-TVWDDVAFgpvNMGLDKDEVERR---VEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 155 IFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL--KDMVRTAD-RLT 231
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLtdEDIVEQAGlRLP 239
|
250 260
....*....|....*....|.
gi 491378809 232 IDIPL---LPDHVLATIQTTI 249
Cdd:PRK13647 240 LVAQIfedLPELGQSKLPLTV 260
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-215 |
1.02e-32 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 120.33 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 5 IDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGStmtpenyaVKAMIGVvpqDV 84
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--------VSSLLGL---GG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 85 AVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAV 164
Cdd:cd03220 94 GFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491378809 165 DPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG 215
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-253 |
1.20e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 123.37 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRY----GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMlSLLNY-DKGTIKLFGSTMT----PENYAV 73
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCI-NLLERpTSGRVLVDGQDLTalseKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 74 KAMIGVVPQDvavFEELS---VQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAH 150
Cdd:PRK11153 81 RRQIGMIFQH---FNLLSsrtVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 151 KPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGT--------KESL- 220
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTvsevfshpKHPLt 237
|
250 260 270
....*....|....*....|....*....|...
gi 491378809 221 KDMVRTADRLTidiplLPDHVLATIQTTITADG 253
Cdd:PRK11153 238 REFIQSTLHLD-----LPEDYLARLQAEPTTGS 265
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-216 |
2.51e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 123.13 E-value: 2.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT---PENYAVKamig 78
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThvpAENRHVN---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 VVPQDVAVFEELSVQENIDYfcGLYVAD--KEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIF 156
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAF--GLRMQKtpAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491378809 157 LDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGT 216
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-235 |
3.31e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 120.92 E-value: 3.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 16 VALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYA---VKAMIGVVPQ--DVAVFEEl 90
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdIRKKVGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 91 SVQENIDY---FCGLYVADKEKRqalIEEVIQLVGL--ENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVD 165
Cdd:PRK13637 100 TIEKDIAFgpiNLGLSEEEIENR---VKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491378809 166 PQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKDMVRTADRLTIDIP 235
Cdd:PRK13637 177 PKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLESIGLAVP 247
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-232 |
5.24e-32 |
|
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: 125.90 E-value: 5.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVVPQDVAVFEELSVQENI 96
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 97 DYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESI 176
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 177 KELnRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKDMVRTADRLTI 232
Cdd:TIGR01257 1105 LKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTL 1159
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-215 |
5.58e-32 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 117.65 E-value: 5.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 25 VQEGEVLGLLGPNGSGKSTAINCMLSLLNY--DKGTIKLFGSTMTPENYavKAMIGVVPQDVAVFEELSVQENIDYfcgl 102
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSF--RKIIGYVPQDDILHPTLTVRETLMF---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 103 yvadkekrqalieeVIQLVGLenfvtfhpgelSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ 182
Cdd:cd03213 106 --------------AAKLRGL-----------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT 160
|
170 180 190
....*....|....*....|....*....|....
gi 491378809 183 GATIVYTTHYM-EEVEILCDQIVIMDQGQVIAKG 215
Cdd:cd03213 161 GRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-220 |
1.46e-31 |
|
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: 119.77 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRY----GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLL---NYDKGTIKLFG---STMTPEny 71
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGedlLKLSEK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 72 AVKAM----IGVVPQDVA--------VFEelSVQENIDYFCGLyvaDKEKRQALIEEVIQLVGL---ENFVTFHPGELSG 136
Cdd:COG0444 79 ELRKIrgreIQMIFQDPMtslnpvmtVGD--QIAEPLRIHGGL---SKAEARERAIELLERVGLpdpERRLDRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 137 GLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG 215
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
....*
gi 491378809 216 TKESL 220
Cdd:COG0444 234 PVEEL 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-218 |
1.84e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 120.19 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTpENYAVKAMIGVV 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-RLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEELSVQENIDYfcGLYVADKEKR---QALIEEVIQL---VGLENFVTFHPGELSGGLKRRLNIACGIAHKPRL 154
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAF--GLTVLPRRERpnaAAIKAKVTQLlemVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491378809 155 IFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKE 218
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-213 |
3.45e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 117.27 E-value: 3.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFV----ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT-PEnyavkA 75
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgPG-----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 76 MIGVVPQDVAVFEELSVQENIDYfcGLYVA--DKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPR 153
Cdd:COG4525 77 DRGVVFQKDALLPWLNVLDNVAF--GLRLRgvPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491378809 154 LIFLDEPTVAVDPQSRnkilESIKEL-----NRQGATIVYTTHYMEEVEILCDQIVIMD--QGQVIA 213
Cdd:COG4525 155 FLLMDEPFGALDALTR----EQMQELlldvwQRTGKGVFLITHSVEEALFLATRLVVMSpgPGRIVE 217
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-222 |
5.14e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.01 E-value: 5.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVVP 81
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 82 --QDVAVFEELSVQENI----------DYFCGLYVAD---KEKRQALIEEVIQL--VGLENFVTFHPGELSGGLKRRLNI 144
Cdd:PRK11300 85 tfQHVRLFREMTVIENLlvaqhqqlktGLFSGLLKTPafrRAESEALDRAATWLerVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491378809 145 ACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKD 222
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-268 |
1.19e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 116.37 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYG---DFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPEN-YAVKAMI 77
Cdd:PRK13650 4 IIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDV-AVFEELSVQENIDYfcGLY---VADKEKRQAlIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPR 153
Cdd:PRK13650 84 GMVFQNPdNQFVGATVEDDVAF--GLEnkgIPHEEMKER-VNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 154 LIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEiLCDQIVIMDQGQVIAKGTKESLKDMVRTADRLTI 232
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNDLLQLGL 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 491378809 233 DIPLlpdhvLATIQTTITADGIVYKEGQLqvTTTEL 268
Cdd:PRK13650 240 DIPF-----TTSLVQSLRQNGYDLPEGYL--TEKEL 268
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3-215 |
1.43e-30 |
|
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: 114.51 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDfvALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAmIGVVPQ 82
Cdd:cd03298 1 VRLDKIRFSYGE--QPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP-VSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 83 DVAVFEELSVQENIdyfcGLYVA-----DKEKRQAlIEEVIQLVGLENFVTFHPGELSGGLKRRLNIA-CGIAHKPRLIf 156
Cdd:cd03298 78 ENNLFAHLTVEQNV----GLGLSpglklTAEDRQA-IEVALARVGLAGLEKRLPGELSGGERQRVALArVLVRDKPVLL- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 157 LDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG 215
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-212 |
3.60e-30 |
|
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: 113.12 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 4 EIDKLVKRYGDFV-ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGStmtPENYAVKA-MIGVVP 81
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERRkSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 82 QDV--AVFEElSVQENIDYFCGLYVADKEKrqalIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDE 159
Cdd:cd03226 78 QDVdyQLFTD-SVREELLLGLKELDAGNEQ----AETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491378809 160 PTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVI 212
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-218 |
8.95e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.57 E-value: 8.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPENYAVKamI 77
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpiSMLSSRQLARR--L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEELSVQENIDY----FCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPR 153
Cdd:PRK11231 79 ALLPQHHLTPEGITVRELVAYgrspWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491378809 154 LIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKE 218
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-222 |
9.28e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 113.95 E-value: 9.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGT---IKLFGSTMTPENYAV----- 73
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQREGRLArdirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 74 -KAMIGVVPQDVAVFEELSVQENIDY----------FCGLYVADKEKRQALieEVIQLVGLENFVTFHPGELSGGLKRRL 142
Cdd:PRK09984 84 sRANTGYIFQQFNLVNRLSVLENVLIgalgstpfwrTCFSWFTREQKQRAL--QALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 143 NIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLK 221
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFD 241
|
.
gi 491378809 222 D 222
Cdd:PRK09984 242 N 242
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
1.36e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 114.41 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYG-----DFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTI-------KLFGSTMTP 68
Cdd:PRK13651 1 MQIKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 69 ENYAVKAMI------------------GVVPQ--DVAVFEElSVQENIDYFCGLYVADKEKRQALIEEVIQLVGL-ENFV 127
Cdd:PRK13651 81 EKVLEKLVIqktrfkkikkikeirrrvGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 128 TFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMD 207
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
250
....*....|....*.
gi 491378809 208 QGQVIAKG-TKESLKD 222
Cdd:PRK13651 240 DGKIIKDGdTYDILSD 255
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-231 |
1.83e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 112.94 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTaincMLSLL----NYDKGTIKLFG---STMTPENYAv 73
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKST----LLRALsgelSPDSGEVRLNGrplADWSPAELA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 74 kAMIGVVPQDVAVFEELSVQENIDYfcGLY--VADKEKRQALIEEVIQLVGLENFVT-FHPgELSGGLKRRLNIA---CG 147
Cdd:PRK13548 76 -RRRAVLPQHSSLSFPFTVEEVVAM--GRAphGLSRAEDDALVAAALAQVDLAHLAGrDYP-QLSGGEQQRVQLArvlAQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 148 IAH---KPRLIFLDEPTVAVDPQSRNKILESIKEL-NRQGATIV-------YTTHYmeeveilCDQIVIMDQGQVIAKGT 216
Cdd:PRK13548 152 LWEpdgPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIvvlhdlnLAARY-------ADRIVLLHQGRLVADGT 224
|
250
....*....|....*
gi 491378809 217 KESlkdmVRTADRLT 231
Cdd:PRK13548 225 PAE----VLTPETLR 235
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-220 |
4.02e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 111.52 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 6 DKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGS--TMTPENYAVKAMIGVVPQD 83
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdiSLLPLHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 84 VAVFEELSVQENIdyFCGLYVAD---KEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEP 160
Cdd:PRK10895 87 ASIFRRLSVYDNL--MAVLQIRDdlsAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 161 TVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-215 |
5.03e-29 |
|
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: 110.76 E-value: 5.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 23 LQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAV-KAMIGVVPQDVAVFEElSVQENIDYFCg 101
Cdd:cd03245 25 LTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlRRNIGYVPQDVTLFYG-TLRDNITLGA- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 102 LYVADKEkrqalIEEVIQLVGLENFVTFHP-------GE----LSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRN 170
Cdd:cd03245 103 PLADDER-----ILRAAELAGVTDFVNKHPngldlqiGErgrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491378809 171 KILESIKELNRqGATIVYTTHYMEEVEiLCDQIVIMDQGQVIAKG 215
Cdd:cd03245 178 RLKERLRQLLG-DKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-272 |
6.52e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 112.13 E-value: 6.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTP-----ENYAVKAMIGVVPQ--DVAVFEE 89
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStskqkEIKPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 90 lSVQENIDYFCGLYVADKEKRQALIEEVIQLVGL-ENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQS 168
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 169 RNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKEslkDMVRTADrltidipLLPDHVLATIQTT 248
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPS---DVFQEVD-------FLKAHELGVPKAT 249
|
250 260
....*....|....*....|....*...
gi 491378809 249 ITADGI----VYKEGQLQVTTTELNTVL 272
Cdd:PRK13643 250 HFADQLqktgAVTFEKLPITRAELVTLL 277
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
2-238 |
7.90e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.43 E-value: 7.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRY-GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPEN-YAVKAMIGV 79
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENiREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQ--DVAVFEElSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFL 157
Cdd:PRK13652 83 VFQnpDDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 158 DEPTVAVDPQSRNKILESIKEL-NRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKDMVRTADRLTIDIPL 236
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVHLDLPS 241
|
..
gi 491378809 237 LP 238
Cdd:PRK13652 242 LP 243
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-209 |
8.29e-29 |
|
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: 110.25 E-value: 8.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT---PENYavkamigVVPQDVAVFEELSVQE 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepgPDRM-------VVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 95 NIDYF--CGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKI 172
Cdd:TIGR01184 74 NIALAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 491378809 173 LESIKEL-NRQGATIVYTTHYMEEVEILCDQIVIMDQG 209
Cdd:TIGR01184 154 QEELMQIwEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-220 |
1.28e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.01 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPENYAVKAMIg 78
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlSHVPPYQRPINMMF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 vvpQDVAVFEELSVQENIDYfcGLYvADKEKR---QALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLI 155
Cdd:PRK11607 98 ---QSYALFPHMTVEQNIAF--GLK-QDKLPKaeiASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 156 FLDEPTVAVDPQSRNKI-LESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-240 |
2.10e-28 |
|
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: 110.28 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRY--GDFV-------ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPE 69
Cdd:TIGR02769 2 LLEVRDVTHTYrtGGLFgakqrapVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 70 NY-AVKAMIGVVPQDV--AVFEELSVQENI-DYFCGLYVADKEKRQALIEEVIQLVGLENFVT-FHPGELSGGLKRRLNI 144
Cdd:TIGR02769 82 QRrAFRRDVQLVFQDSpsAVNPRMTVRQIIgEPLRHLTSLDESEQKARIAELLDMVGLRSEDAdKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 145 ACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGAT-IVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKDM 223
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF 241
|
250
....*....|....*....
gi 491378809 224 VRTADRLTID--IPLLPDH 240
Cdd:TIGR02769 242 KHPAGRNLQSavLPEHPVR 260
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-206 |
3.55e-28 |
|
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: 113.54 E-value: 3.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGD-FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAV-KAMIGVV 80
Cdd:TIGR02857 322 LEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEElSVQENIdyfcglYVADKEKRQALIEEVIQLVGLENFVTFHP-------GE----LSGGLKRRLNIACGIA 149
Cdd:TIGR02857 402 PQHPFLFAG-TIAENI------RLARPDASDAEIREALERAGLDEFVAALPqgldtpiGEggagLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491378809 150 HKPRLIFLDEPTVAVDPQSRNKILESIKELnRQGATIVYTTHYMEEVEiLCDQIVIM 206
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAA-LADRIVVL 529
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-219 |
4.50e-28 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 108.56 E-value: 4.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINcMLSLLNY-DKGTIKL----FGSTMTPENYAVKA 75
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEMpRSGTLNIagnhFDFSKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 76 M---IGVVPQDVAVFEELSVQEN-IDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHK 151
Cdd:PRK11124 80 LrrnVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491378809 152 PRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHymeEVEI---LCDQIVIMDQGQVIAKGTKES 219
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTH---EVEVarkTASRVVYMENGHIVEQGDASC 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-307 |
5.05e-28 |
|
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: 114.34 E-value: 5.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYG--DFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGV 79
Cdd:TIGR01257 1937 ILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDE 159
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 160 PTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKDMVRTADRLTIDIP---- 235
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKspkd 2176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 236 -LLPDhvLATIQTTITAD--GIVYKEG-----QLQVTTTELNTvllpILTLLQAEKISY--GKIATKEATLNDVFLEITG 305
Cdd:TIGR01257 2177 dLLPD--LNPVEQFFQGNfpGSVQRERhynmlQFQVSSSSLAR----IFQLLISHKDSLliEEYSVTQTTLDQVFVNFAK 2250
|
..
gi 491378809 306 KE 307
Cdd:TIGR01257 2251 QQ 2252
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-270 |
6.39e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.12 E-value: 6.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDF--VALNHFDLQVQEGEVLGLLGPNGSGKSTA---INCMLSLLNYDKGTIKLFGSTMTPEN-YAVKA 75
Cdd:PRK13640 5 IVEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTIsklINGLLLPDDNPNSKITVDGITLTAKTvWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 76 MIGVVPQdvavfeelsvqeNID-YFCGLYVAD------------KEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRL 142
Cdd:PRK13640 85 KVGIVFQ------------NPDnQFVGATVGDdvafglenravpRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 143 NIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKEL-NRQGATIVYTTHYMEEVEiLCDQIVIMDQGQVIAKGTKESLK 221
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIF 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 491378809 222 DMVRTADRLTIDIPLLPDHVLATIQTTITADGIVYKEGQLQVTTTELNT 270
Cdd:PRK13640 232 SKVEMLKEIGLDIPFVYKLKNKLKEKGISVPQEINTEEKLVQYLCQLNS 280
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-221 |
6.55e-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: 6.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINcMLSLLNY-DKGTIKLFGS----TMTPENYAVKA 75
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLETpDSGQLNIAGHqfdfSQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 76 M---IGVVPQDVAVFEELSVQEN-IDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHK 151
Cdd:COG4161 80 LrqkVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491378809 152 PRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHymeEVEI---LCDQIVIMDQGQVIAKGTKESLK 221
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTH---EVEFarkVASQVVYMEKGRIIEQGDASHFT 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-211 |
7.53e-28 |
|
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: 107.49 E-value: 7.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRY-GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTpeNYAVKAM----- 76
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGRAIpylrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 77 -IGVVPQDVAVFEELSVQENIDYfcGLYVADKEKR--QALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPR 153
Cdd:cd03292 79 kIGVVFQDFRLLPDRNVYENVAF--ALEVTGVPPReiRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 154 LIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQV 211
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-231 |
8.22e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 108.28 E-value: 8.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPENYAvkAMIGV 79
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplAAWSPWELA--RRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEELSVQENIDYfcGLYV--ADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIA-------CGIAH 150
Cdd:COG4559 80 LPQHSSLAFPFTVEEVVAL--GRAPhgSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLArvlaqlwEPVDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 151 KPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTH-------YmeeveilCDQIVIMDQGQVIAKGTKESlkdm 223
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHdlnlaaqY-------ADRILLLHQGRLVAQGTPEE---- 226
|
....*...
gi 491378809 224 VRTADRLT 231
Cdd:COG4559 227 VLTDELLE 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-220 |
9.09e-28 |
|
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: 107.70 E-value: 9.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGD--FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYA-VKAMIGV 79
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAsLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEElSVQENIDYfcglyvADKEKRQALIEEVIQLVGLENFVTFHP-------GE----LSGGLKRRLNIACGI 148
Cdd:cd03251 81 VSQDVFLFND-TVAENIAY------GRPGATREEVEEAARAANAHEFIMELPegydtviGErgvkLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491378809 149 AHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVyTTHYMEEVEiLCDQIVIMDQGQVIAKGTKESL 220
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMKNRTTFV-IAHRLSTIE-NADRIVVLEDGKIVERGTHEEL 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
2-220 |
1.15e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 108.54 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFV-ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG-STMTPENY-AVKAMIG 78
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKLqGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 VVPQDVAV-FEELSVQENIDYFC-GLYVADKEKRQaLIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIF 156
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFGPeNLCLPPIEIRK-RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491378809 157 LDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEIlCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENV 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-211 |
1.71e-27 |
|
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: 104.99 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVA--LNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPENYavKAMI 77
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadiSQWDPNEL--GDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEElSVQENIdyfcglyvadkekrqalieeviqlvglenfvtfhpgeLSGGLKRRLNIACGIAHKPRLIFL 157
Cdd:cd03246 79 GYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491378809 158 DEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEiLCDQIVIMDQGQV 211
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
2-212 |
2.60e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 107.09 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENyavkAMIGVVP 81
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 82 QDVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPT 161
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491378809 162 VAVDPQSRNKILESIKEL-NRQGATIVYTTHYMEEVEILCDQIVIM--DQGQVI 212
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLspGPGRVV 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-216 |
3.51e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.14 E-value: 3.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGS--TMTPENYAVKAM---IGVVPQ--DVAVFEE 89
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTliTSTSKNKDIKQIrkkVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 90 lSVQENIDYFCGLYVADKEKRQALIEEVIQLVGL-ENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQS 168
Cdd:PRK13649 102 -TVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491378809 169 RNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGT 216
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-230 |
3.84e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 109.55 E-value: 3.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMtpENYAVKAM---I 77
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV--EALSARAAsrrV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEELSVQENIDY--------FCGLYVADKekrqALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIA 149
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMgrtphrsrFDTWTETDR----AAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 150 HKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESlkdmVRTADR 229
Cdd:PRK09536 156 QATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD----VLTADT 231
|
.
gi 491378809 230 L 230
Cdd:PRK09536 232 L 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-216 |
4.37e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 105.93 E-value: 4.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 10 KRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGStmtpenyaVKAMIGV----VPqdva 85
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR--------VSALLELgagfHP---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 86 vfeELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFV-----TFhpgelSGGLKRRLNIACGIAHKPRLIFLDEP 160
Cdd:COG1134 102 ---ELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIdqpvkTY-----SSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 161 TVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGT 216
Cdd:COG1134 174 LAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-220 |
9.51e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 109.91 E-value: 9.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGD--FVALNHFDLQVQEGEVLGLLGPNGSGKSTaincMLSLL--NYD--KGTIKLFGSTMT--PENyAVK 74
Cdd:PRK11160 339 LTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLLtrAWDpqQGEILLNGQPIAdySEA-ALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 75 AMIGVVPQDVAVFEElSVQENidyfcgLYVADKEKRQALIEEVIQLVGLENFVTFHPG----------ELSGGLKRRLNI 144
Cdd:PRK11160 414 QAISVVSQRVHLFSA-TLRDN------LLLAAPNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 145 ACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNrQGATIVYTTHYMEEVEILcDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQEL 560
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-222 |
2.05e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 105.30 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPE--NYAVKAM---IGVVPQ--DVAVFEEl 90
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgNKNLKKLrkkVSLVFQfpEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 91 SVQENIDY----FCglYVADKEKRQALieEVIQLVGL-ENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVD 165
Cdd:PRK13641 102 TVLKDVEFgpknFG--FSEDEAKEKAL--KWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 166 PQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGT-KESLKD 222
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASpKEIFSD 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-225 |
2.34e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 108.33 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGST---MTPEnYAVKAMIGV 79
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHK-LAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEELSVQENI-------DYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKP 152
Cdd:PRK09700 85 IYQELSVIDELTVLENLyigrhltKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491378809 153 RLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKE--SLKDMVR 225
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSdvSNDDIVR 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-220 |
2.43e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 106.34 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTpENYAVKAMIGVVPQ 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT-HRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 83 DVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491378809 163 AVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-237 |
4.69e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 104.32 E-value: 4.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 14 DFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTiKLFGSTMTPENYA-------VKAMIGVVPQ--DV 84
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDYAIPANLKkikevkrLRKEIGLVFQfpEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 85 AVFEElSVQENIDYFCGLYVADKEKRQALIEEVIQLVGL-ENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVA 163
Cdd:PRK13645 102 QLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491378809 164 VDPQSRNKILESIKELNR-QGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKDMVRTADRLTIDIPLL 237
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKeYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIEIDPPKL 255
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
14-235 |
5.03e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.48 E-value: 5.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 14 DFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPEN-----YAVKAMIGVVPQ--DVAV 86
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyiRPVRKRIGMVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 87 FEElSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLE-NFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVD 165
Cdd:PRK13646 99 FED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491378809 166 PQSRNKILESIKELN-RQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKDMVRTADRLTIDIP 235
Cdd:PRK13646 178 PQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADWHIGLP 248
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-220 |
1.13e-25 |
|
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: 101.92 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTpeNYAVKAMIGVVPQDVAVFEElSVQ 93
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidiRDIS--RKSLRSMIGVVLQDTFLFSG-TIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 94 ENIDYFcglyvaDKEKRQALIEEVIQLVGLENFVTFHP-----------GELSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:cd03254 95 ENIRLG------RPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 163 AVDPQSRNKILESIKELnRQGATIVYTTHYMEEVEiLCDQIVIMDQGQVIAKGTKESL 220
Cdd:cd03254 169 NIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIK-NADKILVLDDGKIIEEGTHDEL 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-196 |
2.02e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.39 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 11 RYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTaincmlsLLNYDKGTIKLFGSTMTpenYAVKAMIGVVPQDVAVFEEL 90
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKST-------LLKVLAGVLRPTSGTVR---RAGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 91 --SVQENIDYfcGLY-------VADKEKRqALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPT 161
Cdd:NF040873 71 plTVRDLVAM--GRWarrglwrRLTRDDR-AAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|....*
gi 491378809 162 VAVDPQSRNKILESIKELNRQGATIVYTTHYMEEV 196
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
2-227 |
2.07e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 101.49 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT--PENYAVKAMIGV 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEELSVQENIDYfcGLYVADKEKRQALIEEVIQLVG-LENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLD 158
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAM--GGFFAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491378809 159 EPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL--KDMVRTA 227
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALlaNEAVRSA 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-212 |
4.43e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 100.88 E-value: 4.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKST---AINCMLSLlnYD----KGTIKLFGstmtpEN---- 70
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDL--IPgarvEGEILLDG-----EDiydp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 71 ----YAVKAMIGVVPQDVAVFEeLSVQENIDYfcGL---YVADKEKRQALIEEVIQLVGLENFVT---FHPG-ELSGGLK 139
Cdd:COG1117 84 dvdvVELRRRVGMVFQKPNPFP-KSIYDNVAY--GLrlhGIKSKSELDEIVEESLRKAALWDEVKdrlKKSAlGLSGGQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491378809 140 RRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELnRQGATIVYTTHYMEEVEILCDQIVIMDQGQVI 212
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-211 |
8.57e-25 |
|
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: 98.27 E-value: 8.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENY--AVKAMIGVVPQD---VAVFEELS 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrdAIRAGIAYVPEDrkrEGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 92 VQENIdyfcglyvadkekrqalieeviqlvGLENFvtfhpgeLSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNK 171
Cdd:cd03215 95 VAENI-------------------------ALSSL-------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491378809 172 ILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQV 211
Cdd:cd03215 143 IYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-213 |
1.47e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.17 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENY--AVKAMIGVVPQD---VAVFEELS 91
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrdAIRAGIAYVPEDrkgEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 92 VQENI-----DYFCGLYVADKEKRQALIEEVIQLV-----GLENFVtfhpGELSGGLKRRLNIACGIAHKPRLIFLDEPT 161
Cdd:COG1129 347 IRENItlaslDRLSRGGLLDRRRERALAEEYIKRLriktpSPEQPV----GNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491378809 162 VAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIA 213
Cdd:COG1129 423 RGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-220 |
2.22e-24 |
|
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: 98.46 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPEnyAVKAMIGVVPQDVAVFEElSVQE 94
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLD--SLRRAIGVVPQDTVLFND-TIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 95 NIDYFCgLYVADKE----KRQALIEEVIQLV--GLENFVtfhpGE----LSGGLKRRLNIACGIAHKPRLIFLDEPTVAV 164
Cdd:cd03253 94 NIRYGR-PDATDEEvieaAKAAQIHDKIMRFpdGYDTIV----GErglkLSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 165 DPQSRNKILESIKELnRQGATIVYTTHYMEEVeILCDQIVIMDQGQVIAKGTKESL 220
Cdd:cd03253 169 DTHTEREIQAALRDV-SKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEEL 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-236 |
2.31e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.78 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRY---GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPEN-YAVKAMI 77
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDV-AVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIF 156
Cdd:PRK13642 84 GMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 157 LDEPTVAVDPQSRNKILESIKEL-NRQGATIVYTTHYMEEVEIlCDQIVIMDQGQVIAKGTKESLKDMVRTADRLTIDIP 235
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIkEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDVP 242
|
.
gi 491378809 236 L 236
Cdd:PRK13642 243 F 243
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-220 |
2.61e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.50 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYgDFVALnHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGS--TMTPENyavKAMIGVV 80
Cdd:PRK10771 2 LKLTDITWLY-HHLPM-RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPS---RRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEELSVQENIDYfcGLYVADK--EKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIA-CGIAHKPRLIfL 157
Cdd:PRK10771 77 FQENNLFSHLTVAQNIGL--GLNPGLKlnAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALArCLVREQPILL-L 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491378809 158 DEPTVAVDPQSRNKILESIKEL-NRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK10771 154 DEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-218 |
3.91e-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: 102.19 E-value: 3.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNY--DKGTI--------------------- 59
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 60 --KLFGSTMTPEN-----------YAVKAMIGVVPQDV-AVFEELSVQENIdyFCGL----YVADKEKRQALieEVIQLV 121
Cdd:TIGR03269 81 pcPVCGGTLEPEEvdfwnlsdklrRRIRKRIAIMLQRTfALYGDDTVLDNV--LEALeeigYEGKEAVGRAV--DLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 122 GLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKEL-NRQGATIVYTTHYMEEVEILC 200
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLS 236
|
250
....*....|....*...
gi 491378809 201 DQIVIMDQGQVIAKGTKE 218
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPD 254
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-212 |
3.93e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 3.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLfGSTMTpenyavkamIGVVP 81
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK---------IGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 82 QDVAVF-EELSVQENIDyfcglYVADKEKRQalieEVIQLvgLENFVtFHP-------GELSGGLKRRLNIACGIAHKPR 153
Cdd:COG0488 385 QHQEELdPDKTVLDELR-----DGAPGGTEQ----EVRGY--LGRFL-FSGddafkpvGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491378809 154 LIFLDEPTVAVDPQSRNKILESIKELnrQGaTIVYTTHYMEEVEILCDQIVIMDQGQVI 212
Cdd:COG0488 453 VLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
8.45e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.38 E-value: 8.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFV-ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIkLFGSTmtPENYAVKAM---- 76
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGK--PIDYSRKGLmklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 77 --IGVVPQ--DVAVFEElSVQENIDY-FCGLYVADKEKRQAlIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHK 151
Cdd:PRK13636 82 esVGMVFQdpDNQLFSA-SVYQDVSFgAVNLKLPEDEVRKR-VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 152 PRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL---KDMVRTA 227
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVfaeKEMLRKV 239
|
....*
gi 491378809 228 D-RLT 231
Cdd:PRK13636 240 NlRLP 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-213 |
1.10e-23 |
|
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: 100.67 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLL---NYDkGTIKLFGSTMTPENY--AVKAM 76
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgTWD-GEIYWSGSPLKASNIrdTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 77 IGVVPQDVAVFEELSVQENIdyFCGLYVADKEKRQAL------IEEVIQLVGLENF-VTFHPGELSGGLKRRLNIACGIA 149
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENI--FLGNEITLPGGRMAYnamylrAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491378809 150 HKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIA 213
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVA 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
10-216 |
1.51e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.38 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 10 KRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVVPQDVAVFEE 89
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKIKNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 90 L------------------SVQENIDYF-CGLYVADKEKRQaLIEEVIQLVGL-ENFVTFHPGELSGGLKRRLNIACGIA 149
Cdd:PRK13631 114 LrrrvsmvfqfpeyqlfkdTIEKDIMFGpVALGVKKSEAKK-LAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491378809 150 HKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGT 216
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-216 |
1.93e-23 |
|
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: 95.64 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGD--FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPEnyAVKAMI 77
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiSKIGLH--DLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEElSVQENIDYFCglYVADKEkrqalIEEVIQLVGLENFVTFHPGEL-----------SGGLKRRLNIAC 146
Cdd:cd03244 81 SIIPQDPVLFSG-TIRSNLDPFG--EYSDEE-----LWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 147 GIAHKPRLIFLDEPTVAVDPQSRNKILESIKElNRQGATIVYTTHYMEEVeILCDQIVIMDQGQVIAKGT 216
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTI-IDSDRILVLDKGRVVEFDS 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-222 |
2.11e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 96.76 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIkLFGSTMTPEN-----YAVKAM 76
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LFDGENIPAMsrsrlYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 77 IGVVPQDVAVFEELSVQENIDYfcglyvADKEKRQaLIEEVI--------QLVGLENFVTFHPGELSGGLKRRLNIACGI 148
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAY------PLREHTQ-LPAPLLhstvmmklEAVGLRGAAKLMPSELSGGMARRAALARAI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491378809 149 AHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKD 222
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-219 |
2.37e-23 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 96.88 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGstmTPENYAVKA-MIGVVPQdvavfeelsvQEN 95
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG---QPTRQALQKnLVAYVPQ----------SEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 96 IDYFCGLYVAD----------------KEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDE 159
Cdd:PRK15056 89 VDWSFPVLVEDvvmmgryghmgwlrraKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 160 PTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIViMDQGQVIAKGTKES 219
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTET 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-212 |
3.79e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 95.91 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 8 LVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAM----IGVVPQD 83
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrdIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 84 V--AVFEELSVQENID----YFCGLyvaDKEKRQALIEEVIQLVGL-ENFVTFHPGELSGGLKRRLNIACGIAHKPRLIF 156
Cdd:PRK10419 98 SisAVNPRKTVREIIReplrHLLSL---DKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491378809 157 LDEPTVAVDPQSRNKILESIKELNRQGAT-IVYTTHYMEEVEILCDQIVIMDQGQVI 212
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-220 |
7.68e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.24 E-value: 7.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 8 LVKRYGDF-VALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNyDKGTIKLFGSTMtpENYAVKAMIGVVPQDVAV 86
Cdd:PRK15134 291 ILKRTVDHnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPL--HNLNRRQLLPVRHRIQVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 87 FEE--------LSVQENIDYfcGLYVADK----EKRQALIEEVIQLVGLENfVTFH--PGELSGGLKRRLNIACGIAHKP 152
Cdd:PRK15134 368 FQDpnsslnprLNVLQIIEE--GLRVHQPtlsaAQREQQVIAVMEEVGLDP-ETRHryPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491378809 153 RLIFLDEPTVAVDPQSRNKILESIKEL-NRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
18-219 |
7.94e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.87 E-value: 7.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQE----GEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGST---------MTPEnyavKAMIGVVPQDV 84
Cdd:PRK11144 10 LGDLCLTVNLtlpaQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgicLPPE----KRRIGYVFQDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 85 AVFEELSVQENIDYFCglyvadKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAV 164
Cdd:PRK11144 86 RLFPHYKVRGNLRYGM------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 165 DPQSRNKILESIKELNRQGAT-IVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKES 219
Cdd:PRK11144 160 DLPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-220 |
1.01e-22 |
|
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: 97.83 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 10 KRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDkGTIKLFGSTMTP----ENYAVKAMIGVVPQDva 85
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGlsrrALRPLRRRMQVVFQD-- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 86 VFEELS--------VQEnidyfcGLYV----ADKEKRQALIEEVIQLVGL-ENFVTFHPGELSGGLKRRLNIACGIAHKP 152
Cdd:COG4172 371 PFGSLSprmtvgqiIAE------GLRVhgpgLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEP 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491378809 153 RLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:COG4172 445 KLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-220 |
1.60e-22 |
|
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: 93.76 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPEN-YAVKAMIGVVPQDVAVFEeLSVQENI 96
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNlRWLRSQIGLVSQEPVLFD-GTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 97 DYfcGLYVADKE-----KRQALIEEVIQLV--GLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSR 169
Cdd:cd03249 98 RY--GKPDATDEeveeaAKKANIHDFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491378809 170 NKILESIKELnRQGATIVYTTHYMEEVEiLCDQIVIMDQGQVIAKGTKESL 220
Cdd:cd03249 176 KLVQEALDRA-MKGRTTIVIAHRLSTIR-NADLIAVLQNGQVVEQGTHDEL 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-222 |
2.01e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.04 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPeNYAVKAMIG 78
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcARLTP-AKAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 VVPQDVAVFEELSVQENIDYfcGLyvadkEKRQALIEEVIQLVGLENfVTFHPGELSGGL----KRRLNIACGIAHKPRL 154
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILF--GL-----PKRQASMQKMKQLLAALG-CQLDLDSSAGSLevadRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 155 IFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESLKD 222
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLST 229
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-216 |
2.24e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 97.04 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 26 QEGEVLGLLGPNGSGKSTAINCMLSLLNYD---KGTIKLFGSTMTPENyaVKAMIGVVPQDVAVFEELSVQENIDYFCGL 102
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKE--MRAISAYVQQDDLFIPTLTVREHLMFQAHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 103 YVAD---KEKRQALIEEVIQLVGL---ENFVTFHPGE---LSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKIL 173
Cdd:TIGR00955 127 RMPRrvtKKEKRERVDEVLQALGLrkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491378809 174 ESIKELNRQGATIVYTTHY-MEEVEILCDQIVIMDQGQVIAKGT 216
Cdd:TIGR00955 207 QVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGS 250
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-220 |
2.34e-22 |
|
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: 97.09 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYG--DFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMtpENY---AVKAMI 77
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL--ADYtlaSLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEElSVQENIDYFCGLYVADKEkrqalIEEVIQLVGLENFVTFHP-----------GELSGGLKRRLNIAC 146
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYGRTEQADRAE-----IERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIAR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491378809 147 GIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVyTTHYMEEVEiLCDQIVIMDQGQVIAKGTKESL 220
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLV-IAHRLSTIE-KADRIVVMDDGRIVERGTHNEL 554
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
6-226 |
2.47e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.87 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 6 DKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAV-----KAMIGVV 80
Cdd:PRK10070 32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrRKKIAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEP 160
Cdd:PRK10070 112 FQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491378809 161 TVAVDPQSRNKILESIKELN-RQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL-----KDMVRT 226
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIlnnpaNDYVRT 263
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-220 |
3.10e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.54 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYD--KGTIKLFGSTMTPENY--AVKAMI 77
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIrdTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEELSVQENIdyFCG-----LYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKP 152
Cdd:PRK13549 85 AIIHQELALVKELSVLENI--FLGneitpGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 153 RLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-213 |
3.82e-22 |
|
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: 92.50 E-value: 3.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGD----FVALNHFDLQVQEGEVLGLLGPNGSGKSTaincMLSLL----NYDKGTIKLFGSTMTPEN--- 70
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKST----LLGLLagldRPTSGTVRLAGQDLFALDeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 71 -YAVKA-MIGVVPQDVAVFEELSVQENidyfcglyVA-------DKEKRQAlIEEVIQLVGLENFVTFHPGELSGGLKRR 141
Cdd:COG4181 84 rARLRArHVGFVFQSFQLLPTLTALEN--------VMlplelagRRDARAR-ARALLERVGLGHRLDHYPAQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491378809 142 LNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNR-QGATIVYTTHymeEVEIL--CDQIVIMDQGQVIA 213
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTH---DPALAarCDRVLRLRAGRLVE 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-211 |
4.12e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.10 E-value: 4.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 10 KRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTpENYAVKAMIGVVPQDVAVFEE 89
Cdd:PRK11000 11 KAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-DVPPAERGVGMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 90 LSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSR 169
Cdd:PRK11000 90 LSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491378809 170 NKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQV 211
Cdd:PRK11000 170 VQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-220 |
4.28e-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: 92.55 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYG--DFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTM-TPENYAVKAMIGV 79
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEElSVQENIDyfcglyVADKEKRQALIEEVIQLVGLENFVTFHP-------GE----LSGGLKRRLNIACGI 148
Cdd:cd03252 81 VLQENVLFNR-SIRDNIA------LADPGMSMERVIEAAKLAGAHDFISELPegydtivGEqgagLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491378809 149 AHKPRLIFLDEPTVAVDPQSRNKILESIKELNrQGATIVYTTHYMEEVEiLCDQIVIMDQGQVIAKGTKESL 220
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVK-NADRIIVMEKGRIVEQGSHDEL 223
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-218 |
7.07e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 92.07 E-value: 7.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPENYAVKamIGV 79
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvATTPSRELAKR--LAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEELSVQENIDYfcGLY--------VADKEKrqalIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHK 151
Cdd:COG4604 80 LRQENHINSRLTVRELVAF--GRFpyskgrltAEDREI----IDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 152 PRLIFLDEPTVAVDPQ-SRN--KILESI-KELNRqgaTIV-------YTTHYmeeveilCDQIVIMDQGQVIAKGTKE 218
Cdd:COG4604 154 TDYVLLDEPLNNLDMKhSVQmmKLLRRLaDELGK---TVVivlhdinFASCY-------ADHIVAMKDGRVVAQGTPE 221
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-225 |
9.48e-22 |
|
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: 95.20 E-value: 9.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 16 VALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTM---TPENYAvkAMIGVVPQDVAVFEElSV 92
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwDREELG--RHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 93 QENIDYFCGlyvADKEKrqalIEEVIQLVGLENFV--------TfHPGE----LSGGLKRRLNIACGIAHKPRLIFLDEP 160
Cdd:COG4618 423 AENIARFGD---ADPEK----VVAAAKLAGVHEMIlrlpdgydT-RIGEggarLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 161 TVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEIlCDQIVIMDQGQVIAKGTK-ESLKDMVR 225
Cdd:COG4618 495 NSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRdEVLARLAR 559
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-215 |
1.33e-21 |
|
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: 90.79 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKST---AINCMLSLLNYDKGTIKLFGSTMTPenYAVKAMIGVVPQDVAVFEELSVQE 94
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNGQPRKP--DQFQKCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 95 NIdYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGE-----LSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSR 169
Cdd:cd03234 101 TL-TYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGnlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491378809 170 NKILESIKELNRQGATIVYTTHY-MEEVEILCDQIVIMDQGQVIAKG 215
Cdd:cd03234 180 LNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-257 |
3.31e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.97 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRY-GD-FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYA-VKAMIG 78
Cdd:PRK13648 7 IIVFKNVSFQYqSDaSFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEkLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 VVPQDVA-VFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFL 157
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 158 DEPTVAVDPQSRNKILESIKELNR-QGATIVYTTHYMEEVeILCDQIVIMDQGQVIAKGTKESLKDMVRTADRLTIDIP- 235
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSeHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEIFDHAEELTRIGLDLPf 245
|
250 260
....*....|....*....|...
gi 491378809 236 -LLPDHVLATIQTTITADGIVYK 257
Cdd:PRK13648 246 pIKINQMLGHQTSFLTYEGLVDQ 268
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-210 |
3.47e-21 |
|
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: 89.80 E-value: 3.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRygdFV----------ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSllNY--DKGTIkLFGSTMTPE 69
Cdd:COG4778 4 LLEVENLSKT---FTlhlqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG--NYlpDSGSI-LVRHDGGWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 70 NYAV----------KAMIGVVPQ-----------DVaVFEELsvqenidyfcglyVADKEKRQALIEEVIQLvgLENF-- 126
Cdd:COG4778 78 DLAQaspreilalrRRTIGYVSQflrviprvsalDV-VAEPL-------------LERGVDREEARARAREL--LARLnl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 127 ---------VTFhpgelSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVE 197
Cdd:COG4778 142 perlwdlppATF-----SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVRE 216
|
250
....*....|...
gi 491378809 198 ILCDQIVIMDQGQ 210
Cdd:COG4778 217 AVADRVVDVTPFS 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-215 |
3.92e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 88.52 E-value: 3.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 14 DFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVVPQDVAVFEElSVQ 93
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT-TLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 94 ENIdyfcglyvadkekrqalieeviqlvGLEnfvtfhpgeLSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKIL 173
Cdd:cd03247 93 NNL-------------------------GRR---------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491378809 174 ESIKELNRqGATIVYTTHYMEEVEILcDQIVIMDQGQVIAKG 215
Cdd:cd03247 139 SLIFEVLK-DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-212 |
5.47e-21 |
|
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: 88.62 E-value: 5.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFV--ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPEnyAVKAMI 77
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidiSTIPLE--DLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEElSVQENIDYFcGLYvADKEKRQAL-IEEviqlvGLENfvtfhpgeLSGGLKRRLNIACGIAHKPRLIF 156
Cdd:cd03369 85 TIIPQDPTLFSG-TIRSNLDPF-DEY-SDEEIYGALrVSE-----GGLN--------LSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 157 LDEPTVAVDPQSRNKILESIKELnRQGATIVYTTHYMEEVeILCDQIVIMDQGQVI 212
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREE-FTNSTILTIAHRLRTI-IDYDKILVMDAGEVK 202
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-215 |
5.66e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.90 E-value: 5.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYD-----KGTIKLFGSTMTPENY---AVK 74
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVdpiEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 75 AMIGVVPQDVAVFEELSVQENIDY---FCGLYVADKE---------KRQALIEEViqlvglENFVTFHPGELSGGLKRRL 142
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIgvkLNGLVKSKKEldervewalKKAALWDEV------KDRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491378809 143 NIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQgATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG 215
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-220 |
1.04e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.46 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 28 GEVLGLLGPNGSGKSTaincMLSLLNYDK----GTIKLFGSTMtpENYAVKAM---IGVVPQDVAVFEELSVQENIDyfC 100
Cdd:PRK10575 37 GKVTGLIGHNGSGKST----LLKMLGRHQppseGEILLDAQPL--ESWSSKAFarkVAYLPQQLPAAEGMTVRELVA--I 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 101 GLY----------VADKEKrqalIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRN 170
Cdd:PRK10575 109 GRYpwhgalgrfgAADREK----VEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491378809 171 KILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK10575 185 DVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-211 |
1.16e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.97 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 5 IDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIkLFGSTMTPEnyaVKAMIGVVPQDV 84
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAE---AREDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 85 AVFEELSVQENIdyfcGLYVADKEKRQALieEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAV 164
Cdd:PRK11247 91 RLLPWKKVIDNV----GLGLKGQWRDAAL--QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491378809 165 DPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQV 211
Cdd:PRK11247 165 DALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-222 |
1.33e-20 |
|
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: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 25 VQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTP-ENYAVKAMIGVVPQDVAVFEElSVQENIDYfcGLY 103
Cdd:TIGR00958 504 LHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLFSG-SVRENIAY--GLT 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 104 VADKEKRQAlieeVIQLVGLENFVTFHP-------GE----LSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKI 172
Cdd:TIGR00958 581 DTPDEEIMA----AAKAANAHDFIMEFPngydtevGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491378809 173 LESIKelnRQGATIVYTTHYMEEVEiLCDQIVIMDQGQVIAKGTKESLKD 222
Cdd:TIGR00958 657 QESRS---RASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLME 702
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-220 |
1.71e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 91.81 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPEnyAVKAMIGVVPQDVAVFEElSVQE 94
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDVTQA--SLRAAIGIVPQDTVLFND-TIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 95 NIDYfcglyvADKEKRQALIEEVIQLVGLENFVTFHP-------GE----LSGGLKRRLNIACGIAHKPRLIFLDEPTVA 163
Cdd:COG5265 451 NIAY------GRPDASEEEVEAAARAAQIHDFIESLPdgydtrvGErglkLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491378809 164 VDPQSRNKILESIKELNRQGATIVyTTHYMEEVeILCDQIVIMDQGQVIAKGTKESL 220
Cdd:COG5265 525 LDSRTERAIQAALREVARGRTTLV-IAHRLSTI-VDADEILVLEAGRIVERGTHAEL 579
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-220 |
1.87e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.49 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT--------------P 68
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 69 ENYAVKAMIGVVPQDVAVFEELSVQENID----YFCGLYVADKEKRQaliEEVIQLVGL-ENFVTFHPGELSGGLKRRLN 143
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMeapiQVLGLSKQEARERA---VKYLAKVGIdERAQGKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491378809 144 IACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-215 |
2.09e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.53 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 11 RYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGStmtPENYAVKAMIGVVPQDVAVFEEL 90
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYSKRGLLALRQQVATVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 91 SVQ---ENIDY-----FCGLYVADKEKRQAlIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:PRK13638 87 EQQifyTDIDSdiafsLRNLGVPEAEITRR-VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491378809 163 AVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG 215
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-220 |
2.64e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 91.02 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRY-----GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIK-LFGST---MT---PE 69
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEwvdMTkpgPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 70 NYA-VKAMIGVVPQDVAVFEELSVQENIDYFCGLYVADK-EKRQALIeeVIQLVGL-----ENFVTFHPGELSGGLKRRL 142
Cdd:TIGR03269 359 GRGrAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDElARMKAVI--TLKMVGFdeekaEEILDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 143 NIACGIAHKPRLIFLDEPTVAVDPQSRNKILESI----KELNRqgaTIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKE 218
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQ---TFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
..
gi 491378809 219 SL 220
Cdd:TIGR03269 514 EI 515
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-218 |
6.13e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 87.14 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKST---AINCMlSLLNYD---KGTIKLFGSTM-TPENYAV- 73
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTllrSINRM-NDLNPEvtiTGSIVYNGHNIySPRTDTVd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 74 -KAMIGVVPQDVAVFEeLSVQENIDYfcGLYVA---DKEKRQALIEEVIQLVGLENFVTFHPGE----LSGGLKRRLNIA 145
Cdd:PRK14239 84 lRKEIGMVFQQPNPFP-MSIYENVVY--GLRLKgikDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491378809 146 CGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELnRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG-TKE 218
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNdTKQ 233
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-191 |
6.26e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.70 E-value: 6.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYA-VKAMIGv 79
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeACHYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 vPQDvAVFEELSVQENIDYFCGLYVAdkekRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIA-CGIAHKPRLIfLD 158
Cdd:PRK13539 80 -HRN-AMKPALTVAENLEFWAAFLGG----EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALArLLVSNRPIWI-LD 152
|
170 180 190
....*....|....*....|....*....|...
gi 491378809 159 EPTVAVDPQSRNKILESIKELNRQGATIVYTTH 191
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-212 |
6.49e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 6.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 5 IDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIklfgsTMTPenyavKAMIGVVPQDV 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-----SIPK-----GLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 85 AVFEELSVQENI-DYFCGLYVADKEKRQAL-------------------------------IEEVIQLVGLENFVTFHP- 131
Cdd:COG0488 71 PLDDDLTVLDTVlDGDAELRALEAELEELEaklaepdedlerlaelqeefealggweaearAEEILSGLGFPEEDLDRPv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 132 GELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDpqsrnkiLESIKEL-----NRQGATIVyTTH---YMEEVeilCDQI 203
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEWLeeflkNYPGTVLV-VSHdryFLDRV---ATRI 219
|
....*....
gi 491378809 204 VIMDQGQVI 212
Cdd:COG0488 220 LELDRGKLT 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-191 |
8.76e-20 |
|
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: 89.34 E-value: 8.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 13 GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG-STMTPENYAVKAMIGVVPQDVAVFEElS 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvPVSSLDQDEVRRRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 92 VQENidyfcgLYVADKEKRQALIEEVIQLVGLENFVTFHP-------GE----LSGGLKRRLNIACGIAHKPRLIFLDEP 160
Cdd:TIGR02868 425 VREN------LRLARPDATDEELWAALERVGLADWLRALPdgldtvlGEggarLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|.
gi 491378809 161 TVAVDPQSRNKILESIKELNrQGATIVYTTH 191
Cdd:TIGR02868 499 TEHLDAETADELLEDLLAAL-SGRTVVLITH 528
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-211 |
1.25e-19 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 85.60 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 14 DFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTP-ENYAVKAMIGVVPQDVAVFEElSV 92
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 93 QENIDYfcGLYVADKEKrqalIEEVIQLVGLENFVTFHP-----------GELSGGLKRRLNIACGIAHKPRLIFLDEPT 161
Cdd:cd03248 105 QDNIAY--GLQSCSFEC----VKEAAQKAHAHSFISELAsgydtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491378809 162 VAVDPQSRNKILESIKELNRQgATIVYTTHYMEEVEiLCDQIVIMDQGQV 211
Cdd:cd03248 179 SALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-220 |
1.63e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 88.75 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 22 DLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYdKGTIKLFG---STMTPENYavKAMIGVVPQDVAVFEElSVQENIdy 98
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGielRELDPESW--RKHLSWVGQNPQLPHG-TLRDNV-- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 99 fcglYVADKEKRQALIEEVIQLVGLENFVTFHP-------GE----LSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQ 167
Cdd:PRK11174 444 ----LLGNPDASDEQLQQALENAWVSEFLPLLPqgldtpiGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491378809 168 SRNKILESIKElNRQGATIVYTTHYMEEVEiLCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK11174 520 SEQLVMQALNA-ASRRQTTLMVTHQLEDLA-QWDQIWVMQDGQIVQQGDYAEL 570
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-220 |
2.21e-19 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 86.71 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRY---GDFV--------ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMT 67
Cdd:COG4608 7 LLEVRDLKKHFpvrGGLFgrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGqdiTGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 68 PEnyAVKAM---IGVVPQD----------VA--VFEELSVQEnidyfcglyVADKEKRQALIEEVIQLVGL-ENFVTFHP 131
Cdd:COG4608 87 GR--ELRPLrrrMQMVFQDpyaslnprmtVGdiIAEPLRIHG---------LASKAERRERVAELLELVGLrPEHADRYP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 132 GELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQ 210
Cdd:COG4608 156 HEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGK 235
|
250
....*....|
gi 491378809 211 VIAKGTKESL 220
Cdd:COG4608 236 IVEIAPRDEL 245
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
2-218 |
3.39e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 86.33 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGD----FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKgtiKLFGSTMTPENYAVKAMI 77
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPG---RVMAEKLEFNGQDLQRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 -----GVVPQDVA-VFEELSVQENIDYFCGLYVAD----------KEKRQALIEeVIQLVGL---ENFVTFHPGELSGGL 138
Cdd:PRK11022 80 ekerrNLVGAEVAmIFQDPMTSLNPCYTVGFQIMEaikvhqggnkKTRRQRAID-LLNQVGIpdpASRLDVYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 139 KRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTK 217
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
.
gi 491378809 218 E 218
Cdd:PRK11022 239 H 239
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-220 |
5.64e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 84.33 E-value: 5.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTM-------TPENYAVK 74
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 75 AMIGVVPQDVAVFEELSVQENIDYFCGLY-VADKEKRQALIEEVIQLVGL----ENFVTFHPGELSGGLKRRLNIACGIA 149
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHgIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491378809 150 HKPRLIFLDEPTVAVDPQSRNKILESIKELNRQgATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-212 |
7.03e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 84.37 E-value: 7.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 16 VALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT--PEnYAVKAMIGVVPQDVAV--FEELS 91
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklPE-YKRAKYIGRVFQDPMMgtAPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 92 VQENidyfcgLYVA-------------DKEKRQALIEEVIQL-VGLENFVTFHPGELSGGlkRRLNIACGIA--HKPRLI 155
Cdd:COG1101 99 IEEN------LALAyrrgkrrglrrglTKKRRELFRELLATLgLGLENRLDTKVGLLSGG--QRQALSLLMAtlTKPKLL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 156 FLDEPTVAVDPQSRNKILESIKEL-NRQGATIVYTTHYMEEVEILCDQIVIMDQGQVI 212
Cdd:COG1101 171 LLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-210 |
2.30e-18 |
|
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: 81.36 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 22 DLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGStmtpenyavkamIGVVPQdVAVFEELSVQENIdyfCG 101
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQ-EPWIQNGTIRENI---LF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 102 LYVADKEKrqalIEEVIQLVGLEN-FVTFHPGE----------LSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRN 170
Cdd:cd03250 89 GKPFDEER----YEKVIKACALEPdLEILPDGDlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491378809 171 KILES-IKELNRQGATIVYTTHymeEVEIL--CDQIVIMDQGQ 210
Cdd:cd03250 165 HIFENcILGLLLNNKTRILVTH---QLQLLphADQIVVLDNGR 204
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-191 |
3.81e-18 |
|
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: 80.87 E-value: 3.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPENYAVKAMIGV 79
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPqdvAVFEELSVQENIDYFCglyvADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDE 159
Cdd:TIGR01189 81 LP---GLKPELSALENLHFWA----AIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|...
gi 491378809 160 PTVAVDPQSRNKILESIKE-LNRQGATIVyTTH 191
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAhLARGGIVLL-TTH 185
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-213 |
4.10e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.28 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT---PENyAVKAMIGVVPQDVAVFEELSVQ 93
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPKS-SQEAGIGIIHQELNLIPQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 94 ENIdyFCGLYVADKEKR---QALIEEVIQLVGLENfVTFHP----GELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDP 166
Cdd:PRK10762 98 ENI--FLGREFVNRFGRidwKKMYAEADKLLARLN-LRFSSdklvGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491378809 167 QSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIA 213
Cdd:PRK10762 175 TETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIA 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-230 |
4.59e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.19 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 4 EIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTaincMLSLL--NY--DKGTIKL------FGSTMTpenyAV 73
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKST----LLKILsgNYqpDAGSILIdgqemrFASTTA----AL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 74 KAMIGVVPQDVAVFEELSVQENIdyFCG-----LYVADkekRQALIEEV-IQLVGLEnfVTFHP----GELSGGLKRRLN 143
Cdd:PRK11288 78 AAGVAIIYQELHLVPEMTVAENL--YLGqlphkGGIVN---RRLLNYEArEQLEHLG--VDIDPdtplKYLSIGQRQMVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 144 IACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAkgTKESLKDM 223
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA--TFDDMAQV 228
|
....*..
gi 491378809 224 VRtaDRL 230
Cdd:PRK11288 229 DR--DQL 233
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-195 |
5.30e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.75 E-value: 5.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINC---MLSLLN----------YDKgtiKLFGSTMTP 68
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPgfrvegkvtfHGK---NLYAPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 69 enYAVKAMIGVVPQDVAVFEElSVQENIDYFCGL--YVADKE-------KRQALIEEV---IQLVGLEnfvtfhpgeLSG 136
Cdd:PRK14243 87 --VEVRRRIGMVFQKPNPFPK-SIYDNIAYGARIngYKGDMDelverslRQAALWDEVkdkLKQSGLS---------LSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491378809 137 GLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQgATIVYTTHYMEE 195
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQ 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-235 |
9.61e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 83.62 E-value: 9.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPENYAV--KAMIGVVPQDVAVFEELSV 92
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdvATLDADALAQlrREHFGFIFQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 93 QENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKI 172
Cdd:PRK10535 104 AQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491378809 173 LESIKELNRQGATIVYTTHyMEEVEILCDQIVIMDQGQVIAKGTKESLKDMVRTADRLTIDIP 235
Cdd:PRK10535 184 MAILHQLRDRGHTVIIVTH-DPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTEPVVNTAS 245
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
12-191 |
9.71e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 79.99 E-value: 9.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 12 YGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVVPQDVAVFEELS 91
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 92 VQENidyfCgLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNK 171
Cdd:PRK13540 91 LREN----C-LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|
gi 491378809 172 ILESIKELNRQGATIVYTTH 191
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSH 185
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-191 |
1.77e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.86 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGD----FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAM- 76
Cdd:PRK11629 5 LLQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 77 ----IGVVPQDVAVFEELSVQENIDYfcGLYVADKEKRQA--LIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAH 150
Cdd:PRK11629 85 rnqkLGFIYQFHHLLPDFTALENVAM--PLLIGKKKPAEInsRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491378809 151 KPRLIFLDEPTVAVDPQSRNKILESIKELN-RQGATIVYTTH 191
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTH 204
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-191 |
1.82e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 79.82 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGD----FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAM- 76
Cdd:PRK10584 6 IVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 77 ----IGVVPQDVAVFEELSVQENIDYFCGLY-VADKEKRQALIEEVIQLvGLENFVTFHPGELSGGLKRRLNIACGIAHK 151
Cdd:PRK10584 86 rakhVGFVFQSFMLIPTLNALENVELPALLRgESSRQSRNGAKALLEQL-GLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491378809 152 PRLIFLDEPTVAVDPQSRNKILESIKELNR-QGATIVYTTH 191
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNReHGTTLILVTH 205
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-211 |
1.82e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 81.43 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRY-GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPENYAVkAMig 78
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvNELEPADRDI-AM-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 vVPQDVAVFEELSVQENIDYfcGLYVA--DKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRlnIACG--IAHKPRL 154
Cdd:PRK11650 81 -VFQNYALYPHMSVRENMAY--GLKIRgmPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQR--VAMGraIVREPAV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 155 IFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQV 211
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-220 |
2.76e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.03 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 6 DKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMtpENYAVKAM---IGVVPQ 82
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI--QHYASKEVarrIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 83 DVAVFEELSVQENIDY----FCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLD 158
Cdd:PRK10253 89 NATTPGDITVQELVARgrypHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491378809 159 EPTVAVDPQSRNKILESIKELNR-QGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-211 |
4.62e-17 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 81.48 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTmtpenyavkAMIGVvpqDVAVFEELSVQENI 96
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA---------ALIAI---SSGLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 97 DYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESI 176
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190
....*....|....*....|....*....|....*
gi 491378809 177 KELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQV 211
Cdd:PRK13545 187 NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-218 |
1.07e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.03 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLN-YDKGTIK---------LFGSTMTPENYA 72
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElYPEARVSgevyldgqdIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 73 VKaMIGVVPQDVAvfeELSVQENIDYFCGL--YVADKEKRQALIEEVIQLVGL----ENFVTFHPGELSGGLKRRLNIAC 146
Cdd:PRK14247 84 VQ-MVFQIPNPIP---NLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491378809 147 GIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQgATIVYTTHYMEEVEILCDQIVIMDQGQVIAKG-TKE 218
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGpTRE 231
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-274 |
1.52e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.92 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 28 GEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKaMIGVVPQDVAVFEELSVQENIdYFCGLY---- 103
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILK-RTGFVTQDDILYPHLTVRETL-VFCSLLrlpk 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 104 VADKEKRQALIEEVIQLVGL---ENFV---TFHPGeLSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIK 177
Cdd:PLN03211 172 SLTKQEKILVAESVISELGLtkcENTIignSFIRG-ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 178 ELNRQGATIVYTTHY-MEEVEILCDQIVIMDQGQVIAKGtKESLKDMVRTADRLTIDIPLLP-DHVLATIQTTITADGIV 255
Cdd:PLN03211 251 SLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG-KGSDAMAYFESVGFSPSFPMNPaDFLLDLANGVCQTDGVS 329
|
250 260
....*....|....*....|.
gi 491378809 256 YKE--GQLQVTTTELNTVLLP 274
Cdd:PLN03211 330 EREkpNVKQSLVASYNTLLAP 350
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-210 |
1.71e-16 |
|
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: 74.79 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLfGSTMTpenyavkamIGVVPQ 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK---------IGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 83 dvavfeelsvqenidyfcglyvadkekrqalieeviqlvglenfvtfhpgeLSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491378809 163 AVDPQSRNKILESIKELNRqgaTIVYTTH---YMEEVeilCDQIVIMDQGQ 210
Cdd:cd03221 100 HLDLESIEALEEALKEYPG---TVILVSHdryFLDQV---ATKIIELEDGK 144
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-191 |
2.03e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 75.99 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVVPQ 82
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 83 DVAVFEELSVQENIDYFCGLYVADKekrqalIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180
....*....|....*....|....*....
gi 491378809 163 AVDPQSRNKILESIKELNRQGATIVYTTH 191
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-231 |
2.81e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.80 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 21 FDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYdKGTIKLFG---STMTPENYAVK-AMIG---VVPQDVAVFEELSvq 93
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGrplSDWSAAELARHrAYLSqqqSPPFAMPVFQYLA-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 94 enidyfcgLY---VADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIAC-------GIAHKPRLIFLDEPTVA 163
Cdd:COG4138 92 --------LHqpaGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAvllqvwpTINPEGQLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 164 VDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESlkdmVRTADRLT 231
Cdd:COG4138 164 LDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE----VMTPENLS 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-213 |
2.87e-16 |
|
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: 79.10 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTAINCML-SLLNYDKGTIKLFGSTMTPEN--YAVKAMIGVVPQDV---AVFEELS 91
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFgAYPGKFEGNVFINGKPVDIRNpaQAIRAGIAMVPEDRkrhGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 92 VQENI-----DYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHP-GELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVD 165
Cdd:TIGR02633 356 VGKNItlsvlKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491378809 166 PQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIA 213
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-220 |
4.82e-16 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 78.63 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYG-DFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTP-ENYAVKAMIGVV 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEElSVQENidyfcgLYVADKEKrqALIEEVIQLV--------------GLENFVTFHPGELSGGLKRRLNIAC 146
Cdd:TIGR01193 554 PQEPYIFSG-SILEN------LLLGAKEN--VSQDEIWAACeiaeikddienmplGYQTELSEEGSSISGGQKQRIALAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491378809 147 GIAHKPRLIFLDEPTVAVDPQSRNKILESIkeLNRQGATIVYTTHYMeEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNL--LNLQDKTIIFVAHRL-SVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-220 |
5.60e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.89 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 20 HFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLL----NYDKGTIKLFGSTMTPENYAVKAMIGVVPQDVAVFEELS---- 91
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPVAPCALRGRKIATIMQNPRSAFNPLHtmht 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 92 -VQENidyfcgLYVADKEKRQALIEEVIQLVGLEN---FVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQ 167
Cdd:PRK10418 101 hARET------CLALGKPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491378809 168 SRNKILESIKELNR-QGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK10418 175 AQARILDLLESIVQkRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-220 |
6.20e-16 |
|
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: 77.80 E-value: 6.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGD----FVALNHFDLQVQEGEVLGLLGPNGSGKS-TAincmLSLLN-------YDKGTIKLFGSTMT-- 67
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTA----LSILRllpdpaaHPSGSILFDGQDLLgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 68 PEnyavKAMIGVVPQDVA-VFEE------------------LSVQENIDyfcglyvadKEKRQALIEEVIQLVGL---EN 125
Cdd:COG4172 82 SE----RELRRIRGNRIAmIFQEpmtslnplhtigkqiaevLRLHRGLS---------GAAARARALELLERVGIpdpER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 126 FVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIV 204
Cdd:COG4172 149 RLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVA 228
|
250
....*....|....*.
gi 491378809 205 IMDQGQVIAKGTKESL 220
Cdd:COG4172 229 VMRQGEIVEQGPTAEL 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-211 |
6.93e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 6.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRygDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPEN--YAVKAMIGV 79
Cdd:PRK09700 265 VFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSplDAVKKGMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQ---DVAVFEELSVQENIDY-----------FCGLYVADKEKRQAliEEVIQLVGLE-NFVTFHPGELSGGLKRRLNI 144
Cdd:PRK09700 343 ITEsrrDNGFFPNFSIAQNMAIsrslkdggykgAMGLFHEVDEQRTA--ENQRELLALKcHSVNQNITELSGGNQQKVLI 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491378809 145 ACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQV 211
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-204 |
7.93e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.14 E-value: 7.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPENYavKAMI 77
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGediSTLKPEIY--RQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEElSVQENIdYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFL 157
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNL-IFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491378809 158 DEPTVAVDPQSRNKILESIKELNR-QGATIVYTTHYMEEVEiLCDQIV 204
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVReQNIAVLWVTHDKDEIN-HADKVI 208
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-240 |
1.63e-15 |
|
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: 74.89 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRY--GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDkGTIKLFG---STMTPENYavKAMI 77
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGvswNSVPLQKW--RKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEElSVQENID-YFCG-----LYVADKEKRQALIEeviQLVGLENFVTFHPG-ELSGGLKRRLNIACGIAH 150
Cdd:cd03289 80 GVIPQKVFIFSG-TFRKNLDpYGKWsdeeiWKVAEEVGLKSVIE---QFPGQLDFVLVDGGcVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 151 KPRLIFLDEPTVAVDPQSRNKILESIKElNRQGATIVYTTHYMEEVeILCDQIVIMDQGQV-----IAK--GTKESLKDM 223
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAM-LECQRFLVIEENKVrqydsIQKllNEKSHFKQA 233
|
250
....*....|....*..
gi 491378809 224 VRTADRLTidipLLPDH 240
Cdd:cd03289 234 ISPSDRLK----LFPRR 246
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-213 |
1.70e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 76.69 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTM--TPENYAVKAMIGVVPQDVAVFEELSVQE 94
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKEALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 95 NIdyFCGLY-----VADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSR 169
Cdd:PRK10982 93 NM--WLGRYptkgmFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491378809 170 NKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIA 213
Cdd:PRK10982 171 NHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-191 |
1.89e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 77.07 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 13 GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLN--YDKGTIKLFGSTMTPENYAvkAMIGVVPQDVAVFEEL 90
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgVITGGDRLVNGRPLDSSFQ--RSIGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 91 SVQENIDYFCGL----YVADKEKRQaLIEEVIQLVGLENFVTFHPGELSGGL----KRRLNIACGIAHKPR-LIFLDEPT 161
Cdd:TIGR00956 852 TVRESLRFSAYLrqpkSVSKSEKME-YVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKlLLFLDEPT 930
|
170 180 190
....*....|....*....|....*....|
gi 491378809 162 VAVDPQSRNKILESIKELNRQGATIVYTTH 191
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-220 |
2.68e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.05 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAV--------KAMIGVVPQDVA-VF 87
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVielseqsaAQMRHVRGADMAmIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 88 EELSVQENIDYFCGLYVADK-------EKRQALIE-----EVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLI 155
Cdd:PRK10261 111 QEPMTSLNPVFTVGEQIAESirlhqgaSREEAMVEakrmlDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 156 FLDEPTVAVDPQSRNKILESIKELNRQGAT-IVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
14-220 |
2.69e-15 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 74.08 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 14 DFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGStmtpenyavkamIGVVPQDVAVFEELSVQ 93
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE------------VSVIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 94 ENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKIL 173
Cdd:PRK13546 104 ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491378809 174 ESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK13546 184 DKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-231 |
3.77e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.43 E-value: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 21 FDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYdKGTIKLFG---STMTPENYAVK----AMIGVVPQDVAVFEELSvq 93
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGqplEAWSAAELARHraylSQQQTPPFAMPVFQYLT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 94 enidyfcgLYVADK---EKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGI-----AHKP--RLIFLDEPTVA 163
Cdd:PRK03695 92 --------LHQPDKtrtEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 164 VDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESlkdmVRTADRLT 231
Cdd:PRK03695 164 LDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE----VLTPENLA 227
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
3-221 |
5.13e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 74.17 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKlvkRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNyDKGTIKL----FGS----TMTPEnyAVK 74
Cdd:COG4170 11 IEIDT---PQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTAdrfrWNGidllKLSPR--ERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 75 AMIGvvpQDVA-VFEELS------------VQENID--YFCGLYVadkEKRQALIEEVIQL---VGLENfvtfH------ 130
Cdd:COG4170 85 KIIG---REIAmIFQEPSscldpsakigdqLIEAIPswTFKGKWW---QRFKWRKKRAIELlhrVGIKD----Hkdimns 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 131 -PGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNR-QGATIVYTTHYMEEVEILCDQIVIMDQ 208
Cdd:COG4170 155 yPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYC 234
|
250
....*....|...
gi 491378809 209 GQVIAKGTKESLK 221
Cdd:COG4170 235 GQTVESGPTEQIL 247
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2-222 |
5.62e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.04 E-value: 5.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAvkAM----- 76
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLY--ALseaer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 77 -------IGVVPQDVA------------VFEELSVQENIDYfcglyvaDKEKRQAL--IEEV-IQLVGLENfvtfHPGEL 134
Cdd:PRK11701 84 rrllrteWGFVHQHPRdglrmqvsaggnIGERLMAVGARHY-------GDIRATAGdwLERVeIDAARIDD----LPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 135 SGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIA 213
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
250
....*....|
gi 491378809 214 KG-TKESLKD 222
Cdd:PRK11701 233 SGlTDQVLDD 242
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
2-211 |
6.02e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.60 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRY-GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT----PENYAVKAM 76
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 77 IGVVPQDVAVFEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIF 156
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491378809 157 LDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQV 211
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-223 |
1.35e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.98 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYD--KGTIKLFGSTMTPENYAVKAMIGV 79
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VpqdvavfeeLSVQ--------ENIDYfcgLYVADKEKRQA-------------LIEEVIQLVGL-ENFVTFHPGE-LSG 136
Cdd:CHL00131 87 F---------LAFQypieipgvSNADF---LRLAYNSKRKFqglpeldplefleIINEKLKLVGMdPSFLSRNVNEgFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 137 GLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVE-ILCDQIVIMDQGQVIAKG 215
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDyIKPDYVHVMQNGKIIKTG 234
|
....*...
gi 491378809 216 TKESLKDM 223
Cdd:CHL00131 235 DAELAKEL 242
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-225 |
1.38e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 73.98 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENY-AVKAMIGVVPQDVAVFEElSVQEN 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLdSWRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 96 IDYFCglyvadKEKRQALIEEVIQLVGLENFVTFHP-------GE----LSGGLKRRLNIACGIAHKPRLIFLDEPTVAV 164
Cdd:PRK10789 409 IALGR------PDATQQEIEHVARLASVHDDILRLPqgydtevGErgvmLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 165 DPQSRNKILESIKELnRQGATIVYTTHYMEEVeILCDQIVIMDQGQVIAKGTKESL-------KDMVR 225
Cdd:PRK10789 483 DGRTEHQILHNLRQW-GEGRTVIISAHRLSAL-TEASEILVMQHGHIAQRGNHDQLaqqsgwyRDMYR 548
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-216 |
2.19e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.46 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG---STMTPEnyAVKAMIGVVPQDVAVFEElSVQ 93
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRA--SLRRNIAVVFQDAGLFNR-SIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 94 ENIDyfCGLYVA-DKEKRQAL--------IEEviQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAV 164
Cdd:PRK13657 427 DNIR--VGRPDAtDEEMRAAAeraqahdfIER--KPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491378809 165 DPQSRNKILESIKELnRQGATIVYTTHYMEEVEIlCDQIVIMDQGQVIAKGT 216
Cdd:PRK13657 503 DVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGS 552
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-220 |
3.08e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 73.13 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMtpENYAVKAM---IGVVPQDVAVFEElSVQ 93
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL--RDYTLASLrnqVALVSQNVHLFND-TIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 94 ENIDYFCGlyvaDKEKRQAlIEEVIQLVGLENFVTFHP-------GE----LSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:PRK11176 435 NNIAYART----EQYSREQ-IEEAARMAYAMDFINKMDngldtviGEngvlLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 163 AVDPQSRNKILESIKEL--NRqgaTIVYTTHYMEEVEiLCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK11176 510 ALDTESERAIQAALDELqkNR---TSLVIAHRLSTIE-KADEILVVEDGEIVERGTHAEL 565
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
13-218 |
3.27e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.06 E-value: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 13 GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYD---KGTIKLFGSTMT--PENYAVK------AMIGvvp 81
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILnlPEKELNKlraeqiSMIF--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 82 QD--------VAVFEELsvQENIDYFCGLyvadkEKRQALIEEVIQLVGLE-----NFVTFHPGELSGGLKRRLNIACGI 148
Cdd:PRK09473 104 QDpmtslnpyMRVGEQL--MEVLMLHKGM-----SKAEAFEESVRMLDAVKmpearKRMKMYPHEFSGGMRQRVMIAMAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491378809 149 AHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKE 218
Cdd:PRK09473 177 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-222 |
3.42e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 69.86 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNY--DKGTIKLFGstmtpenyavkamigvv 80
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKG----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 pQDVAvfeELSVQENIDyfCGLYVAdkekRQALIEevIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEP 160
Cdd:cd03217 64 -EDIT---DLPPEERAR--LGIFLA----FQYPPE--IPGVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491378809 161 TVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVE-ILCDQIVIMDQGQVIAKGTKESLKD 222
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-220 |
3.58e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.82 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 23 LQVQEGEVLGLLGPNGSGKSTAINCMLSLLN-----YDKGTIKLFGSTMTpeNYAVKAMIGVVPQDVA-VFEELSVQENi 96
Cdd:PRK15134 30 LQIEAGETLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGESLL--HASEQTLRGVRGNKIAmIFQEPMVSLN- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 97 dyfcGLYVADKE-----------KRQALIEEVIQL---VGLENF---VTFHPGELSGGLKRRLNIACGIAHKPRLIFLDE 159
Cdd:PRK15134 107 ----PLHTLEKQlyevlslhrgmRREAARGEILNCldrVGIRQAakrLTDYPHQLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491378809 160 PTVAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK15134 183 PTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-220 |
4.26e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 71.66 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPEN----YAVKAMIGVVPQDVavFEELSV 92
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddewRAVRSDIQMIFQDP--LASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 93 QENIdyfcGLYVAD-------KEKRQALIEEVIQL---VGL-ENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPT 161
Cdd:PRK15079 114 RMTI----GEIIAEplrtyhpKLSRQEVKDRVKAMmlkVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 162 VAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-218 |
8.83e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 71.46 E-value: 8.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKlfgstmtpenYAVKAMIGVVPQ 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK----------WSENANIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 83 DVAvfEELSVQENIDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:PRK15064 390 DHA--YDFENDLTLFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTN 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491378809 163 AVDpqsrnkiLESIKELNR-----QGaTIVYTTHYMEEVEILCDQIV-IMDQGQVIAKGTKE 218
Cdd:PRK15064 468 HMD-------MESIESLNMalekyEG-TLIFVSHDREFVSSLATRIIeITPDGVVDFSGTYE 521
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-220 |
9.93e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.93 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 25 VQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYA-VKAMIGVVPQDVAVFEElSVQENIDYFCGLY 103
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTdLRRVLSIIPQSPVLFSG-TVRFNIDPFSEHN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 104 VAD--KEKRQALIEEVIQL--VGLENFVtFHPGE-LSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKE 178
Cdd:PLN03232 1338 DADlwEALERAHIKDVIDRnpFGLDAEV-SEGGEnFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE 1416
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491378809 179 LNRQgATIVYTTHYMEEVeILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PLN03232 1417 EFKS-CTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
6-206 |
1.08e-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: 69.70 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 6 DKLVKRYGDfvalNHFDLQ----VQEGEVLGLLGPNGSGKSTAINCMLS-----LLNYDK-----GTIKLF-GSTMtpEN 70
Cdd:cd03236 4 DEPVHRYGP----NSFKLHrlpvPREGQVLGLVGPNGIGKSTALKILAGklkpnLGKFDDppdwdEILDEFrGSEL--QN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 71 YAVKAMIGVV-----PQDVAVFEElSVQENIdyfcGLYVADKEKRQALiEEVIQLVGLENFVTFHPGELSGGLKRRLNIA 145
Cdd:cd03236 78 YFTKLLEGDVkvivkPQYVDLIPK-AVKGKV----GELLKKKDERGKL-DELVDQLELRHVLDRNIDQLSGGELQRVAIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491378809 146 CGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIM 206
Cdd:cd03236 152 AALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
25-216 |
1.70e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.05 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 25 VQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKA----MIGVVP-------QDVAVFEELSVQ 93
Cdd:PRK15112 36 LREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqrirMIFQDPstslnprQRISQILDFPLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 94 ENIDyfcgLYVADKEKRqalIEEVIQLVGL-ENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKI 172
Cdd:PRK15112 116 LNTD----LEPEQREKQ---IIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491378809 173 LESIKELN-RQGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGT 216
Cdd:PRK15112 189 INLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-220 |
2.72e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.03 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 21 FDLQvqEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENyavkamigvvPQD------VAVFEE----- 89
Cdd:PRK10762 273 FTLR--KGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS----------PQDglangiVYISEDrkrdg 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 90 ----LSVQEN-----IDYFCglYVADKEKRQALIEEVIQLVGLENFVTfhP------GELSGGLKRRLNIACGIAHKPRL 154
Cdd:PRK10762 341 lvlgMSVKENmsltaLRYFS--RAGGSLKHADEQQAVSDFIRLFNIKT--PsmeqaiGLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491378809 155 IFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQV-----IAKGTKESL 220
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRIsgeftREQATQEKL 487
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-211 |
2.78e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 25 VQEGEVLGLLGPNGSGKSTAINCML-SLLNYDKGTIKLFGSTMTPEN--YAVKAMIGVVPQDV---AVFEELSVQENI-- 96
Cdd:PRK13549 285 LRRGEILGIAGLVGAGRTELVQCLFgAYPGRWEGEIFIDGKPVKIRNpqQAIAQGIAMVPEDRkrdGIVPVMGVGKNItl 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 97 ---DYFCGLYVADKEKRQALIEEVIQLVGLEnfvTFHP----GELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSR 169
Cdd:PRK13549 365 aalDRFTGGSRIDDAAELKTILESIQRLKVK---TASPelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAK 441
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491378809 170 NKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQV 211
Cdd:PRK13549 442 YEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-218 |
3.22e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.78 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTaincmLSLL-----NY--DKGTIKLFG---STMTPENYAvKAMIGVVPQDVAVF 87
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKST-----LAKVlmghpKYevTSGSILLDGediLELSPDERA-RAGIFLAFQYPVEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 88 EELSVQenidYFcgLYVADKEKRQ---------ALIEEVIQLVGL-ENFVTFHPGE-LSGGLKRRLNIACGIAHKPRLIF 156
Cdd:COG0396 90 PGVSVS----NF--LRTALNARRGeelsareflKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491378809 157 LDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHY---MEEVEIlcDQIVIMDQGQVIAKGTKE 218
Cdd:COG0396 164 LDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYqriLDYIKP--DFVHVLVDGRIVKSGGKE 226
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-191 |
5.40e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.80 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 22 DLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFG-STMTPENYAVKAMIGVVPqdvAVFEELSVQENIDYFC 100
Cdd:PRK13543 31 DFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGkTATRGDRSRFMAYLGHLP---GLKADLSTLENLHFLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 101 GLYvadKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQS---RNKILESik 177
Cdd:PRK13543 108 GLH---GRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGitlVNRMISA-- 182
|
170
....*....|....
gi 491378809 178 ELNRQGATIVyTTH 191
Cdd:PRK13543 183 HLRGGGAALV-TTH 195
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-201 |
1.02e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.98 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 23 LQVQEGEVLGLLGPNGSGKSTAINCM--LSLLNYD---KGTIKLFGSTMtpenYAVKAMIGVVPQDVA-VFEE-----LS 91
Cdd:PRK14258 28 MEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEvrvEGRVEFFNQNI----YERRVNLNRLRRQVSmVHPKpnlfpMS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 92 VQENIDYfcGLYVAD---KEKRQALIEEVIQLVGLENFVT--FHPG--ELSGGLKRRLNIACGIAHKPRLIFLDEPTVAV 164
Cdd:PRK14258 104 VYDNVAY--GVKIVGwrpKLEIDDIVESALKDADLWDEIKhkIHKSalDLSGGQQQRLCIARALAVKPKVLLMDEPCFGL 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 491378809 165 DPQSRNKILESIKELN-RQGATIVYTTHYMEEVEILCD 201
Cdd:PRK14258 182 DPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSD 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-240 |
1.06e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 68.78 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDkGTIKLFG---STMTPENYavKAMIGVVPQDVAVFEElSVQE 94
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvswNSVTLQTW--RKAFGVIPQKVFIFSG-TFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 95 NIDYFCGLyvADKEkrqalIEEVIQLVGLENFVTFHPGE-----------LSGGLKRRLNIACGIAHKPRLIFLDEPTVA 163
Cdd:TIGR01271 1311 NLDPYEQW--SDEE-----IWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPSAH 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 164 VDPQSRNKILESIKElNRQGATIVYTTHYMEEVeILCDQIVIMDQGQV-----IAKGTKES--LKDMVRTADRLTidipL 236
Cdd:TIGR01271 1384 LDPVTLQIIRKTLKQ-SFSNCTVILSEHRVEAL-LECQQFLVIEGSSVkqydsIQKLLNETslFKQAMSAADRLK----L 1457
|
....
gi 491378809 237 LPDH 240
Cdd:TIGR01271 1458 FPLH 1461
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
2-218 |
1.06e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKlfgstmtpenYAVKAMIGVVP 81
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------RNGKLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 82 QDVAVFEELSVqeNIDYFCGLYVADKekrQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPT 161
Cdd:PRK09544 74 QKLYLDTTLPL--TVNRFLRLRPGTK---KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 162 VAVDPQSRNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQgQVIAKGTKE 218
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPE 205
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-220 |
1.24e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.21 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRY-GDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAV-KAMIGVV 80
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 PQDVAVFEElSVQENIDYfcGLYVADKEKRQALieEVIQLV----GLENFVTFHPGE----LSGGLKRRLNIACGIAHKP 152
Cdd:PRK10790 421 QQDPVVLAD-TFLANVTL--GRDISEEQVWQAL--ETVQLAelarSLPDGLYTPLGEqgnnLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 153 RLIFLDEPTVAVDPQSRNKILESIKELnRQGATIVYTTHYMEEVeILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAV-REHTTLVVIAHRLSTI-VEADTILVLHRGQAVEQGTHQQL 561
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-211 |
2.04e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.38 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 20 HFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAVKAMIGVV--PQDVAV---FEELSVQE 94
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylPEDRQSsglYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 95 NIdyfCGLYVAD-----KEKRQALIEEV------IQLVGLENFVtfhpGELSGGLKRRLNIACGIAHKPRLIFLDEPTVA 163
Cdd:PRK15439 361 NV---CALTHNRrgfwiKPARENAVLERyrralnIKFNHAEQAA----RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491378809 164 VDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQV 211
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-220 |
4.14e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.89 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 14 DFVaLNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPEN-YAVKAMIGVVPQDVAVFEElSV 92
Cdd:TIGR00957 1299 DLV-LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlHDLRFKITIIPQDPVLFSG-SL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 93 QENIDYFcGLYvADKEKRQALieeviQLVGLENFVTFHP----------GE-LSGGLKRRLNIACGIAHKPRLIFLDEPT 161
Cdd:TIGR00957 1377 RMNLDPF-SQY-SDEEVWWAL-----ELAHLKTFVSALPdkldhecaegGEnLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491378809 162 VAVDPQSRNKILESIKElNRQGATIVYTTHYMEEVeILCDQIVIMDQGQVIAKGTKESL 220
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTI-MDYTRVIVLDKGEVAEFGAPSNL 1506
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-213 |
4.29e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.20 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKL-VKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYA--VKAMIG 78
Cdd:COG3845 257 VLEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRerRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 79 VVPQD---VAVFEELSVQENI-------DYFCGLYVADKEKRQALIEEVIQ-----LVGLENFVtfhpGELSGGLKRRLN 143
Cdd:COG3845 337 YIPEDrlgRGLVPDMSVAENLilgryrrPPFSRGGFLDRKAIRAFAEELIEefdvrTPGPDTPA----RSLSGGNQQKVI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 144 IACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVIA 213
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVG 482
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-212 |
4.34e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.35 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINcMLSLL----NYD-----KGTIKLFGSTMTPEnya 72
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMK-VLSGVyphgSYEgeilfDGEVCRFKDIRDSE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 73 vKAMIGVVPQDVAVFEELSVQENIdyFCGLYVA-----DKEKRQALIEEVIQLVGLENfvtfHPGELSGGL---KRRL-N 143
Cdd:NF040905 77 -ALGIVIIHQELALIPYLSIAENI--FLGNERAkrgviDWNETNRRARELLAKVGLDE----SPDTLVTDIgvgKQQLvE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491378809 144 IACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQVI 212
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-222 |
6.18e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.51 E-value: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGStmtpenyavkamIGVVPQDvAVFEELSVQENID 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS------------VAYVPQQ-AWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 98 YFCGLyvadKEKR-QALIEEVIQLVGLENFVTFHPGE-------LSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSR 169
Cdd:TIGR00957 721 FGKAL----NEKYyQQVLEACALLPDLEILPSGDRTEigekgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 170 NKILESI--KELNRQGATIVYTTH---YMEEVeilcDQIVIMDQGQVIAKGTKESLKD 222
Cdd:TIGR00957 797 KHIFEHVigPEGVLKNKTRILVTHgisYLPQV----DVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-210 |
6.50e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.76 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGD--FvALNHFDLQVQEGEVLGLLGPNGSGKSTAinCML--SLLNYDKGTIKLFGSTMTPEN-YAVKAMI 77
Cdd:PRK10522 323 LELRNVTFAYQDngF-SVGPINLTIKRGELLFLIGGNGSGKSTL--AMLltGLYQPQSGEILLDGKPVTAEQpEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 78 GVVPQDVAVFEELSVQENidyfcglyvadKEKRQALIEEVIQLVGLENFVTFHPGE-----LSGGLKRRLNIACGIAHKP 152
Cdd:PRK10522 400 SAVFTDFHLFDQLLGPEG-----------KPANPALVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491378809 153 RLIFLDEPTVAVDPQSR----NKILESIKElnrQGATIVYTTH---YMeeveILCDQIVIMDQGQ 210
Cdd:PRK10522 469 DILLLDEWAADQDPHFRrefyQVLLPLLQE---MGKTIFAISHddhYF----IHADRLLEMRNGQ 526
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-211 |
8.00e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 8.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 23 LQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPEN--YAVKAMIGVVPQD------VAVfeeLSVQE 94
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSprDAIRAGIMLCPEDrkaegiIPV---HSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 95 NIDYFC-------GLYVADK-EKRQAliEEVIQLVgleNFVTFHP----GELSGGLKRRLNIACGIAHKPRLIFLDEPTV 162
Cdd:PRK11288 351 NINISArrhhlraGCLINNRwEAENA--DRFIRSL---NIKTPSReqliMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491378809 163 AVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQV 211
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-195 |
8.81e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.42 E-value: 8.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTaincMLSLLNYD-----KGTIKLF----GSTMTPenYAV 73
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKST----LLSLITGDhpqgySNDLTLFgrrrGSGETI--WDI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 74 KAMIGVVP----QDVAVfeELSVQENI--DYF--CGLYVADKEKRQALIEEVIQLVGLENFVT---FHpgELSGGLKRRL 142
Cdd:PRK10938 335 KKHIGYVSsslhLDYRV--STSVRNVIlsGFFdsIGIYQAVSDRQQKLAQQWLDILGIDKRTAdapFH--SLSWGQQRLA 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491378809 143 NIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGAT-IVYTTHYMEE 195
Cdd:PRK10938 411 LIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHHAED 464
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-209 |
1.19e-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: 62.65 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 25 VQEGEVLGLLGPNGSGKSTAINCmLSL---LNYDKGTIKLFGSTMtPENYAVKamIGVVPQDVAVFEELSVQENIDYFCG 101
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDV-LAGrktAGVITGEILINGRPL-DKNFQRS--TGYVEQQDVHSPNLTVREALRFSAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 102 LyvadkekRQALIEEviqlvglenfvtfhpgelsgglKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNR 181
Cdd:cd03232 106 L-------RGLSVEQ----------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLAD 156
|
170 180
....*....|....*....|....*....
gi 491378809 182 QGATIVYTTHYMEEVEI-LCDQIVIMDQG 209
Cdd:cd03232 157 SGQAILCTIHQPSASIFeKFDRLLLLKRG 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-161 |
1.29e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.96 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLfGSTmtpenyaVKamIGVVP 81
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GET-------VK--LAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 82 Q-------DVAVFEELS----------VQENIDYFCGLYV---ADKEKRQalieeviqlvglenfvtfhpGELSGGLKRR 141
Cdd:TIGR03719 392 QsrdaldpNKTVWEEISggldiiklgkREIPSRAYVGRFNfkgSDQQKKV--------------------GQLSGGERNR 451
|
170 180
....*....|....*....|
gi 491378809 142 LNIACGIAHKPRLIFLDEPT 161
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPT 471
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-206 |
1.47e-11 |
|
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: 64.81 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 6 DKLVKRYGDfvalNHFDL----QVQEGEVLGLLGPNGSGKSTAINcMLSllnydkGTIKL-FGSTMTPENYAvkamigvv 80
Cdd:COG1245 77 EDPVHRYGE----NGFRLyglpVPKKGKVTGILGPNGIGKSTALK-ILS------GELKPnLGDYDEEPSWD-------- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 pqdvAVFEELSVQENIDYFCGLYvaDKEKRQAL----------------------------IEEVIQLVGLENFVTFHPG 132
Cdd:COG1245 138 ----EVLKRFRGTELQDYFKKLA--NGEIKVAHkpqyvdlipkvfkgtvrellekvdergkLDELAEKLGLENILDRDIS 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491378809 133 ELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIM 206
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-206 |
1.72e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 15 FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLnydkgtiklfgsTMTPENYAVKAMIGVVPQDVAVFEELSVQE 94
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL------------KGTPVAGCVDVPDNQFGREASLIDAIGRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 95 NIDyfcglyvadkekrQALieEVIQLVGLENFVTF--HPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKI 172
Cdd:COG2401 111 DFK-------------DAV--ELLNAVGLSDAVLWlrRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180 190
....*....|....*....|....*....|....*
gi 491378809 173 LESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIM 206
Cdd:COG2401 176 ARNLQKLARRaGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-220 |
1.78e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.58 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 30 VLGLLGPNGSGKST------AINCMLSLLNYdKGTIKLFGSTMTpeNY----AVKAMIGVVPQDVAVFEeLSVQENIdyF 99
Cdd:PRK14271 49 VTSLMGPTGSGKTTflrtlnRMNDKVSGYRY-SGDVLLGGRSIF--NYrdvlEFRRRVGMLFQRPNPFP-MSIMDNV--L 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 100 CGL----YVADKEKR---QALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKI 172
Cdd:PRK14271 123 AGVrahkLVPRKEFRgvaQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491378809 173 LESIKELNRQgATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK14271 203 EEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-220 |
2.24e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.49 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 21 FDLQvqEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTM-TPENYAVKAM---IGVVPQDVavFEELSVQENI 96
Cdd:PRK10261 345 FDLW--PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSPGKLQALrrdIQFIFQDP--YASLDPRQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 97 DYFC-------GLYvaDKEKRQALIEEVIQLVGLE-NFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQS 168
Cdd:PRK10261 421 GDSImeplrvhGLL--PGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491378809 169 RNKILESIKELNRQ-GATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK10261 499 RGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
7-207 |
2.40e-11 |
|
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: 62.81 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 7 KLVKRYGDFvALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTmtpenyavkamIGVVPQDVAV 86
Cdd:cd03237 5 TMKKTLGEF-TLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-----------VSYKPQYIKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 87 FEELSVqeniDYFCGLYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDP 166
Cdd:cd03237 73 DYEGTV----RDLLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491378809 167 QSR---NKILESIKELNRQGATIVYTTHYMeeVEILCDQIVIMD 207
Cdd:cd03237 149 EQRlmaSKVIRRFAENNEKTAFVVEHDIIM--IDYLADRLIVFE 190
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-206 |
2.72e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 6 DKLVKRYGDfvalNHFDL----QVQEGEVLGLLGPNGSGKSTAINcMLSllnydkGTIKL-FGSTMTPENYAvkamigvv 80
Cdd:PRK13409 77 EEPVHRYGV----NGFKLyglpIPKEGKVTGILGPNGIGKTTAVK-ILS------GELIPnLGDYEEEPSWD-------- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 pqdvAVFEELSVQENIDYFCGLYvaDKEKRQAL----------------------------IEEVIQLVGLENFVTFHPG 132
Cdd:PRK13409 138 ----EVLKRFRGTELQNYFKKLY--NGEIKVVHkpqyvdlipkvfkgkvrellkkvdergkLDEVVERLGLENILDRDIS 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491378809 133 ELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNrQGATIVYTTHYMEEVEILCDQIVIM 206
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-191 |
3.84e-11 |
|
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: 60.63 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLfgstmtPEnyavKAMIGVVPQDVavfeelsvqenid 97
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM------PE----GEDLLFLPQRP------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 98 yfcglYVADKEKRQALIeeviqlvglenfvtfHP--GELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILES 175
Cdd:cd03223 74 -----YLPLGTLREQLI---------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170
....*....|....*.
gi 491378809 176 IKELnrqGATIVYTTH 191
Cdd:cd03223 134 LKEL---GITVISVGH 146
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-191 |
6.90e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.59 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 20 HFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMT---PENYAVKAMIGVVPqdvAVFEELSVQENI 96
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrDEYHQDLLYLGHQP---GIKTELTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 97 DYFCGLY-VADKEK-RQALieeviQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILE 174
Cdd:PRK13538 96 RFYQRLHgPGDDEAlWEAL-----AQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEA 170
|
170
....*....|....*..
gi 491378809 175 SIKELNRQGATIVYTTH 191
Cdd:PRK13538 171 LLAQHAEQGGMVILTTH 187
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
28-216 |
1.65e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.17 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 28 GEVLGLLGPNGSGKSTAINCMLSLLN--YDKGTIKLFGSTMTPENYAvkAMIGVVPQDVAVFEELSVQENIDYFCGLYVA 105
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKKQETFA--RISGYCEQNDIHSPQVTVRESLIYSAFLRLP 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 106 ---DKEKRQALIEEVIQLVGLENF---VTFHPG--ELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIK 177
Cdd:PLN03140 984 kevSKEEKMMFVDEVMELVELDNLkdaIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVR 1063
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491378809 178 ELNRQGATIVYTTHyMEEVEIL--CDQIVIMDQ-GQVIAKGT 216
Cdd:PLN03140 1064 NTVDTGRTVVCTIH-QPSIDIFeaFDELLLMKRgGQVIYSGP 1104
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-212 |
2.12e-10 |
|
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: 59.20 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYD---KGTIKLFGSTMTPENYAVKAMIGVVPQDVAVFEELSVQE 94
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 95 NIDYfcglyvadkekrqalieeVIQLVGLENFVTFhpgelSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILE 174
Cdd:cd03233 103 TLDF------------------ALRCKGNEFVRGI-----SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491378809 175 SIKELNRQ-GATIVYTThYMEEVEI--LCDQIVIMDQGQVI 212
Cdd:cd03233 160 CIRTMADVlKTTTFVSL-YQASDEIydLFDKVLVLYEGRQI 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-187 |
2.66e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVaLNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIklfgstmtpeNYAVKamIGVVP 81
Cdd:PRK13409 340 LVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV----------DPELK--ISYKP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 82 QDVAVFEELSVQENIDyfcglYVADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPT 161
Cdd:PRK13409 407 QYIKPDYDGTVEDLLR-----SITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180
....*....|....*....|....*...
gi 491378809 162 VAVDPQSRNKILESIKEL--NRQGATIV 187
Cdd:PRK13409 482 AHLDVEQRLAVAKAIRRIaeEREATALV 509
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-191 |
2.92e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.98 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKST---AINcmlSLLNYDKGTIKLfgstmtPENyaVKAMigVVPQDVavfeelsvqe 94
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTllrAIA---GLWPYGSGRIAR------PAG--ARVL--FLPQRP---------- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 95 nidyfcglYVADKEKRQAL-------------IEEVIQLVGLENFVTfHPGE-------LSGGLKRRLNIACGIAHKPRL 154
Cdd:COG4178 436 --------YLPLGTLREALlypataeafsdaeLREALEAVGLGHLAE-RLDEeadwdqvLSLGEQQRLAFARLLLHKPDW 506
|
170 180 190
....*....|....*....|....*....|....*..
gi 491378809 155 IFLDEPTVAVDPQSRNKILESIKElNRQGATIVYTTH 191
Cdd:COG4178 507 LFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-213 |
9.95e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 59.04 E-value: 9.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 21 FDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYAV-KAMIGVVPQDVAVFEElsvqenidyf 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyRQLFSAVFSDFHLFDR---------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 100 cgLYVADKEKRQALIEEVIQLVGLENFVTFHPG-----ELSGGLKRRLNIACGIA-HKPRLIFlDEPTVAVDPQSR---- 169
Cdd:COG4615 421 --LLGLDGEADPARARELLERLELDHKVSVEDGrfsttDLSQGQRKRLALLVALLeDRPILVF-DEWAADQDPEFRrvfy 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491378809 170 NKILesiKELNRQGATIVYTTH---YMEeveiLCDQIVIMDQGQVIA 213
Cdd:COG4615 498 TELL---PELKARGKTVIAISHddrYFD----LADRVLKMDYGKLVE 537
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-220 |
1.02e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.66 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 17 ALNHFDLQVQEGEVLGLLGPNGSGKS---TAInCMLSLLNY----DK---GTIKLFGSTMTPENYAVK---AMIGVVPQD 83
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSliaKAI-CGVTKDNWrvtaDRmrfDDIDLLRLSPRERRKLVGhnvSMIFQEPQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 84 VAVFEELSVQENIDYFCGLYVADK-------EKRQALieEVIQLVGLEN---FVTFHPGELSGGLKRRLNIACGIAHKPR 153
Cdd:PRK15093 101 CLDPSERVGRQLMQNIPGWTYKGRwwqrfgwRKRRAI--ELLHRVGIKDhkdAMRSFPYELTEGECQKVMIAIALANQPR 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 154 LIFLDEPTVAVDPQSRNKILESIKELNR-QGATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-187 |
1.17e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.03 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVaLNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLfgstmtpenyAVKamIGVVP 81
Cdd:COG1245 341 LVEYPDLTKSYGGFS-LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE----------DLK--ISYKP 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 82 QDVAVFEELSVQENidyfcgLYVADKEKRQA--LIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDE 159
Cdd:COG1245 408 QYISPDYDGTVEEF------LRSANTDDFGSsyYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190
....*....|....*....|....*....|
gi 491378809 160 PTVAVDPQSRNKILESIKEL--NRQGATIV 187
Cdd:COG1245 482 PSAHLDVEQRLAVAKAIRRFaeNRGKTAMV 511
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-220 |
2.37e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFV--ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPENYA-VKAMIGV 79
Cdd:PLN03130 1238 IKFEDVVLRYRPELppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMdLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEElSVQENIDYFCGLYVAD--KEKRQALIEEVIQL--VGLENFVTfHPGE-LSGGLKRRLNIACGIAHKPRL 154
Cdd:PLN03130 1318 IPQAPVLFSG-TVRFNLDPFNEHNDADlwESLERAHLKDVIRRnsLGLDAEVS-EAGEnFSVGQRQLLSLARALLRRSKI 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 155 IFLDEPTVAVDPQSRNKILESIKELNRQgATIVYTTHYMEEVeILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALIQKTIREEFKS-CTMLIIAHRLNTI-IDCDRILVLDAGRVVEFDTPENL 1459
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
27-217 |
3.56e-09 |
|
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: 55.06 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 27 EGEVLGLLGPNGSGKSTAINCMLsllnydkgtiklfgstmtpenyavkamigvvpqdVAVFEELSVQENIDYF-CGLYVA 105
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG----------------------------------LALGGAQSATRRRSGVkAGCIVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 106 DKEKRqaLIEEVIQLvglenfvtfhpgelSGGLKRRLNIACGIAH---KPR-LIFLDEPTVAVDPQSRNKILESIKELNR 181
Cdd:cd03227 66 AVSAE--LIFTRLQL--------------SGGEKELSALALILALaslKPRpLYILDEIDRGLDPRDGQALAEAILEHLV 129
|
170 180 190
....*....|....*....|....*....|....*.
gi 491378809 182 QGATIVYTTHYmEEVEILCDQIVIMdqGQVIAKGTK 217
Cdd:cd03227 130 KGAQVIVITHL-PELAELADKLIHI--KKVITGVYK 162
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-191 |
8.91e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 8.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 1 MIIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLfGSTMtpenyavkamigvv 80
Cdd:PRK11147 318 IVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKL-------------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 81 pqDVAVF----EEL----SVQENidyfcglyVAD--KE------KRQALieeviqlvG-LENFVtFHPGE-------LSG 136
Cdd:PRK11147 383 --EVAYFdqhrAELdpekTVMDN--------LAEgkQEvmvngrPRHVL--------GyLQDFL-FHPKRamtpvkaLSG 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491378809 137 GLKRRLNIAcGIAHKP-RLIFLDEPTVAVDPQSrnkiLESIKEL--NRQGaTIVYTTH 191
Cdd:PRK11147 444 GERNRLLLA-RLFLKPsNLLILDEPTNDLDVET----LELLEELldSYQG-TVLLVSH 495
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-220 |
1.16e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLnydkgtiklfgSTMTPENYAVKAMIGVVPQDVAVFEElSVQENId 97
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL-----------SHAETSSVVIRGSVAYVPQVSWIFNA-TVRENI- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 98 yfcgLYVADKEKRQalIEEVIQLVGLENFVTFHPGE-----------LSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDP 166
Cdd:PLN03232 700 ----LFGSDFESER--YWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491378809 167 QSRNKILESIKELNRQGATIVYTT---HYMEEVeilcDQIVIMDQGQVIAKGTKESL 220
Cdd:PLN03232 774 HVAHQVFDSCMKDELKGKTRVLVTnqlHFLPLM----DRIILVSEGMIKEEGTFAEL 826
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-187 |
3.87e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLfgSTMTPENYAVKAMIGVVP 81
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL--AKGIKLGYFAQHQLEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 82 QDVAVFEELSvqenidyfcglYVADKEKRQALiEEVIQLVGLE-NFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEP 160
Cdd:PRK10636 390 ADESPLQHLA-----------RLAPQELEQKL-RDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
|
170 180
....*....|....*....|....*..
gi 491378809 161 TVAVDPQSRNKILESIKELnrQGATIV 187
Cdd:PRK10636 458 TNHLDLDMRQALTEALIDF--EGALVV 482
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
18-225 |
3.88e-08 |
|
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: 53.03 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYD--KGTIKLFG---STMTPENYAvKAMIGVVPQDVavfEELSV 92
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEvtSGTILFKGqdlLELEPDERA-RAGLFLAFQYP---EEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 93 QENIDYFCGLYVADKEKRQA----------LIEEVIQLVGL-ENFVTFHPGE-LSGGLKRRLNIACGIAHKPRLIFLDEP 160
Cdd:TIGR01978 92 VSNLEFLRSALNARRSARGEepldlldfekLLKEKLALLDMdEEFLNRSVNEgFSGGEKKRNEILQMALLEPKLAILDEI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 161 TVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVE-ILCDQIVIMDQGQVIAKGTKESLKDMVR 225
Cdd:TIGR01978 172 DSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNyIKPDYVHVLLDGRIVKSGDVELAKELEA 237
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-180 |
5.02e-08 |
|
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: 53.98 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 16 VALNHFDLQVQEGEVLGLLGPNGSGKStaincmlSLLNYDKGTIKLFGSTMT-PEnyavKAMIGVVPQDvAVFEELSVQE 94
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKS-------SLFRILGELWPVYGGRLTkPA----KGKLFYVPQR-PYMTLGTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 95 NIDYFCGLY-VADKEKRQALIEEVIQLVGLENFVTFHPG---------ELSGGLKRRLNIACGIAHKPRLIFLDEPTVAV 164
Cdd:TIGR00954 534 QIIYPDSSEdMKRRGLSDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170
....*....|....*.
gi 491378809 165 DPQSRNKILESIKELN 180
Cdd:TIGR00954 614 SVDVEGYMYRLCREFG 629
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
106-220 |
5.08e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 53.43 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 106 DKEKRQALIEEVIQLVGLE-NFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQ-G 183
Cdd:PRK11308 126 SAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElG 205
|
90 100 110
....*....|....*....|....*....|....*..
gi 491378809 184 ATIVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK11308 206 LSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
18-215 |
1.95e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.33 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNY--DKGTIKLFGSTMT---PENYAVKAMIGVVPQDVAV------ 86
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLLelsPEDRAGEGIFMAFQYPVEIpgvsnq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 87 -FEELSVQENIDYFcGLYVADKEKRQALIEEVIQLVGL-ENFVTFHPGE-LSGGLKRRLNIACGIAHKPRLIFLDEPTVA 163
Cdd:PRK09580 97 fFLQTALNAVRSYR-GQEPLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491378809 164 VDPQSRNKILESIKELNRQGATIVYTTHYMEEVE-ILCDQIVIMDQGQVIAKG 215
Cdd:PRK09580 176 LDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDyIKPDYVHVLYQGRIVKSG 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
31-168 |
2.21e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.86 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 31 LGLLGPNGSGKSTAINCMLSLlnyDKgtiKLFGSTMTPENYAVkamiGVVPQDVAVFEELSVQENI-----------DYF 99
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGV---DK---DFNGEARPQPGIKV----GYLPQEPQLDPTKTVRENVeegvaeikdalDRF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 100 CGLYV------ADKEK---RQALIEEVIQLVGLENF----------VTFHPGE-----LSGGLKRRLNIACGIAHKPRLI 155
Cdd:TIGR03719 104 NEISAkyaepdADFDKlaaEQAELQEIIDAADAWDLdsqleiamdaLRCPPWDadvtkLSGGERRRVALCRLLLSKPDML 183
|
170
....*....|...
gi 491378809 156 FLDEPTVAVDPQS 168
Cdd:TIGR03719 184 LLDEPTNHLDAES 196
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-229 |
2.44e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 21 FDLQvqEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTM--TPENYAVKAMIGVVPQD---VAVFEELSVQ-- 93
Cdd:PRK10982 269 FDLH--KGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnHNANEAINHGFALVTEErrsTGIYAYLDIGfn 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 94 ---ENID-YFCGLYVADKEKRQALIEEVIQL--VGLENFVTfHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQ 167
Cdd:PRK10982 347 sliSNIRnYKNKVGLLDNSRMKSDTQWVIDSmrVKTPGHRT-QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVG 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491378809 168 SRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQV--IAKGTKESLKDMVRTADR 229
Cdd:PRK10982 426 AKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVagIVDTKTTTQNEILRLASL 489
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-220 |
3.52e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLnydkgtiklfgSTMTPENYAVKAMIGVVPQDVAVFEElSVQENId 97
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGEL-----------PPRSDASVVIRGTVAYVPQVSWIFNA-TVRDNI- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 98 YFCGLYVADKekrqalIEEVIQLVGLENFVTFHPG-----------ELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDP 166
Cdd:PLN03130 700 LFGSPFDPER------YERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491378809 167 QSRNKILES-IK-ELnrQGATIVYTT---HYMEEVeilcDQIVIMDQGQVIAKGTKESL 220
Cdd:PLN03130 774 HVGRQVFDKcIKdEL--RGKTRVLVTnqlHFLSQV----DRIILVHEGMIKEEGTYEEL 826
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-161 |
3.62e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 2 IIEIDKLVKRYGDFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLfGSTmtpenyaVKamIGVVP 81
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GET-------VK--LAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 82 Q-------DVAVFEELSvqENIDYfcgLYVADKE--KRqalieeviQLVGLENF--------VtfhpGELSGGLKRRLNI 144
Cdd:PRK11819 394 QsrdaldpNKTVWEEIS--GGLDI---IKVGNREipSR--------AYVGRFNFkggdqqkkV----GVLSGGERNRLHL 456
|
170
....*....|....*..
gi 491378809 145 ACGIAHKPRLIFLDEPT 161
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPT 473
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
7-205 |
8.14e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.34 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 7 KLVKRYGDFvALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTmtpenyavkamIGVVPQDVav 86
Cdd:cd03222 5 DCVKRYGVF-FLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT-----------PVYKPQYI-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 87 feelsvqenidyfcglyvadkekrqalieeviqlvglenfvtfhpgELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDP 166
Cdd:cd03222 71 ----------------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI 104
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491378809 167 QSRNKILESIKELNRQGA-TIVYTTHYMEEVEILCDQIVI 205
Cdd:cd03222 105 EQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHV 144
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
73-220 |
1.22e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 73 VKAMIGVVPQDVAVFEeLSVQENIDYfcGLYVADKE--KRQ---ALIEEVIQlvGLENFVTFHPG----ELSGGLKRRLN 143
Cdd:PTZ00265 1294 LRNLFSIVSQEPMLFN-MSIYENIKF--GKEDATREdvKRAckfAAIDEFIE--SLPNKYDTNVGpygkSLSGGQKQRIA 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 144 IACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKEL-NRQGATIVYTTHYMEEVEiLCDQIVIMDQGQ-----VIAKGTK 217
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkDKADKTIITIAHRIASIK-RSDKIVVFNNPDrtgsfVQAHGTH 1447
|
...
gi 491378809 218 ESL 220
Cdd:PTZ00265 1448 EEL 1450
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-227 |
1.69e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 16 VALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNydkGTIKLFGSTMTPE---NYAVKAMI---------GVVPQD 83
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLT---GGGAPRGARVTGDvtlNGEPLAAIdaprlarlrAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 84 VAVFEELSVQENIDYFCGLYV----ADKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAH--------- 150
Cdd:PRK13547 92 AQPAFAFSAREIVLLGRYPHArragALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 151 KPRLIFLDEPTVAVDPQSRNKILESIKELNRQ---GA-TIVyttHYMEEVEILCDQIVIMDQGQVIAKGTKeslKDMVRT 226
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnlGVlAIV---HDPNLAARHADRIAMLADGAIVAHGAP---ADVLTP 245
|
.
gi 491378809 227 A 227
Cdd:PRK13547 246 A 246
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
63-221 |
1.71e-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: 49.63 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 63 GSTMTPENYAVKamigVVPQDVAVFEELSVQENIDYFCGLYVADKEKrqALIEEVIQL----------VGLEnFVTFH-- 130
Cdd:TIGR00630 413 GTRLKPEALAVT----VGGKSIADVSELSIREAHEFFNQLTLTPEEK--KIAEEVLKEirerlgflidVGLD-YLSLSra 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 131 PGELSGGLKRRLNIACGIAHKPR--LIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHyMEEVEILCDQIVIMDQ 208
Cdd:TIGR00630 486 AGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEH-DEDTIRAADYVIDIGP 564
|
170
....*....|....*....
gi 491378809 209 ------GQVIAKGTKESLK 221
Cdd:TIGR00630 565 gagehgGEVVASGTPEEIL 583
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-226 |
1.91e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 16 VALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIklfgstmtpenYAVKAmIGVVPQDvAVFEELSVQEN 95
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------WAERS-IAYVPQQ-AWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 96 IDYFcglyvadKEKRQALIEEVIQLVGLENFVTFHPG-----------ELSGGLKRRLNIACGIAHKPRLIFLDEPTVAV 164
Cdd:PTZ00243 741 ILFF-------DEEDAARLADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491378809 165 DPQSRNKILESIKELNRQGATIVYTTHYMEEVEiLCDQIVIMDQGQVIAKGtkeSLKDMVRT 226
Cdd:PTZ00243 814 DAHVGERVVEECFLGALAGKTRVLATHQVHVVP-RADYVVALGDGRVEFSG---SSADFMRT 871
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
134-210 |
3.47e-06 |
|
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: 46.55 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 134 LSGGLKRRLNIA--CGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHymeEVEILC--DQIVIMDQG 209
Cdd:cd03238 88 LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEH---NLDVLSsaDWIIDFGPG 164
|
.
gi 491378809 210 Q 210
Cdd:cd03238 165 S 165
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
104-191 |
5.43e-06 |
|
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: 47.00 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 104 VADKEKRQALIEEVIQLVGLENFVTFHPG--------ELSGGLKR--RLNIACGIA-HKPRLIFLDEPTVAVDPQSRNKI 172
Cdd:pfam13304 199 LSDLGEGIEKSLLVDDRLRERGLILLENGgggelpafELSDGTKRllALLAALLSAlPKGGLLLIDEPESGLHPKLLRRL 278
|
90
....*....|....*....
gi 491378809 173 LESIKELNRQGATIVYTTH 191
Cdd:pfam13304 279 LELLKELSRNGAQLILTTH 297
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
87-245 |
5.51e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 87 FEELSVQENIDYFCGLyvadKEKRQAlIEEVIQlvGLENFVTF---------HP----GELSGGLKRRLNIA-------C 146
Cdd:PRK00635 424 FQQMSLQELFIFLSQL----PSKSLS-IEEVLQ--GLKSRLSIlidlglpylTPeralATLSGGEQERTALAkhlgaelI 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 147 GIAHkprliFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHyMEEVEILCDQIVIMDQ------GQVIAKGTKesl 220
Cdd:PRK00635 497 GITY-----ILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEH-DEQMISLADRIIDIGPgagifgGEVLFNGSP--- 567
|
170 180 190
....*....|....*....|....*....|....
gi 491378809 221 KDMVRTADRLT---------IDIPLLPDHVLATI 245
Cdd:PRK00635 568 REFLAKSDSLTakylrqeltIPIPEKRTNSLGTL 601
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-209 |
2.14e-05 |
|
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: 44.63 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 14 DFVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGtiKLFGSTMTPENYAVKAMIGVVPQDVAVFEE---- 89
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG--KVHWSNKNESEPSFEATRSRNRYSVAYAAQkpwl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 90 --LSVQENIDYFCGLyvaDKEKRQAlieeVIQLVGLENFVTFHP-------GE----LSGGLKRRLNIACGIAHKPRLIF 156
Cdd:cd03290 91 lnATVEENITFGSPF---NKQRYKA----VTDACSLQPDIDLLPfgdqteiGErginLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491378809 157 LDEPTVAVDPQSRNKILES--IKELNRQGATIVYTTHYMEEVeILCDQIVIMDQG 209
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYL-PHADWIIAMKDG 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-187 |
3.60e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 21 FDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIkLFGSTMTPENYAVK---AMIGVVPQDVAVFEElSVQENID 97
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-IINDSHNLKDINLKwwrSKIGVVSQDPLLFSN-SIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 98 YfcGLYV-------------------ADKEKRQA--------------------LIE-----------EVIQL---VGLE 124
Cdd:PTZ00265 482 Y--SLYSlkdlealsnyynedgndsqENKNKRNScrakcagdlndmsnttdsneLIEmrknyqtikdsEVVDVskkVLIH 559
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 125 NFVTFHP-----------GELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKEL--NRQGATIV 187
Cdd:PTZ00265 560 DFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITII 635
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-245 |
4.38e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 134 LSGGLKRRLNIACGI---AHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEIlCDQIVIMDQ-- 208
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKV-ADYVLELGPeg 888
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 491378809 209 ----GQVIAKGTKESLKDM-VRTADRL------TIDIPLLPD-----HVLATI 245
Cdd:PRK00635 889 gnlgGYLLASCSPEELIHLhTPTAKALrpylssPQELPYLPDpspkpPVPADI 941
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-231 |
4.66e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 15 FVALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLS-LLNYDKGTiklfGSTMTPENYAVKAMIGVVPQDVAV------- 86
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFHIGV----EGVITYDGITPEEIKKHYRGDVVYnaetdvh 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 87 FEELSVQENIDY----------FCGLyvaDKEKRQALIEEVIQLV-GLENFVTFHPGE-----LSGGLKRRLNIACGIAH 150
Cdd:TIGR00956 150 FPHLTVGETLDFaarcktpqnrPDGV---SREEYAKHIADVYMATyGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 151 KPRLIFLDEPTVAVDPQSrnkILESIKELnRQGATIVYTTHYM------EEVEILCDQIVIMDQGQVI----AKGTKESL 220
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSAT---ALEFIRAL-KTSANILDTTPLVaiyqcsQDAYELFDKVIVLYEGYQIyfgpADKAKQYF 302
|
250
....*....|....*...
gi 491378809 221 KDM-------VRTADRLT 231
Cdd:TIGR00956 303 EKMgfkcpdrQTTADFLT 320
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-220 |
6.33e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 43.74 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 3 IEIDKLVKRYGDFV--ALNHFDLQVQEGEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTP-ENYAVKAMIGV 79
Cdd:cd03288 20 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 80 VPQDVAVFEElSVQENIDYFCGlyVADKEKRQALieEVIQLV--------GLENFVTFHPGELSGGLKRRLNIACGIAHK 151
Cdd:cd03288 100 ILQDPILFSG-SIRFNLDPECK--CTDDRLWEAL--EIAQLKnmvkslpgGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491378809 152 PRLIFLDEPTVAVDPQSRNkILESIKELNRQGATIVYTTHYMEEVeILCDQIVIMDQGQVIAKGTKESL 220
Cdd:cd03288 175 SSILIMDEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVSTI-LDADLVLVLSRGILVECDTPENL 241
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-191 |
7.85e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.98 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 28 GEVLGLLGPNGSGKSTAINCMLSLLNYDKGTIKLFGSTMTPEnyavkamigvvpqdvavfEELSVQENIDYFCGLYVADK 107
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILE------------------EVLDQLLLIIVGGKKASGSG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 108 EKRQALIEEVIQlvglenfvtfhpgelsgglkrrlniacgiAHKPRLIFLDEPTVAVDPQSRNKILESI------KELNR 181
Cdd:smart00382 64 ELRLRLALALAR-----------------------------KLKPDVLILDEITSLLDAEQEALLLLLEelrlllLLKSE 114
|
170
....*....|
gi 491378809 182 QGATIVYTTH 191
Cdd:smart00382 115 KNLTVILTTN 124
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
106-220 |
3.76e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 106 DKEKRQALIEEVIQLVGLENFVTFHPGELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGAT 185
Cdd:PRK10938 108 DEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGIT 187
|
90 100 110
....*....|....*....|....*....|....*
gi 491378809 186 IVYTTHYMEEVEILCDQIVIMDQGQVIAKGTKESL 220
Cdd:PRK10938 188 LVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
35-204 |
1.68e-03 |
|
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: 38.74 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 35 GPNGSGKSTAINCMLSLL------NYDKGTI--KLFGSTmtpenyAVKAMI-----GVVPQDVAVFEELSVQENIdYFCg 101
Cdd:cd03240 29 GQNGAGKTTIIEALKYALtgelppNSKGGAHdpKLIREG------EVRAQVklafeNANGKKYTITRSLAILENV-IFC- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 102 lyvadkekRQaliEEVIQLVGLenfvtfHPGELSGGLKRRLNIA--CGIAH----KPRLIFLDEPTVAVDPQSR-NKILE 174
Cdd:cd03240 101 --------HQ---GESNWPLLD------MRGRCSGGEKVLASLIirLALAEtfgsNCGILALDEPTTNLDEENIeESLAE 163
|
170 180 190
....*....|....*....|....*....|..
gi 491378809 175 SIKELNRQGA--TIVYTTHymEEVEILCDQIV 204
Cdd:cd03240 164 IIEERKSQKNfqLIVITHD--EELVDAADHIY 193
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
18-191 |
3.39e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 38.83 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 18 LNHFDLQVQEGEVLgLLGPNGSGKST---AINCMLSLLNYDK----------------GTIKL-FGSTMTP--ENYAVKA 75
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSileALRLLLGPSSSRKfdeedfylgddpdlpeIEIELtFGSLLSRllRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 76 MIGVVPQDVAVFEEL------SVQENIDYFCGLYVADKE-------KRQALIEEVIQLVgLENFVTFHPGELSGGLKRRL 142
Cdd:COG3593 93 DKEELEEALEELNEElkealkALNELLSEYLKELLDGLDlelelslDELEDLLKSLSLR-IEDGKELPLDRLGSGFQRLI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491378809 143 NIACGIA-------HKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTH 191
Cdd:COG3593 172 LLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
132-178 |
7.00e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 35.29 E-value: 7.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 132 GELSGGLKR-------------RLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKE 178
Cdd:pfam13558 31 GGLSGGEKQllaylplaaalaaQYGSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
132-218 |
8.26e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.85 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491378809 132 GELSGGLKRRLNIACGIAHKPRLIFLDEPTVAVDPQSRNKILESIKELNRQGATIVYTTHYMEEVEILCDQIVIMDQGQV 211
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
....*..
gi 491378809 212 IAKGTKE 218
Cdd:NF040905 483 TGELPRE 489
|
|
| |
