|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-239 |
1.15e-110 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 320.09 E-value: 1.15e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLVP 83
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPT 163
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 164 AGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLqLETFILDIAENS 239
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL-LEDVFLELTGEE 234
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-299 |
1.08e-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: 243.84 E-value: 1.08e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 11 KTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLVPQEFNFNQ 90
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 91 FETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIEL 170
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 171 RRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTS---MKDLLAKLQLETFILDIAENSPPAPQLSG 247
Cdd:TIGR01188 160 RRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTpeeLKRRLGKDTLESRPRDIQSLKVEVSMLIA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648246410 248 VISQTMLNG-SLQIELEKTK--------GLNSVFSQLTEQGITVLSMRNKANRLEELFVSI 299
Cdd:TIGR01188 240 ELGETGLGLlAVTVDSDRIKilvpdgdeTVPEIVEAAIRNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-213 |
3.96e-78 |
|
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: 235.37 E-value: 3.96e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLVP 83
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEFNFNQFETVEQIVlqqagyygvtkalakeraekylskldlwekrkerarNLSGGMKRRLMIARALMHEPKLLILDEPT 163
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 648246410 164 AGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGEL 213
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-214 |
4.75e-77 |
|
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: 234.19 E-value: 4.75e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLVP 83
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPT 163
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 648246410 164 AGVDIELRRSMWEFLTEINA-QGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-242 |
5.86e-74 |
|
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: 227.05 E-value: 5.86e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLVP 83
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPT 163
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 164 AGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQLE----TFILDIAENS 239
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEnledAFVALIGSEE 240
|
...
gi 648246410 240 PPA 242
Cdd:COG4555 241 GEA 243
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-214 |
2.09e-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: 217.37 E-value: 2.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGG-FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLV 82
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQeFN--FNQFeTVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILD 160
Cdd:cd03263 81 PQ-FDalFDEL-TVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 648246410 161 EPTAGVDIELRRSMWEFLTEInAQGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-303 |
6.84e-68 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 213.43 E-value: 6.84e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDlelAKQHIGLV 82
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNFNQFETV-EQIVlqqagYY----GVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLL 157
Cdd:COG4152 77 PEERGLYPKMKVgEQLV-----YLarlkGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 158 ILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQLETFILDIAE 237
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 238 NSPPAPQLSGVISQTMLNGSLQIELEKTKGLNSVFSQLTEQGiTVLSMRNKANRLEELFVSIVQQQ 303
Cdd:COG4152 232 DAGWLRALPGVTVVEEDGDGAELKLEDGADAQELLRALLARG-PVREFEEVRPSLNEIFIEVVGEK 296
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-228 |
3.06e-60 |
|
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: 191.78 E-value: 3.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI-DKDLELAKQHIGLV 82
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQefN-FNQF--ETVEQIV---LQQagyYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKL 156
Cdd:COG1122 81 FQ--NpDDQLfaPTVEEDVafgPEN---LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648246410 157 LILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQL 228
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-214 |
1.56e-59 |
|
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: 189.33 E-value: 1.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGfEALKGVSLQVEKGdFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLVP 83
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPT 163
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 648246410 164 AGVDIELRRSMWEFLTEInAQGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:cd03264 159 AGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-211 |
1.13e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 185.68 E-value: 1.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGfdidKDLELAKQHIG 80
Cdd:COG1121 4 MPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFNFN-QFE-TVEQIVLqqAGYYGVTKAL------AKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMH 152
Cdd:COG1121 79 YVPQRAEVDwDFPiTVRDVVL--MGRYGRRGLFrrpsraDREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 153 EPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRG 211
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
3-230 |
1.35e-56 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 182.49 E-value: 1.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLV 82
Cdd:TIGR03864 1 ALEVAGLSFRY-GARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEP 162
Cdd:TIGR03864 80 FQQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 163 TAGVDIELRRSMWEFLTEINA-QGITIILTTHYLEEAEMLCRNIgIINRGELIENTSMKDLLAKLQLET 230
Cdd:TIGR03864 160 TVGLDPASRAAITAHVRALARdQGLSVLWATHLVDEIEASDRLV-VLHRGRVLADGAAAELRGATGGAD 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-200 |
4.46e-56 |
|
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: 180.76 E-value: 4.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGG---FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK--DLELAK-- 76
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 77 -QHIGLVPQEFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPK 155
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 648246410 156 LLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEM 200
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-212 |
6.27e-55 |
|
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: 177.27 E-value: 6.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 5 EIEQLRKTYAGGFE-ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI-DKDLELAKQHIGLV 82
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNfNQF--ETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILD 160
Cdd:cd03225 81 FQNPD-DQFfgPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 648246410 161 EPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGE 212
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-214 |
6.08e-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: 175.25 E-value: 6.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTY---AGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIG 80
Cdd:cd03266 2 ITADALTKRFrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILD 160
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 648246410 161 EPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-278 |
2.25e-53 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 176.82 E-value: 2.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTY---------AGGF-----------EALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVK 62
Cdd:COG4586 1 IIEVENLSKTYrvyekepglKGALkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 63 VFGFDIDKD-LELAKQhIGLVpqefnFNQ-------------FETVEQIvlqqagyYGVTKALAKERAEKYLSKLDLWEK 128
Cdd:COG4586 81 VLGYVPFKRrKEFARR-IGVV-----FGQrsqlwwdlpaidsFRLLKAI-------YRIPDAEYKKRLDELVELLDLGEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 129 RKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGI 207
Cdd:COG4586 148 LDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIV 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648246410 208 INRGELIENTSMKDLLAKLQLETFI-LDIAENSPPAPQLSGVISQTMLNGSLQIELEKTKGLNSVFSQLTEQ 278
Cdd:COG4586 228 IDHGRIIYDGSLEELKERFGPYKTIvLELAEPVPPLELPRGGEVIEREGNRVRLEVDPRESLAEVLARLLAR 299
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-214 |
1.69e-52 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 172.55 E-value: 1.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID----KDLELAKQH 78
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTalrgRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 79 IGLVPQEFNFnqfetVEQI-VLQ-----QAGYYGVTKALA-------KERAEKYLSKLDLWEKRKERARNLSGGMKRRLM 145
Cdd:COG3638 82 IGMIFQQFNL-----VPRLsVLTnvlagRLGRTSTWRSLLglfppedRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648246410 146 IARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINA-QGITIILTTHYLEEAEMLC-RNIGiINRGELI 214
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDLARRYAdRIIG-LRDGRVV 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-224 |
5.31e-52 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 173.07 E-value: 5.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLV 82
Cdd:PRK13537 7 PIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEP 162
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648246410 163 TAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-202 |
1.24e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 170.66 E-value: 1.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYA---GGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGfdidKDLELAKQHI 79
Cdd:COG1116 7 ALELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 80 GLVPQEFNFNQFETVEQ---IVLQQAGyygVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKL 156
Cdd:COG1116 83 GVVFQEPALLPWLTVLDnvaLGLELRG---VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 648246410 157 LILDEPTAGVDIELRRSMWEFLTEI-NAQGITIILTTHYLEEAEMLC 202
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLA 206
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-211 |
3.20e-51 |
|
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: 168.10 E-value: 3.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 5 EIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELakqhIGLVPQ 84
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR----IGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 85 EFNFN-QFE-TVEQIVL----QQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLI 158
Cdd:cd03235 76 RRSIDrDFPiSVRDVVLmglyGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 648246410 159 LDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRG 211
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-196 |
1.24e-50 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 166.77 E-value: 1.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI----DKDLELAKQHI 79
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlkRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 80 GLVPQEFNF----NQFETVEqIVLQQAGYygvTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPK 155
Cdd:COG2884 82 GVVFQDFRLlpdrTVYENVA-LPLRVTGK---SRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 648246410 156 LLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLE 196
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-214 |
8.30e-50 |
|
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: 164.38 E-value: 8.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDkdlELAKQHIGLVP 83
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPT 163
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 648246410 164 AGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-218 |
8.76e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 164.83 E-value: 8.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGG---FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK--DLELAK- 76
Cdd:COG1136 4 LLELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlsERELARl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 77 --QHIGLVPQEFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:COG1136 84 rrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 155 KLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIgIINRGELIENTS 218
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVI-RLRDGRIVSDER 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
20-197 |
1.10e-49 |
|
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: 165.26 E-value: 1.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSG-TVKVFG--------FDIdkdlelaKQHIGLVPQEF--NF 88
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGerrggedvWEL-------RKRIGLVSPALqlRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 89 NQFETVEQIVLqqAGYYGVT------KALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEP 162
Cdd:COG1119 92 PRDETVLDVVL--SGFFDSIglyrepTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 648246410 163 TAGVDIELRRSMWEFLTEINAQG-ITIILTTHYLEE 197
Cdd:COG1119 170 TAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEE 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-227 |
1.30e-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: 164.68 E-value: 1.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGG---FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID----KDLELAK 76
Cdd:cd03258 2 IELKNVSKVFGDTggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 77 QHIGLVPQEFNFNQFETVEQIV---LQQAGyygVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHE 153
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENValpLEIAG---VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 154 PKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQ 227
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-216 |
2.85e-48 |
|
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: 160.08 E-value: 2.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLElAKQHIGLVP 83
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-ALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEFNFNQFETVEQIVLQQAGYYGvtkaLAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPT 163
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLG----IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 648246410 164 AGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIEN 216
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-212 |
6.48e-48 |
|
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: 157.41 E-value: 6.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 5 EIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI-DKDLELAKQHIGLVP 83
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QefnfnqfetveqivlqqagyygvtkalakeraekylskldlwekrkerarnLSGGMKRRLMIARALMHEPKLLILDEPT 163
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 648246410 164 AGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGE 212
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-242 |
9.70e-48 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 162.94 E-value: 9.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGG---FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI----DKDLELAK 76
Cdd:COG1135 2 IELENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalsERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 77 QHIGLVPQEFN-FNQfETVEQIV---LQQAGyygVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMH 152
Cdd:COG1135 82 RKIGMIFQHFNlLSS-RTVAENValpLEIAG---VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 153 EPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHyleeaEM-----LCRNIGIINRGELIENTSMKDLLAKL 226
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITH-----EMdvvrrICDRVAVLENGRIVEQGPVLDVFANP 232
|
250
....*....|....*....
gi 648246410 227 QLET---FILDIAENSPPA 242
Cdd:COG1135 233 QSELtrrFLPTVLNDELPE 251
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-214 |
3.25e-47 |
|
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: 159.05 E-value: 3.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID--KDLELAK-- 76
Cdd:COG0411 2 DPLLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglPPHRIARlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 77 -----QHIGLVPQEfnfnqfeTVEQ---IVLQQAGYYGVTKAL------------AKERAEKYLSKLDLWEKRKERARNL 136
Cdd:COG0411 81 iartfQNPRLFPEL-------TVLEnvlVAAHARLGRGLLAALlrlprarreereARERAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 137 SGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINA-QGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-210 |
4.11e-47 |
|
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: 157.63 E-value: 4.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGG---FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGfdidKDLELAKQHIG 80
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFNFNQFETVEQIV---LQQAGyygVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLL 157
Cdd:cd03293 77 YVFQQDALLPWLTVLDNValgLELQG---VPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 648246410 158 ILDEPTAGVDIELRRSMWEFLTEI-NAQGITIILTTHYLEEAEMLCRNIGIINR 210
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-214 |
5.86e-47 |
|
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: 157.73 E-value: 5.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI----DKDLELAKQHI 79
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 80 GLVPQEFNF-NQFETVEQIVLQQAGYYGVTKALA-------KERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALM 151
Cdd:cd03256 81 GMIFQQFNLiERLSVLENVLSGRLGRRSTWRSLFglfpkeeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648246410 152 HEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-224 |
9.91e-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: 164.31 E-value: 9.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTY----AGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID----KDLELA 75
Cdd:COG1123 261 LEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 76 KQHIGLVPQefN----FNQFETVEQIV---LQQAGyyGVTKALAKERAEKYLSKLDLWEKRKER-ARNLSGGMKRRLMIA 147
Cdd:COG1123 341 RRRVQMVFQ--DpyssLNPRMTVGDIIaepLRLHG--LLSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648246410 148 RALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-214 |
2.01e-46 |
|
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: 156.34 E-value: 2.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYA-----GGF---------------EALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKV 63
Cdd:cd03267 1 IEVSNLSKSYRvyskePGLigslkslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 64 FGFDIDKDLELAKQHIGLVpqefnFNQFETV-------EQIVLQQAgYYGVTKALAKERAEKYLSKLDLWEKRKERARNL 136
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVV-----FGQKTQLwwdlpviDSFYLLAA-IYDLPPARFKKRLDELSELLDLEELLDTPVRQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 137 SGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-214 |
2.16e-46 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 159.61 E-value: 2.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIG 80
Cdd:PRK13536 39 TVAIDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILD 160
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 648246410 161 EPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-214 |
2.52e-46 |
|
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: 156.06 E-value: 2.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID--KDLELAKQHIGL 81
Cdd:cd03219 1 LEVRGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITglPPHEIARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 ---VPQEF-NFNQFETVEQIVLQQAGYYGVTKALAK------ERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALM 151
Cdd:cd03219 80 tfqIPRLFpELTVLENVMVAAQARTGSGLLLARARReerearERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648246410 152 HEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-214 |
1.67e-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: 154.43 E-value: 1.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID--KDLELAKQhIG 80
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAslSRRELARR-IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQE----FNFnqfeTVEQIVLQ-----QAGYYGVTKAlAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALM 151
Cdd:COG1120 79 YVPQEppapFGL----TVRELVALgryphLGLFGRPSAE-DREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648246410 152 HEPKLLILDEPTAGVDIELRRSMWEFLTEINA-QGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-214 |
5.01e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 156.03 E-value: 5.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDkDLELAKQHIG 80
Cdd:COG3842 3 MPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-GLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFN-FNQFeTVEQIV---LQQAGyygVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKL 156
Cdd:COG3842 81 MVFQDYAlFPHL-TVAENVafgLRMRG---VPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 157 LILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-215 |
2.01e-44 |
|
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: 151.12 E-value: 2.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGG---FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI----DKDLELAK 76
Cdd:cd03257 2 LEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 77 QHIGLVPQE--FNFNQFETVEQIVLQ--QAGYYGVTKALAKERAEKYLSKLDLWEKRKER-ARNLSGGMKRRLMIARALM 151
Cdd:cd03257 82 KEIQMVFQDpmSSLNPRMTIGEQIAEplRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRyPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 152 HEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIE 215
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-164 |
1.45e-43 |
|
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: 146.25 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI-DKDLELAKQHIGLVPQEFNFNQFETVEQIV 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 99 LQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARN----LSGGMKRRLMIARALMHEPKLLILDEPTA 164
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-224 |
2.48e-43 |
|
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: 147.97 E-value: 2.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDL--ELAKQHIGL 81
Cdd:cd03224 1 LEVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPphERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQEFN-FNQFeTVEQIVLqqAGYYGVTKALAKERAEKYLSKL-DLWEKRKERARNLSGGMKRRLMIARALMHEPKLLIL 159
Cdd:cd03224 80 VPEGRRiFPEL-TVEENLL--LGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 160 DEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-212 |
3.00e-43 |
|
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: 146.18 E-value: 3.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID---KDLELAKQHIG 80
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdleDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFNFNQFETVEQIVlqqagyygvtkALAkeraekylskldlwekrkerarnLSGGMKRRLMIARALMHEPKLLILD 160
Cdd:cd03229 80 MVFQDFALFPHLTVLENI-----------ALG-----------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 648246410 161 EPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGE 212
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-215 |
4.27e-43 |
|
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: 146.90 E-value: 4.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDLELAKQHIGLVP 83
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEF----NFNQFETVeQIVLQQAGyygVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLIL 159
Cdd:cd03259 79 QDYalfpHLTVAENI-AFGLKLRG---VPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 648246410 160 DEPTAGVDIELRRSMWEFLTEI-NAQGITIILTTHYLEEAEMLCRNIGIINRGELIE 215
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-193 |
8.32e-43 |
|
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: 146.14 E-value: 8.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID---KDLELAKQHIG 80
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFN-FNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLIL 159
Cdd:cd03262 80 MVFQQFNlFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190
....*....|....*....|....*....|....
gi 648246410 160 DEPTAGVDIELRRSMWEFLTEINAQGITIILTTH 193
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-227 |
7.12e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 151.21 E-value: 7.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGG-FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKT---SGTVKVFGFDIDK-DLELAKQ 77
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLElSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 78 HIGLVPQEFnFNQF--ETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPK 155
Cdd:COG1123 84 RIGMVFQDP-MTQLnpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648246410 156 LLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQ 227
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-214 |
1.33e-40 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 141.00 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID-KDLELAKQHIGLV 82
Cdd:TIGR03740 1 LETKNLSKRF-GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTrKDLHKIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNFNQFETVeQIVLQQAGyygvtkaLAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEP 162
Cdd:TIGR03740 80 PLYENLTARENL-KVHTTLLG-------LPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 163 TAGVDI----ELRrsmwEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:TIGR03740 152 TNGLDPigiqELR----ELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-200 |
1.49e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 141.28 E-value: 1.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID---KDLELAKQHIG 80
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFN-FNQFeTVEQ------IVLQqagyyGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHE 153
Cdd:COG1126 81 MVFQQFNlFPHL-TVLEnvtlapIKVK-----KMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 648246410 154 PKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHyleeaEM 200
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTH-----EM 196
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-224 |
7.85e-40 |
|
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: 139.35 E-value: 7.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKdL---ELAKQHIG 80
Cdd:COG0410 4 LEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG-LpphRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFN-FNQFeTVEQiVLQQAGYYGVTKALAKERAEKYLSKL-DLWEKRKERARNLSGGMKRRLMIARALMHEPKLLI 158
Cdd:COG0410 82 YVPEGRRiFPSL-TVEE-NLLLGAYARRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 159 LDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:COG0410 160 LDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-213 |
1.01e-39 |
|
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: 138.91 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDLELAKQHIGLVP 83
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEFNFNQFETVEQIV---LQQAGyygVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILD 160
Cdd:cd03300 79 QNYALFPHLTVFENIafgLRLKK---LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 648246410 161 EPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGEL 213
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-214 |
1.96e-39 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 138.24 E-value: 1.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDLEL---AKQ 77
Cdd:COG1137 1 MMTLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLPMhkrARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 78 HIGLVPQEFNFnqFE--TVEQ---IVLQQAGyygVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMH 152
Cdd:COG1137 79 GIGYLPQEASI--FRklTVEDnilAVLELRK---LSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 153 EPKLLILDEPTAGVD----IELRRsMWEFLTEinaQGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:COG1137 154 NPKFILLDEPFAGVDpiavADIQK-IIRHLKE---RGIGVLITDHNVRETLGICDRAYIISEGKVL 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-215 |
2.49e-39 |
|
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: 137.70 E-value: 2.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVN-----KTSGTVKVFGFDIDKD----LEL 74
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLdvdvLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 75 AKQhIGLVPQE---FNFNQFETVEqIVLQQAGYygVTKALAKERAEKYLSKLDLWE--KRKERARNLSGGMKRRLMIARA 149
Cdd:cd03260 80 RRR-VGMVFQKpnpFPGSIYDNVA-YGLRLHGI--KLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 150 LMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQgITIILTTHYLEEAEMLCRNIGIINRGELIE 215
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-260 |
3.43e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 140.71 E-value: 3.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 5 EIEQLRKTYAGG---FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI----DKDLELAKQ 77
Cdd:PRK11153 3 ELKNISKVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 78 HIGLVPQEFNFNQFETVEQIV---LQQAGyygVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNValpLELAG---TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 155 KLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQLET--- 230
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLtre 239
|
250 260 270
....*....|....*....|....*....|
gi 648246410 231 FILDIAENSPPaPQLSGVISQTMLNGSLQI 260
Cdd:PRK11153 240 FIQSTLHLDLP-EDYLARLQAEPTTGSGPL 268
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-224 |
8.96e-39 |
|
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: 136.65 E-value: 8.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI----DKDLELAKQH 78
Cdd:COG1127 5 MIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 79 IGLVpqefnFNQ---FE--TVEQIV---LQQagYYGVTKALAKERAEKYLSKLDLwekrkERARN-----LSGGMKRRLM 145
Cdd:COG1127 84 IGML-----FQGgalFDslTVFENVafpLRE--HTDLSEAEIRELVLEKLELVGL-----PGAADkmpseLSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 146 IARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-199 |
1.01e-38 |
|
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: 135.30 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLVP 83
Cdd:COG4133 3 LEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEFNFNQFETVEQIVLQQAGYYGVtkALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPT 163
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 648246410 164 AGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAE 199
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
34-213 |
1.21e-38 |
|
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: 145.16 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 34 ALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLVPQEFNFNQFETVEQIVLQQAGYYGVTKALAK 113
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQ 1039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 114 ERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAqGITIILTTH 193
Cdd:TIGR01257 1040 LEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTH 1118
|
170 180
....*....|....*....|
gi 648246410 194 YLEEAEMLCRNIGIINRGEL 213
Cdd:TIGR01257 1119 HMDEADLLGDRIAIISQGRL 1138
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-227 |
3.95e-38 |
|
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: 135.32 E-value: 3.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTY---AGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK--DLELAKQ 77
Cdd:COG1124 1 MLEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRrrRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 78 hIGLVPQ--EFNFNQFETVEQIV---LQQAGyygvtKALAKERAEKYLSKLDLWEK-RKERARNLSGGMKRRLMIARALM 151
Cdd:COG1124 81 -VQMVFQdpYASLHPRHTVDRILaepLRIHG-----LPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648246410 152 HEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQ 227
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-214 |
1.63e-37 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 131.40 E-value: 1.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 5 EIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID--KDLELAKqHIGLV 82
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAslSPKELAR-KIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQefnfnqfetveqivlqqagyygvtkalakeraekYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEP 162
Cdd:cd03214 79 PQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 648246410 163 TAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-214 |
1.92e-37 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 130.63 E-value: 1.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG--FDIDKDLELAKQHIGL 81
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQefnfnqfetveqivlqqagyygvtkalakeraekylskldlwekrkerarnLSGGMKRRLMIARALMHEPKLLILDE 161
Cdd:cd03216 80 VYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 648246410 162 PTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-215 |
2.39e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 135.66 E-value: 2.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLVP 83
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEF----NFNQFETVeQIVLQQAgyyGVTKALAKERAEKYLSKLDL--WEKRkeRARNLSGGMKRRLMIARALMHEPKLL 157
Cdd:COG1118 82 QHYalfpHMTVAENI-AFGLRVR---PPSKAEIRARVEELLELVQLegLADR--YPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 158 ILDEPTAGVDIELRRSMWEFLTEI-NAQGITIILTTHYLEEAEMLCRNIGIINRGELIE 215
Cdd:COG1118 156 LLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQ 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-224 |
1.34e-36 |
|
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: 130.88 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI-DKDLELAKQHIGLV 82
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIrEQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNFNQFETVEQ---IVLQQAGYygvTKALAKERAEKYLSKLDLwEKRKERAR---NLSGGMKRRLMIARALMHEPKL 156
Cdd:cd03295 81 IQQIGLFPHMTVEEniaLVPKLLKW---PKEKIRERADELLALVGL-DPAEFADRyphELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 157 LILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-213 |
2.65e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 132.89 E-value: 2.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDkDLELAKQHIG 80
Cdd:COG3839 1 MASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-DLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEF----NFnqfeTVEQIV---LQQAgyyGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHE 153
Cdd:COG3839 79 MVFQSYalypHM----TVYENIafpLKLR---KVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648246410 154 PKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGEL 213
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-213 |
3.92e-36 |
|
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: 129.06 E-value: 3.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI----DKDLELAKQHI 79
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 80 GLVPQEF----NFNQFETVeQIVLQQAGyygVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPK 155
Cdd:cd03292 81 GVVFQDFrllpDRNVYENV-AFALEVTG---VPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 648246410 156 LLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGEL 213
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-224 |
1.28e-35 |
|
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: 128.55 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDL---ELAKQHIG 80
Cdd:TIGR04406 2 LVAENLIKSY-KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI-THLpmhERARLGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFNFNQFETVEQ---IVLQQAgyYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLL 157
Cdd:TIGR04406 80 YLPQEASIFRKLTVEEnimAVLEIR--KDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648246410 158 ILDEPTAGVD----IELRRSMwEFLTEinaQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:TIGR04406 158 LLDEPFAGVDpiavGDIKKII-KHLKE---RGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-226 |
1.36e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 134.00 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG--FDIDKDLELAKQH 78
Cdd:COG3845 3 PPALELRGITKRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 79 IGLVPQEF----NFnqfeTV-EQIVLQQAGYYGVTKALAKERA------EKYLSKLDLwekrKERARNLSGGMKRRLMIA 147
Cdd:COG3845 82 IGMVHQHFmlvpNL----TVaENIVLGLEPTKGGRLDRKAARArirelsERYGLDVDP----DAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 148 RALMHEPKLLILDEPTAG-----VDiELrrsmWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDL 222
Cdd:COG3845 154 KALYRGARILILDEPTAVltpqeAD-EL----FEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
....*...
gi 648246410 223 ----LAKL 226
Cdd:COG3845 229 seeeLAEL 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-222 |
1.51e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 133.61 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGfdidKDLEL-----A 75
Cdd:COG1129 2 EPLLEMRGISKSF-GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG----EPVRFrsprdA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 76 KQH-IGLVPQEFN-FNQFeTV-EQIVL--QQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARAL 150
Cdd:COG1129 77 QAAgIAIIHQELNlVPNL-SVaENIFLgrEPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 151 MHEPKLLILDEPTA---GVDIElrrSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDL 222
Cdd:COG1129 156 SRDARVLILDEPTAsltEREVE---RLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
13-193 |
1.80e-35 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 126.38 E-value: 1.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 13 YAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID---KDLELAKQHIGLVPQEFNFN 89
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysrKGLLERRQRVGLVFQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 90 QFE-TVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDI 168
Cdd:TIGR01166 81 LFAaDVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180
....*....|....*....|....*
gi 648246410 169 ELRRSMWEFLTEINAQGITIILTTH 193
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-202 |
1.89e-35 |
|
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: 126.99 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 5 EIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDLELAKQhIGLVPQ 84
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-KAKERRKS-IGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 85 EFNFNQF-ETVEQIVLQQAGYYGvtkaLAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPT 163
Cdd:cd03226 79 DVDYQLFtDSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 648246410 164 AGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLC 202
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVC 193
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-225 |
4.07e-35 |
|
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: 133.34 E-value: 4.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHIGL 81
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQE---FNfnqfETV-------------EQI--VLQQAGYYGVTKALAkeraEKYLSKLDlwekrkERARNLSGGMKRR 143
Cdd:COG4988 416 VPQNpylFA----GTIrenlrlgrpdasdEELeaALEAAGLDEFVAALP----DGLDTPLG------EGGRGLSGGQAQR 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 144 LMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEInAQGITIILTTHYLEEAEmLCRNIGIINRGELIENTSMKDLL 223
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLA-QADRILVLDDGRIVEQGTHEELL 559
|
..
gi 648246410 224 AK 225
Cdd:COG4988 560 AK 561
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-224 |
4.24e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 127.89 E-value: 4.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID---KDLELAKQHIG 80
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFNFNQFE-TVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLIL 159
Cdd:PRK13639 82 IVFQNPDDQLFApTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 160 DEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-213 |
5.94e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.70 E-value: 5.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHIGLV 82
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQE---FnfnqFETVEQIVLQQAGYYGvtKALAKERAEKYLSKLDLWEKRKER-ARNLSGGMKRRLMIARALMHEPKLLI 158
Cdd:COG4619 80 PQEpalW----GGTVRDNLPFPFQLRE--RKFDRERALELLERLGLPPDILDKpVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 159 LDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGEL 213
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-224 |
9.75e-35 |
|
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: 125.73 E-value: 9.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKD--LELAKQHIGL 81
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmHKRARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQEFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDE 161
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 162 PTAGVD---IELRRSMWEFLTEinaQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:cd03218 160 PFAGVDpiaVQDIQKIIKILKD---RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-217 |
4.36e-34 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 124.08 E-value: 4.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGG---FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI---DKDlELAK 76
Cdd:COG4181 8 IIELRGLTKTVGTGageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfalDED-ARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 77 ---QHIGLVPQEF----NFNQFETVeQIVLQQAGyygvtKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARA 149
Cdd:COG4181 87 lraRHVGFVFQSFqllpTLTALENV-MLPLELAG-----RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 150 LMHEPKLLILDEPTAGVDIELRRSMWEFLTEINA-QGITIILTTHYLEEAEMlCRNIGIINRGELIENT 217
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDT 228
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-225 |
4.36e-34 |
|
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: 131.49 E-value: 4.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAG-GFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDLELAK--QHI 79
Cdd:COG2274 473 DIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL-RQIDPASlrRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 80 GLVPQE---FN---------FNQFETVEQIV--LQQAGYYGVTKALAKeraeKYLSKLDlwekrkERARNLSGGMKRRLM 145
Cdd:COG2274 552 GVVLQDvflFSgtirenitlGDPDATDEEIIeaARLAGLHDFIEALPM----GYDTVVG------EGGSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 146 IARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEInAQGITIILTTHYLEEAEmLCRNIGIINRGELIENTSMKDLLAK 225
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-212 |
8.51e-34 |
|
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: 121.34 E-value: 8.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGF-EALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHIGL 81
Cdd:cd03228 1 IEFKNVSFSYPGRPkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQEFnfnqfetveqivlqqagyygvtkalakeraekYLSKLDLWEkrkerarN-LSGGMKRRLMIARALMHEPKLLILD 160
Cdd:cd03228 81 VPQDP--------------------------------FLFSGTIRE-------NiLSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 648246410 161 EPTAGVDIELRRSMWEFLTEInAQGITIILTTHYLEEAEMlCRNIGIINRGE 212
Cdd:cd03228 122 EATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-224 |
1.55e-33 |
|
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: 125.17 E-value: 1.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTY---AGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLV---NKTSGTVKVFGFDI----DKDL- 72
Cdd:COG0444 2 LEVRNLKVYFptrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLlklsEKELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 73 ELAKQHIGLVPQE-FN-FNQFETV-EQI--VLQQAGyyGVTKALAKERAEKYLSKLDLwEKRKERARN----LSGGMKRR 143
Cdd:COG0444 82 KIRGREIQMIFQDpMTsLNPVMTVgDQIaePLRIHG--GLSKAEARERAIELLERVGL-PDPERRLDRypheLSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 144 LMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDL 222
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
..
gi 648246410 223 LA 224
Cdd:COG0444 239 FE 240
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-215 |
2.17e-33 |
|
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: 122.44 E-value: 2.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEaLKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDLELAKQHIGLVP 83
Cdd:cd03299 1 LKVENLSKDW-KEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEF----NFNQFETVEqivlqqagyYGVTKALA--KERAEKYLS---KLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:cd03299 78 QNYalfpHMTVYKNIA---------YGLKKRKVdkKEIERKVLEiaeMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648246410 155 KLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIE 215
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-225 |
2.43e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 128.35 E-value: 2.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 2 YALEIEQLRKTYAG-GFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHI 79
Cdd:COG4987 332 PSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 80 GLVPQE---FNfnqfETV-------------EQI--VLQQAGYYGVTKALAKeraekylsKLDLWekRKERARNLSGGMK 141
Cdd:COG4987 412 AVVPQRphlFD----TTLrenlrlarpdatdEELwaALERVGLGDWLAALPD--------GLDTW--LGEGGRRLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 142 RRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEInAQGITIILTTHYLEEAEMLCRnIGIINRGELIENTSMKD 221
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERMDR-ILVLEDGRIVEQGTHEE 555
|
....
gi 648246410 222 LLAK 225
Cdd:COG4987 556 LLAQ 559
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-214 |
2.90e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 123.31 E-value: 2.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 2 YALEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLE-LAKQHIG 80
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFNFNQFE-TVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLIL 159
Cdd:PRK13647 83 LVFQDPDDQVFSsTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 160 DEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-259 |
3.69e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 122.38 E-value: 3.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI----DKD-------- 71
Cdd:PRK10619 6 LNVIDLHKRY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrDKDgqlkvadk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 72 --LELAKQHIGLVPQEFNFNQFETV-EQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKER-ARNLSGGMKRRLMIA 147
Cdd:PRK10619 85 nqLRLLRTRLTMVFQHFNLWSHMTVlENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 148 RALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLaklq 227
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF---- 240
|
250 260 270
....*....|....*....|....*....|..
gi 648246410 228 letfildiaeNSPPAPQLsgvisQTMLNGSLQ 259
Cdd:PRK10619 241 ----------GNPQSPRL-----QQFLKGSLK 257
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-215 |
4.23e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 122.04 E-value: 4.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG--FDI-----DKDLELA 75
Cdd:COG4161 2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqFDFsqkpsEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 76 KQHIGLVPQEFNFNQFETVEQIVLQQ-AGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648246410 155 KLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIE 215
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
15-245 |
9.05e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.97 E-value: 9.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 15 GGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID---KDLELAKQHIGLVPQEFN-FNQ 90
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQEAGMVFQQFYlFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 91 FETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIEL 170
Cdd:PRK09493 92 LTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 171 RRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLaklqletfildiaeNSPPAPQL 245
Cdd:PRK09493 172 RHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI--------------KNPPSQRL 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-215 |
5.02e-32 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 118.96 E-value: 5.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG--FDI-----DKDLELA 75
Cdd:PRK11124 2 SIQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFsktpsDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 76 KQHIGLVPQEFNFNQFETV-EQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVqQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648246410 155 KLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIE 215
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-224 |
5.36e-32 |
|
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: 118.76 E-value: 5.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID----KDLELAKQHI 79
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 80 GLVpqeFNFNQ-FE--TVEQIV---LQQAgyygvTKALAKERAEKYLSKLD---LWEKRKERARNLSGGMKRRLMIARAL 150
Cdd:cd03261 80 GML---FQSGAlFDslTVFENVafpLREH-----TRLSEEEIREIVLEKLEavgLRGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 151 MHEPKLLILDEPTAGVD-------IELRRSMWEflteinAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLL 223
Cdd:cd03261 152 ALDPELLLYDEPTAGLDpiasgviDDLIRSLKK------ELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
.
gi 648246410 224 A 224
Cdd:cd03261 226 A 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-222 |
8.68e-32 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 118.01 E-value: 8.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKD--LELAKQHIGL 81
Cdd:TIGR03410 1 LEVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLppHERARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQ--EFnFNQFETVEQIvlqQAGYYGVTKALAKERAEKYlsklDLW----EKRKERARNLSGGMKRRLMIARALMHEPK 155
Cdd:TIGR03410 80 VPQgrEI-FPRLTVEENL---LTGLAALPRRSRKIPDEIY----ELFpvlkEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648246410 156 LLILDEPTAGV------DIElrrsmwEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDL 222
Cdd:TIGR03410 152 LLLLDEPTEGIqpsiikDIG------RVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-224 |
1.75e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 119.42 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 17 FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKD---LELAKQHIGLVPQEFNFNQFET 93
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktKEKEKVLEKLVIQKTRFKKIKK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 94 VEQI------VLQQAGY-----------------YGVTKALAKERAEKYLSKLDLWEKRKERAR-NLSGGMKRRLMIARA 149
Cdd:PRK13651 100 IKEIrrrvgvVFQFAEYqlfeqtiekdiifgpvsMGVSKEEAKKRAAKYIELVGLDESYLQRSPfELSGGQKRRVALAGI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 150 LMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-198 |
1.83e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 118.65 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 19 ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI--DKDLELAKQHIGLVPQEFNfNQFetVEQ 96
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdEENLWDIRNKAGMVFQNPD-NQI--VAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 97 IVLQQAGY----YGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRR 172
Cdd:PRK13633 102 IVEEDVAFgpenLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180
....*....|....*....|....*..
gi 648246410 173 SMWEFLTEINAQ-GITIILTTHYLEEA 198
Cdd:PRK13633 182 EVVNTIKELNKKyGITIILITHYMEEA 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-214 |
1.92e-31 |
|
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: 116.63 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVE---KGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG---FDIDKDLELAKQ--HIGLVPQEFN-FNQ 90
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKKINLPPQqrKIGLVFQQYAlFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 91 FETVEQIVLqqaGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIEL 170
Cdd:cd03297 90 LNVRENLAF---GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 648246410 171 RRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:cd03297 167 RLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
3-228 |
2.73e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 118.31 E-value: 2.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGG--FE--ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI-----DKDLE 73
Cdd:PRK13649 2 GINLQNVSYTYQAGtpFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstskNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 74 LAKQHIGLVpqeFNFNQFETVEQIVLQQAGY----YGVTKALAKERAEKYLSKLDLWEKRKERAR-NLSGGMKRRLMIAR 148
Cdd:PRK13649 82 QIRKKVGLV---FQFPESQLFEETVLKDVAFgpqnFGVSQEEAEALAREKLALVGISESLFEKNPfELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 149 ALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQL 228
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDF 238
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-224 |
1.04e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 116.85 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGG--FEA--LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI-----DKDLE 73
Cdd:PRK13641 2 SIKFENVDYIYSPGtpMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 74 LAKQHIGLVpqeFNFNQFETVEQIVLQQAGY----YGVTKALAKERAEKYLSKLDLWEKRKERAR-NLSGGMKRRLMIAR 148
Cdd:PRK13641 82 KLRKKVSLV---FQFPEAQLFENTVLKDVEFgpknFGFSEDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 149 ALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-229 |
1.17e-30 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 115.62 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYAGGfEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQ--- 77
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQ-TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 78 ------HIGLVPQEFNFNQFETV-EQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARAL 150
Cdd:PRK11264 80 irqlrqHVGFVFQNFNLFPHRTVlENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 151 MHEPKLLILDEPTAGVDIELrrsMWEFLTEINA---QGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQ 227
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPEL---VGEVLNTIRQlaqEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
..
gi 648246410 228 LE 229
Cdd:PRK11264 237 QP 238
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-245 |
1.33e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 116.06 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHI 79
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKeNIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 80 GLVPQEFNFNQFE-TVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLI 158
Cdd:PRK13652 81 GLVFQNPDDQIFSpTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 159 LDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELI------ENTSMKDLLAKLQLETf 231
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVaygtveEIFLQPDLLARVHLDL- 239
|
250
....*....|....
gi 648246410 232 ildiaensPPAPQL 245
Cdd:PRK13652 240 --------PSLPKL 245
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-213 |
1.52e-30 |
|
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: 114.27 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDkDLELAKQHIGLVP 83
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-DLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEF----NFNQFETVEqIVLQQAgyyGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLIL 159
Cdd:cd03301 79 QNYalypHMTVYDNIA-FGLKLR---KVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 160 DEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGEL 213
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-233 |
5.31e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 113.84 E-value: 5.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYAGGfEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfgfdIDKDLEL------ 74
Cdd:PRK10895 1 MATLTAKNLAKAYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIII----DDEDISLlplhar 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 75 AKQHIGLVPQEFN-FNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHE 153
Cdd:PRK10895 76 ARRGIGYLPQEASiFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 154 PKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQLETFIL 233
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYL 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-213 |
7.41e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 113.95 E-value: 7.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGfEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLV--NKTSGT-VKVFGFDID------KDLEL 74
Cdd:PRK09984 5 IRVEKLAKTFNQH-QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRTVQregrlaRDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 75 AKQHIGLVPQEFNF-NQFETVEQIVLqqaGYYGVT----------KALAKERAEKYLSKLDLWEKRKERARNLSGGMKRR 143
Cdd:PRK09984 84 SRANTGYIFQQFNLvNRLSVLENVLI---GALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648246410 144 LMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGEL 213
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-237 |
8.35e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 114.35 E-value: 8.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGG--FE--ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI-----DKDLEL 74
Cdd:PRK13634 3 ITFQKVEHRYQYKtpFErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 75 AKQHIGLVPQeFNFNQF--ETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERAR-NLSGGMKRRLMIARALM 151
Cdd:PRK13634 83 LRKKVGIVFQ-FPEHQLfeETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 152 HEPKLLILDEPTAGVDIELRRSMWEFLTEIN-AQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQ-LE 229
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDeLE 241
|
....*...
gi 648246410 230 TFILDIAE 237
Cdd:PRK13634 242 AIGLDLPE 249
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-215 |
9.57e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 116.09 E-value: 9.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFeALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDLELAKQHIGLVP 83
Cdd:PRK11607 20 LEIRNLTKSFDGQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEFNFNQFETVEQIV---LQQAGyygVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILD 160
Cdd:PRK11607 98 QSYALFPHMTVEQNIafgLKQDK---LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 161 EPTAGVDIELRRSM-WEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIE 215
Cdd:PRK11607 175 EPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-235 |
1.32e-29 |
|
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: 113.51 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 7 EQLRKTyaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI----DKDL-ELAKQHIGL 81
Cdd:cd03294 29 EILKKT--GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELrELRRKKISM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQEFNFNQFETVeqivLQQAGY----YGVTKALAKERAEKYLSKLDL--WEKRKERArnLSGGMKRRLMIARALMHEPK 155
Cdd:cd03294 107 VFQSFALLPHRTV----LENVAFglevQGVPRAEREERAAEALELVGLegWEHKYPDE--LSGGMQQRVGLARALAVDPD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 156 LLILDEPTAGVDIELRRSMWEFLTEINA-QGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLL---AKLQLETF 231
Cdd:cd03294 181 ILLMDEAFSALDPLIRREMQDELLRLQAeLQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILtnpANDYVREF 260
|
....
gi 648246410 232 ILDI 235
Cdd:cd03294 261 FRGV 264
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-215 |
1.69e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 112.63 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRkTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVN-----KTSGTVKVFGFDI---DKDL 72
Cdd:PRK14267 2 KFAIETVNLR-VYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIyspDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 73 ELAKQHIGLVPQEFNFNQFETVEQIVLQQAGYYGVTKALAK--ERAEKYLSKLDLWEKRKER----ARNLSGGMKRRLMI 146
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALWDEVKDRlndyPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 147 ARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQgITIILTTHYLEEAEMLCRNIGIINRGELIE 215
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-198 |
1.85e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 112.65 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYAGGFE---ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI---DKDLEL 74
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 75 AKQHIGLVPQefnFNQFETVEqIVLQQAGyygVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:COG4525 81 VFQKDALLPW---LNVLDNVA-FGLRLRG---VPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 648246410 155 KLLILDEPTAGVDIELRRSMWEFLTEI-NAQGITIILTTHYLEEA 198
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEA 198
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-216 |
2.39e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 117.52 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGG---FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI-----DKDLELA 75
Cdd:PRK10535 5 LELKDIRRSYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldaDALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 76 KQHIGLVPQEFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPK 155
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648246410 156 LLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGiINRGELIEN 216
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIE-IRDGEIVRN 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-199 |
3.35e-29 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 117.53 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 15 GGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID-KDLElAKQHIGLVPQEFNFNQFET 93
Cdd:NF033858 277 GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDaGDIA-TRRRVGYMSQAFSLYGELT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 94 VEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRS 173
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180
....*....|....*....|....*..
gi 648246410 174 MWEFLTEIN-AQGITIILTTHYLEEAE 199
Cdd:NF033858 436 FWRLLIELSrEDGVTIFISTHFMNEAE 462
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-215 |
3.38e-29 |
|
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: 111.66 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 2 YALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDLELAKQHIGL 81
Cdd:cd03296 1 MSIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQEFNFNQFETVEQIV---LQ-QAGYYGVTKALAKERAEKYLS--KLDLWEKRkeRARNLSGGMKRRLMIARALMHEPK 155
Cdd:cd03296 79 VFQHYALFRHMTVFDNVafgLRvKPRSERPPEAEIRAKVHELLKlvQLDWLADR--YPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648246410 156 LLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIE 215
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQ 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-214 |
2.26e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.52 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGG--FE--ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI-DKDLELA--K 76
Cdd:PRK13637 3 IKIENLTHIYMEGtpFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItDKKVKLSdiR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 77 QHIGLVPQEFNFNQFE-TVEQIVLQQAGYYGVTKALAKERAEKYLSKLDL-WEKRKERAR-NLSGGMKRRLMIARALMHE 153
Cdd:PRK13637 83 KKVGLVFQYPEYQLFEeTIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdYEDYKDKSPfELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648246410 154 PKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-193 |
3.49e-28 |
|
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: 108.51 E-value: 3.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNK---TSGTVKVFGFDIDKDLelAKQHIGLVPQEFNFNQFETVEQ 96
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQ--FQKCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 97 IVlqqagYYGVTKALAKERAEKYLSKLDLWEK---------RKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 167
Cdd:cd03234 101 TL-----TYTAILRLPRKSSDAIRKKRVEDVLlrdlaltriGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180
....*....|....*....|....*.
gi 648246410 168 IELRRSMWEFLTEINAQGITIILTTH 193
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-224 |
3.65e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 108.69 E-value: 3.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFeaLKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKdLELAKQHIGLVP 83
Cdd:COG3840 2 LRLDDLTYRY-GDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-LPPAERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEFN-FNQFeTVEQIVlqqagYYGVTKAL-----AKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLL 157
Cdd:COG3840 78 QENNlFPHL-TVAQNI-----GLGLRPGLkltaeQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648246410 158 ILDEPTAGVDIELRRSMWEFLTEINA-QGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-225 |
4.14e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 113.72 E-value: 4.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDLELAK--QHIG 80
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI-RDLTLESlrRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQE-FNFNqfETVEQIVLqqagyYG--------VTKALAKERAEKYLSKLDlwekrK-------ERARNLSGGMKRRL 144
Cdd:COG1132 418 VVPQDtFLFS--GTIRENIR-----YGrpdatdeeVEEAAKAAQAHEFIEALP-----DgydtvvgERGVNLSGGQRQRI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 145 MIARALMHEPKLLILDEPTAGVDIE----LRRSMWEFLteinaQGITIILTTHYLEEAEMlCRNIGIINRGELIENTSMK 220
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTEtealIQEALERLM-----KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHE 559
|
....*
gi 648246410 221 DLLAK 225
Cdd:COG1132 560 ELLAR 564
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-304 |
5.40e-28 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 110.98 E-value: 5.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTtiGIISSLVNKTSGTVKVFGFDI-DKDLELAKQHIGL 81
Cdd:NF000106 13 AVEVRGLVKHF-GEVKAVDGVDLDVREGTVLGVLGP*GAA**R--GALPAHV*GPDAGRRPWRF*TwCANRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 -VPQEFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILD 160
Cdd:NF000106 90 hRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 161 EPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQLETFILDIAeNSP 240
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPA-HAA 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 241 PAPQLSGVISQTML-----------NGSLQIELEKTKGLNSVFSQLTEQGITVLSMRNKANRLEELFVSIVQQQS 304
Cdd:NF000106 249 ELDRMVGAIAQAGLdgiagatadheDGVVNVPIVSDEQLSAVVGMLGERGFTISGHQHPSAQL*EVFLAITGQKT 323
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-199 |
6.67e-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: 112.77 E-value: 6.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI-DKDLELAKQHIGL 81
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLaDADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQE-FNFNQfeTV-EQI--------------VLQQAGYYGVTKALakerAEKYLSKLDlwekrkERARNLSGGMKRRLM 145
Cdd:TIGR02857 401 VPQHpFLFAG--TIaENIrlarpdasdaeireALERAGLDEFVAAL----PQGLDTPIG------EGGAGLSGGQAQRLA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 648246410 146 IARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEInAQGITIILTTHYLEEAE 199
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAA 521
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-215 |
6.82e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.59 E-value: 6.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 2 YALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKST---TIGIISSLV--NKTSGTVKVFGFDI---DKDLE 73
Cdd:COG1117 10 PKIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIpgARVEGEILLDGEDIydpDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 74 LAKQHIGLVPQE---FNFNQFETVEqivlqqagyYGV------TKALAKERAEKYLSKLDLWEKRKER----ARNLSGGM 140
Cdd:COG1117 89 ELRRRVGMVFQKpnpFPKSIYDNVA---------YGLrlhgikSKSELDEIVEESLRKAALWDEVKDRlkksALGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 141 KRRLMIARALMHEPKLLILDEPTAGVD------IElrrsmwEFLTEInAQGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDpistakIE------ELILEL-KKDYTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
.
gi 648246410 215 E 215
Cdd:COG1117 233 E 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-225 |
1.75e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.01 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 2 YALEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID---KDLELAKQH 78
Cdd:PRK13636 4 YILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 79 IGLVPQEFNFNQFE-TVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLL 157
Cdd:PRK13636 84 VGMVFQDPDNQLFSaSVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 158 ILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAK 225
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-225 |
2.80e-27 |
|
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: 106.16 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAG-GFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDLELA--KQHIG 80
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV-RDYTLAslRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQE-FNFNqfETVEQIVLqqagyYGVTKALAKE--RAEKYLSKLDLWEKRK--------ERARNLSGGMKRRLMIARA 149
Cdd:cd03251 80 LVSQDvFLFN--DTVAENIA-----YGRPGATREEveEAARAANAHEFIMELPegydtvigERGVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 150 LMHEPKLLILDEPTAGVDIELRRSMWEFLTEInAQGITIILTTHYL---EEAEMLCrnigIINRGELIENTSMKDLLAK 225
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLstiENADRIV----VLEDGKIVERGTHEELLAQ 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-215 |
3.02e-27 |
|
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: 105.69 E-value: 3.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 10 RKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGfDIDKDLELAkqhIGLVPqEFnfn 89
Cdd:cd03220 28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSLLGLG---GGFNP-EL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 90 qfeTVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIE 169
Cdd:cd03220 100 ---TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 648246410 170 LRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIE 215
Cdd:cd03220 177 FQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-198 |
4.11e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.62 E-value: 4.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 15 GGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGfdidkdlelaKQHIGLVPQefnfnQFE-- 92
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----------GARVAYVPQ-----RSEvp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 93 -----TVEQIV----LQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPT 163
Cdd:NF040873 68 dslplTVRDLVamgrWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|....*
gi 648246410 164 AGVDIELRRSMWEFLTEINAQGITIILTTHYLEEA 198
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-227 |
4.13e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 107.17 E-value: 4.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 17 FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI-----DKDLELAKQHIGLVPQEFNFNQF 91
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkDKYIRPVRKRIGMVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 92 E-TVEQIVLQQAGYYGVTKALAKERAEKYLskLDLWEKRKERARN---LSGGMKRRLMIARALMHEPKLLILDEPTAGVD 167
Cdd:PRK13646 100 EdTVEREIIFGPKNFKMNLDEVKNYAHRLL--MDLGFSRDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648246410 168 IELRRSMWEFLTEINA-QGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQ 227
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-237 |
4.48e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 106.61 E-value: 4.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGGFE-ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKD-LELAKQHIG 80
Cdd:PRK13632 7 MIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFNfNQF--ETVEQIVLqqagyYG-----VTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHE 153
Cdd:PRK13632 87 IIFQNPD-NQFigATVEDDIA-----FGlenkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 154 PKLLILDEPTAGVDIELRRSMWEFLTEINAQGI-TIILTTHYLEEAeMLCRNIGIINRGELI------ENTSMKDLLAKL 226
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKLIaqgkpkEILNNKEILEKA 239
|
250
....*....|..
gi 648246410 227 QLET-FILDIAE 237
Cdd:PRK13632 240 KIDSpFIYKLSK 251
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-304 |
4.65e-27 |
|
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: 111.26 E-value: 4.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFE-ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLV 82
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEP 162
Cdd:TIGR01257 2018 PQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 163 TAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQlETFILDIAENSPP- 241
Cdd:TIGR01257 2098 TTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFG-DGYIVTMKIKSPKd 2176
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648246410 242 --APQLSGV--ISQTMLNGSLQIELE--------KTKGLNSVFSQLTEQGITVLSMRNKANR--LEELFVSIVQQQS 304
Cdd:TIGR01257 2177 dlLPDLNPVeqFFQGNFPGSVQRERHynmlqfqvSSSSLARIFQLLISHKDSLLIEEYSVTQttLDQVFVNFAKQQT 2253
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-214 |
7.15e-27 |
|
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: 104.50 E-value: 7.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 24 SLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKdLELAKQHIGLVPQEFNFNQFETVEQIVlqqag 103
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA-APPADRPVSMLFQENNLFAHLTVEQNV----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 104 YYGVTKALA-----KERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFL 178
Cdd:cd03298 92 GLGLSPGLKltaedRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 648246410 179 TEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:cd03298 172 LDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-228 |
8.93e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 106.36 E-value: 8.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 19 ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI-----DKDLELAKQHIGLVpqeFNFNQFET 93
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstskQKEIKPVRKKVGVV---FQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 94 VEQIVLQQAGYYGVTKALAKERAEKY---------LSKlDLWEKRkerARNLSGGMKRRLMIARALMHEPKLLILDEPTA 164
Cdd:PRK13643 98 FEETVLKDVAFGPQNFGIPKEKAEKIaaeklemvgLAD-EFWEKS---PFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648246410 165 GVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQL 228
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDF 237
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-168 |
1.01e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.24 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID--KDLELAKqHIG 80
Cdd:PRK13548 2 MLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwSPAELAR-RRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQE----FNFnqfeTVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALM----- 151
Cdd:PRK13548 80 VLPQHsslsFPF----TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170
....*....|....*...
gi 648246410 152 -HEPKLLILDEPTAGVDI 168
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDL 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-195 |
1.64e-26 |
|
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: 108.99 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI-DKDLELAKQHIGLV 82
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVsSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNFnqFETV--EQIVLQQAGYYG--VTKALAKERAEKYLSKLD--LWEKRKERARNLSGGMKRRLMIARALMHEPKL 156
Cdd:TIGR02868 415 AQDAHL--FDTTvrENLRLARPDATDeeLWAALERVGLADWLRALPdgLDTVLGEGGARLSGGERQRLALARALLADAPI 492
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 648246410 157 LILDEPTAGVDIELRRSMwefLTEINA--QGITIILTTHYL 195
Cdd:TIGR02868 493 LLLDEPTEHLDAETADEL---LEDLLAalSGRTVVLITHHL 530
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-223 |
1.89e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 104.61 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVN-----KTSGTVKVFGFDIDK-DLEL 74
Cdd:PRK14247 1 MNKIEIRDLKVSF-GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKmDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 75 AKQHIGLVPQEFN-FNQFETVEQIVLQ-QAGYYGVTKALAKERAEKYLSKLDLWEKRKER----ARNLSGGMKRRLMIAR 148
Cdd:PRK14247 80 LRRRVQMVFQIPNpIPNLSIFENVALGlKLNRLVKSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 149 ALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQgITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLL 223
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-193 |
2.12e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.23 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 6 IEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVkvfgfDIDKDLElakqhIGLVPQE 85
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-----SIPKGLR-----IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 86 FNFNQFETVEQIVLQ--------QAGYYGVTKALAKE------------------------RAEKYLSKLDLWEKRKERA 133
Cdd:COG0488 70 PPLDDDLTVLDTVLDgdaelralEAELEELEAKLAEPdedlerlaelqeefealggweaeaRAEEILSGLGFPEEDLDRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648246410 134 -RNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRsmW--EFLteINAQGiTIILTTH 193
Cdd:COG0488 150 vSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFL--KNYPG-TVLVVSH 207
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-213 |
2.27e-26 |
|
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: 102.29 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFEA-LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHIGL 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQEFNFnqFE-TVEQIVlqqagyygvtkalakeraekylskldlwekrkerarnLSGGMKRRLMIARALMHEPKLLILD 160
Cdd:cd03246 81 LPQDDEL--FSgSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 648246410 161 EPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRnIGIINRGEL 213
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADR-ILVLEDGRV 173
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-214 |
3.59e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 105.32 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 17 FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLVPQEF-NFNQFETVE 95
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKIkNFKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 96 QIVLQQAGY-----------------YGVTKALAKERAEKYLSKLDLWEKRKERAR-NLSGGMKRRLMIARALMHEPKLL 157
Cdd:PRK13631 119 SMVFQFPEYqlfkdtiekdimfgpvaLGVKKSEAKKLAKFYLNKMGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 648246410 158 ILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3-257 |
4.09e-26 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 104.19 E-value: 4.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLElaKQHIGLV 82
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ--KNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQ--EFNFNQFETVEQIVLQqaGYYG------VTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:PRK15056 84 PQseEVDWSFPVLVEDVVMM--GRYGhmgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 155 KLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCrnigiiNRGELIENTsmkdLLAKLQLETFIld 234
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFC------DYTVMVKGT----VLASGPTETTF-- 229
|
250 260
....*....|....*....|...
gi 648246410 235 IAENSPPApqLSGVISQTMLNGS 257
Cdd:PRK15056 230 TAENLELA--FSGVLRHVALNGS 250
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-244 |
5.45e-26 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 103.73 E-value: 5.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYA-GGF-------EALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLEL 74
Cdd:TIGR02769 3 LEVRDVTHTYRtGGLfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQlDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 75 AK---QHIGLVPQEF--NFNQFETVEQIVLQQAGYYgvTKALAKERAEKYLSKLDLWEKRKE----RARNLSGGMKRRLM 145
Cdd:TIGR02769 83 RRafrRDVQLVFQDSpsAVNPRMTVRQIIGEPLRHL--TSLDESEQKARIAELLDMVGLRSEdadkLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 146 IARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLL- 223
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLs 240
|
250 260
....*....|....*....|....*
gi 648246410 224 ----AKLQLETFILdiaensPPAPQ 244
Cdd:TIGR02769 241 fkhpAGRNLQSAVL------PEHPV 259
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
15-211 |
9.77e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 105.31 E-value: 9.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 15 GGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID-KDLELAKQHIGLVPQE----FNFn 89
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVASVPQDtslsFEF- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 90 qfeTVEQIV-------LQQAGYYGVTKALAKERAekyLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEP 162
Cdd:PRK09536 93 ---DVRQVVemgrtphRSRFDTWTETDRAAVERA---MERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 648246410 163 TAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRG 211
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-215 |
2.43e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 102.02 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 19 ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDL--ELAKQhIGLVPQEFNfNQF--ETV 94
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwDVRRQ-VGMVFQNPD-NQFvgATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 95 EQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSM 174
Cdd:PRK13635 100 QDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREV 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 648246410 175 WEFLTEINAQ-GITIILTTHYLEEAEMLCRNIgIINRGELIE 215
Cdd:PRK13635 180 LETVRQLKEQkGITVLSITHDLDEAAQADRVI-VMNKGEILE 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-168 |
1.27e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 99.80 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLrkTY-AGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID--KDLELAKqHIG 80
Cdd:COG4559 2 LEAENL--SVrLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAawSPWELAR-RRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQE----FNFnqfeTVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRkERA-RNLSGGMKRRLMIARAL----- 150
Cdd:COG4559 79 VLPQHsslaFPF----TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLA-GRSyQTLSGGEQQRVQLARVLaqlwe 153
|
170 180
....*....|....*....|
gi 648246410 151 --MHEPKLLILDEPTAGVDI 168
Cdd:COG4559 154 pvDGGPRWLFLDEPTSALDL 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-225 |
1.87e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 102.98 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 2 YALEIEQLRKTYAGG-FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELA-KQHI 79
Cdd:PRK11160 337 VSLTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 80 GLVPQEFN-FNQF-----------ETVEQI--VLQQAGYygvtkalakeraEKYLS---KLDLWekRKERARNLSGGMKR 142
Cdd:PRK11160 417 SVVSQRVHlFSATlrdnlllaapnASDEALieVLQQVGL------------EKLLEddkGLNAW--LGEGGRQLSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 143 RLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEInAQGITIILTTHYLEEAEMLCRnIGIINRGELIENTSMKDL 222
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGLEQFDR-ICVMDNGQIIEQGTHQEL 560
|
...
gi 648246410 223 LAK 225
Cdd:PRK11160 561 LAQ 563
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-198 |
2.04e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.56 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDkDLELAKQHIGLVP 83
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-HVPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEF----NFNQFETVEqivlqqagyYG-----VTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:PRK09452 93 QSYalfpHMTVFENVA---------FGlrmqkTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 648246410 155 KLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEA 198
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEA 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-225 |
2.13e-24 |
|
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: 98.45 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 5 EIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDLELA--KQHIGLV 82
Cdd:cd03254 4 EFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI-RDISRKslRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQE--------------FNFNQFETVEQIVLQQAGYYGVTKALAKeraekylsklDLWEKRKERARNLSGGMKRRLMIAR 148
Cdd:cd03254 83 LQDtflfsgtimenirlGRPNATDEEVIEAAKEAGAHDFIMKLPN----------GYDTVLGENGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 149 ALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINaQGITIILTTHYL---EEAEMlcrnIGIINRGELIENTSMKDLLAK 225
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLstiKNADK----ILVLDDGKIIEEGTHDELLAK 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-225 |
2.16e-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: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHIGLV 82
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQE---FNFNQFETV---------EQIV--LQQAGYYGVTKALakerAEKYLSKLDlwekrkERARNLSGGMKRRLMIAR 148
Cdd:cd03253 81 PQDtvlFNDTIGYNIrygrpdatdEEVIeaAKAAQIHDKIMRF----PDGYDTIVG------ERGLKLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648246410 149 ALMHEPKLLILDEPTAGVDIELRRSMWEFLTEInAQGITIILTTHYLEEAeMLCRNIGIINRGELIENTSMKDLLAK 225
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-193 |
2.60e-24 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 98.02 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI----DKDLELAKQHI 79
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 80 GLVPQEFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLIL 159
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190
....*....|....*....|....*....|....
gi 648246410 160 DEPTAGVDIELRRSMWEFLTEINAQGITIILTTH 193
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-211 |
2.94e-24 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 98.31 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK---DLELAKQHIGLVPqefnfnqFETVEQ 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpDRMVVFQNYSLLP-------WLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 97 IVlqqagYYGVTKALA-------KERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIE 169
Cdd:TIGR01184 74 NI-----ALAVDRVLPdlskserRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 648246410 170 LRRSMWEFLTEI-NAQGITIILTTHYLEEAEMLCRNIGIINRG 211
Cdd:TIGR01184 149 TRGNLQEELMQIwEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-189 |
3.65e-24 |
|
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: 97.89 E-value: 3.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYA----GG--FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGII---------SSLVNKTSGTVKVFGFDI 68
Cdd:COG4778 5 LEVENLSKTFTlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylpdsgSILVRHDGGWVDLAQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 69 DKDLELAKQHIGLVpqefnfNQF----------ETVEQIVLQQagyyGVTKALAKERAEKYLSKLDLwekrKERARNL-- 136
Cdd:COG4778 85 REILALRRRTIGYV------SQFlrviprvsalDVVAEPLLER----GVDREEARARARELLARLNL----PERLWDLpp 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 137 ---SGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITII 189
Cdd:COG4778 151 atfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-198 |
5.87e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.85 E-value: 5.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGGfEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID---KDLELAKQHI 79
Cdd:PRK11248 1 MLQISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 80 GLVPQEfnfNQFETVEqIVLQQAGyygVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLIL 159
Cdd:PRK11248 80 GLLPWR---NVQDNVA-FGLQLAG---VEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 648246410 160 DEPTAGVDIELRRSMWEFLTEI-NAQGITIILTTHYLEEA 198
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEA 192
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-214 |
6.88e-24 |
|
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: 96.89 E-value: 6.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 18 EALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHIGLVPQE---FN------ 87
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDvtlFYgtlrdn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 88 ---FNQFETVEQIvLQQAGYYGVTKALAKERAekylsKLDLweKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTA 164
Cdd:cd03245 98 itlGAPLADDERI-LRAAELAGVTDFVNKHPN-----GLDL--QIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 648246410 165 GVDIELRRSMWEFLTEInAQGITIILTTHYLEEAEMLCRNIgIINRGELI 214
Cdd:cd03245 170 AMDMNSEERLKERLRQL-LGDKTLIIITHRPSLLDLVDRII-VMDSGRIV 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-205 |
1.63e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.04 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGG---FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-----DLELA 75
Cdd:PRK11629 6 LQCDNLCKRYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaaKAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 76 KQHIGLVPQeF-----NFNQFETVEQIVLqqagYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARAL 150
Cdd:PRK11629 86 NQKLGFIYQ-FhhllpDFTALENVAMPLL----IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 151 MHEPKLLILDEPTAGVDIELRRSMWEFLTEINA-QGITIILTTHYLEEAEMLCRNI 205
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-225 |
2.66e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 100.20 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKdlelaKQH---- 78
Cdd:NF033858 1 VARLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD-----ARHrrav 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 79 ---IGLVPQEFNFNQFET--VEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHE 153
Cdd:NF033858 75 cprIAYMPQGLGKNLYPTlsVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 154 PKLLILDEPTAGVDIELRRSMWEFLTEINAQ--GITIILTTHYLEEAE-------MlcrnigiiNRGELIENTSMKDLLA 224
Cdd:NF033858 155 PDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAErfdwlvaM--------DAGRVLATGTPAELLA 226
|
.
gi 648246410 225 K 225
Cdd:NF033858 227 R 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-232 |
4.56e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 95.61 E-value: 4.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLrKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVN-----KTSGTVKVFGFDI----DKDLEL 74
Cdd:PRK14239 6 LQVSDL-SVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysprTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 75 AKQhIGLVPQEFNFNQFETVEQIVlqqagyYGV------TKALAKERAEKYLSKLDLWEKRKER----ARNLSGGMKRRL 144
Cdd:PRK14239 85 RKE-IGMVFQQPNPFPMSIYENVV------YGLrlkgikDKQVLDEAVEKSLKGASIWDEVKDRlhdsALGLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 145 MIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQgITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLL- 223
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFm 236
|
250
....*....|.
gi 648246410 224 --AKLQLETFI 232
Cdd:PRK14239 237 npKHKETEDYI 247
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-225 |
4.70e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.15 E-value: 4.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 10 RKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGfDIDKDLELAkqhIGLVPqEFnfn 89
Cdd:COG1134 32 RRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSALLELG---AGFHP-EL--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 90 qfeTVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIE 169
Cdd:COG1134 104 ---TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 648246410 170 LR-RSMwEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAK 225
Cdd:COG1134 181 FQkKCL-ARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-193 |
4.97e-23 |
|
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: 93.77 E-value: 4.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 10 RKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVN--KTSGTVKVFGFDIDKDLelAKQHIGLVPQEFN 87
Cdd:cd03213 15 SSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRS--FRKIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 88 FNQFETVEQIVLQQAgyygvtkalakeraekylsKLdlwekrkeraRNLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 167
Cdd:cd03213 93 LHPTLTVRETLMFAA-------------------KL----------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180
....*....|....*....|....*.
gi 648246410 168 IELRRSMWEFLTEINAQGITIILTTH 193
Cdd:cd03213 144 SSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-224 |
5.52e-23 |
|
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: 98.64 E-value: 5.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAG-GFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDLELA--KQHIG 80
Cdd:TIGR02203 331 VEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL-ADYTLAslRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQE---FNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLD--LWEKRKERARNLSGGMKRRLMIARALMHEPK 155
Cdd:TIGR02203 410 LVSQDvvlFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPlgLDTPIGENGVLLSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 156 LLILDEPTAGVDIELRRSMWEFLTEInAQGITIILTTHYLEEAEMLCRnIGIINRGELIENTSMKDLLA 224
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIEKADR-IVVMDDGRIVERGTHNELLA 556
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-223 |
6.53e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.11 E-value: 6.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVN------KTSGTVKVFGFDIDK-DLELAKQHIGLVPQEFN-FNQF 91
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQiDAIKLRKEVGMVFQQPNpFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 92 ETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKER----ARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 167
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 168 IELRRSMWEFLTEINAQgITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLL 223
Cdd:PRK14246 186 IVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-225 |
1.12e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.11 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 13 YAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDLELA--KQHIGLVPQE---FN 87
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI-RTVTRAslRRNIAVVFQDaglFN 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 88 fnqfETVEQIVlqQAGYYGVTKA---LAKERAEKylskLDLWEKRK--------ERARNLSGGMKRRLMIARALMHEPKL 156
Cdd:PRK13657 423 ----RSIEDNI--RVGRPDATDEemrAAAERAQA----HDFIERKPdgydtvvgERGRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648246410 157 LILDEPTAGVDIELRRSMWEFLTEInAQGITIILTTHYL---EEAEMlcrnIGIINRGELIENTSMKDLLAK 225
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLstvRNADR----ILVFDNGRVVESGSFDELVAR 559
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-194 |
1.20e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.98 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTyAGGFEALKGVSLQVEKGDFYALLGPNGAGKST---TI-GIISSLVnkTSGTVKVFGFDIdkdLEL----- 74
Cdd:COG0396 1 LEIKNLHVS-VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLmGHPKYEV--TSGSILLDGEDI---LELspder 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 75 AKQHIGLV---PQEF----NFNQFETVEQIVLQQAgyygVTKALAKERAEKYLSKLDLWEKRKERARN--LSGGMKRRLM 145
Cdd:COG0396 75 ARAGIFLAfqyPVEIpgvsVSNFLRTALNARRGEE----LSAREFLKLLKEKMKELGLDEDFLDRYVNegFSGGEKKRNE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 648246410 146 IARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHY 194
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHY 199
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-235 |
1.39e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.80 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG--FDIDKDLELaKQHIGLVPQEFNfNQF--ETVE 95
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdlLTEENVWDI-RHKIGMVFQNPD-NQFvgATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 96 QIVLQQAGYYGVTKALAKERAEKYLSKLDLWE-KRKERARnLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSM 174
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKERVNEALELVGMQDfKEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648246410 175 WEFLTEINAQ-GITIILTTHYLEEAEMLCRNIgIINRGELIENTSMKDLLAKL-QLETFILDI 235
Cdd:PRK13650 180 IKTIKGIRDDyQMTVISITHDLDEVALSDRVL-VMKNGQVESTSTPRELFSRGnDLLQLGLDI 241
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-225 |
1.58e-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: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 18 EALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDLELA--KQHIGLVPQE---FN----- 87
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI-RDLNLRwlRSQIGLVSQEpvlFDgtiae 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 88 ---FNQFE-TVEQIVlqqagyygvtKALAKERAEKYLSKL-DLWEKR-KERARNLSGGMKRRLMIARALMHEPKLLILDE 161
Cdd:cd03249 96 nirYGKPDaTDEEVE----------EAAKKANIHDFIMSLpDGYDTLvGERGSQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648246410 162 PTAGVDIELRRSMWEFLTEInAQGITIILTTHYL---EEAEmlcrNIGIINRGELIENTSMKDLLAK 225
Cdd:cd03249 166 ATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLstiRNAD----LIAVLQNGQVVEQGTHDELMAQ 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-216 |
1.95e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 93.40 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID--KDLELAKQHIGL 81
Cdd:PRK11614 6 LSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQEFNFNQFETVEQiVLQQAGYYgVTKALAKERAEK-YLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILD 160
Cdd:PRK11614 85 VPEGRRVFSRMTVEE-NLAMGGFF-AERDQFQERIKWvYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 161 EPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCrnigiiNRGELIEN 216
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLA------DRGYVLEN 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-214 |
2.43e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.54 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK--DLELAKqHIGL 81
Cdd:PRK11231 3 LRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlsSRQLAR-RLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQefnfnQFETVEQIVLQQAGYYGVTKALA---------KERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMH 152
Cdd:PRK11231 81 LPQ-----HHLTPEGITVRELVAYGRSPWLSlwgrlsaedNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648246410 153 EPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-193 |
2.54e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.67 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfGfdidkdlelAKQHIGLVP 83
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-G---------ETVKIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEF-NFNQFETVEQIVlqQAGYYGVTKALAKERAEKYLSKLDLWEKRkerARNLSGGMKRRLMIARALMHEPKLLILDEP 162
Cdd:COG0488 385 QHQeELDPDKTVLDEL--RDGAPGGTEQEVRGYLGRFLFSGDDAFKP---VGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
170 180 190
....*....|....*....|....*....|.
gi 648246410 163 TAGVDIELRRSMWEFLteINAQGiTIILTTH 193
Cdd:COG0488 460 TNHLDIETLEALEEAL--DDFPG-TVLLVSH 487
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-193 |
4.96e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 92.15 E-value: 4.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGG---FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG-----FDIDKDLELA 75
Cdd:PRK10584 7 VEVHHLKKSVGQGeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqMDEEARAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 76 KQHIGLVPQEF----NFNQFETVEQIVLQQagyyGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALM 151
Cdd:PRK10584 87 AKHVGFVFQSFmlipTLNALENVELPALLR----GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 648246410 152 HEPKLLILDEPTAGVDIELRRSMWEFLTEINA-QGITIILTTH 193
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNReHGTTLILVTH 205
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-225 |
8.83e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.56 E-value: 8.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHIGLVPQEFNFNQFETVEQIV 98
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLFSGSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 99 --LQQAGYYGVTKALAKERAEKYLSKL--DLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSM 174
Cdd:TIGR00958 577 ygLTDTPDEEIMAAAKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 648246410 175 WEFLteiNAQGITIILTTHYLEEAEMlCRNIGIINRGELIENTSMKDLLAK 225
Cdd:TIGR00958 657 QESR---SRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMED 703
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-211 |
9.45e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.61 E-value: 9.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKdLELAKQHIGLV 82
Cdd:PRK10851 2 SIEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR-LHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNFNQFETV-EQIVlqqagyYGVT---------KALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMH 152
Cdd:PRK10851 80 FQHYALFRHMTVfDNIA------FGLTvlprrerpnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 153 EPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRG 211
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-193 |
1.02e-21 |
|
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: 89.04 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfgfdidkdleLAKQHIGLVP 83
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW----------GSTVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QefnfnqfetveqivlqqagyygvtkalakeraekylskldlwekrkerarnLSGGMKRRLMIARALMHEPKLLILDEPT 163
Cdd:cd03221 70 Q---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190
....*....|....*....|....*....|
gi 648246410 164 AGVDIELRRSMWEFLTEINAqgiTIILTTH 193
Cdd:cd03221 99 NHLDLESIEALEEALKEYPG---TVILVSH 125
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-213 |
1.03e-21 |
|
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: 90.99 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI-DKDLELAKQHIGLVPQEFNFNQFETVEQIV 98
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsQYEHKYLHSKVSLVGQEPVLFARSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 99 --LQQAGYYGVTKALAKERAEKYLSKLDL--WEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSM 174
Cdd:cd03248 110 ygLQSCSFECVKEAAQKAHAHSFISELASgyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 648246410 175 WEFLTEINaQGITIILTTHYLEEAEMlCRNIGIINRGEL 213
Cdd:cd03248 190 QQALYDWP-ERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-194 |
1.03e-21 |
|
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: 90.28 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRkTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKST---TI-GIISSLVnkTSGTVKVFGFDIdKDL---ELAK 76
Cdd:cd03217 1 LEIKDLH-VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTlakTImGHPKYEV--TEGEILFKGEDI-TDLppeERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 77 QHIGLVPQEfnfnqfetveqivlqQAGYYGVTKAlakeraeKYLSKLDLwekrkerarNLSGGMKRRLMIARALMHEPKL 156
Cdd:cd03217 77 LGIFLAFQY---------------PPEIPGVKNA-------DFLRYVNE---------GFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190
....*....|....*....|....*....|....*...
gi 648246410 157 LILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHY 194
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY 163
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-223 |
1.59e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.47 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQH-IGL 81
Cdd:PRK09700 6 ISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKlDHKLAAQLgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQEFN-FNQFETVEQIVLQQ------AGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:PRK09700 85 IYQELSvIDELTVLENLYIGRhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648246410 155 KLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGE-----LIENTSMKDLL 223
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSsvcsgMVSDVSNDDIV 238
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
3-228 |
2.24e-21 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 92.47 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIeQLRKTYaGGFeALKgVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG---FDIDKDLELA--KQ 77
Cdd:COG4148 2 MLEV-DFRLRR-GGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGIFLPphRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 78 HIGLVPQE---FnfnQFETVEQIVLqqagyYGVTKALAKERAEKYLSKLDLWE-----KRkeRARNLSGGMKRRLMIARA 149
Cdd:COG4148 78 RIGYVFQEarlF---PHLSVRGNLL-----YGRKRAPRAERRISFDEVVELLGighllDR--RPATLSGGERQRVAIGRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 150 LMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQL 228
Cdd:COG4148 148 LLSSPRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDL 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-225 |
3.70e-21 |
|
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: 89.85 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAG-GFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHIGL 81
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQEFNFNQFETVEQIVLQQAG--YYGVTKALAKERAEKYLSKLDLWEKR--KERARNLSGGMKRRLMIARALMHEPKLL 157
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGmsMERVIEAAKLAGAHDFISELPEGYDTivGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648246410 158 ILDEPTAGVDIELRRSMWEFLTEINAqGITIILTTHYLeEAEMLCRNIGIINRGELIENTSMKDLLAK 225
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
23-222 |
6.65e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 91.32 E-value: 6.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 23 VSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDlELAKQHIGLVPQEFN-FNQFETVEQIvlqq 101
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHR-SIQQRDICMVFQSYAlFPHMSLGENV---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 102 aGY----YGVTKALAKERAEKYLSKLDL--WEKRkeRARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMW 175
Cdd:PRK11432 100 -GYglkmLGVPKEERKQRVKEALELVDLagFEDR--YVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 648246410 176 EFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDL 222
Cdd:PRK11432 177 EKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
15-193 |
7.52e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 89.28 E-value: 7.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 15 GGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKdleLAKQHI---GLVpQEFN---- 87
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG---LPGHQIarmGVV-RTFQhvrl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 88 FNQFETVEQIVLQQ---------AGY-----YGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHE 153
Cdd:PRK11300 92 FREMTVIENLLVAQhqqlktglfSGLlktpaFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 648246410 154 PKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTH 193
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEH 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-174 |
1.16e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 90.67 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDkDLELAKQHIG 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN-ELEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFNFNQFETVEqivlQQAGY----YGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKL 156
Cdd:PRK11650 80 MVFQNYALYPHMSVR----ENMAYglkiRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170
....*....|....*...
gi 648246410 157 LILDEPTAGVDIELRRSM 174
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQM 173
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-213 |
1.42e-20 |
|
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: 86.72 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRktyagGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKD--LELAKQHIG 80
Cdd:cd03215 4 VLEVRGLS-----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRspRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFN----FNQFETVEQIVLqqagyygvtkalakeraekylskldlwekrkerARNLSGGMKRRLMIARALMHEPKL 156
Cdd:cd03215 79 YVPEDRKreglVLDLSVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 648246410 157 LILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGEL 213
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-225 |
2.25e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.22 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGF----EALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKdLELAK--Q 77
Cdd:COG1101 2 LELKNLSKTFNPGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-LPEYKraK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 78 HIGLVpqefnfnqFE----------TVEQ---IVLQQAGYYGVTKALAKERAEKY---LSKLDL-WEKR-KERARNLSGG 139
Cdd:COG1101 81 YIGRV--------FQdpmmgtapsmTIEEnlaLAYRRGKRRGLRRGLTKKRRELFrelLATLGLgLENRlDTKVGLLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 140 MKRRLMIARALMHEPKLLILDEPTAGVDIelRRSmwEFLTE-----INAQGITIILTTHYLEEA-EMLCRNIgIINRGEL 213
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDP--KTA--ALVLEltekiVEENNLTTLMVTHNMEQAlDYGNRLI-MMHEGRI 227
|
250 260
....*....|....*....|
gi 648246410 214 I--------ENTSMKDLLAK 225
Cdd:COG1101 228 IldvsgeekKKLTVEDLLEL 247
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-162 |
2.40e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.83 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 5 EIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID--KDLELAKqHIGLV 82
Cdd:COG4604 3 EIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAttPSRELAK-RLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNFNQFETVEQIV-----------LQQAGYYGVTKALA----KERAEKYLSkldlwekrkerarNLSGGMKRRLMIA 147
Cdd:COG4604 81 RQENHINSRLTVRELVafgrfpyskgrLTAEDREIIDEAIAyldlEDLADRYLD-------------ELSGGQRQRAFIA 147
|
170
....*....|....*
gi 648246410 148 RALMHEPKLLILDEP 162
Cdd:COG4604 148 MVLAQDTDYVLLDEP 162
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
8-230 |
3.83e-20 |
|
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: 89.02 E-value: 3.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 8 QLRKTYaGGFEaLKgVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG---FDIDKDLELA--KQHIGLV 82
Cdd:TIGR02142 4 RFSKRL-GDFS-LD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKGIFLPpeKRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNFNQFETVEQIVLqqagyYGVTKALAKERA---EKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLIL 159
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLR-----YGMKRARPSERRisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648246410 160 DEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQLET 230
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-235 |
4.53e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.93 E-value: 4.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGGFE-ALKGVSLQVEKGDFYALLGPNGAGKSTtigiISSLVN-------KTSGTVKVFGFDI-DKDLE 73
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKST----ISKLINglllpddNPNSKITVDGITLtAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 74 LAKQHIGLVPQEFNfNQF--ETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALM 151
Cdd:PRK13640 81 DIREKVGIVFQNPD-NQFvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 152 HEPKLLILDEPTAGVDIELRRSMWEFLTEI-NAQGITIILTTHYLEEAEMlCRNIGIINRGELIENTSMKDLLAKLQLET 230
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
....*.
gi 648246410 231 FI-LDI 235
Cdd:PRK13640 239 EIgLDI 244
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-215 |
4.85e-20 |
|
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: 86.39 E-value: 4.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFE-ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHIGL 81
Cdd:cd03244 3 IEFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQE---------FN---FNQFeTVEQI--VLQQAGyygvtkalAKERAEKYLSKLDLweKRKERARNLSGGMKRRLMIA 147
Cdd:cd03244 83 IPQDpvlfsgtirSNldpFGEY-SDEELwqALERVG--------LKEFVESLPGGLDT--VVEEGGENLSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648246410 148 RALMHEPKLLILDEPTAGVDIELRRSMWEFLTEiNAQGITIILTTHYLeEAEMLCRNIGIINRGELIE 215
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRL-DTIIDSDRILVLDKGRVVE 217
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-224 |
6.42e-20 |
|
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: 89.80 E-value: 6.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHIGLV 82
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNFNQFETVEQIVLQqagyygvtkalAKERA--EKYLSKLDLWEKRK--------------ERARNLSGGMKRRLMI 146
Cdd:TIGR01193 554 PQEPYIFSGSILENLLLG-----------AKENVsqDEIWAACEIAEIKDdienmplgyqtelsEEGSSISGGQKQRIAL 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648246410 147 ARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQgiTIILTTHYLEEAEMlCRNIGIINRGELIENTSMKDLLA 224
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLD 697
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-238 |
1.14e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.58 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID--KDLELAKQHIGL 81
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQEFNfNQF--ETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLIL 159
Cdd:PRK13644 82 VFQNPE-TQFvgRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 160 DEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIgIINRGELIENTSMKDLLAKLQLETF------IL 233
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRII-VMDRGKIVLEGEPENVLSDVSLQTLgltppsLI 239
|
....*
gi 648246410 234 DIAEN 238
Cdd:PRK13644 240 ELAEN 244
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-235 |
1.21e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 86.34 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 19 ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID-KDLELAKQHIGLVPQEFNfNQFetVEQI 97
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITdDNFEKLRKHIGIVFQNPD-NQF--VGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 98 VLQQAGY----YGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRS 173
Cdd:PRK13648 101 VKYDVAFglenHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648246410 174 MWEFLTEINA-QGITIILTTHYLEEAeMLCRNIGIINRGELIENTSMKDLLAKLQLETFI-LDI 235
Cdd:PRK13648 181 LLDLVRKVKSeHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEIFDHAEELTRIgLDL 243
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-211 |
2.14e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.18 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGgFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKdLELAKQH---IG 80
Cdd:PRK15439 12 LCARSISKQYSG-VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR-LTPAKAHqlgIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFNFNQFETVEQIVLqqagyYGVTK-ALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLIL 159
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENIL-----FGLPKrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 648246410 160 DEPTAGVD-IELRRsMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRG 211
Cdd:PRK15439 165 DEPTASLTpAETER-LFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-214 |
2.49e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.77 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTyaggfEALKGVSLQVEKGD---FYALLGpngAGKSTTIGIISSLVNKTSGTVKVFGfdidKDLELA---- 75
Cdd:COG1129 256 VLEVEGLSVG-----GVVRDVSFSVRAGEilgIAGLVG---AGRTELARALFGADPADSGEIRLDG----KPVRIRsprd 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 76 --KQHIGLVP---QEFNFNQFETVEQ-IVLQQAGYYG----VTKALAKERAEKYLSKLDLweK---RKERARNLSGGMKR 142
Cdd:COG1129 324 aiRAGIAYVPedrKGEGLVLDLSIREnITLASLDRLSrgglLDRRRERALAEEYIKRLRI--KtpsPEQPVGNLSGGNQQ 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648246410 143 RLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:COG1129 402 KVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-204 |
4.38e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.40 E-value: 4.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKvfgfdidkdlELAKQHIGLVPQEFNFNQFE--TVEQI 97
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------RNGKLRIGYVPQKLYLDTTLplTVNRF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 98 VLQQAGYYG--VTKALAKERAEKYLskldlwekrKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMW 175
Cdd:PRK09544 90 LRLRPGTKKedILPALKRVQAGHLI---------DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY 160
|
170 180 190
....*....|....*....|....*....|....*
gi 648246410 176 EFLTEI-NAQGITIILTTHYL-----EEAEMLCRN 204
Cdd:PRK09544 161 DLIDQLrRELDCAVLMVSHDLhlvmaKTDEVLCLN 195
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-223 |
4.99e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 86.63 E-value: 4.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 19 ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI----DKDL-ELAKQHIGLVPQEFNFNQFET 93
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisDAELrEVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 94 VEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRS 173
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 648246410 174 MWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLL 223
Cdd:PRK10070 203 MQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-199 |
5.03e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 83.30 E-value: 5.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGfEALKGVSLQVEKGDFYALLGPNGAGKST----TIGIISSLVNkTSGTVKVFGFDIDkDLELAKQHI 79
Cdd:COG4136 2 LSLENLTITLGGR-PLLAPLSLTVAPGEILTLMGPSGSGKSTllaaIAGTLSPAFS-ASGEVLLNGRRLT-ALPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 80 GLVPQ-EFNFNQFETVEQIVLQQAGyyGVTKALAKERAEKYLSKLDLwEKRKERARN-LSGGMKRRLMIARALMHEPKLL 157
Cdd:COG4136 79 GILFQdDLLFPHLSVGENLAFALPP--TIGRAQRRARVEQALEEAGL-AGFADRDPAtLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 648246410 158 ILDEPTAGVDIELRRSMWEF-LTEINAQGITIILTTHYLEEAE 199
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTHDEEDAP 198
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-216 |
5.07e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 84.34 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVkVFGfdiDKDLELAKQHIGLVP 83
Cdd:PRK11247 13 LLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG---TAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEFNFNQFETV-EQIVLQQAGYYgvtkalaKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEP 162
Cdd:PRK11247 88 QDARLLPWKKViDNVGLGLKGQW-------RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 163 TAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAemlcrnIGIINRGELIEN 216
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEA------VAMADRVLLIEE 209
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-244 |
1.57e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 83.20 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYAGG--------FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-D 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 72 LELAK---QHIGLVPQEF--NFNQFETVEQIVLQQAGYY-GVTKALAKERAEKYLSKLDL-WEKRKERARNLSGGMKRRL 144
Cdd:PRK10419 81 RAQRKafrRDIQMVFQDSisAVNPRKTVREIIREPLRHLlSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 145 MIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLL 223
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKL 240
|
250 260
....*....|....*....|....*.
gi 648246410 224 -----AKLQLETFILdiaensPPAPQ 244
Cdd:PRK10419 241 tfsspAGRVLQNAVL------PAFPV 260
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-201 |
1.77e-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: 81.75 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 19 ALKGVSLQVEKGDFYALLGPNGAGKSTtigIISSL---VNKTSGTVKVFGfdidkdlelakqHIGLVPQEfNFNQFETV- 94
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSVSVPG------------SIAYVSQE-PWIQNGTIr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 95 EQIV----LQQAGYYGVTKALAKERAEKYLSKLDLWEKrKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIEL 170
Cdd:cd03250 84 ENILfgkpFDEERYEKVIKACALEPDLEILPDGDLTEI-GEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHV 162
|
170 180 190
....*....|....*....|....*....|....*
gi 648246410 171 RRSMWE-FLTEINAQGITIILTTH---YLEEAEML 201
Cdd:cd03250 163 GRHIFEnCILGLLLNNKTRILVTHqlqLLPHADQI 197
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-215 |
1.97e-18 |
|
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: 81.21 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFE-ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLV 82
Cdd:cd03247 1 LSINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNFnqFETVeqiVLQQAGyygvtkalakeraekylskldlwekrkeraRNLSGGMKRRLMIARALMHEPKLLILDEP 162
Cdd:cd03247 81 NQRPYL--FDTT---LRNNLG------------------------------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 648246410 163 TAGVDIELRRSMWEFLTEInAQGITIILTTHYLEEAEMLCRnIGIINRGELIE 215
Cdd:cd03247 126 TVGLDPITERQLLSLIFEV-LKDKTLIWITHHLTGIEHMDK-ILFLENGKIIM 176
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-193 |
2.60e-18 |
|
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: 84.80 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKST----TIGIISSlvnkTSGTVKVFGFDIDK-DLELAKQHIGLVPQEFNFnqFE-T 93
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTlarlLVGVWPP----TAGSVRLDGADLSQwDREELGRHIGYLPQDVEL--FDgT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 94 VEQ-IvlqqAGYYGVTKALAKERAEK-------------YLSKLDlwekrkERARNLSGGMKRRLMIARALMHEPKLLIL 159
Cdd:COG4618 422 IAEnI----ARFGDADPEKVVAAAKLagvhemilrlpdgYDTRIG------EGGARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190
....*....|....*....|....*....|....
gi 648246410 160 DEPTAGVDIELRRSMWEFLTEINAQGITIILTTH 193
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKARGATVVVITH 525
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
18-196 |
2.71e-18 |
|
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: 82.31 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 18 EALKGVSLQVEKGDFYALLGPNGAGKSTTIGII----SSLVnkTSGTVKVFGFDI---------DKDLELAKQHIGLVPQ 84
Cdd:TIGR01978 14 EILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghpSYEV--TSGTILFKGQDLlelepderaRAGLFLAFQYPEEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 85 EFNFNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARN--LSGGMKRRLMIARALMHEPKLLILDEP 162
Cdd:TIGR01978 92 VSNLEFLRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNegFSGGEKKRNEILQMALLEPKLAILDEI 171
|
170 180 190
....*....|....*....|....*....|....
gi 648246410 163 TAGVDIELRRSMWEFLTEINAQGITIILTTHYLE 196
Cdd:TIGR01978 172 DSGLDIDALKIVAEGINRLREPDRSFLIITHYQR 205
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-215 |
3.01e-18 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 82.19 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGfEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTV----------KVFGFDIDKDLE 73
Cdd:TIGR02323 4 LQVSGLSKSYGGG-KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyimrsgaelELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 74 LAKQHIGLVPQEFNFNQFETV-------EQIVLQQAGYYGVTKAlakeRAEKYLSKLDLWEKR-KERARNLSGGMKRRLM 145
Cdd:TIGR02323 83 LMRTEWGFVHQNPRDGLRMRVsaganigERLMAIGARHYGNIRA----TAQDWLEEVEIDPTRiDDLPRAFSGGMQQRLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648246410 146 IARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIE 215
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
22-222 |
3.48e-18 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 81.65 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 22 GVSLQVEKGDFYALLGPNGAGKSTT----IGIISSLVNKTSGTVKVFGFDIDKdLELAKQHIGLVPQE--FNFNQFETVE 95
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTclaiLGLLPPGLTQTSGEILLDGRPLLP-LSIRGRHIATIMQNprTAFNPLFTMG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 96 QIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKR---KERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRR 172
Cdd:TIGR02770 83 NHAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 648246410 173 SMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDL 222
Cdd:TIGR02770 163 RVLKLLRELRQLfGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEI 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-224 |
4.04e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.45 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYA--GGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID-KDLELAKQHIG 80
Cdd:PRK13642 5 LEVENLVFKYEkeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFNfNQF--ETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLI 158
Cdd:PRK13642 85 MVFQNPD-NQFvgATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648246410 159 LDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRnIGIINRGELIENTSMKDLLA 224
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAASSDR-ILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-229 |
4.27e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 82.36 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 17 FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID------KDLELAKQHIGLVpqeFNFNQ 90
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPanlkkiKEVKRLRKEIGLV---FQFPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 91 FETVEQIVLQQAGYYGVTKALAKERAEKYLSKL-DLWEKRKERAR----NLSGGMKRRLMIARALMHEPKLLILDEPTAG 165
Cdd:PRK13645 101 YQLFQETIEKDIAFGPVNLGENKQEAYKKVPELlKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648246410 166 VDIELRRSMWEFLTEINA-QGITIILTTHYLEEA-----EMLCRNIG-IINRGELIENTSMKDLLAKLQLE 229
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKeYKKRIIMVTHNMDQVlriadEVIVMHEGkVISIGSPFEIFSNQELLTKIEID 251
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-228 |
5.45e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.98 E-value: 5.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 18 EALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID---KDLELAKQHIGLVPQEFNFNQFET- 93
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskRGLLALRQQVATVFQDPEQQIFYTd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 94 VEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRS 173
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 174 MWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQL 228
Cdd:PRK13638 175 MIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-222 |
5.97e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.90 E-value: 5.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGgFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG----FDIDKDLELAKqhI 79
Cdd:PRK10762 5 LQLKGIDKAFPG-VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkevtFNGPKSSQEAG--I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 80 GLVPQEFNF-NQFETVEQIVLQQAgyygVTKALAK-------ERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALM 151
Cdd:PRK10762 82 GIIHQELNLiPQLTIAENIFLGRE----FVNRFGRidwkkmyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648246410 152 HEPKLLILDEPT-AGVDIElRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDL 222
Cdd:PRK10762 158 FESKVIIMDEPTdALTDTE-TESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-224 |
8.84e-18 |
|
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: 83.20 E-value: 8.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLR---KTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTT----IGIISSLVNKTSGTVKVFGFDI----DKDL 72
Cdd:COG4172 7 LSVEDLSvafGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLlglsEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 73 -ELAKQHIGLVPQE--FNFNQFETVE-QI--VLQQagYYGVTKALAKERAEKYLSKLDLWEKRKeRAR----NLSGGMKR 142
Cdd:COG4172 87 rRIRGNRIAMIFQEpmTSLNPLHTIGkQIaeVLRL--HRGLSGAAARARALELLERVGIPDPER-RLDayphQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 143 RLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKD 221
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
...
gi 648246410 222 LLA 224
Cdd:COG4172 244 LFA 246
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-198 |
9.36e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 80.98 E-value: 9.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 2 YALEIEQLrKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVN-----KTSGTVKVFGFDI-DKDLELA 75
Cdd:PRK14243 9 TVLRTENL-NVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyAPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 76 --KQHIGLVPQEFNFNQFETVEQIVlqqagyYGVT----KALAKERAEKYLSKLDLWEKRKERAR----NLSGGMKRRLM 145
Cdd:PRK14243 88 evRRRIGMVFQKPNPFPKSIYDNIA------YGARingyKGDMDELVERSLRQAALWDEVKDKLKqsglSLSGGQQQRLC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 648246410 146 IARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQgITIILTTHYLEEA 198
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQA 213
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-222 |
9.77e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.05 E-value: 9.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSL--VNKTSGTVKVFGFDID----KDLEL 74
Cdd:PRK13549 3 EYLLEMKNITKTF-GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQasniRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 75 AKqhIGLVPQEFNFNQFETV-EQIVL-QQAGYYGVTKALAK-ERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALM 151
Cdd:PRK13549 82 AG--IAIIHQELALVKELSVlENIFLgNEITPGGIMDYDAMyLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648246410 152 HEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDL 222
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-225 |
1.07e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 83.14 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFE-ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDLELA--KQHIG 80
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL-RDYTLAslRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQE---FN----------FNQFETVEQIvlqqagyygvtkalakERAEKYLSKLDLWEKRK--------ERARNLSGG 139
Cdd:PRK11176 421 LVSQNvhlFNdtianniayaRTEQYSREQI----------------EEAARMAYAMDFINKMDngldtvigENGVLLSGG 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 140 MKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINaQGITIILTTHYL---EEAEMlcrnIGIINRGELIEN 216
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHRLstiEKADE----ILVVEDGEIVER 559
|
....*....
gi 648246410 217 TSMKDLLAK 225
Cdd:PRK11176 560 GTHAELLAQ 568
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-215 |
1.84e-17 |
|
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: 78.99 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGF-EALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHIGL 81
Cdd:cd03369 7 IEVENLSVRYAPDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQE---FN---------FNQFETVEqivlqqagyygVTKALakeraekylskldlweKRKERARNLSGGMKRRLMIARA 149
Cdd:cd03369 87 IPQDptlFSgtirsnldpFDEYSDEE-----------IYGAL----------------RVSEGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 150 LMHEPKLLILDEPTAGVDIELRRSMWEFLTEiNAQGITIILTTHYLEEAeMLCRNIGIINRGELIE 215
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIRE-EFTNSTILTIAHRLRTI-IDYDKILVMDAGEVKE 203
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-203 |
2.01e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.42 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 7 EQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK--DLELAKQhIGLVPQ 84
Cdd:PRK10253 11 EQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaSKEVARR-IGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 85 EFNFNQFETVEQIVLQqaGYYGVTKALAKERAE------KYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLI 158
Cdd:PRK10253 89 NATTPGDITVQELVAR--GRYPHQPLFTRWRKEdeeavtKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 648246410 159 LDEPTAGVDIELRRSMWEFLTEIN-AQGITIILTTHYLEEAemlCR 203
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQA---CR 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-226 |
1.01e-16 |
|
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: 80.23 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYA----GGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLE------ 73
Cdd:TIGR03269 280 IKVRNVSKRYIsvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTkpgpdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 74 --LAKQHIGLVPQEFNFNQFETV-----EQIVLQQAGYYGVTKAL--------AKERAEKYLSKLdlwekrkerARNLSG 138
Cdd:TIGR03269 360 rgRAKRYIGILHQEYDLYPHRTVldnltEAIGLELPDELARMKAVitlkmvgfDEEKAEEILDKY---------PDELSE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 139 GMKRRLMIARALMHEPKLLILDEPTAGVD----IELRRSMWEFLTEINAqgiTIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQ---TFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
250
....*....|..
gi 648246410 215 ENTSMKDLLAKL 226
Cdd:TIGR03269 508 KIGDPEEIVEEL 519
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-213 |
1.21e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 79.30 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 11 KTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDkDLELAKQHIGLVPQEF---- 86
Cdd:PRK11000 11 KAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-DVPPAERGVGMVFQSYalyp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 87 NFNQFETVeQIVLQQAGyygVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGV 166
Cdd:PRK11000 89 HLSVAENM-SFGLKLAG---AKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 648246410 167 DIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGEL 213
Cdd:PRK11000 165 DAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-221 |
1.55e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 79.45 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTS--------GTVKVFGfDIdKDLELA 75
Cdd:NF040905 2 LEMRGITKTF-PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyegeilfdGEVCRFK-DI-RDSEAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 76 -----KQHIGLVPQefnfnqFETVEQIVL--QQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIAR 148
Cdd:NF040905 79 giviiHQELALIPY------LSIAENIFLgnERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648246410 149 ALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKD 221
Cdd:NF040905 153 ALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRA 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
4-222 |
1.78e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 78.61 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYA---GGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNK---TSGTVKVFGFDI----DKDL- 72
Cdd:PRK09473 13 LDVKDLRVTFStpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpEKELn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 73 ELAKQHIGLVPQE--FNFNQFETV-EQI--VLQQagYYGVTKALAKERAEKYLSKLDLWEKRKeRAR----NLSGGMKRR 143
Cdd:PRK09473 93 KLRAEQISMIFQDpmTSLNPYMRVgEQLmeVLML--HKGMSKAEAFEESVRMLDAVKMPEARK-RMKmyphEFSGGMRQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 144 LMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDL 222
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-194 |
3.66e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 76.60 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTyAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISS--LVNKTSGTVKVFGFDI-DKDLElAKQHIG 80
Cdd:CHL00131 8 LEIKNLHAS-VNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESIlDLEPE-ERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LvpqefnFNQFET------VEQIVLQQAGYYGVTKALAKERAE-----KYLS-KLDLWE-KRKERARNL----SGGMKRR 143
Cdd:CHL00131 86 I------FLAFQYpieipgVSNADFLRLAYNSKRKFQGLPELDpleflEIINeKLKLVGmDPSFLSRNVnegfSGGEKKR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 648246410 144 LMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHY 194
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHY 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-214 |
4.00e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-------DLELA 75
Cdd:COG3845 257 VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlsprerrRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 76 -----KQHIGLVPQefnfnqFETVEQIVLQQAGYYGVTK------ALAKERAEKYLSKLDLwekR----KERARNLSGGM 140
Cdd:COG3845 337 yipedRLGRGLVPD------MSVAENLILGRYRRPPFSRggfldrKAIRAFAEELIEEFDV---RtpgpDTPARSLSGGN 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648246410 141 KRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-193 |
4.68e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNK---TSGTVKVFGFDIDKdlELAKQHIGLVPQ-EFNFNQFETVE 95
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDA--KEMRAISAYVQQdDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 96 QIVLQ-----QAGYYGVTKalaKERAEKYLSKLDLWEKRK------ERARNLSGGMKRRLMIARALMHEPKLLILDEPTA 164
Cdd:TIGR00955 119 HLMFQahlrmPRRVTKKEK---RERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180
....*....|....*....|....*....
gi 648246410 165 GVDIELRRSMWEFLTEINAQGITIILTTH 193
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-222 |
6.16e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.64 E-value: 6.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGgFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG----FD-----IDKDLEL 74
Cdd:PRK11288 5 LSFDGIGKTFPG-VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrFAsttaaLAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 75 AKQHIGLVPQefnfnqfETV-EQIVLQQ----AGYygVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARA 149
Cdd:PRK11288 84 IYQELHLVPE-------MTVaENLYLGQlphkGGI--VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648246410 150 LMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIEN-TSMKDL 222
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQV 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-167 |
8.02e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 76.69 E-value: 8.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTY--AGGF--------EALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK--- 70
Cdd:COG4608 8 LEVRDLKKHFpvRGGLfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGlsg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 71 -DLELAKQHIGLV---PQEfNFNQFETVEQIVLQQAGYYGV-TKALAKERAEKYLSKLDLwekRKERARN----LSGGMK 141
Cdd:COG4608 88 rELRPLRRRMQMVfqdPYA-SLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGL---RPEHADRypheFSGGQR 163
|
170 180
....*....|....*....|....*.
gi 648246410 142 RRLMIARALMHEPKLLILDEPTAGVD 167
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALD 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-231 |
1.69e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 76.76 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSL------------------------------ 53
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriiyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 54 --VNKTSGTVKVFGFDI----DKDLELAKQHIGLVPQE-FNFNQFETVEQIV---LQQAGYYGVTkalAKERAEKYLSKL 123
Cdd:TIGR03269 80 epCPVCGGTLEPEEVDFwnlsDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVleaLEEIGYEGKE---AVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 124 DLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTE-INAQGITIILTTHYLEEAEMLC 202
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|....*....
gi 648246410 203 RNIGIINRGELIENTSMKDLLAKLqLETF 231
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVAVF-MEGV 264
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-201 |
1.77e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.69 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVN-----KTSGTVKVFGFDIDK---DLELAKQHIGLV---PQEFNF 88
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYErrvNLNRLRRQVSMVhpkPNLFPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 89 NQFETVEqivlqqagyYGVT------KALAKERAEKYLSKLDLWEKRKER----ARNLSGGMKRRLMIARALMHEPKLLI 158
Cdd:PRK14258 103 SVYDNVA---------YGVKivgwrpKLEIDDIVESALKDADLWDEIKHKihksALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 648246410 159 LDEPTAGVDIELRRSMWEFLTEINAQG-ITIILTTHYLEEAEML 201
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRL 217
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-215 |
2.25e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.42 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSttigiisSLVN------KTSGTVKVFGFDIdKDLELA-- 75
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKT-------SLLNallgflPYQGSLKINGIEL-RELDPEsw 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 76 KQHIGLVPQefNFNQFE-TVEQIVL---QQAGYYGVTKALAKERAEKYLSKLD--LWEKRKERARNLSGGMKRRLMIARA 149
Cdd:PRK11174 422 RKHLSWVGQ--NPQLPHgTLRDNVLlgnPDASDEQLQQALENAWVSEFLPLLPqgLDTPIGDQAAGLSVGQAQRLALARA 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 150 LMHEPKLLILDEPTAGVDIELRRSMWEFLTEiNAQGITIILTTHYLEEAEMlCRNIGIINRGELIE 215
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQ 563
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-224 |
2.31e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 74.75 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 15 GGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSG-----TVKVFGFDI--DKDLELAKQHIGLVPQEFN 87
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnYRDVLEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 88 FNQFETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARN----LSGGMKRRLMIARALMHEPKLLILDEPT 163
Cdd:PRK14271 112 PFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648246410 164 AGVDIELRRSMWEFLTEInAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-215 |
3.09e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.81 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFD-IDKDL----ELAKQH 78
Cdd:PRK11701 7 LSVRGLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgQLRDLyalsEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 79 igLVPQEFNFnqfetVEQIVLQ------QAG-------------YYGVTKALAK---ERAEKYLSKLDlwekrkERARNL 136
Cdd:PRK11701 86 --LLRTEWGF-----VHQHPRDglrmqvSAGgnigerlmavgarHYGDIRATAGdwlERVEIDAARID------DLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 137 SGGMKRRLMIARALMHEPKLLILDEPTAGVDI-------ELRRSMweflteINAQGITIILTTHYLEEAEMLCRNIGIIN 209
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVsvqarllDLLRGL------VRELGLAVVIVTHDLAVARLLAHRLLVMK 226
|
....*.
gi 648246410 210 RGELIE 215
Cdd:PRK11701 227 QGRVVE 232
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-195 |
3.44e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 74.74 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 19 ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI----DKDLELAKQHIGLVPQE--FNFNQFE 92
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRAVRSDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 93 TVEQIVLQ--QAGYYGVTKALAKERAEKYLSKLDLWEKRKER-ARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIE 169
Cdd:PRK15079 116 TIGEIIAEplRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180
....*....|....*....|....*..
gi 648246410 170 LRRSMWEFLTEINAQ-GITIILTTHYL 195
Cdd:PRK15079 196 IQAQVVNLLQQLQREmGLSLIFIAHDL 222
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-224 |
4.86e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.20 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGgfEALKGVSLQVEKGDFYALLGPNGAGKSTT----IGIISSLVNKTSGTVKVFGFDIDKDlELAKQHI 79
Cdd:PRK10418 5 IELRNIALQAAQ--PLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPC-ALRGRKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 80 GLVPQefN----FNQFET-----VEqiVLQQAGYYGVTKALAKERAEKYLSK----LDLWekrkerARNLSGGMKRRLMI 146
Cdd:PRK10418 82 ATIMQ--NprsaFNPLHTmhthaRE--TCLALGKPADDATLTAALEAVGLENaarvLKLY------PFEMSGGMLQRMMI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 147 ARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINA-QGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQkRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-222 |
5.78e-15 |
|
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: 74.86 E-value: 5.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLV--NKTSGTVKVFGFDI---------DKDL 72
Cdd:TIGR02633 2 LEMKGIVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLkasnirdteRAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 73 ELAKQHIGLVPQefnfnqFETVEQIVL-QQAGYYG--VTKALAKERAEKYLSKLDLWEKRKERA-RNLSGGMKRRLMIAR 148
Cdd:TIGR02633 81 VIIHQELTLVPE------LSVAENIFLgNEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648246410 149 ALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDL 222
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-198 |
7.18e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 72.31 E-value: 7.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 24 SLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDiDKDLELAKQHIGLVPQEFNFNQFETVEQ-IVL--- 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQENNLFSHLTVAQnIGLgln 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 100 -------QQagyygvtKALAKERAEK-----YLSKLdlwekrkerARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 167
Cdd:PRK10771 98 pglklnaAQ-------REKLHAIARQmgiedLLARL---------PGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190
....*....|....*....|....*....|..
gi 648246410 168 IELRRSMWEFLTEI-NAQGITIILTTHYLEEA 198
Cdd:PRK10771 162 PALRQEMLTLVSQVcQERQLTLLMVSHSLEDA 193
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-214 |
1.07e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 73.37 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 34 ALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG---FDIDKDLELA--KQHIGLVPQEFNFNQFETVEQIVLqqagyYGVT 108
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKGICLPpeKRRIGYVFQDARLFPHYKVRGNLR-----YGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 109 KALaKERAEKYLSKLDLwEKRKER-ARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLT----EINa 183
Cdd:PRK11144 103 KSM-VAQFDKIVALLGI-EPLLDRyPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLErlarEIN- 179
|
170 180 190
....*....|....*....|....*....|.
gi 648246410 184 qgITIILTTHYLEEAEMLCRNIGIINRGELI 214
Cdd:PRK11144 180 --IPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-225 |
1.17e-14 |
|
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: 74.09 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIdKDLELA--KQHIG 80
Cdd:COG5265 357 EVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-RDVTQAslRAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQE---FNfnqfETVeqivlqqaGY---YG--------VTKALAKERAEKYLSKL-DLWEKR-KERARNLSGGMKRRL 144
Cdd:COG5265 436 IVPQDtvlFN----DTI--------AYniaYGrpdaseeeVEAAARAAQIHDFIESLpDGYDTRvGERGLKLSGGEKQRV 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 145 MIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEInAQGITIILTTHYLE---EAEmlcrNIGIINRGELIENTSMKD 221
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGRTTLVIAHRLStivDAD----EILVLEAGRIVERGTHAE 578
|
....
gi 648246410 222 LLAK 225
Cdd:COG5265 579 LLAQ 582
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-193 |
1.21e-14 |
|
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: 71.24 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLrkTYA-GGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHI--- 79
Cdd:TIGR01189 1 LAARNL--ACSrGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIlyl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 80 ----GLVPqefnfnqfetvEQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPK 155
Cdd:TIGR01189 79 ghlpGLKP-----------ELSALENLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRP 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 648246410 156 LLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTH 193
Cdd:TIGR01189 148 LWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-193 |
1.40e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.13 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLVPQEFNFNQFETveqivL 99
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLT-----L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 100 QQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDielRRSMWEFLT 179
Cdd:PRK13540 92 RENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELSLLTIIT 168
|
170
....*....|....*..
gi 648246410 180 EIN---AQGITIILTTH 193
Cdd:PRK13540 169 KIQehrAKGGAVLLTSH 185
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
4-171 |
1.74e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 72.69 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYA---GGF------EALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK---- 70
Cdd:PRK11308 6 LQAIDLKKHYPvkrGLFkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 71 DLELAKQHIGLVPQefN----FNQFETVEQIV---LQQAgyygvTKALAKERAEKYLSKLDLWEKRKERARN----LSGG 139
Cdd:PRK11308 86 AQKLLRQKIQIVFQ--NpygsLNPRKKVGQILeepLLIN-----TSLSAAERREKALAMMAKVGLRPEHYDRyphmFSGG 158
|
170 180 190
....*....|....*....|....*....|..
gi 648246410 140 MKRRLMIARALMHEPKLLILDEPTAGVDIELR 171
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-224 |
1.79e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 71.74 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTY---AGGF-----EALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID-KDLEL 74
Cdd:PRK15112 5 LEVRNLSKTFryrTGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 75 AKQHIGLVPQE--FNFNQFETVEQIVlqQAGYYGVTKALAKERAEKYLSKLDLWEKRKERA----RNLSGGMKRRLMIAR 148
Cdd:PRK15112 85 RSQRIRMIFQDpsTSLNPRQRISQIL--DFPLRLNTDLEPEQREKQIIETLRQVGLLPDHAsyypHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648246410 149 ALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINA-QGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-193 |
2.07e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.43 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 2 YALEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISslvnktsgtvkvfGFDIDKDLELAKQ---H 78
Cdd:TIGR03719 3 YIYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVDKDFNGEARPQpgiK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 79 IGLVPQEFNFNQFETVEQIVLQ--------QAGYYGVTKALAKERAE--KYLSK----------LDLW--EKRKERA--- 133
Cdd:TIGR03719 70 VGYLPQEPQLDPTKTVRENVEEgvaeikdaLDRFNEISAKYAEPDADfdKLAAEqaelqeiidaADAWdlDSQLEIAmda 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648246410 134 ----------RNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIE----LRRSMWEFlteinaQGiTIILTTH 193
Cdd:TIGR03719 150 lrcppwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsvawLERHLQEY------PG-TVVAVTH 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-201 |
2.11e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRkTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDkDLELAKQHIGLVP 83
Cdd:PRK13539 3 LEGEDLA-CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID-DPDVAEACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEFnFNQFETVEQIVLQQAGYYGVTKALAKERAEKY-LSKL-DLwekrkeRARNLSGGMKRRLMIARALMHEPKLLILDE 161
Cdd:PRK13539 81 RNA-MKPALTVAENLEFWAAFLGGEELDIAAALEAVgLAPLaHL------PFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 648246410 162 PTAGVDIELRRSMWEFLTEINAQGITIILTTHY---LEEAEML 201
Cdd:PRK13539 154 PTAALDAAAVALFAELIRAHLAQGGIVIAATHIplgLPGAREL 196
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-222 |
3.80e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.45 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 16 GFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID--KDLELAKQHIGLVPQEFNFNQFET 93
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfkSSKEALENGISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 94 V-----------EQIVLQQAGYYGVTKALAKEraekylskLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEP 162
Cdd:PRK10982 90 VmdnmwlgryptKGMFVDQDKMYRDTKAIFDE--------LDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 163 TAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDL 222
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-213 |
6.01e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.01 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 18 EALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLV--------------- 82
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrqssglylda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNfnqfetVEQIVLQQAGYYGVTkalAKERA--EKYLSKLDL-WEKRKERARNLSGGMKRRLMIARALMHEPKLLIL 159
Cdd:PRK15439 357 PLAWN------VCALTHNRRGFWIKP---ARENAvlERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 648246410 160 DEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGEL 213
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-195 |
1.59e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.77 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLRKTYAGG---FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVN---KTSGTVKVF-GFDIDKDLE 73
Cdd:PRK11022 1 MALLNVDKLSVHFGDEsapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgRVMAEKLEFnGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 74 LAKQHI-----GLVPQE--FNFNQ-----FETVEQIVLQQAGyygvTKALAKERAEKYL---------SKLDLWEKRker 132
Cdd:PRK11022 81 KERRNLvgaevAMIFQDpmTSLNPcytvgFQIMEAIKVHQGG----NKKTRRQRAIDLLnqvgipdpaSRLDVYPHQ--- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648246410 133 arnLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYL 195
Cdd:PRK11022 154 ---LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDL 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-193 |
1.72e-13 |
|
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: 67.18 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfgfdidkdleLAKQHIGLVPQEFNFNQFETVEQIVL 99
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM----------PEGEDLLFLPQRPYLPLGTLREQLIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 100 qqagyygvtkalakeraekylskldLWEkrkeraRNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLT 179
Cdd:cd03223 87 -------------------------PWD------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK 135
|
170
....*....|....
gi 648246410 180 EinaQGITIILTTH 193
Cdd:cd03223 136 E---LGITVISVGH 146
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-198 |
2.67e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.04 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIIS-----SLVNKtsgtVKVFG---------FDIdkdlelaKQHIGLVP-- 83
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqGYSND----LTLFGrrrgsgetiWDI-------KKHIGYVSss 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 --QEFNFNQfeTVEQIVLqqAGYY---GVTKALA---KERAEKYLSKLDLwEKRKERA--RNLSGGMKRRLMIARALMHE 153
Cdd:PRK10938 345 lhLDYRVST--SVRNVIL--SGFFdsiGIYQAVSdrqQKLAQQWLDILGI-DKRTADApfHSLSWGQQRLALIVRALVKH 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 648246410 154 PKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIIL-TTHYLEEA 198
Cdd:PRK10938 420 PTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHHAEDA 465
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-195 |
2.93e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.94 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVnKTSGTVKVFGFDID--KDLELAkQHIGLVPQefnfnQFETVEQI 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSdwSAAELA-RHRAYLSQ-----QQSPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 98 -VLQ--QAGYYGVTKALAKERAEKYL-SKLDLWEKRKERARNLSGGMKRRLMIARALMH-------EPKLLILDEPTAGV 166
Cdd:COG4138 85 pVFQylALHQPAGASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSL 164
|
170 180
....*....|....*....|....*....
gi 648246410 167 DIELRRSMWEFLTEINAQGITIILTTHYL 195
Cdd:COG4138 165 DVAQQAALDRLLRELCQQGITVVMSSHDL 193
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-215 |
3.00e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 69.71 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTY----------AGGFEALKGVSLQVEKGDFYALLGPNGAGKSTT----IGIISSlvnktSGTVKVFGFDID 69
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 70 ----KDLELAKQHIGLVPQE-FN-FNQFETVEQIV-----LQQAGyygVTKALAKERAEKYLSKLDLwekrKERARN--- 135
Cdd:COG4172 351 glsrRALRPLRRRMQVVFQDpFGsLSPRMTVGQIIaeglrVHGPG---LSAAERRARVAEALEEVGL----DPAARHryp 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 136 --LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGE 212
Cdd:COG4172 424 heFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
...
gi 648246410 213 LIE 215
Cdd:COG4172 504 VVE 506
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-224 |
3.71e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 69.66 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 24 SLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTvKVFGFDIDKDLELAKQHiGLVPQEFNFNQFE----------- 92
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE-RQSQFSHITRLSFEQLQ-KLVSDEWQRNNTDmlspgeddtgr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 93 TVEQIVL----------QQAGYYGVTKALakERAEKYLSKldlwekrkerarnlsgGMKRRLMIARALMHEPKLLILDEP 162
Cdd:PRK10938 101 TTAEIIQdevkdparceQLAQQFGITALL--DRRFKYLST----------------GETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648246410 163 TAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-205 |
5.00e-13 |
|
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: 66.75 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLrkTYAGGFEAL-KGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVkvfgfdidkdlelakqhigLV 82
Cdd:cd03231 1 LEADEL--TCERDGRALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV-------------------LL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNFNQFETVEQIVL---QQAGYYGVTKAL----------AKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARA 149
Cdd:cd03231 60 NGGPLDFQRDSIARGLLylgHAPGIKTTLSVLenlrfwhadhSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 648246410 150 LMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHY-LEEAEMLCRNI 205
Cdd:cd03231 140 LLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQdLGLSEAGAREL 196
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-171 |
1.08e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFealkgvSLQVEKGDFYA-----LLGPNGAGKSTTIGIISSLVNKTSGtvkvfgfDIDKDLELA-Kq 77
Cdd:PRK13409 341 VEYPDLTKKL-GDF------SLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEG-------EVDPELKISyK- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 78 higlvPQEFNFNQFETVEQIVLQQAGYYG-------VTKALAKERaekylskldLWEKRkerARNLSGGMKRRLMIARAL 150
Cdd:PRK13409 406 -----PQYIKPDYDGTVEDLLRSITDDLGssyykseIIKPLQLER---------LLDKN---VKDLSGGELQRVAIAACL 468
|
170 180
....*....|....*....|.
gi 648246410 151 MHEPKLLILDEPTAGVDIELR 171
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDVEQR 489
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-227 |
1.20e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.19 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 22 GVSLQVEKGDFYALLGPNGAGKSTTIGII-----SSLVNKTSGTVKVFGFDIDKDLE-----LAKQHIGLVPQE--FNFN 89
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSIlrllpSPPVVYPSGDIRFHGESLLHASEqtlrgVRGNKIAMIFQEpmVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 90 QFETVEQivlQQAGYYGVTKALAKE--RAEkYLSKLDLWEKRKERAR------NLSGGMKRRLMIARALMHEPKLLILDE 161
Cdd:PRK15134 107 PLHTLEK---QLYEVLSLHRGMRREaaRGE-ILNCLDRVGIRQAAKRltdyphQLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648246410 162 PTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQ 227
Cdd:PRK15134 183 PTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-193 |
1.40e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 65.34 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSlvNKTSGTVK----VFGFDIDKDLElakQHIGLVPQEFNFNQFETVE 95
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITgeilINGRPLDKNFQ---RSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 96 QIVLQQAgyygvtkalakeraekYLskldlwekrkeraRNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMW 175
Cdd:cd03232 98 EALRFSA----------------LL-------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148
|
170
....*....|....*...
gi 648246410 176 EFLTEINAQGITIILTTH 193
Cdd:cd03232 149 RFLKKLADSGQAILCTIH 166
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-225 |
1.70e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.85 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLR---KTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTtigIISSLVNKTSGTVKV----FGFDiDKDL- 72
Cdd:COG4170 1 MPLLDIRNLTieiDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSL---IAKAICGITKDNWHVtadrFRWN-GIDLl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 73 --------ELAKQHIGLVPQEFN--FNQFETV-EQIVlqQA-------GYYGVTKALAKERAEKYLSKLDLweKRKERAR 134
Cdd:COG4170 77 klsprerrKIIGREIAMIFQEPSscLDPSAKIgDQLI--EAipswtfkGKWWQRFKWRKKRAIELLHRVGI--KDHKDIM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 135 N-----LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINA-QGITIILTTHYLEEAEMLCRNIGII 208
Cdd:COG4170 153 NsypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVL 232
|
250
....*....|....*..
gi 648246410 209 NRGELIENTSMKDLLAK 225
Cdd:COG4170 233 YCGQTVESGPTEQILKS 249
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-225 |
2.25e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.44 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHIGL 81
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQefnfnqfetvEQIVLQQAGYYGVT--KALAKERAEKYLSKLDLWEKRK-----------ERARNLSGGMKRRLMIAR 148
Cdd:PRK10790 420 VQQ----------DPVVLADTFLANVTlgRDISEEQVWQALETVQLAELARslpdglytplgEQGNNLSVGQKQLLALAR 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 149 ALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQgITIILTTHYLE---EAEmlcrNIGIINRGELIENTSMKDLLAK 225
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLStivEAD----TILVLHRGQAVEQGTHQQLLAA 564
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-193 |
2.27e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.12 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 14 AGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKdlelakqhigLVPQEFNfnqfet 93
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST----------LKPEIYR------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 94 veqivlQQAGYYGVTKALAKERAekYLSKLDLWEKRKER----------AR-------------NLSGGMKRRLMIARAL 150
Cdd:PRK10247 81 ------QQVSYCAQTPTLFGDTV--YDNLIFPWQIRNQQpdpaiflddlERfalpdtiltkniaELSGGEKQRISLIRNL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 648246410 151 MHEPKLLILDEPTAGVDIELRRSMWEFLTEINA-QGITIILTTH 193
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTH 196
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-193 |
2.79e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.90 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 5 EIEQLRKTYAGGfEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfgfdiDKDLELA--KQH-IGL 81
Cdd:PRK11147 321 EMENVNYQIDGK-QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-----GTKLEVAyfDQHrAEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQEfnfnqfeTVEQIVLQqaGYYGVTKALAKERAEKYLSKLDLWEKRkerARN----LSGGMKRRLMIARALMHEPKLL 157
Cdd:PRK11147 395 DPEK-------TVMDNLAE--GKQEVMVNGRPRHVLGYLQDFLFHPKR---AMTpvkaLSGGERNRLLLARLFLKPSNLL 462
|
170 180 190
....*....|....*....|....*....|....*...
gi 648246410 158 ILDEPTAGVDIElrrsMWEFLTEI--NAQGiTIILTTH 193
Cdd:PRK11147 463 ILDEPTNDLDVE----TLELLEELldSYQG-TVLLVSH 495
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-193 |
3.03e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.98 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 17 FEALKGVSLQVEKGDFYALLGPNGAGKST----TIGIISSLvnKTSGTVKVFGFDIDKDLELAKQhiglVPQEFNFNQfe 92
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTllrlLAGALKGT--PVAGCVDVPDNQFGREASLIDA----IGRKGDFKD-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 93 TVEqiVLQQAGyygvtkalakeraekyLSKLDLWekrKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVD----I 168
Cdd:COG2401 115 AVE--LLNAVG----------------LSDAVLW---LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtaK 173
|
170 180
....*....|....*....|....*
gi 648246410 169 ELRRSMWEFLTEinaQGITIILTTH 193
Cdd:COG2401 174 RVARNLQKLARR---AGITLVVATH 195
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-169 |
5.55e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.91 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 9 LRKTYAGGFEALKGVSLQvekgdFY-----ALLGPNGAGKSTTIGIISSlvnktsgtvkvfgfdIDKDLE----LAKQH- 78
Cdd:PRK11819 12 VSKVVPPKKQILKDISLS-----FFpgakiGVLGLNGAGKSTLLRIMAG---------------VDKEFEgearPAPGIk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 79 IGLVPQEFNFNQFETVEQIVlqQAGYYGVTKALAK--ERAEKY--------------------LSKLDLW--EKRKERA- 133
Cdd:PRK11819 72 VGYLPQEPQLDPEKTVRENV--EEGVAEVKAALDRfnEIYAAYaepdadfdalaaeqgelqeiIDAADAWdlDSQLEIAm 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 648246410 134 ------------RNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIE 169
Cdd:PRK11819 150 dalrcppwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE 197
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-225 |
9.00e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.38 E-value: 9.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID-KDLELAKQHIGLV 82
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 pqefnFNQFETVEQiVLQQAGyygvtKALAKERAEKYLSKLDLWEKRKE---RARN--LSGGMKRRLMIARALMHEPKLL 157
Cdd:PRK10522 403 -----FTDFHLFDQ-LLGPEG-----KPANPALVEKWLERLKMAHKLELedgRISNlkLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648246410 158 ILDEPTAGVDIELRRSMW-EFLTEINAQGITIILTTH---YLEEAEMLCRnigiINRGELIENT-SMKDLLAK 225
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYqVLLPLLQEMGKTIFAISHddhYFIHADRLLE----MRNGQLSELTgEERDAASR 540
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-169 |
1.38e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.91 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 3 ALEIEQLRKTYAGGfEALKGVSLQVEKGDFYALLGPNGAGKSTtigIISSLVNK---TSGTVKVfgfdidkdLELAKqhI 79
Cdd:PRK15064 319 ALEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTT---LLRTLVGElepDSGTVKW--------SENAN--I 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 80 GLVPQ--EFNFNQFETV-------------EQIVlqqagyygvtkalakeRAekYLSKL-----DLwekrKERARNLSGG 139
Cdd:PRK15064 385 GYYAQdhAYDFENDLTLfdwmsqwrqegddEQAV----------------RG--TLGRLlfsqdDI----KKSVKVLSGG 442
|
170 180 190
....*....|....*....|....*....|
gi 648246410 140 MKRRLMIARALMHEPKLLILDEPTAGVDIE 169
Cdd:PRK15064 443 EKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-193 |
1.45e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.83 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDfyALL--GPNGAGKSTTIGIISSLVNKTSGTVKVfgfdidkdleLAKQHIGLVPQEFNFNQfETVEQI 97
Cdd:COG4178 379 LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIAR----------PAGARVLFLPQRPYLPL-GTLREA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 98 VL--QQAGYYG---VTKALAKERAEKYLSKLDL---WEKRkerarnLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIE 169
Cdd:COG4178 446 LLypATAEAFSdaeLREALEAVGLGHLAERLDEeadWDQV------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180
....*....|....*....|....
gi 648246410 170 LRRSMWEFLTEiNAQGITIILTTH 193
Cdd:COG4178 520 NEAALYQLLRE-ELPGTTVISVGH 542
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-171 |
2.04e-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: 64.42 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFealkgvSLQVEKGDFY-----ALLGPNGAGKSTTIGIISSLVNKTSGtvkvfgfDIDKDLELA-Kq 77
Cdd:COG1245 342 VEYPDLTKSY-GGF------SLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEG-------EVDEDLKISyK- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 78 higlvPQEFNFNQFETVEQiVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRkerARNLSGGMKRRLMIARALMHEPKLL 157
Cdd:COG1245 407 -----PQYISPDYDGTVEE-FLRSANTDDFGSSYYKTEIIKPLGLEKLLDKN---VKDLSGGELQRVAIAACLSRDADLY 477
|
170
....*....|....
gi 648246410 158 ILDEPTAGVDIELR 171
Cdd:COG1245 478 LLDEPSAHLDVEQR 491
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-193 |
2.11e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.52 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfgfdIDKDLELAKQ---HIGLVPQEFNFNQFETVEQ 96
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTI----LANNRKPTKQilkRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 97 iVLQQAGYYGVTKALAKER----AEKYLSKLDLWEKRK-----ERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 167
Cdd:PLN03211 160 -TLVFCSLLRLPKSLTKQEkilvAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180
....*....|....*....|....*.
gi 648246410 168 IELRRSMWEFLTEINAQGITIILTTH 193
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-215 |
2.48e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 19 ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNkTSGTVKVFG-----FDIDKDLELAKQhIGLVPQEFN--FNQF 91
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGqplhnLNRRQLLPVRHR-IQVVFQDPNssLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 92 ETVEQIVLQ--QAGYYGVTKALAKERAEKYLSKLDL-WEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDI 168
Cdd:PRK15134 379 LNVLQIIEEglRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDK 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 648246410 169 ELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIE 215
Cdd:PRK15134 459 TVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-225 |
2.75e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.20 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 2 YALEIEQLRKTYAGGFE-ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfgfdidkdlelaKQHIG 80
Cdd:TIGR00957 635 NSITVHNATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM------------KGSVA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 81 LVPQEFNFNQFETVEQIV----LQQAGYYGVTKALAKERAEKYLSKLDLWEKrKERARNLSGGMKRRLMIARALMHEPKL 156
Cdd:TIGR00957 703 YVPQQAWIQNDSLRENILfgkaLNEKYYQQVLEACALLPDLEILPSGDRTEI-GEKGVNLSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 157 LILDEPTAGVDIELRRSMWEFLteINAQGI----TIILTTH---YLEEAEMlcrnIGIINRGELIENTSMKDLLAK 225
Cdd:TIGR00957 782 YLFDDPLSAVDAHVGKHIFEHV--IGPEGVlknkTRILVTHgisYLPQVDV----IIVMSGGKISEMGSYQELLQR 851
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-215 |
2.94e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 21 KGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID--KDLELAKQHIGLVPQEFN----FNQFETV 94
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprSPLDAVKKGMAYITESRRdngfFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 95 EQIV----LQQAGYYGvTKALAKERAEKYLS---KLDLWEKRKERARN---LSGGMKRRLMIARALMHEPKLLILDEPTA 164
Cdd:PRK09700 360 QNMAisrsLKDGGYKG-AMGLFHEVDEQRTAenqRELLALKCHSVNQNiteLSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 648246410 165 GVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIE 215
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-222 |
4.01e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.34 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 17 FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKD----LELAKQH-----------IGL 81
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRsrqvIELSEQSaaqmrhvrgadMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQE--FNFNQFETV-EQIVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERAR---NLSGGMKRRLMIARALMHEPK 155
Cdd:PRK10261 109 IFQEpmTSLNPVFTVgEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRyphQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648246410 156 LLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDL 222
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
129-190 |
5.01e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 5.01e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648246410 129 RKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIIL 190
Cdd:PRK10762 389 MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIIL 450
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-256 |
9.15e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHIGLVPQ---------EFNFN 89
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQspvlfsgtvRFNID 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 90 QFETVEQIVLQQAgyygVTKALAKERAEKYLSKLDlwEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIE 169
Cdd:PLN03232 1332 PFSEHNDADLWEA----LERAHIKDVIDRNPFGLD--AEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 170 LRRSMWEFLTEiNAQGITIILTTHYLEEAeMLCRNIGIINRGELIENTSMKDLLAKlQLETFILDIAENSPPAPQ-LSGV 248
Cdd:PLN03232 1406 TDSLIQRTIRE-EFKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSR-DTSAFFRMVHSTGPANAQyLSNL 1482
|
....*...
gi 648246410 249 ISQTMLNG 256
Cdd:PLN03232 1483 VFERRENG 1490
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-195 |
1.34e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 23 VSLQVEKGDFYALLGPNGAGKSTTIGIISSLVnKTSGTVKVFGfdidKDL------ELAKQHIGLVPQE---FNFNQFEt 93
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAG----QPLeawsaaELARHRAYLSQQQtppFAMPVFQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 94 veqiVLQQAGYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRR-------LMIARALMHEPKLLILDEPTAGV 166
Cdd:PRK03695 89 ----YLTLHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSL 164
|
170 180
....*....|....*....|....*....
gi 648246410 167 DIELRRSMWEFLTEINAQGITIILTTHYL 195
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGIAVVMSSHDL 193
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-215 |
1.44e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 19 ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDID----KDLELAKQHIGLVPQE--FNFNQFE 92
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspGKLQALRRDIQFIFQDpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 93 TVEQIVLQQAGYYGVTKA-LAKERAEKYLSKLDLWEKRKER-ARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIEL 170
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGkAAAARVAWLLERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 648246410 171 RRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIE 215
Cdd:PRK10261 499 RGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-224 |
1.86e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.44 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQL----RKTYAGGFE-ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVkvfgfDIDKDLELA 75
Cdd:PRK13545 16 MYNKPFDKLkdlfFRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 76 KQHIGLVpqefnfNQFETVEQIVLQQAgYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPK 155
Cdd:PRK13545 91 AISSGLN------GQLTGIENIELKGL-MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 156 LLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLA 224
Cdd:PRK13545 164 ILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
24-193 |
1.96e-10 |
|
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: 61.30 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 24 SLQVEKGDFYALLGPNGAGKSTTIGIISSLVnktsgtvKVFGFDIDKDlelAKQHIGLVPQEFNFNQFETVEQIVLQQAG 103
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELW-------PVYGGRLTKP---AKGKLFYVPQRPYMTLGTLRDQIIYPDSS 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 104 YYGVTKALAKERAEKYLSKLDL---------WEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSM 174
Cdd:TIGR00954 542 EDMKRRGLSDKDLEQILDNVQLthilereggWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM 621
|
170
....*....|....*....
gi 648246410 175 WEFLTEInaqGITIILTTH 193
Cdd:TIGR00954 622 YRLCREF---GITLFSVSH 637
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
8-171 |
3.39e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 59.34 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 8 QLRKTYaGGFealkgvSLQVEKGDFY-----ALLGPNGAGKSTTIGIISSLVNKTSGtvkvfgfDIDKDLElakqHIGLV 82
Cdd:cd03237 5 TMKKTL-GEF------TLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEG-------DIEIELD----TVSYK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNFNQFETVEQIVLQQ-AGYYgvTKALAKERAEKYLSKLDLWEKRkerARNLSGGMKRRLMIARALMHEPKLLILDE 161
Cdd:cd03237 67 PQYIKADYEGTVRDLLSSItKDFY--THPYFKTEIAKPLQIEQILDRE---VPELSGGELQRVAIAACLSKDADIYLLDE 141
|
170
....*....|
gi 648246410 162 PTAGVDIELR 171
Cdd:cd03237 142 PSAYLDVEQR 151
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
17-193 |
3.45e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.66 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 17 FEALkgvSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQ---HIG--------LVPQE 85
Cdd:PRK13538 17 FSGL---SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQdllYLGhqpgikteLTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 86 -FNFNQfetveqivlQQAGYYGvtkalaKERAEKYLSKLDLweKRKER--ARNLSGGMKRRLMIARALMHEPKLLILDEP 162
Cdd:PRK13538 94 nLRFYQ---------RLHGPGD------DEALWEALAQVGL--AGFEDvpVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 648246410 163 -----TAGVDiELRRSMWEFLteinAQGITIILTTH 193
Cdd:PRK13538 157 ftaidKQGVA-RLEALLAQHA----EQGGMVILTTH 187
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-239 |
7.42e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 58.29 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 17 FEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGfdidkDLELAKQHIGLVPQefnFNQFETVEQ 96
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----EVSVIAISAGLSGQ---LTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 97 IVLqqagYYGVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWE 176
Cdd:PRK13546 109 KML----CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648246410 177 FLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKlqLETFILDIAENS 239
Cdd:PRK13546 185 KIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK--YEAFLNDFKKKS 245
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-194 |
1.13e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.88 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYAGGfEALKGVSLQVEKGDFYALLGPNGAGKSTtigIISSLVNK-----TSGTVKVFGFDIdkdLELAKQH 78
Cdd:PRK09580 2 LSIKDLHVSVEDK-AILRGLNLEVRPGEVHAIMGPNGSGKST---LSATLAGRedyevTGGTVEFKGKDL---LELSPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 79 IGlvpQEFNFNQFE-TVE------QIVLQQAgyygvTKALAKERAEKYLSKLDLWEKRKERARNL--------------- 136
Cdd:PRK09580 75 RA---GEGIFMAFQyPVEipgvsnQFFLQTA-----LNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgf 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 648246410 137 SGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHY 194
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHY 204
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
135-213 |
2.22e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.02 E-value: 2.22e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 135 NLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGEL 213
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-229 |
2.46e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.10 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHIGLVPQEFNFNQFETVEQIV 98
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 99 lqQAGYYGVTKALAK------ERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRR 172
Cdd:PRK10575 107 --AIGRYPWHGALGRfgaadrEKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 648246410 173 SMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGELIENTSMKDLLAKLQLE 229
Cdd:PRK10575 185 DVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLE 242
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
136-213 |
3.62e-09 |
|
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: 57.53 E-value: 3.62e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648246410 136 LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGEL 213
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-224 |
4.38e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 56.73 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 1 MYALEIEQLR---KTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSlVNKTSGTVKV--FGFDiDKDL--- 72
Cdd:PRK15093 1 MPLLDIRNLTiefKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTAdrMRFD-DIDLlrl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 73 ------ELAKQHIGLVPQEFN--FNQFETVEQIVLQQ------AGYYGVTKALAKERAEKYLSKLDLwEKRKERARN--- 135
Cdd:PRK15093 79 sprerrKLVGHNVSMIFQEPQscLDPSERVGRQLMQNipgwtyKGRWWQRFGWRKRRAIELLHRVGI-KDHKDAMRSfpy 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 136 -LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQ-GITIILTTHYLEEAEMLCRNIGIINRGEL 213
Cdd:PRK15093 158 eLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
250
....*....|.
gi 648246410 214 IENTSMKDLLA 224
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-230 |
5.22e-09 |
|
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: 57.23 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 11 KTYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNkTSGTVKVFGFDIDK-DLELAKQHIGLVPQE-FNF 88
Cdd:TIGR01271 1226 KYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSvTLQTWRKAFGVIPQKvFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 89 N-----QFETVEQIVLQQagYYGVTKALA-KERAEKYLSKLDLweKRKERARNLSGGMKRRLMIARALMHEPKLLILDEP 162
Cdd:TIGR01271 1305 SgtfrkNLDPYEQWSDEE--IWKVAEEVGlKSVIEQFPDKLDF--VLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648246410 163 TAGVDIE----LRRSMWEFLTEinaqgITIILTTHYLeEAEMLCRNIGIinrgelIENTSMK--DLLAKLQLET 230
Cdd:TIGR01271 1381 SAHLDPVtlqiIRKTLKQSFSN-----CTVILSEHRV-EALLECQQFLV------IEGSSVKqyDSIQKLLNET 1442
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-197 |
6.13e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.93 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 23 VSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK----DLELAKQHIGLVPQE----FNFNQFETV 94
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsRLYTVRKRMSMLFQSgalfTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 95 EQIVLQQAGyygVTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSM 174
Cdd:PRK11831 106 AYPLREHTQ---LPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182
|
170 180
....*....|....*....|....
gi 648246410 175 WEFLTEIN-AQGITIILTTHYLEE 197
Cdd:PRK11831 183 VKLISELNsALGVTCVVVSHDVPE 206
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-212 |
6.87e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.64 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 19 ALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI-DKDLELAKQHIGLVPQE-FNFNqfETVEQ 96
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtKLQLDSWRSRLAVVSQTpFLFS--DTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 97 -IVLqqaGYYGVTKALAKERA-------------EKYLSKLDlwekrkERARNLSGGMKRRLMIARALMHEPKLLILDEP 162
Cdd:PRK10789 408 nIAL---GRPDATQQEIEHVArlasvhddilrlpQGYDTEVG------ERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 163 TAGVDIELRRSMWEFLTEInAQGITIILTTHYL----EEAEMLCRNIG-IINRGE 212
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLsaltEASEILVMQHGhIAQRGN 532
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-225 |
7.58e-09 |
|
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: 56.88 E-value: 7.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKST-TIGIISsLVNKTSGTVKVFGFDIDK-DLELAKQHIGLVPQE---------FNF 88
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSlTLGLFR-INESAEGEIIIDGLNIAKiGLHDLRFKITIIPQDpvlfsgslrMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 89 NQFETV--EQI--VLQQAGYYGVTKALAkeraekylSKLDlwEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTA 164
Cdd:TIGR00957 1381 DPFSQYsdEEVwwALELAHLKTFVSALP--------DKLD--HECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648246410 165 GVDIElRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIgIINRGELIENTSMKDLLAK 225
Cdd:TIGR00957 1451 AVDLE-TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVI-VLDKGEVAEFGAPSNLLQQ 1509
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-213 |
1.14e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 23 VSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG--FDIDKDLELAKQHIGLVPQEFNFnqfetvEQIV-- 98
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGIMLCPEDRKA------EGIIpv 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 99 --------------LQQAGYYgVTKALAKERAEKYLSKLDLweK---RKERARNLSGGMKRRLMIARALMHEPKLLILDE 161
Cdd:PRK11288 346 hsvadninisarrhHLRAGCL-INNRWEAENADRFIRSLNI--KtpsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 648246410 162 PTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGIINRGEL 213
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
51-193 |
1.21e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.19 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 51 SSLVNKTSGTVKVFGFDI-DKDLELAKQHIGLVPQE---FNFNQFETVEqivlqqagyYGVTKALAKE--RAEKYLSKLD 124
Cdd:PTZ00265 1269 DSTVFKNSGKILLDGVDIcDYNLKDLRNLFSIVSQEpmlFNMSIYENIK---------FGKEDATREDvkRACKFAAIDE 1339
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648246410 125 LWEKRKER--------ARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQG-ITIILTTH 193
Cdd:PTZ00265 1340 FIESLPNKydtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAH 1417
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-167 |
1.75e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 18 EALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELA--KQHIGLVPQE---------- 85
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKwwRSKIGVVSQDpllfsnsikn 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 86 ------FNFNQFETVEQIVLQ-----QAGYYGVTKALAKERAE-----KYLSKLDLWEKRKE------------------ 131
Cdd:PTZ00265 479 nikyslYSLKDLEALSNYYNEdgndsQENKNKRNSCRAKCAGDlndmsNTTDSNELIEMRKNyqtikdsevvdvskkvli 558
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 648246410 132 -----------------RARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 167
Cdd:PTZ00265 559 hdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-193 |
1.78e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKST---------TIGIIsslvnkTSGTVKVFGFDIDKDLElakQHIGLVPQEFNFNQ 90
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTllnvlaervTTGVI------TGGDRLVNGRPLDSSFQ---RSIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 91 FETVEQiVLQQAGYYGVTKALAKERAEKYLSK-LDLWEKRK-------ERARNLSGGMKRRLMIARALMHEPKLLI-LDE 161
Cdd:TIGR00956 850 TSTVRE-SLRFSAYLRQPKSVSKSEKMEYVEEvIKLLEMESyadavvgVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDE 928
|
170 180 190
....*....|....*....|....*....|..
gi 648246410 162 PTAGVDIELRRSMWEFLTEINAQGITIILTTH 193
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-193 |
2.05e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 25 LQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTvkvfgFDIDKDLELAK--QHiglVPQEFNFNQFETVEQIVLQQA 102
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGR-----IIYEQDLIVARlqQD---PPRNVEGTVYDFVAEGIEEQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 103 G----YYGVTKALAKERAEKYLSKL----------DLW--EKR------------KERARNLSGGMKRRLMIARALMHEP 154
Cdd:PRK11147 96 EylkrYHDISHLVETDPSEKNLNELaklqeqldhhNLWqlENRinevlaqlgldpDAALSSLSGGWLRKAALGRALVSNP 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 648246410 155 KLLILDEPTAGVDIELRRSMWEFLteINAQGiTIILTTH 193
Cdd:PRK11147 176 DVLLLDEPTNHLDIETIEWLEGFL--KTFQG-SIIFISH 211
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
14-167 |
3.04e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.04 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 14 AGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVN---KTSGTVKVFGFDIDKDLELAKQHIGLVPQEFNFNQ 90
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648246410 91 FETVEQIVlqqagyygvtKALAKERAEKYLskldlwekrkeraRNLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 167
Cdd:cd03233 97 TLTVRETL----------DFALRCKGNEFV-------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-180 |
3.51e-08 |
|
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: 54.56 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfGFDIdkdlelakqHIGLVP 83
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV---------KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEF-NFNQFETVEQIVLQQAGYYGVTKALAKERAekYLSKLDL-WEKRKERARNLSGGMKRRLMIARALMHEPKLLILDE 161
Cdd:TIGR03719 392 QSRdALDPNKTVWEEISGGLDIIKLGKREIPSRA--YVGRFNFkGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
170
....*....|....*....
gi 648246410 162 PTAGVDIELRRSMWEFLTE 180
Cdd:TIGR03719 470 PTNDLDVETLRALEEALLN 488
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-168 |
4.35e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK----DLelaKQHIGLVPQ---------EF 86
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfglmDL---RKVLGIIPQapvlfsgtvRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 87 NFNQFETVEQIVLQQAgyygVTKALAKERAEKYLSKLDlwEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGV 166
Cdd:PLN03130 1332 NLDPFNEHNDADLWES----LERAHLKDVIRRNSLGLD--AEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
..
gi 648246410 167 DI 168
Cdd:PLN03130 1406 DV 1407
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-180 |
7.50e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 7.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKV-----FGFDIDKDLELAK------QHIG-LVPQEfn 87
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLakgikLGYFAQHQLEFLRadesplQHLArLAPQE-- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 88 fnqfetVEQIVLQQAGYYGVTKalakeraekylskldlwEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 167
Cdd:PRK10636 406 ------LEQKLRDYLGGFGFQG-----------------DKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
170
....*....|...
gi 648246410 168 IELRRSMWEFLTE 180
Cdd:PRK10636 463 LDMRQALTEALID 475
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
136-207 |
1.54e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.05 E-value: 1.54e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648246410 136 LSGGMKRRLMIARALMHEPK----LLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGI 207
Cdd:cd03227 78 LSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-208 |
2.14e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.09 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 28 EKGDFYALLGPNGAGKSTTIGIIS-----------------SLVNKTSGTV------KVfgfdIDKDLELAK--QHIGLV 82
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSgelkpnlgdydeepswdEVLKRFRGTElqdyfkKL----ANGEIKVAHkpQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 PQEFNfnqfetveqivlqqagyyGVTKALAK---ER--AEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLL 157
Cdd:COG1245 173 PKVFK------------------GTVRELLEkvdERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 648246410 158 ILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGII 208
Cdd:COG1245 235 FFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-196 |
2.75e-07 |
|
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: 50.41 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 12 TYAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLVPQEFNFNQ- 90
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 91 ---FETVEQIV-----LQQAGYYGVTKALAKERAEKYLSKLDLWEKrKERARNLSGGMKRRLMIARALMHEPKLLILDEP 162
Cdd:cd03290 89 wllNATVEENItfgspFNKQRYKAVTDACSLQPDIDLLPFGDQTEI-GERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 648246410 163 TAGVDIEL-----RRSMWEFLTEINAqgiTIILTTHYLE 196
Cdd:cd03290 168 FSALDIHLsdhlmQEGILKFLQDDKR---TLVLVTHKLQ 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-169 |
3.22e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 13 YAGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTV--------KVF------GFDIDKD--LELAK 76
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmAVFsqhhvdGLDLSSNplLYMMR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 77 QHIGlVPqefnfnqfetvEQIVLQQAGYYGVTKALAkeraekylskldlwekrKERARNLSGGMKRRLMIARALMHEPKL 156
Cdd:PLN03073 598 CFPG-VP-----------EQKLRAHLGSFGVTGNLA-----------------LQPMYTLSGGQKSRVAFAKITFKKPHI 648
|
170
....*....|...
gi 648246410 157 LILDEPTAGVDIE 169
Cdd:PLN03073 649 LLLDEPSNHLDLD 661
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-223 |
3.27e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 50.62 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYA-GGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNkTSGTVKVFGFDIDK-DLELAKQHIGL 81
Cdd:cd03289 3 MTVKDLTAKYTeGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQEF---------NFNQFET-VEQIVLQQAGYYGVtkalaKERAEKYLSKLDLweKRKERARNLSGGMKRRLMIARALM 151
Cdd:cd03289 82 IPQKVfifsgtfrkNLDPYGKwSDEEIWKVAEEVGL-----KSVIEQFPGQLDF--VLVDGGCVLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648246410 152 HEPKLLILDEPTAGVDIELRRSMWEFLTEINAqGITIILTTHYLeEAEMLCRNIGIINRGELIENTSMKDLL 223
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQAFA-DCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLL 224
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-208 |
5.88e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 27 VEKGDFYALLGPNGAGKSTTIGIIS-----------------SLVNKTSGTV------KVfgfdIDKDLELAK--QHIGL 81
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSgelipnlgdyeeepswdEVLKRFRGTElqnyfkKL----YNGEIKVVHkpQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 82 VPQEFNfnqfETVEQIVlqqagyygvTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDE 161
Cdd:PRK13409 172 IPKVFK----GKVRELL---------KKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 648246410 162 PTAGVDIELRRSMWEFLTEInAQGITIILTTHYLEEAEMLCRNIGII 208
Cdd:PRK13409 239 PTSYLDIRQRLNVARLIREL-AEGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
129-193 |
8.30e-07 |
|
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: 49.70 E-value: 8.30e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648246410 129 RKERARNLSGGMKR---RLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTH 193
Cdd:pfam13304 230 GELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-213 |
8.53e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 23 VSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKvfgfdIDKDLELAKqhigLVPQEFNFNQFETVEQIVLQQA 102
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVS-----LDPNERLGK----LRQDQFAFEEFTVLDTVIMGHT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 103 GYYGVTK------ALAKERAEKYLSKLDLWEKRKE--------RA------------------RNLSGGMKRRLMIARAL 150
Cdd:PRK15064 91 ELWEVKQerdriyALPEMSEEDGMKVADLEVKFAEmdgytaeaRAgelllgvgipeeqhyglmSEVAPGWKLRVLLAQAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648246410 151 MHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLeeaEMLCRNIGIINRGEL 213
Cdd:PRK15064 171 FSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFL---NSVCTHMADLDYGEL 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-226 |
9.90e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTI-GIISSLVNKTSGTVKVFGfdidkdlelakqHIGLVPQ-EFNFNQfeTVEQI 97
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLIsAMLGELSHAETSSVVIRG------------SVAYVPQvSWIFNA--TVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 98 VL-----QQAGYYGVTKALAKERAEKYLSKLDLWEKrKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRR 172
Cdd:PLN03232 699 ILfgsdfESERYWRAIDVTALQHDLDLLPGRDLTEI-GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 173 SMWEFLTEINAQGITIILTT---HYLEEAE--MLCRNIGIINRGELIENTSMKDLLAKL 226
Cdd:PLN03232 778 QVFDSCMKDELKGKTRVLVTnqlHFLPLMDriILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-193 |
1.04e-06 |
|
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: 47.37 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 29 KGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfgfdidkdlelakqhiglvpqefnfnqfetveqivlqqagyygvt 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 109 kaLAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWE------FLTEIN 182
Cdd:smart00382 36 --IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLLLLKS 113
|
170
....*....|.
gi 648246410 183 AQGITIILTTH 193
Cdd:smart00382 114 EKNLTVILTTN 124
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-224 |
1.24e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTI-GIISSLVNKTSGTVKVFGfdidkdlelakqHIGLVPQ-EFNFNQfeTVEQI 97
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLIsAMLGELPPRSDASVVIRG------------TVAYVPQvSWIFNA--TVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 98 VL-----QQAGYYGVTKALAKERAEKYLSKLDLWEKrKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRR 172
Cdd:PLN03130 699 ILfgspfDPERYERAIDVTALQHDLDLLPGGDLTEI-GERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGR 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 173 SMWEFLTEINAQGITIILTT---HYLEEAEmlcrNIGIINRGELIENTSMKDLLA 224
Cdd:PLN03130 778 QVFDKCIKDELRGKTRVLVTnqlHFLSQVD----RIILVHEGMIKEEGTYEELSN 828
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-168 |
1.26e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 15 GGFEALKGVSLQVEKGDFYALLGPNGAGKSTTI---------GIISS----------LVNKTSGTVKVFGFDIDKdLELA 75
Cdd:PLN03073 188 GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLrymamhaidGIPKNcqilhveqevVGDDTTALQCVLNTDIER-TQLL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 76 KQHIGLVPQEFNFNQFETVEQIVLQQAGyyGVTKALAKERAEKYLSKLDLW--------------------EKRKERARN 135
Cdd:PLN03073 267 EEEAQLVAQQRELEFETETGKGKGANKD--GVDKDAVSQRLEEIYKRLELIdaytaearaasilaglsftpEMQVKATKT 344
|
170 180 190
....*....|....*....|....*....|...
gi 648246410 136 LSGGMKRRLMIARALMHEPKLLILDEPTAGVDI 168
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
12-193 |
1.26e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.31 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 12 TYAGGFEALKG-VSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDI---DKDLELAK-QHIGLVPQEF 86
Cdd:PRK13543 18 AFSRNEEPVFGpLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAtrgDRSRFMAYlGHLPGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 87 NfnqfeTVEQIVLQQA--GYYgvtkalAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTA 164
Cdd:PRK13543 98 S-----TLENLHFLCGlhGRR------AKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180 190
....*....|....*....|....*....|..
gi 648246410 165 GVDIE---LRRSMweFLTEINAQGITiILTTH 193
Cdd:PRK13543 167 NLDLEgitLVNRM--ISAHLRGGGAA-LVTTH 195
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-208 |
1.97e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.13 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 27 VEKGDFYALLGPNGAGKSTTIGIISS-----------------LVNKTSGTV--KVFGFDIDKDLELAK--QHIGLVPQE 85
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdwdeILDEFRGSElqNYFTKLLEGDVKVIVkpQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 86 FNFNqfetVEQIVlqqagyygvTKALAKERAEKYLSKLDLWEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAG 165
Cdd:cd03236 103 VKGK----VGELL---------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 648246410 166 VDIELRRSMWEFLTEINAQGITIILTTHYLEEAEMLCRNIGII 208
Cdd:cd03236 170 LDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-176 |
3.14e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.75 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGfdidkdlelakqHIGLVPQeFNFNQFETVEQIVL 99
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQ-TSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 100 QQAGY--YGVTKALAKERAEKYLSKLDlwEKRK----ERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRS 173
Cdd:TIGR01271 509 FGLSYdeYRYTSVIKACQLEEDIALFP--EKDKtvlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
...
gi 648246410 174 MWE 176
Cdd:TIGR01271 587 IFE 589
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
116-214 |
8.56e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 116 AEKYLSKL-----DLWEKrkerARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIIL 190
Cdd:NF040905 384 AEEYRKKMniktpSVFQK----VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIV 459
|
90 100
....*....|....*....|....
gi 648246410 191 TTHYLEEAEMLCRNIGIINRGELI 214
Cdd:NF040905 460 ISSELPELLGMCDRIYVMNEGRIT 483
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
16-193 |
8.79e-06 |
|
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: 46.53 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 16 GFEALKGVSLQVEKgDFYALLGPNGAGKSTTIGIISSLVNKTSG-TVKVFGFDIDKDLELAKQHIGLV------------ 82
Cdd:COG3593 10 NFRSIKDLSIELSD-DLTVLVGENNSGKSSILEALRLLLGPSSSrKFDEEDFYLGDDPDLPEIEIELTfgsllsrllrll 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 83 -----PQEFN-------------FNQF-ETVEQIVLQQAGYYGVTKALAKERAEKYLSKLDLW--EKRKERARNLSGGMK 141
Cdd:COG3593 89 lkeedKEELEealeelneelkeaLKALnELLSEYLKELLDGLDLELELSLDELEDLLKSLSLRieDGKELPLDRLGSGFQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 648246410 142 RRLMIA--RALMH-----EPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTH 193
Cdd:COG3593 169 RLILLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-176 |
1.04e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 46.00 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGfdidkDLELAKQHIGLVPQEFNFNqfeTVEQIVL 99
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----RISFSSQFSWIMPGTIKEN---IIFGVSY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 100 QQAGYYGVTKALakeRAEKYLSKLDlwEKRK----ERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMW 175
Cdd:cd03291 125 DEYRYKSVVKAC---QLEEDITKFP--EKDNtvlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIF 199
|
.
gi 648246410 176 E 176
Cdd:cd03291 200 E 200
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
136-210 |
2.77e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 2.77e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648246410 136 LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHylEEAEMLcrniGIINR 210
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISS--EMPELL----GITDR 460
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-193 |
9.48e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.55 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 37 GPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDKdleLAKQHIGLVPQEFNFNQFETVEQIVLQQAGYYGVTKALakERA 116
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN---IAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETL--YAA 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648246410 117 EKYLSKLDLWEkrkERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWEFLT-EINAQGItIILTTH 193
Cdd:PRK13541 108 IHYFKLHDLLD---EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGI-VLLSSH 181
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-180 |
1.35e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.18 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 4 LEIEQLRKTYaGGFEALKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfGfdidkdlELAKqhIGLVP 83
Cdd:PRK11819 325 IEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G-------ETVK--LAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 84 QEF-NFNQFETVEQIVLQQAGYYGVTKALAKERAekYLSKL-----DlwekRKERARNLSGGMKRRLMIARALMHEPKLL 157
Cdd:PRK11819 394 QSRdALDPNKTVWEEISGGLDIIKVGNREIPSRA--YVGRFnfkggD----QQKKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
170 180
....*....|....*....|...
gi 648246410 158 ILDEPTAGVDIELRRSMWEFLTE 180
Cdd:PRK11819 468 LLDEPTNDLDVETLRALEEALLE 490
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
20-225 |
9.81e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 39.89 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGFDIDK-DLELAKQHIGLVPQE---------FNFN 89
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlPLHTLRSRLSIILQDpilfsgsirFNLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 90 QFETVEQIVLQQAgyygVTKALAKERAEKYLSKLDlwEKRKERARNLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIE 169
Cdd:cd03288 117 PECKCTDDRLWEA----LEIAQLKNMVKSLPGGLD--AVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 648246410 170 LRRSMWEFLTEINAQG--ITIILTTHYLEEAEMLCrnigIINRGELIENTSMKDLLAK 225
Cdd:cd03288 191 TENILQKVVMTAFADRtvVTIAHRVSTILDADLVL----VLSRGILVECDTPENLLAQ 244
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
136-211 |
1.21e-03 |
|
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: 38.84 E-value: 1.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648246410 136 LSGGMKRRLMIARALMHEPK--LLILDEPTAGVDIELRRSMWEFLTEINAQGITIILTTHYLeeaEMLCRNIGIINRG 211
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL---DVLSSADWIIDFG 162
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
139-196 |
4.46e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 38.10 E-value: 4.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648246410 139 GMKRRLMIARALM---HEPKLLILDEPTAGVDIELRRSMWE-FLTEINAQGITIILTTHYLE 196
Cdd:COG1106 206 GTKRLLALAGALLdalAKGGVLLIDEIEASLHPSLLRKLLKlFLDLANKNNAQLIFTTHSTE 267
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-193 |
7.68e-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: 36.82 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 37 GPNGAGKSTtigIISSLVNKTSGTVKVFGFDIDKDLELA--KQHIGLVPQEF------------NFNQFETVeqIVLQQA 102
Cdd:cd03240 29 GQNGAGKTT---IIEALKYALTGELPPNSKGGAHDPKLIreGEVRAQVKLAFenangkkytitrSLAILENV--IFCHQG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 103 GyygVTKALAKERAekylskldlwekrkerarNLSGGMKR------RLMIARALMHEPKLLILDEPTAGVDIE-LRRSMW 175
Cdd:cd03240 104 E---SNWPLLDMRG------------------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLA 162
|
170
....*....|....*....
gi 648246410 176 EFLTEINAQGI-TIILTTH 193
Cdd:cd03240 163 EIIEERKSQKNfQLIVITH 181
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-169 |
8.34e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.84 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 20 LKGVSLQVEKGDFYALLGPNGAGKSTtigIISSLVNKTSGTVKVFGFDIDKDLELAKQHIGLVPQ---------EFNFNQ 90
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKST---LLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQpaleyvidgDREYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648246410 91 FETVEQIVLQQ------AGYYGVTKALA----KERAEKYLSKLDLWEKRKER-ARNLSGGMKRRLMIARALMHEPKLLIL 159
Cdd:PRK10636 94 LEAQLHDANERndghaiATIHGKLDAIDawtiRSRAASLLHGLGFSNEQLERpVSDFSGGWRMRLNLAQALICRSDLLLL 173
|
170
....*....|
gi 648246410 160 DEPTAGVDIE 169
Cdd:PRK10636 174 DEPTNHLDLD 183
|
|
| |
