|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-226 |
5.86e-111 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 320.86 E-value: 5.86e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLVP 83
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPT 163
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 164 AGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLGKL 226
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-298 |
1.20e-78 |
|
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: 241.14 E-value: 1.20e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 11 KTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLVPQEFNFNP 90
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 91 FETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIEL 170
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 171 RRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGL---LGKLHVETFILDI------------ 235
Cdd:TIGR01188 160 RRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELkrrLGKDTLESRPRDIqslkvevsmlia 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 236 ------DNEEKLQPLTDVVSQRVVDGSleielektQGMNHVFTQLSEQGVNVMSMRNKANRLEELFVSI 298
Cdd:TIGR01188 240 elgetgLGLLAVTVDSDRIKILVPDGD--------ETVPEIVEAAIRNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-213 |
1.78e-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: 236.14 E-value: 1.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLVP 83
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVMqqagyygvsrtlakeraekyltqldlwekrkerarnLSGGMKRRLMIARALMHEPQLLILDEPT 163
Cdd:cd03230 80 EEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2019142000 164 AGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGEL 213
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-214 |
5.10e-75 |
|
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: 229.18 E-value: 5.10e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLVP 83
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPT 163
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2019142000 164 AGVDIELRRSMWEFLKQIN-SQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKeEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-214 |
1.52e-73 |
|
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: 225.46 E-value: 1.52e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGG-FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLV 82
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEP 162
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2019142000 163 TAGVDIELRRSMWEFLKQInSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-241 |
1.66e-71 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 220.88 E-value: 1.66e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLVP 83
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPT 163
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 164 AGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLGKLHVE----TFILDIDNEE 239
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEnledAFVALIGSEE 240
|
..
gi 2019142000 240 KL 241
Cdd:COG4555 241 GE 242
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-304 |
9.21e-64 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 203.03 E-value: 9.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDthlEQAKQHLGLV 82
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQEFNFNPFETV-EQIVmqqagYY----GVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLL 157
Cdd:COG4152 77 PEERGLYPKMKVgEQLV-----YLarlkGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 158 ILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLGKLHVETFILDIDN 237
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 238 E-EKLQPLTDVVSQRVVDGSLEIELEKTQGMNHVFTQLSEQGvNVMSMRNKANRLEELFVSIVRQQSQ 304
Cdd:COG4152 232 DaGWLRALPGVTVVEEDGDGAELKLEDGADAQELLRALLARG-PVREFEEVRPSLNEIFIEVVGEKAE 298
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-214 |
1.93e-59 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 189.47 E-value: 1.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGLV 82
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQefnfNP-----FETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLL 157
Cdd:COG1122 81 FQ----NPddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 158 ILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
3-230 |
4.98e-59 |
|
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: 188.65 E-value: 4.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLV 82
Cdd:TIGR03864 1 ALEVAGLSFRY-GARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEP 162
Cdd:TIGR03864 80 FQQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 163 TAGVDIELRRSMWEFLKQ-INSQGITIILTTHYLEEAEMLCRHIgIINRGELIENTTMKGLLGKLHVET 230
Cdd:TIGR03864 160 TVGLDPASRAAITAHVRAlARDQGLSVLWATHLVDEIEASDRLV-VLHRGRVLADGAAAELRGATGGAD 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-214 |
2.61e-57 |
|
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: 183.55 E-value: 2.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGfEALKGVSLTVNKGdFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLVP 83
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPT 163
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 164 AGVDIELRRSMWEFLKQInSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:cd03264 159 AGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-211 |
2.84e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 184.52 E-value: 2.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdthlEQAKQHLG 80
Cdd:COG1121 4 MPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP----RRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFN---PFeTVEQIVM----QQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHE 153
Cdd:COG1121 79 YVPQRAEVDwdfPI-TVRDVVLmgryGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 154 PQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRG 211
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-200 |
1.31e-54 |
|
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: 176.91 E-value: 1.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGG---FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAK---- 76
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 77 -QHLGLVPQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQ 155
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2019142000 156 LLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEM 200
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-214 |
2.06e-54 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 179.23 E-value: 2.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLV 82
Cdd:PRK13537 7 PIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEP 162
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2019142000 163 TAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKI 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-212 |
3.28e-54 |
|
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: 175.73 E-value: 3.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 5 EIDQLRKTYAGGFE-ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGLV 82
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQEFN---FNPfeTVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLIL 159
Cdd:cd03225 81 FQNPDdqfFGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 160 DEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGE 212
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-214 |
6.41e-53 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 173.32 E-value: 6.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH----LEQAKQH 78
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgraLRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 79 LGLVPQEFNFNPFETVEQIVMQ-QAGYYGVSRTLA-------KERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARAL 150
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAgRLGRTSTWRSLLglfppedRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019142000 151 MHEPQLLILDEPTAGVDIELRRSMWEFLKQINS-QGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-214 |
1.18e-52 |
|
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: 171.78 E-value: 1.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTY---AGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGhnIDTHLE--QAKQH 78
Cdd:cd03266 2 ITADALTKRFrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEpaEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 79 LGLVPQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLI 158
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2019142000 159 LDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-205 |
2.63e-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: 169.50 E-value: 2.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYA---GGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdthlEQAKQHL 79
Cdd:COG1116 7 ALELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV----TGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 80 GLVPQEFNFNPFETVEQIVM---QQAGyygVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQL 156
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVAlglELRG---VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2019142000 157 LILDEPTAGVDIELRRSMWEFLKQI-NSQGITIILTTHYLEEAEMLCRHI 205
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRV 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-216 |
3.00e-51 |
|
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: 167.78 E-value: 3.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGhNIDTHLEQAKQHLGLVP 83
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-KSYQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVMQQAGYYGVSrtlaKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPT 163
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 164 AGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIEN 216
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-217 |
1.16e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 166.76 E-value: 1.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAGG---FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHL---EQAK 76
Cdd:COG1136 4 LLELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI-SSLserELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 77 ---QHLGLVPQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHE 153
Cdd:COG1136 83 lrrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019142000 154 PQLLILDEPTAGVDIELRRSMWEFLKQIN-SQGITIILTTHYLEEAEMlCRHIGIINRGELIENT 217
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSDE 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-211 |
1.82e-49 |
|
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: 163.47 E-value: 1.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 5 EIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHnidtHLEQAKQHLGLVPQ 84
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK----PLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 85 EFNFNP-FE-TVEQIVM----QQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLI 158
Cdd:cd03235 76 RRSIDRdFPiSVRDVVLmglyGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 159 LDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRG 211
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-277 |
4.03e-49 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 166.03 E-value: 4.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTY---------AGGF-----------EALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVK 62
Cdd:COG4586 1 IIEVENLSKTYrvyekepglKGALkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 63 VFGHNIDTHLEQAKQHLGLV------------PQE-FNFNpfetveqivmqqAGYYGVSRTLAKERAEKYLTQLDLWEKR 129
Cdd:COG4586 81 VLGYVPFKRRKEFARRIGVVfgqrsqlwwdlpAIDsFRLL------------KAIYRIPDAEYKKRLDELVELLDLGELL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 130 KERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQIN-SQGITIILTTHYLEEAEMLCRHIGII 208
Cdd:COG4586 149 DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNrERGTTILLTSHDMDDIEALCDRVIVI 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 209 NRGELIENTTMKGLLGKLHVETFI-LDIDN---EEKLQPLTDVVSQRvvDGSLEIELEKTQGMNHVFTQLSEQ 277
Cdd:COG4586 229 DHGRIIYDGSLEELKERFGPYKTIvLELAEpvpPLELPRGGEVIERE--GNRVRLEVDPRESLAEVLARLLAR 299
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-214 |
4.29e-49 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 163.67 E-value: 4.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAK-QHL 79
Cdd:COG0411 2 DPLLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGLPPHRiARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 80 GLV-----PQEF-NFNPFETVeQIVMQQAGYYGVSRTL------------AKERAEKYLTQLDLWEKRKERARNLSGGMK 141
Cdd:COG0411 80 GIArtfqnPRLFpELTVLENV-LVAAHARLGRGLLAALlrlprarreereARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019142000 142 RRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQIN-SQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-214 |
5.01e-49 |
|
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: 162.99 E-value: 5.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLVp 83
Cdd:cd03219 1 LEVRGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEF-NFNPFE--TVEQIVM-----QQAGYYGVSRTL-----AKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARAL 150
Cdd:cd03219 79 RTFqIPRLFPelTVLENVMvaaqaRTGSGLLLARARreereARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019142000 151 MHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-215 |
5.33e-49 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 162.53 E-value: 5.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT----HLEQAKQHL 79
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 80 GLVPQEFNFNPFETVEQ---IVMQQAGYygvSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQL 156
Cdd:COG2884 82 GVVFQDFRLLPDRTVYEnvaLPLRVTGK---SRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 157 LILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-214 |
8.89e-49 |
|
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: 161.68 E-value: 8.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDthlEQAKQHLGLVP 83
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPT 163
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 164 AGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-210 |
1.28e-48 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 161.49 E-value: 1.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGG---FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGhnidTHLEQAKQHLG 80
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILD 160
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 161 EPTAGVDIELRRSMWEFLKQI-NSQGITIILTTHYLEEAEMLCRHIGIINR 210
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-214 |
1.92e-48 |
|
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: 161.58 E-value: 1.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI----DTHLEQAKQHL 79
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 80 GLVPQEFNFNPFETV-EQIVMQQAGYYGVSRTLA-------KERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALM 151
Cdd:cd03256 81 GMIFQQFNLIERLSVlENVLSGRLGRRSTWRSLFglfpkeeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019142000 152 HEPQLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
20-197 |
5.38e-48 |
|
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: 160.64 E-value: 5.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSG-TVKVFGHNI-DTHLEQAKQHLGLVPQEF--NFNPFETVE 95
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKRIGLVSPALqlRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 96 QIVMqqAGYYGVSR------TLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIE 169
Cdd:COG1119 99 DVVL--SGFFDSIGlyreptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLG 176
|
170 180
....*....|....*....|....*....
gi 2019142000 170 LRRSMWEFLKQINSQG-ITIILTTHYLEE 197
Cdd:COG1119 177 ARELLLALLDKLAAEGaPTLVLVTHHVEE 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-215 |
7.98e-48 |
|
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: 167.00 E-value: 7.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTY----AGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAK--- 76
Cdd:COG1123 261 LEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 77 -QHLGLVPQefN----FNPFETVEQIVMQQAGYYGV-SRTLAKERAEKYLTQLDLWEKRKER-ARNLSGGMKRRLMIARA 149
Cdd:COG1123 341 rRRVQMVFQ--DpyssLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 150 LMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-214 |
1.11e-47 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 162.96 E-value: 1.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAKQHLG 80
Cdd:COG3842 3 MPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFN-FnPFETVEQIVmqqaGYY----GVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQ 155
Cdd:COG3842 81 MVFQDYAlF-PHLTVAENV----AFGlrmrGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 156 LLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-212 |
1.97e-47 |
|
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: 156.25 E-value: 1.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 5 EIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGLVP 83
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QefnfnpfetveqivmqqagyygvsrtlakeraekyltqldlwekrkerarnLSGGMKRRLMIARALMHEPQLLILDEPT 163
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2019142000 164 AGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGE 212
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-214 |
7.91e-47 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 160.38 E-value: 7.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLG 80
Cdd:PRK13536 39 TVAIDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILD 160
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2019142000 161 EPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-225 |
2.11e-46 |
|
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: 156.20 E-value: 2.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGG---FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT----HLEQAK 76
Cdd:cd03258 2 IELKNVSKVFGDTggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 77 QHLGLVPQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQL 156
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 157 LILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLGK 225
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-214 |
4.55e-46 |
|
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: 155.97 E-value: 4.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT--HLEQAKQhLG 80
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlsRRELARR-IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFNPFETVEQIVMQ-QAGYYGVSRTLAKE---RAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQL 156
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALgRYPHLGLFGRPSAEdreAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 157 LILDEPTAGVDIELRRSMWEFLKQIN-SQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-215 |
1.17e-45 |
|
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: 154.20 E-value: 1.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGG---FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQ--- 77
Cdd:cd03257 2 LEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 78 -HLGLVPQE--FNFNPFETVEQIVMQ--QAGYYGVSRTLAKERAEKYLTQLDLWEKRKER-ARNLSGGMKRRLMIARALM 151
Cdd:cd03257 82 kEIQMVFQDpmSSLNPRMTIGEQIAEplRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRyPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019142000 152 HEPQLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-215 |
2.90e-45 |
|
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: 152.67 E-value: 2.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAKQHLGLVP 83
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVmqqaGY----YGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLIL 159
Cdd:cd03259 79 QDYALFPHLTVAENI----AFglklRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 160 DEPTAGVDIELRRSMWEFLKQI-NSQGITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-212 |
7.64e-45 |
|
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: 150.42 E-value: 7.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH---LEQAKQHLG 80
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedeLPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFNPFETVEQIVMqqagyYGvsrtlakeraekyltqldlwekrkerarnLSGGMKRRLMIARALMHEPQLLILD 160
Cdd:cd03229 80 MVFQDFALFPHLTVLENIA-----LG-----------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 161 EPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGE 212
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-164 |
2.34e-44 |
|
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: 148.18 E-value: 2.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGLVPQEFNFNPFETVEQIV 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 99 MQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARN----LSGGMKRRLMIARALMHEPQLLILDEPTA 164
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-214 |
5.17e-43 |
|
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: 147.48 E-value: 5.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYA-----GGF---------------EALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKV 63
Cdd:cd03267 1 IEVSNLSKSYRvyskePGLigslkslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 64 FGHNIDTHLEQAKQHLGLVPQE-----FNFNPFETVEQIvmqqAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSG 138
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVVFGQktqlwWDLPVIDSFYLL----AAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 139 GMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-223 |
5.57e-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: 146.81 E-value: 5.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHL---EQAKQHLG 80
Cdd:cd03224 1 LEVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI-TGLpphERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFNPFETVEQ-IVMqqaGYYGVSRTLAKERAEKYLTQL-DLWEKRKERARNLSGGMKRRLMIARALMHEPQLLI 158
Cdd:cd03224 79 YVPEGRRIFPELTVEEnLLL---GAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019142000 159 LDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLL 223
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-215 |
1.11e-42 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 149.46 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGG---FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT----HLEQAK 76
Cdd:COG1135 2 IELENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 77 QHLGLVPQefNFNPFE--TVEQIV---MQQAGyygVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALM 151
Cdd:COG1135 82 RKIGMIFQ--HFNLLSsrTVAENValpLEIAG---VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 152 HEPQLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHyleeaEM-----LCRHIGIINRGELIE 215
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITH-----EMdvvrrICDRVAVLENGRIVE 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-193 |
1.13e-42 |
|
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: 145.75 E-value: 1.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNID---THLEQAKQHLG 80
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFNPFETV-EQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLIL 159
Cdd:cd03262 80 MVFQQFNLFPHLTVlENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190
....*....|....*....|....*....|....
gi 2019142000 160 DEPTAGVDIELRRSMWEFLKQINSQGITIILTTH 193
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-214 |
1.61e-42 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 146.33 E-value: 1.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHL---EQAKQ 77
Cdd:COG1137 1 MMTLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLpmhKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 78 HLGLVPQEfnfnP--FE--TVEQ---IVMQQAGyygVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARAL 150
Cdd:COG1137 79 GIGYLPQE----AsiFRklTVEDnilAVLELRK---LSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 151 MHEPQLLILDEPTAGVD----IELRRsMWEFLKQinsQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:COG1137 152 ATNPKFILLDEPFAGVDpiavADIQK-IIRHLKE---RGIGVLITDHNVRETLGICDRAYIISEGKVL 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-224 |
1.68e-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: 152.75 E-value: 1.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAGG-FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKT---SGTVKVFGHNIDTHLEQAK-Q 77
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 78 HLGLVPQEF--NFNPfETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQ 155
Cdd:COG1123 84 RIGMVFQDPmtQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 156 LLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLG 224
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-213 |
7.31e-42 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 144.30 E-value: 7.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAKQHLGLVP 83
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPT 163
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 164 AGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGEL 213
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-214 |
1.86e-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: 140.61 E-value: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH-LEQAKQHLGLV 82
Cdd:TIGR03740 1 LETKNLSKRF-GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKdLHKIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQEFNFNPFETVeQIVMQQAGyygvsrtLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEP 162
Cdd:TIGR03740 80 PLYENLTARENL-KVHTTLLG-------LPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2019142000 163 TAGVDI----ELRrsmwEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:TIGR03740 152 TNGLDPigiqELR----ELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-205 |
3.40e-40 |
|
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: 139.15 E-value: 3.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLVP 83
Cdd:COG4133 3 LEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVMQQAGYYGVSRTlaKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPT 163
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2019142000 164 AGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEmLCRHI 205
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA-AARVL 200
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-223 |
7.10e-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: 7.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNID---THlEQAKQHLG 80
Cdd:COG0410 4 LEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITglpPH-RIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQE---FnfnPFETVEQ-IVMqqAGYYGVSRTLAKERAEKYLTQL-DLWEKRKERARNLSGGMKRRLMIARALMHEPQ 155
Cdd:COG0410 82 YVPEGrriF---PSLTVEEnLLL--GAYARRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 156 LLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLL 223
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-214 |
8.63e-40 |
|
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: 137.18 E-value: 8.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 5 EIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT--HLEQAKqHLGLV 82
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlsPKELAR-KIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQefnfnpfetveqivmqqagyygvsrtlakeraekYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEP 162
Cdd:cd03214 79 PQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 163 TAGVDIELRRSMWEFLKQIN-SQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-200 |
9.75e-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: 138.97 E-value: 9.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNID---THLEQAKQHLG 80
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFNPFETVEQIVM------QqagyyGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTlapikvK-----KMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2019142000 155 QLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHyleeaEM 200
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTH-----EM 196
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-213 |
1.27e-39 |
|
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: 147.85 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 16 GFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLVPQEFNFNPFETVE 95
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 96 QIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMW 175
Cdd:TIGR01257 1022 EHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190
....*....|....*....|....*....|....*...
gi 2019142000 176 EFLKQINSqGITIILTTHYLEEAEMLCRHIGIINRGEL 213
Cdd:TIGR01257 1102 DLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-223 |
7.49e-39 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 136.86 E-value: 7.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTY---AGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQH 78
Cdd:COG1124 1 MLEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 79 LGLVPQ--EFNFNPFETVEQIVMQQAGYYGVSRTlaKERAEKYLTQLDLWEK-RKERARNLSGGMKRRLMIARALMHEPQ 155
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILAEPLRIHGLPDR--EERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 156 LLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLL 223
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-225 |
2.04e-38 |
|
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: 142.59 E-value: 2.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT-HLEQAKQHLGL 81
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQE---FN---------FNPFETVEQI--VMQQAGYYGVSRTLAkeraEKYLTQLDlwekrkERARNLSGGMKRRLMIA 147
Cdd:COG4988 416 VPQNpylFAgtirenlrlGRPDASDEELeaALEAAGLDEFVAALP----DGLDTPLG------EGGRGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 148 RALMHEPQLLILDEPTAGVDIELRRSMWEFLKQInSQGITIILTTHYLEEAEmLCRHIGIINRGELIENTTMKGLLGK 225
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLA-QADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-232 |
4.60e-38 |
|
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: 134.74 E-value: 4.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGLV 82
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIrEQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLwEKRKERAR---NLSGGMKRRLMIARALMHEPQLLIL 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGL-DPAEFADRyphELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 160 DEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLGKLH---VETFI 232
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAndfVAEFV 236
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-215 |
8.60e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.82 E-value: 8.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLVP 83
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLT--QLDLWEKRkeRARNLSGGMKRRLMIARALMHEPQLLILDE 161
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLElvQLEGLADR--YPSQLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2019142000 162 PTAGVDIELRRSMWEFLKQI-NSQGITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:COG1118 160 PFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQ 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-214 |
1.95e-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: 1.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGhnidthleqakqhlglvp 83
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNF-NPFEtveqivMQQAGYYGVSrtlakeraekyltQLdlwekrkerarnlSGGMKRRLMIARALMHEPQLLILDEP 162
Cdd:cd03216 62 KEVSFaSPRD------ARRAGIAMVY-------------QL-------------SVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2019142000 163 TAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-223 |
2.33e-37 |
|
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: 132.80 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT----HLEQAKQH 78
Cdd:COG1127 5 MIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 79 LGLVPQE---FNFnpfETVEQIV---MQQagYYGVSRTLAKERAEKYLTQLDLwekrkERARN-----LSGGMKRRLMIA 147
Cdd:COG1127 84 IGMLFQGgalFDS---LTVFENVafpLRE--HTDLSEAEIRELVLEKLELVGL-----PGAADkmpseLSGGMRKRVALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 148 RALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLL 223
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-213 |
9.01e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 134.43 E-value: 9.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAKQHLG 80
Cdd:COG3839 1 MASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEF-NFnPFETVEQ-IvmqqaGYY----GVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:COG3839 79 MVFQSYaLY-PHMTVYEnI-----AFPlklrKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 155 QLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGEL 213
Cdd:COG3839 153 KVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-213 |
1.14e-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: 130.22 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI----DTHLEQAKQHL 79
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 80 GLVPQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLIL 159
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2019142000 160 DEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGEL 213
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-214 |
3.80e-36 |
|
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: 129.59 E-value: 3.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHL---EQAKQHLG 80
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLpmhKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFnpFE--TVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLI 158
Cdd:cd03218 79 YLPQEASI--FRklTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 159 LDEPTAGVD----IELRRsmweFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:cd03218 157 LDEPFAGVDpiavQDIQK----IIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVL 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-213 |
6.03e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.40 E-value: 6.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT-HLEQAKQHLGLV 82
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQEfnfnPF---ETVEQIVmqQAGYYGVSRTLAKERAEKYLTQLDLWEKRKER-ARNLSGGMKRRLMIARALMHEPQLLI 158
Cdd:COG4619 80 PQE----PAlwgGTVRDNL--PFPFQLRERKFDRERALELLERLGLPPDILDKpVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2019142000 159 LDEPTAGVDIELRRSMWEFLKQ-INSQGITIILTTHYLEEAEMLCRHIGIINRGEL 213
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-215 |
7.54e-36 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 128.98 E-value: 7.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNID-------THLEQA 75
Cdd:COG4161 2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqkpseKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 76 KQHLGLVPQEFNFNPFETVEQ-IVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMEnLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 155 QLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-215 |
2.92e-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: 127.39 E-value: 2.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHL---EQAKQHLG 80
Cdd:TIGR04406 2 LVAENLIKSY-KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI-THLpmhERARLGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFNPFETVEQ---IVMQQAgyYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLL 157
Cdd:TIGR04406 80 YLPQEASIFRKLTVEEnimAVLEIR--KDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019142000 158 ILDEPTAGVD----IELRRSMwEFLKQinsQGITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:TIGR04406 158 LLDEPFAGVDpiavGDIKKII-KHLKE---RGIGVLITDHNVRETLDICDRAYIISDGKVLA 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-222 |
2.99e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.83 E-value: 2.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNID-THLEQAKQH- 78
Cdd:COG1129 2 EPLLEMRGISKSF-GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfRSPRDAQAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 79 LGLVPQEFNFNPFETV-EQIVM--QQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQ 155
Cdd:COG1129 81 IAIIHQELNLVPNLSVaENIFLgrEPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 156 LLILDEPTA---GVDIElrrSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGL 222
Cdd:COG1129 161 VLILDEPTAsltEREVE---RLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-212 |
4.64e-35 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 124.80 E-value: 4.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGF-EALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH-LEQAKQHLGL 81
Cdd:cd03228 1 IEFKNVSFSYPGRPkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLdLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQEFNFnpFetveqivmqqagyygvSRTLAKeraekyltqldlwekrkerarN-LSGGMKRRLMIARALMHEPQLLILD 160
Cdd:cd03228 81 VPQDPFL--F----------------SGTIRE---------------------NiLSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2019142000 161 EPTAGVDIELRRSMWEFLKQInSQGITIILTTHYLEEAEMlCRHIGIINRGE 212
Cdd:cd03228 122 EATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-223 |
5.70e-35 |
|
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: 132.97 E-value: 5.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 2 YALEIDQLRKTYAG-GFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQA-KQHL 79
Cdd:COG4987 332 PSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 80 GLVPQE---FN---------FNPFETVEQI--VMQQAGYYGVSRTLAkeraEKYLTQLDlwekrkERARNLSGGMKRRLM 145
Cdd:COG4987 412 AVVPQRphlFDttlrenlrlARPDATDEELwaALERVGLGDWLAALP----DGLDTWLG------EGGRRLSGGERRRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 146 IARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQInSQGITIILTTHYLEEAEMLCRHIgIINRGELIENTTMKGLL 223
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERMDRIL-VLEDGRIVEQGTHEELL 557
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-214 |
6.26e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 132.07 E-value: 6.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGH--NIDTHLEQAKQH 78
Cdd:COG3845 3 PPALELRGITKRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 79 LGLVPQEFN-FNPFeTV-EQIVMQQAGYYGVSRTLAKERA------EKYLTQLDLwekrKERARNLSGGMKRRLMIARAL 150
Cdd:COG3845 82 IGMVHQHFMlVPNL-TVaENIVLGLEPTKGGRLDRKAARArirelsERYGLDVDP----DAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 151 MHEPQLLILDEPTAG-----VDiELrrsmWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:COG3845 157 YRGARILILDEPTAVltpqeAD-EL----FEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-215 |
1.05e-34 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 125.90 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNID-------THLEQA 75
Cdd:PRK11124 2 SIQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfsktpsdKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 76 KQHLGLVPQEFNFNPFETV-EQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVqQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 155 QLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-218 |
1.34e-34 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 128.38 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 5 EIDQLRKTYAGG---FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI----DTHLEQAKQ 77
Cdd:PRK11153 3 ELKNISKVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 78 HLGLVPQEFNFNPFETVEQIV---MQQAGyygVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNValpLELAG---TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019142000 155 QLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTT 218
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-215 |
1.35e-34 |
|
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: 125.37 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVN-----KTSGTVKVFGHNI---DTHLEQA 75
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydlDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 76 KQHLGLVPQEFNfnPFE-TV-EQIVmqqagyYGV------SRTLAKERAEKYLTQLDLWE--KRKERARNLSGGMKRRLM 145
Cdd:cd03260 80 RRRVGMVFQKPN--PFPgSIyDNVA------YGLrlhgikLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 146 IARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQgITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-215 |
3.19e-34 |
|
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: 126.71 E-value: 3.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTY---AGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLV---NKTSGTVKVFGHNIdTHLEQAK- 76
Cdd:COG0444 2 LEVRNLKVYFptrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDL-LKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 77 -----QHLGLVPQE-FN-FNPFETVEQIVMQQAGYY-GVSRTLAKERAEKYLTQLDLwEKRKERARN----LSGGMKRRL 144
Cdd:COG0444 81 rkirgREIQMIFQDpMTsLNPVMTVGDQIAEPLRIHgGLSKAEARERAIELLERVGL-PDPERRLDRypheLSGGMRQRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019142000 145 MIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVE 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-218 |
5.36e-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: 5.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAGG---FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQA---- 75
Cdd:COG4181 8 IIELRGLTKTVGTGageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDArarl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 76 -KQHLGLVPQEFNFNPFETVEQIVM---QQAGyygvsRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALM 151
Cdd:COG4181 88 rARHVGFVFQSFQLLPTLTALENVMlplELAG-----RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 152 HEPQLLILDEPTAGVDIELRRSMWEFLKQINS-QGITIILTTHYLEEAEMlCRHIGIINRGELIENTT 218
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTA 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-220 |
6.31e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 124.80 E-value: 6.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNID---THLEQAKQHLG 80
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LV---PQEFNFNPfeTVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLL 157
Cdd:PRK13639 82 IVfqnPDDQLFAP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 158 ILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMK 220
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-202 |
8.68e-34 |
|
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: 122.75 E-value: 8.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 5 EIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdtHLEQAKQHLGLVPQ 84
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI--KAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 85 EFNFNPF-ETVEQIVmqqagYYGVSRT-LAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEP 162
Cdd:cd03226 79 DVDYQLFtDSVREEL-----LLGLKELdAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2019142000 163 TAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLC 202
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVC 193
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-216 |
1.15e-33 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 129.84 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGG---FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQA----- 75
Cdd:PRK10535 5 LELKDIRRSYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 76 KQHLGLVPQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQ 155
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 156 LLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINrGELIEN 216
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRD-GEIVRN 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-225 |
1.22e-33 |
|
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: 129.95 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAG-GFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLG 80
Cdd:COG2274 473 DIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLrQIDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQE---FN---------FNPFETVEQIV--MQQAGYYGVsrtlAKERAEKYLTQLDlwekrkERARNLSGGMKRRLMI 146
Cdd:COG2274 553 VVLQDvflFSgtirenitlGDPDATDEEIIeaARLAGLHDF----IEALPMGYDTVVG------EGGSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 147 ARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQInSQGITIILTTHYLEEAEmLCRHIGIINRGELIENTTMKGLLGK 225
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-224 |
3.21e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 122.77 E-value: 3.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI------DTHLEQAKQ 77
Cdd:PRK10619 6 LNVIDLHKRY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkDGQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 78 H--------LGLVPQEFNFNPFETVEQIVMQQ-AGYYGVSRTLAKERAEKYLTQLDLWEKRKER-ARNLSGGMKRRLMIA 147
Cdd:PRK10619 85 NqlrllrtrLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 148 RALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLG 224
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
13-193 |
5.21e-33 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 120.22 E-value: 5.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 13 YAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNID---THLEQAKQHLGLV---PQEF 86
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysrKGLLERRQRVGLVfqdPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 87 NFNPfeTVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGV 166
Cdd:TIGR01166 81 LFAA--DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180
....*....|....*....|....*..
gi 2019142000 167 DIELRRSMWEFLKQINSQGITIILTTH 193
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-225 |
2.47e-32 |
|
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: 119.75 E-value: 2.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEaLKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAKQHLGLVP 83
Cdd:cd03299 1 LKVENLSKDW-KEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVMqqagyYGVsRTLAKERAEKYLTQLDLWEK--------RKerARNLSGGMKRRLMIARALMHEPQ 155
Cdd:cd03299 78 QNYALFPHMTVYKNIA-----YGL-KKRKVDKKEIERKVLEIAEMlgidhllnRK--PETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 156 LLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLGK 225
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-218 |
5.70e-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: 5.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHL---- 79
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 80 GLVpqeFNFNP-FE--TVEQIV---MQQagYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHE 153
Cdd:cd03261 80 GML---FQSGAlFDslTVFENVafpLRE--HTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019142000 154 PQLLILDEPTAGVD-------IELRRSmwefLKQinSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTT 218
Cdd:cd03261 155 PELLLYDEPTAGLDpiasgviDDLIRS----LKK--ELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-215 |
1.10e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 121.48 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFeALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAKQHLGLVP 83
Cdd:PRK11607 20 LEIRNLTKSFDGQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPT 163
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 164 AGVDIELRRSM-WEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:PRK11607 178 GALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-214 |
1.30e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 118.68 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 2 YALEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQ-AKQHLG 80
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFNPFE-TVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLIL 159
Cdd:PRK13647 83 LVFQDPDDQVFSsTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2019142000 160 DEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-198 |
5.94e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 117.88 E-value: 5.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 17 FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH----------------------LEQ 74
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviqktrfkkIKK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 75 AKQ---HLGLVPQEFNFNPFE-TVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERAR-NLSGGMKRRLMIARA 149
Cdd:PRK13651 100 IKEirrRVGVVFQFAEYQLFEqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRSPfELSGGQKRRVALAGI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2019142000 150 LMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEA 198
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNV 228
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-222 |
7.49e-31 |
|
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: 115.70 E-value: 7.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHL---EQAKQHLG 80
Cdd:TIGR03410 1 LEVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI-TKLpphERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFNPFETVEQIVmqQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILD 160
Cdd:TIGR03410 79 YVPQGREIFPRLTVEENL--LTGLAALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 161 EPTAGV------DIElrrsmwEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGL 222
Cdd:TIGR03410 157 EPTEGIqpsiikDIG------RVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-223 |
9.88e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 116.00 E-value: 9.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYAGGfEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH--------- 71
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQ-TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 72 LEQAKQHLGLVPQEFNFNPFETV-EQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARAL 150
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLFPHRTVlENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 151 MHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLL 223
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-213 |
2.44e-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: 113.89 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVkVFGHNIDTHLEQAKQHLGLVP 83
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI-YIGGRDVTDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPT 163
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 164 AGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGEL 213
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-213 |
3.38e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 114.72 E-value: 3.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGfEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLV--NKTSGT-VKVFGHNIDTH------LEQ 74
Cdd:PRK09984 5 IRVEKLAKTFNQH-QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRTVQREgrlardIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 75 AKQHLGLVPQEFNF-NPFETVEQIVMQQAGYYGVSRT-------LAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMI 146
Cdd:PRK09984 84 SRANTGYIFQQFNLvNRLSVLENVLIGALGSTPFWRTcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 147 ARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQIN-SQGITIILTTHYLEEAEMLCRHIGIINRGEL 213
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINqNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
3.85e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.90 E-value: 3.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHL 79
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 80 GLV---PQEFNFNPfeTVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQL 156
Cdd:PRK13652 81 GLVfqnPDDQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 157 LILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMK------GLLGKLHVE 229
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEeiflqpDLLARVHLD 238
|
....
gi 2019142000 230 TFIL 233
Cdd:PRK13652 239 LPSL 242
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-198 |
6.67e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.41 E-value: 6.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 19 ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfgHNIDT----HLEQAKQHLGLVPQefnfNP-FET 93
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV--DGLDTsdeeNLWDIRNKAGMVFQ----NPdNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 94 VEQIVMQQAGY----YGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIE 169
Cdd:PRK13633 99 VATIVEEDVAFgpenLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190
....*....|....*....|....*....|
gi 2019142000 170 LRRSMWEFLKQINSQ-GITIILTTHYLEEA 198
Cdd:PRK13633 179 GRREVVNTIKELNKKyGITIILITHYMEEA 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-214 |
8.68e-30 |
|
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: 112.39 E-value: 8.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 23 VSLTVNkGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKV-----FGHNIDTHLEQAKQHLGLVPQEFNFNPFETVEQI 97
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlFDSRKKINLPPQQRKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 98 VmqQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEF 177
Cdd:cd03297 96 L--AFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 2019142000 178 LKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:cd03297 174 LKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-193 |
9.05e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 118.34 E-value: 9.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH-LEQAKQHLGL 81
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLtLESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQE---FN---------FNPFETVEQI--VMQQAGYYGVSRTLAkeraEKYLTQLDlwekrkERARNLSGGMKRRLMIA 147
Cdd:COG1132 419 VPQDtflFSgtireniryGRPDATDEEVeeAAKAAQAHEFIEALP----DGYDTVVG------ERGVNLSGGQRQRIAIA 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2019142000 148 RALMHEPQLLILDEPTAGVDIE----LRRSMWEFLKqinsqGITIILTTH 193
Cdd:COG1132 489 RALLKDPPILILDEATSALDTEtealIQEALERLMK-----GRTTIVIAH 533
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-294 |
9.12e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 116.20 E-value: 9.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAKQHLGLVP 83
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIV-----MQQagyygVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLI 158
Cdd:PRK09452 93 QSYALFPHMTVFENVafglrMQK-----TPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 159 LDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLL---GKLHVETFILD 234
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYeepKNLFVARFIGE 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 235 IDNeeklqpLTDVVSQRVVDGSLEIELEKTQGMNHVFTQLSE-QGVNVMsMRNKANRLEEL 294
Cdd:PRK09452 248 INI------FDATVIERLDEQRVRANVEGRECNIYVNFAVEPgQKLHVL-LRPEDLRVEEI 301
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-223 |
3.90e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 111.00 E-value: 3.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFeaLKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAKQHLGLVP 83
Cdd:COG3840 2 LRLDDLTYRY-GDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPPAERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVmqqagYYGVSRTL-----AKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLI 158
Cdd:COG3840 78 QENNLFPHLTVAQNI-----GLGLRPGLkltaeQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2019142000 159 LDEPTAGVDIELRRSMWEFLKQIN-SQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLL 223
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCrERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-198 |
5.29e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.49 E-value: 5.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYAGGFE---ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDThlEQAKQ 77
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 78 hlGLVPQEFNFNPFETVEQIV---MQQAGyygVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:COG4525 79 --GVVFQKDALLPWLNVLDNVafgLRLRG---VPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2019142000 155 QLLILDEPTAGVDIELRRSMWEFLKQI-NSQGITIILTTHYLEEA 198
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEA 198
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-215 |
5.44e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 111.47 E-value: 5.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRkTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVN-----KTSGTVKVFGHNI---DTHL 72
Cdd:PRK14267 2 KFAIETVNLR-VYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIyspDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 73 EQAKQHLGLVPQEFNFNPFETVEQIVMQQAGYYGV--SRTLAKERAEKYLTQLDLWEKRKER----ARNLSGGMKRRLMI 146
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRlndyPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 147 ARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQgITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-215 |
7.71e-29 |
|
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: 109.93 E-value: 7.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 10 RKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGhNIDTHLEqakqhLGLvpqefNFN 89
Cdd:cd03220 28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSLLG-----LGG-----GFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 90 PFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIE 169
Cdd:cd03220 97 PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2019142000 170 LRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:cd03220 177 FQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
12-214 |
1.04e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 111.37 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 12 TYAGG--FE--ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH-----LEQAKQHLGLV 82
Cdd:PRK13649 11 TYQAGtpFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkdIKQIRKKVGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 pqeFNFNPFETVEQIVMQQAGY----YGVSRTLAKERAEKYLTQLDLWEKRKERAR-NLSGGMKRRLMIARALMHEPQLL 157
Cdd:PRK13649 91 ---FQFPESQLFEETVLKDVAFgpqnFGVSQEEAEALAREKLALVGISESLFEKNPfELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 158 ILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-236 |
1.10e-28 |
|
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: 110.81 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 19 ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI----DTHLEQAKQH-LGLVPQEFNFNPFET 93
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELRELRRKkISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 94 VEQIVMQQAGYYGVSRTLAKERAEKYLTQLDL--WEKRKERArnLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELR 171
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLegWEHKYPDE--LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIR 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 172 RSMW-EFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLGKL---HVETFILDID 236
Cdd:cd03294 197 REMQdELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPandYVREFFRGVD 265
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-214 |
1.74e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.88 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGG--FE--ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-----DTHLEQ 74
Cdd:PRK13634 3 ITFQKVEHRYQYKtpFErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 75 AKQHLGLVPQEFNFNPFE-TVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERAR-NLSGGMKRRLMIARALMH 152
Cdd:PRK13634 83 LRKKVGIVFQFPEHQLFEeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 153 EPQLLILDEPTAGVDIELRRSMWEFLKQIN-SQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
7-242 |
2.17e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 110.64 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 7 DQLRKTYAGG----FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-----DTHLEQAKQ 77
Cdd:PRK13646 6 DNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkDKYIRPVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 78 HLGLVPQEFNFNPFE-TVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERAR-NLSGGMKRRLMIARALMHEPQ 155
Cdd:PRK13646 86 RIGMVFQFPESQLFEdTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 156 LLILDEPTAGVDIELRRSMWEFLKQIN-SQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLGKL-HVETFIL 233
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKkKLADWHI 245
|
....*....
gi 2019142000 234 DIDNEEKLQ 242
Cdd:PRK13646 246 GLPEIVQLQ 254
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-215 |
2.73e-28 |
|
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: 108.97 E-value: 2.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 2 YALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVkVFGHNIDTHLEQAKQHLGL 81
Cdd:cd03296 1 MSIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI-LFGGEDATDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQEFNFNPFETVEQIVM----QQAGYYGVSRTLAKERAEKYL--TQLDLWEKRkeRARNLSGGMKRRLMIARALMHEPQ 155
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAfglrVKPRSERPPEAEIRAKVHELLklVQLDWLADR--YPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 156 LLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQ 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-205 |
3.26e-28 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 113.54 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQA--KQHLG 80
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL-ADADADswRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQE-FNFN-----------PFETVEQI--VMQQAGYYgvsrTLAKERAEKYLTQLDlwekrkERARNLSGGMKRRLMI 146
Cdd:TIGR02857 400 WVPQHpFLFAgtiaenirlarPDASDAEIreALERAGLD----EFVAALPQGLDTPIG------EGGAGLSGGQAQRLAL 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 147 ARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQInSQGITIILTTHYLEEAEmLCRHI 205
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAA-LADRI 526
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-211 |
3.43e-28 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 114.73 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFE-ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLV 82
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQefnfnpFETVEQIVM--QQAGYYGVSRTLAKERAEKY----LTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQL 156
Cdd:TIGR01257 2018 PQ------FDAIDDLLTgrEHLYLYARLRGVPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2019142000 157 LILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRG 211
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-233 |
7.90e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 108.06 E-value: 7.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYAGGfEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT---HlEQAKQ 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlplH-ARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 78 HLGLVPQEFN-FNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQL 156
Cdd:PRK10895 79 GIGYLPQEASiFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 157 LILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLGKLHVETFIL 233
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYL 235
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-199 |
8.43e-28 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 113.30 E-value: 8.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 15 GGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLVPQEFNFNPFETV 94
Cdd:NF033858 277 GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 95 EQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSM 174
Cdd:NF033858 357 RQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMF 436
|
170 180
....*....|....*....|....*.
gi 2019142000 175 WEFLKQIN-SQGITIILTTHYLEEAE 199
Cdd:NF033858 437 WRLLIELSrEDGVTIFISTHFMNEAE 462
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-193 |
9.44e-28 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 106.48 E-value: 9.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 10 RKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVN--KTSGTVKVFGHNIdtHLEQAKQHLGLVPQEFN 87
Cdd:cd03213 15 SSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPL--DKRSFRKIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 88 FNPFETVEQIVMQQAgyygvsrtlakeraekyltqldlwekrkeRARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVD 167
Cdd:cd03213 93 LHPTLTVRETLMFAA-----------------------------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180
....*....|....*....|....*.
gi 2019142000 168 IELRRSMWEFLKQINSQGITIILTTH 193
Cdd:cd03213 144 SSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-168 |
9.71e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.94 E-value: 9.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNID--THLEQAKqHLG 80
Cdd:PRK13548 2 MLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwSPAELAR-RRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFN-PFeTVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALM------HE 153
Cdd:PRK13548 80 VLPQHSSLSfPF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170
....*....|....*
gi 2019142000 154 PQLLILDEPTAGVDI 168
Cdd:PRK13548 159 PRWLLLDEPTSALDL 173
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
15-216 |
1.48e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.10 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 15 GGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGT-----VKVFGHNIDTHLeqAKQHLGLVPQEFNFN 89
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdgLKVNDPKVDERL--IRQEAGMVFQQFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 90 PFET-VEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDI 168
Cdd:PRK09493 90 PHLTaLENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2019142000 169 ELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIEN 216
Cdd:PRK09493 170 ELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-215 |
1.81e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 107.43 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 2 YALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKST---TIGIISSLV--NKTSGTVKVFGHNI---DTHLE 73
Cdd:COG1117 10 PKIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIpgARVEGEILLDGEDIydpDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 74 QAKQHLGLVPQefNFNPF-----ETVEqivmqqagyYGV------SRTLAKERAEKYLTQLDLWEKRKER----ARNLSG 138
Cdd:COG1117 89 ELRRRVGMVFQ--KPNPFpksiyDNVA---------YGLrlhgikSKSELDEIVEESLRKAALWDEVKDRlkksALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 139 GMKRRLMIARALMHEPQLLILDEPTAGVD------IElrrsmwEFLKQINSQgITIILTTHYLEEAEMLCRHIGIINRGE 212
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDpistakIE------ELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGE 230
|
...
gi 2019142000 213 LIE 215
Cdd:COG1117 231 LVE 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-214 |
1.98e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.31 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 6 IDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfghnidthleQAKQHLGLVPQE 85
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI----------PKGLRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 86 FNFNPFETVEQIVMQ--------QAGYYGVSRTLAKE------------------------RAEKYLTQLDLWEKRKERA 133
Cdd:COG0488 70 PPLDDDLTVLDTVLDgdaelralEAELEELEAKLAEPdedlerlaelqeefealggweaeaRAEEILSGLGFPEEDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 134 -RNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRsmW--EFLKqiNSQGiTIILTTH---YLEEaemLCRHIGI 207
Cdd:COG0488 150 vSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLK--NYPG-TVLVVSHdryFLDR---VATRILE 221
|
....*..
gi 2019142000 208 INRGELI 214
Cdd:COG0488 222 LDRGKLT 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-198 |
2.62e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.01 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 15 GGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHnidthleqakQHLGLVPQEFNFN---PF 91
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----------ARVAYVPQRSEVPdslPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 92 eTVEQIVM----QQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVD 167
Cdd:NF040873 73 -TVRDLVAmgrwARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|.
gi 2019142000 168 IELRRSMWEFLKQINSQGITIILTTHYLEEA 198
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-214 |
3.69e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 106.35 E-value: 3.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLrkTY-AGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH-LEQAKQHLGL 81
Cdd:COG4559 2 LEAENL--SVrLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWsPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQ--EFNFnPFeTVEQIV-MQQAGyYGVSRTLAKERAEKYLTQLDLWEKRkERA-RNLSGGMKRRLMIARAL------- 150
Cdd:COG4559 80 LPQhsSLAF-PF-TVEEVVaLGRAP-HGSSAAQDRQIVREALALVGLAHLA-GRSyQTLSGGEQQRVQLARVLaqlwepv 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019142000 151 MHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:COG4559 156 DGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-214 |
5.28e-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: 104.88 E-value: 5.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 24 SLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAKQHLGLVPQEFNFNPFETVEQIVMqqag 103
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNLFAHLTVEQNVG---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 104 yYGVSRTLA-----KERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFL 178
Cdd:cd03298 93 -LGLSPGLKltaedRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 2019142000 179 KQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:cd03298 172 LDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-220 |
5.54e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.84 E-value: 5.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAGG--FEA--LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-----DTHLE 73
Cdd:PRK13641 2 SIKFENVDYIYSPGtpMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 74 QAKQHLGLVpqeFNFNPFETVEQIVMQQAGY----YGVSRTLAKERAEKYLTQLDLWEKRKERAR-NLSGGMKRRLMIAR 148
Cdd:PRK13641 82 KLRKKVSLV---FQFPEAQLFENTVLKDVEFgpknFGFSEDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019142000 149 ALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMK 220
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPK 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-193 |
8.07e-27 |
|
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: 104.66 E-value: 8.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNK---TSGTVKVFGHNIDTHleQAKQHLGLVPQEFNFNPFETVEQ 96
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPD--QFQKCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 97 ----IVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRR 172
Cdd:cd03234 101 tltyTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180
....*....|....*....|.
gi 2019142000 173 SMWEFLKQINSQGITIILTTH 193
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTIH 201
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-230 |
2.04e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.47 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 13 YAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVN-----KTSGTVKVFGHNI---DTHLEQAKQHLGLVPQ 84
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 85 EFNFNPFETVEQIVmqqagyYGVSRTLAKERA------EKYLTQLDLWEKRKER----ARNLSGGMKRRLMIARALMHEP 154
Cdd:PRK14239 94 QPNPFPMSIYENVV------YGLRLKGIKDKQvldeavEKSLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 155 QLLILDEPTAGVDIELRRSMWEFLKQINSQgITIILTTHYLEEAEMLCRHIGIINRGELIE-NTTMKGLLGKLHVET 230
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEyNDTKQMFMNPKHKET 243
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-193 |
2.40e-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: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfGHNIdthleqakqHLGLVP 83
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---------KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEF-NFNPFETVEQIVMQqagyygVSRTLAKERAEKYLTQL----DLWEKRkerARNLSGGMKRRLMIARALMHEPQLLI 158
Cdd:COG0488 385 QHQeELDPDKTVLDELRD------GAPGGTEQEVRGYLGRFlfsgDDAFKP---VGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190
....*....|....*....|....*....|....*
gi 2019142000 159 LDEPTAGVDIELRRSMWEFLKqiNSQGiTIILTTH 193
Cdd:COG0488 456 LDEPTNHLDIETLEALEEALD--DFPG-TVLLVSH 487
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-225 |
3.77e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 107.99 E-value: 3.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 2 YALEIDQLRKTYAGG-FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQA-KQHL 79
Cdd:PRK11160 337 VSLTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 80 GLVPQE---FN---------FNPFETVEQI--VMQQAGYygvsrtlakeraEKYLTQ---LDLWekRKERARNLSGGMKR 142
Cdd:PRK11160 417 SVVSQRvhlFSatlrdnlllAAPNASDEALieVLQQVGL------------EKLLEDdkgLNAW--LGEGGRQLSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 143 RLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQInSQGITIILTTHYLEEAEMLCRhIGIINRGELIENTTMKGL 222
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGLEQFDR-ICVMDNGQIIEQGTHQEL 560
|
...
gi 2019142000 223 LGK 225
Cdd:PRK11160 561 LAQ 563
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-218 |
3.98e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 104.33 E-value: 3.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 19 ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGH--NIDTHLEQAKQhLGLVPQefnfNP---F-- 91
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlSEETVWDVRRQ-VGMVFQ----NPdnqFvg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 92 ETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELR 171
Cdd:PRK13635 97 ATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2019142000 172 RSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIgIINRGELIENTT 218
Cdd:PRK13635 177 REVLETVRQLKEQkGITVLSITHDLDEAAQADRVI-VMNKGEILEEGT 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-211 |
8.18e-26 |
|
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: 102.16 E-value: 8.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDthlEQAKQHLgLVPQEFNFNPFETVEQIVm 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT---EPGPDRM-VVFQNYSLLPWLTVRENI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 100 qqagYYGVSRTLA-------KERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRR 172
Cdd:TIGR01184 76 ----ALAVDRVLPdlskserRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2019142000 173 SMWEFLKQI-NSQGITIILTTHYLEEAEMLCRHIGIINRG 211
Cdd:TIGR01184 152 NLQEELMQIwEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
107-303 |
8.81e-26 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 104.82 E-value: 8.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 107 VSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGI 186
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 187 TIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLGKLHVETFILDIDNEEKLQPLTDVVSQRVV-----------DG 255
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAHAAELDRMVGAIAQAGLdgiagatadheDG 275
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2019142000 256 SLEIELEKTQGMNHVFTQLSEQGVNVMSMRNKANRLEELFVSIVRQQS 303
Cdd:NF000106 276 VVNVPIVSDEQLSAVVGMLGERGFTISGHQHPSAQL*EVFLAITGQKT 323
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-225 |
9.39e-26 |
|
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: 102.31 E-value: 9.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAG-GFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGL 81
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQE-FNFNpfETVEQIVMqqagyYGVSRTLAKE--RAEKYLTQLDLWEKRK--------ERARNLSGGMKRRLMIARAL 150
Cdd:cd03251 81 VSQDvFLFN--DTVAENIA-----YGRPGATREEveEAARAANAHEFIMELPegydtvigERGVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 151 MHEPQLLILDEPTAGVDIELRRSMWEFLKQInSQGITIILTTHYL---EEAEMLCrhigIINRGELIENTTMKGLLGK 225
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLstiENADRIV----VLEDGKIVERGTHEELLAQ 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-214 |
1.30e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.20 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGG--FE--ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI---DTHLEQAK 76
Cdd:PRK13637 3 IKIENLTHIYMEGtpFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 77 QHLGLVPQEFNFNPFE-TVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDL-WEKRKERAR-NLSGGMKRRLMIARALMHE 153
Cdd:PRK13637 83 KKVGLVFQYPEYQLFEeTIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdYEDYKDKSPfELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019142000 154 PQLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-214 |
1.39e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 102.76 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAGGFE-ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH-LEQAKQHLG 80
Cdd:PRK13632 7 MIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQefnfNP---F--ETVEQIVMqqagyYG-----VSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARAL 150
Cdd:PRK13632 87 IIFQ----NPdnqFigATVEDDIA-----FGlenkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019142000 151 MHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGI-TIILTTHYLEEAeMLCRHIGIINRGELI 214
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKLI 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3-202 |
1.80e-25 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 102.27 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQakQHLGLV 82
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK--NLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQ--EFNFNPFETVEQIVMQqaGYYG----VSRTLAKERA--EKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:PRK15056 84 PQseEVDWSFPVLVEDVVMM--GRYGhmgwLRRAKKRDRQivTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2019142000 155 QLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLC 202
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFC 209
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-221 |
3.44e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 100.66 E-value: 3.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGG---FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAK---- 76
Cdd:PRK11629 6 LQCDNLCKRYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 77 -QHLGLVPQEFNFNP-FETVEQIVMQQAgYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:PRK11629 86 nQKLGFIYQFHHLLPdFTALENVAMPLL-IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 155 QLLILDEPTAGVDIELRRSMWEFLKQIN-SQGITIILTTHYLEEAEMLCRHIGIINrGELIENTTMKG 221
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDLQLAKRMSRQLEMRD-GRLTAELSLMG 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-218 |
3.78e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 101.73 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 19 ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfGHNIDTHLEQAKQ------HLGLVpqeFNFNPFE 92
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEikpvrkKVGVV---FQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 93 TVEQIVMQQAGY----YGVSRTLAKERAEKYLTQLDL----WEKRkerARNLSGGMKRRLMIARALMHEPQLLILDEPTA 164
Cdd:PRK13643 97 LFEETVLKDVAFgpqnFGIPKEKAEKIAAEKLEMVGLadefWEKS---PFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2019142000 165 GVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTT 218
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-214 |
4.12e-25 |
|
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: 99.97 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 18 EALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT-HLEQAKQHLGLVPQE---FN------ 87
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDvtlFYgtlrdn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 88 ---FNPFETVEQIvMQQAGYYGVSrTLAKERAEKYLTQLdlwekrKERARNLSGGMKRRLMIARALMHEPQLLILDEPTA 164
Cdd:cd03245 98 itlGAPLADDERI-LRAAELAGVT-DFVNKHPNGLDLQI------GERGRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2019142000 165 GVDIELRRSMWEFLKQINSqGITIILTTHYLEEAEMLCRHIgIINRGELI 214
Cdd:cd03245 170 AMDMNSEERLKERLRQLLG-DKTLIIITHRPSLLDLVDRII-VMDSGRIV 217
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-215 |
4.18e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.54 E-value: 4.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 10 RKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGhNIDTHLEqakqhLGLvpqefNFN 89
Cdd:COG1134 32 RRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSALLE-----LGA-----GFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 90 PFETVEQIVMQQAGYYGVSRTLAKER-------AEkyltqldLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEP 162
Cdd:COG1134 101 PELTGRENIYLNGRLLGLSRKEIDEKfdeivefAE-------LGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2019142000 163 TAGVDIELR-RSMwEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:COG1134 174 LAVGDAAFQkKCL-ARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-262 |
5.44e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 104.36 E-value: 5.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGgFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAKQH-LG-- 80
Cdd:PRK15439 12 LCARSISKQYSG-VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC-ARLTPAKAHqLGiy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFNPFETVEQIVMqqagyYGVSRT-LAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLIL 159
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENIL-----FGLPKRqASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 160 DEPTAGVD-IELRRsmweFLKQINS---QGITIILTTHYLEEAEMLCRHIGIINRGELIenttmkgLLGKLHvetfilDI 235
Cdd:PRK15439 165 DEPTASLTpAETER----LFSRIREllaQGVGIVFISHKLPEIRQLADRISVMRDGTIA-------LSGKTA------DL 227
|
250 260
....*....|....*....|....*..
gi 2019142000 236 DNEEKLQPLTDVVSQRVVDGSLEIELE 262
Cdd:PRK15439 228 STDDIIQAITPAAREKSLSASQKLWLE 254
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-215 |
6.52e-25 |
|
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: 100.65 E-value: 6.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYA-GGF-------EALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHL--E 73
Cdd:TIGR02769 3 LEVRDVTHTYRtGGLfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDL-YQLdrK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 74 QAK---QHLGLVPQEF--NFNPFETVEQIVMQQAGYYgvSRTLAKERAEKYLTQLDLWEKRKE----RARNLSGGMKRRL 144
Cdd:TIGR02769 82 QRRafrRDVQLVFQDSpsAVNPRMTVRQIIGEPLRHL--TSLDESEQKARIAELLDMVGLRSEdadkLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019142000 145 MIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-218 |
7.07e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.85 E-value: 7.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 17 FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKV----FGHNIDTH----------LEQAKQHLGLV 82
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHelitnpyskkIKNFKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQEFNFNPFE----TVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERAR-NLSGGMKRRLMIARALMHEPQLL 157
Cdd:PRK13631 119 SMVFQFPEYQlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 158 ILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTT 218
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
15-211 |
9.26e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 102.61 E-value: 9.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 15 GGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNID-THLEQAKQHLGLVPQE----FNFn 89
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVASVPQDtslsFEF- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 90 pfeTVEQIV-MQQAGYYG--VSRTLAKERA-EKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAG 165
Cdd:PRK09536 93 ---DVRQVVeMGRTPHRSrfDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2019142000 166 VDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRG 211
Cdd:PRK09536 170 LDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-198 |
1.66e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 99.39 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAGGfEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdthlEQAKQHLGLV 82
Cdd:PRK11248 1 MLQISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV----EGPGAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEP 162
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 2019142000 163 TAGVDIELRRSMWEFLKQI-NSQGITIILTTHYLEEA 198
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEA 192
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-225 |
2.14e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.54 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 2 YALEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH---LEQAKQH 78
Cdd:PRK13636 4 YILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSrkgLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 79 LGLVPQEFNFNPFE-TVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLL 157
Cdd:PRK13636 84 VGMVFQDPDNQLFSaSVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 158 ILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLGK 225
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-216 |
2.67e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 98.41 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAK---QHLG 80
Cdd:PRK11614 6 LSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-TDWQTAKimrEAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFNPFETVEQ-IVMqqaGYYGVSRTLAKERAEK-YLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLI 158
Cdd:PRK11614 84 IVPEGRRVFSRMTVEEnLAM---GGFFAERDQFQERIKWvYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 159 LDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCrhigiiNRGELIEN 216
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLA------DRGYVLEN 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-213 |
2.78e-24 |
|
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: 96.52 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFEA-LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT-HLEQAKQHLGL 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQEFNFNPFETVEQIvmqqagyygvsrtlakeraekyltqldlwekrkerarnLSGGMKRRLMIARALMHEPQLLILDE 161
Cdd:cd03246 81 LPQDDELFSGSIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2019142000 162 PTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRhIGIINRGEL 213
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADR-ILVLEDGRV 173
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-195 |
3.45e-24 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 98.00 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 18 EALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGLVPQE---FN----FN 89
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrDLNLRWLRSQIGLVSQEpvlFDgtiaEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 90 -----PFETVEQI--VMQQAGYYGVSRTLakerAEKYLTQLDlwekrkERARNLSGGMKRRLMIARALMHEPQLLILDEP 162
Cdd:cd03249 97 irygkPDATDEEVeeAAKKANIHDFIMSL----PDGYDTLVG------ERGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190
....*....|....*....|....*....|...
gi 2019142000 163 TAGVDIELRRSMWEFLKQInSQGITIILTTHYL 195
Cdd:cd03249 167 TSALDAESEKLVQEALDRA-MKGRTTIVIAHRL 198
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-193 |
4.66e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 97.54 E-value: 4.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGG---FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAK---- 76
Cdd:PRK10584 7 VEVHHLKKSVGQGeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 77 -QHLGLVPQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQ 155
Cdd:PRK10584 87 aKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 2019142000 156 LLILDEPTAGVDIELRRSMWEFLKQIN-SQGITIILTTH 193
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNrEHGTTLILVTH 205
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-194 |
5.07e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 97.83 E-value: 5.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTyAGGFEALKGVSLTVNKGDFYALLGPNGAGKST---TI-GIISSLVnkTSGTVKVFGHNIdTHL---EQAK 76
Cdd:COG0396 1 LEIKNLHVS-VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLmGHPKYEV--TSGSILLDGEDI-LELspdERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 77 QHLGLV---PQEF----NFNPFETVEQIVMQQAgyygVSRTLAKERAEKYLTQLDLWEKRKERARN--LSGGMKRRLMIA 147
Cdd:COG0396 77 AGIFLAfqyPVEIpgvsVSNFLRTALNARRGEE----LSAREFLKLLKEKMKELGLDEDFLDRYVNegFSGGEKKRNEIL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2019142000 148 RALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHY 194
Cdd:COG0396 153 QMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHY 199
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-189 |
5.24e-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: 97.50 E-value: 5.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYA----GG--FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGII--SSLVNKTSGTVKVFGHNIDthLEQA 75
Cdd:COG4778 5 LEVENLSKTFTlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYLPDSGSILVRHDGGWVD--LAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 76 ---------KQHLGLVPQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLwekrKERARNL-----SGGMK 141
Cdd:COG4778 83 spreilalrRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNL----PERLWDLppatfSGGEQ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2019142000 142 RRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITII 189
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-225 |
6.32e-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: 97.30 E-value: 6.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 13 YAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGLVPQE------ 85
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIrDISRKSLRSMIGVVLQDtflfsg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 86 --------FNFNPFETVEQIVMQQAGYYGVSRTLAKeraeKYLTQLdlwekrKERARNLSGGMKRRLMIARALMHEPQLL 157
Cdd:cd03254 92 timenirlGRPNATDEEVIEAAKEAGAHDFIMKLPN----GYDTVL------GENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 158 ILDEPTAGVDIELRRSMWEFLKQINsQGITIILTTHYL---EEAEMlcrhIGIINRGELIENTTMKGLLGK 225
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLstiKNADK----ILVLDDGKIIEEGTHDELLAK 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-215 |
6.99e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 97.68 E-value: 6.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVN-----KTSGTVKVFGHNI----DTH 71
Cdd:PRK14247 1 MNKIEIRDLKVSF-GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIfkmdVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 72 LEQAKQHLGLVPQEF-NFNPFETVEqiVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKER----ARNLSGGMKRRLMI 146
Cdd:PRK14247 80 LRRRVQMVFQIPNPIpNLSIFENVA--LGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 147 ARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQgITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVE 225
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-225 |
1.89e-23 |
|
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: 96.15 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGLV 82
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIrEVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQE---FN---------FNPFETVEQIV--MQQAGYYGVSRTLAkeraEKYLTQLDlwekrkERARNLSGGMKRRLMIAR 148
Cdd:cd03253 81 PQDtvlFNdtigyniryGRPDATDEEVIeaAKAAQIHDKIMRFP----DGYDTIVG------ERGLKLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 149 ALMHEPQLLILDEPTAGVDIELRRSMWEFLKQInSQGITIILTTHYLEEAeMLCRHIGIINRGELIENTTMKGLLGK 225
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-194 |
3.33e-23 |
|
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: 94.52 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRkTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKST---TI-GIISSLVnkTSGTVKVFGHNIdTHL---EQAK 76
Cdd:cd03217 1 LEIKDLH-VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTlakTImGHPKYEV--TEGEILFKGEDI-TDLppeERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 77 QHLGLVPQEfnfnPFEtveqivmqqagYYGVsrtlakeRAEKYLTQLDLwekrkerarNLSGGMKRRLMIARALMHEPQL 156
Cdd:cd03217 77 LGIFLAFQY----PPE-----------IPGV-------KNADFLRYVNE---------GFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190
....*....|....*....|....*....|....*...
gi 2019142000 157 LILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHY 194
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY 163
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
15-218 |
3.55e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.83 E-value: 3.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 15 GGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLVpQEFN----FNP 90
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVV-RTFQhvrlFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 91 FETVEQIVMQQ---------AGY-----YGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQL 156
Cdd:PRK11300 95 MTVIENLLVAQhqqlktglfSGLlktpaFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 157 LILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTT 218
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-195 |
3.60e-23 |
|
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: 99.36 E-value: 3.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHL-GLV 82
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRvSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQE---FNfnpfETVEQIVMQQAGYYG---VSRTLAKERAEKYLTQLD--LWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:TIGR02868 415 AQDahlFD----TTVRENLRLARPDATdeeLWAALERVGLADWLRALPdgLDTVLGEGGARLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2019142000 155 QLLILDEPTAGVDIELRRSMWEFLKQInSQGITIILTTHYL 195
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLAA-LSGRTVVLITHHL 530
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-211 |
3.80e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 97.46 E-value: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAKQHLGLV 82
Cdd:PRK10851 2 SIEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQEFNFNPFETVEQIVMqqagyYGVSRTLAKERAEKY-----------LTQLDLWEKRkeRARNLSGGMKRRLMIARALM 151
Cdd:PRK10851 80 FQHYALFRHMTVFDNIA-----FGLTVLPRRERPNAAaikakvtqlleMVQLAHLADR--YPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 152 HEPQLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRG 211
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
3-214 |
5.70e-23 |
|
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: 97.09 E-value: 5.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDqLRKTYaGGFeALKgVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG---------HNIDTHle 73
Cdd:COG4148 2 MLEVD-FRLRR-GGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargIFLPPH-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 74 qaKQHLGLVPQE---FnfnPFETVEQIVMqqagyYGVSRTLAKERAEKY---LTQLDLWEKRKERARNLSGGMKRRLMIA 147
Cdd:COG4148 76 --RRRIGYVFQEarlF---PHLSVRGNLL-----YGRKRAPRAERRISFdevVELLGIGHLLDRRPATLSGGERQRVAIG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 148 RALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-199 |
7.32e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 98.66 E-value: 7.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNID--THLEQAKQHLG 80
Cdd:NF033858 1 VARLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdaRHRRAVCPRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEF--NFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLI 158
Cdd:NF033858 80 YMPQGLgkNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2019142000 159 LDEPTAGVDIELRRSMWEFLKQINSQ--GITIILTTHYLEEAE 199
Cdd:NF033858 160 LDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAE 202
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-214 |
2.22e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.54 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHL--EQAKQHLGL 81
Cdd:PRK11231 3 LRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI-SMLssRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQEFnfnpfETVEQIVMQQAGYYGVSRTLA---------KERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMH 152
Cdd:PRK11231 81 LPQHH-----LTPEGITVRELVAYGRSPWLSlwgrlsaedNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019142000 153 EPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-240 |
2.91e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 93.23 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGF----EALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAK--Q 77
Cdd:COG1101 2 LELKNLSKTFNPGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEYKraK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 78 HLGLVPQefnfNPFE------TVEQ---IVMQQAGYYGVSRTLAKERAEKY---LTQLDL-WEKR-KERARNLSGGMKRR 143
Cdd:COG1101 81 YIGRVFQ----DPMMgtapsmTIEEnlaLAYRRGKRRGLRRGLTKKRRELFrelLATLGLgLENRlDTKVGLLSGGQRQA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 144 LMIARALMHEPQLLILDEPTAGVD-------IELRRsmweflKQINSQGITIILTTHYLEEAemlcrhIGIINRgeLIen 216
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDpktaalvLELTE------KIVEENNLTTLMVTHNMEQA------LDYGNR--LI-- 220
|
250 260
....*....|....*....|....
gi 2019142000 217 ttMkgllgkLHVETFILDIDNEEK 240
Cdd:COG1101 221 --M------MHEGRIILDVSGEEK 236
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-193 |
6.20e-22 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 89.43 E-value: 6.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfGHNIDthleqakqhLGLVP 83
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK---------IGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QefnfnpfetveqivmqqagyygvsrtlakeraekyltqldlwekrkerarnLSGGMKRRLMIARALMHEPQLLILDEPT 163
Cdd:cd03221 70 Q---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190
....*....|....*....|....*....|
gi 2019142000 164 AGVDIELRRSMWEFLKQINSqgiTIILTTH 193
Cdd:cd03221 99 NHLDLESIEALEEALKEYPG---TVILVSH 125
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-223 |
9.18e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.85 E-value: 9.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNID--THLEQAKQHLGL 81
Cdd:PRK09700 6 ISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQEFNfnpfeTVEQIVMQQAGYYG------------VSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARA 149
Cdd:PRK09700 85 IYQELS-----VIDELTVLENLYIGrhltkkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 150 LMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGE-----LIENTTMKGLL 223
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSsvcsgMVSDVSNDDIV 238
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-193 |
1.35e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.70 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI----DTHLEQAKQHL 79
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 80 GLVPQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLIL 159
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190
....*....|....*....|....*....|....
gi 2019142000 160 DEPTAGVDIELRRSMWEFLKQINSQGITIILTTH 193
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-211 |
1.62e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 92.98 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAKQHLG 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-NELEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFNPFETVEqivmQQAGY----YGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQL 156
Cdd:PRK11650 80 MVFQNYALYPHMSVR----ENMAYglkiRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2019142000 157 LILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRG 211
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGG 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-205 |
1.72e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 90.94 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKvfghnidthlEQAKQHLGLVPQEFNFNPFE--TVEQI 97
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------RNGKLRIGYVPQKLYLDTTLplTVNRF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 98 VMQQAGYYGVSRTLAKERAE-KYLTQLDLwekrkeraRNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWE 176
Cdd:PRK09544 90 LRLRPGTKKEDILPALKRVQaGHLIDAPM--------QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 2019142000 177 FLKQINSQ-GITIILTTHYL-----EEAEMLC--RHI 205
Cdd:PRK09544 162 LIDQLRRElDCAVLMVSHDLhlvmaKTDEVLClnHHI 198
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-193 |
1.97e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 90.91 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 5 EIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGLVP 83
Cdd:COG4604 3 EIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVaTTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVMqqAGYYGVSR---TLAKERA-EKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLIL 159
Cdd:COG4604 82 QENHINSRLTVRELVA--FGRFPYSKgrlTAEDREIiDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190
....*....|....*....|....*....|....*
gi 2019142000 160 DEPTAGVDIELRRSMWEFLKQI-NSQGITIILTTH 193
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLH 194
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-223 |
3.09e-21 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 93.63 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAG-GFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGL 81
Cdd:TIGR02203 331 VEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLaDYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQE---FNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLD--LWEKRKERARNLSGGMKRRLMIARALMHEPQL 156
Cdd:TIGR02203 411 VSQDvvlFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPlgLDTPIGENGVLLSGGQRQRLAIARALLKDAPI 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 157 LILDEPTAGVDIELRRSMWEFLKQInSQGITIILTTHYLEEAEMLCRhIGIINRGELIENTTMKGLL 223
Cdd:TIGR02203 491 LILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIEKADR-IVVMDDGRIVERGTHNELL 555
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-218 |
5.46e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.20 E-value: 5.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 19 ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH-LEQAKQHLGLVPQefnfNP-FETVEQ 96
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDnFEKLRKHIGIVFQ----NPdNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 97 IVMQQAGY----YGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRR 172
Cdd:PRK13648 100 IVKYDVAFglenHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2019142000 173 SMWEFLKQINS-QGITIILTTHYLEEAeMLCRHIGIINRGELIENTT 218
Cdd:PRK13648 180 NLLDLVRKVKSeHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGT 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-222 |
5.54e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 93.25 E-value: 5.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI---DTHLeqAKQHLGLVPQE----------- 85
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLvqyDHHY--LHRQVALVGQEpvlfsgsvren 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 86 ----FNFNPFETVeQIVMQQAGyygvSRTLAKERAEKYLTQLDlwekrkERARNLSGGMKRRLMIARALMHEPQLLILDE 161
Cdd:TIGR00958 575 iaygLTDTPDEEI-MAAAKAAN----AHDFIMEFPNGYDTEVG------EKGSQLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 162 PTAGVDIELRRSMWEFLKQinsQGITIILTTHYLEEAEMlCRHIGIINRGELIENTTMKGL 222
Cdd:TIGR00958 644 ATSALDAECEQLLQESRSR---ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-225 |
6.21e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.18 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGLVPQEFNfNPF--ETVEQ 96
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLtEENVWDIRHKIGMVFQNPD-NQFvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 97 IVMQQAGYYGVSRTLAKERAEKYLTQLDLWE-KRKERARnLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMW 175
Cdd:PRK13650 102 DVAFGLENKGIPHEEMKERVNEALELVGMQDfKEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 176 EFLKQINSQ-GITIILTTHYLEEAEMLCRHIgIINRGELIENTTMKGLLGK 225
Cdd:PRK13650 181 KTIKGIRDDyQMTVISITHDLDEVALSDRVL-VMKNGQVESTSTPRELFSR 230
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-213 |
9.46e-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: 88.68 E-value: 9.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdthleQAKQH------LGLVPQEFNFNPFET 93
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI-----SQYEHkylhskVSLVGQEPVLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 94 VEQIV--MQQAGYYGVSRTLAKERAEKYLTQLDL--WEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIE 169
Cdd:cd03248 105 QDNIAygLQSCSFECVKEAAQKAHAHSFISELASgyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2019142000 170 LRRSMWEFLKQINSQGiTIILTTHYLEEAEMlCRHIGIINRGEL 213
Cdd:cd03248 185 SEQQVQQALYDWPERR-TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-216 |
1.13e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.97 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVkVFGhniDTHLEQAKQHLGLVP 83
Cdd:PRK11247 13 LLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG---TAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETVEQIVmqQAGYYGVSRtlakERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPT 163
Cdd:PRK11247 88 QDARLLPWKKVIDNV--GLGLKGQWR----DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2019142000 164 AGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAemlcrhIGIINRGELIEN 216
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEA------VAMADRVLLIEE 209
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-215 |
1.36e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.95 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVN------KTSGTVKVFGHNI-DTHLEQAKQHLGLVPQEFNFNPFE 92
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIfQIDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 93 TVEQIVMQQAGYYGVS-RTLAKERAEKYLTQLDLWEKRKER----ARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVD 167
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2019142000 168 IELRRSMWEFLKQINSQgITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:PRK14246 186 IVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
8-213 |
1.71e-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: 90.17 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 8 QLRKTYaGGFEaLKgVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG-------HNIDTHLEqaKQHLG 80
Cdd:TIGR02142 4 RFSKRL-GDFS-LD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPPE--KRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFNPFETVEQIVMqqagyYGVSRTLAKERA---EKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLL 157
Cdd:TIGR02142 79 YVFQEARLFPHLSVRGNLR-----YGMKRARPSERRisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 158 ILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGEL 213
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-213 |
2.38e-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: 86.33 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 19 ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGH--NIDTHLEQAKQHLGLVPQEFNfnpfetVEQ 96
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvTRRSPRDAIRAGIAYVPEDRK------REG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 97 IVMQQagyyGVSRTLAkeraekyLTQLdlwekrkerarnLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWE 176
Cdd:cd03215 89 LVLDL----SVAENIA-------LSSL------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYR 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 2019142000 177 FLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGEL 213
Cdd:cd03215 146 LIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-193 |
2.79e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.88 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNK---TSGTVKVFGHNIDthLEQAKQHLGLVPQEFNFNPFETVEQ 96
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID--AKEMRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 97 IVMQQAgYYGVSRTLAK----ERAEKYLTQLDLWEKRK------ERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGV 166
Cdd:TIGR00955 119 HLMFQA-HLRMPRRVTKkekrERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180
....*....|....*....|....*..
gi 2019142000 167 DIELRRSMWEFLKQINSQGITIILTTH 193
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-198 |
2.90e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.92 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 13 YAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVN-----KTSGTVKVFGHNI-DTHLE--QAKQHLGLVPQ 84
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyAPDVDpvEVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 85 EFNFNPFETVEQIVM--QQAGYYGVsrtlAKERAEKYLTQLDLWEKRKERAR----NLSGGMKRRLMIARALMHEPQLLI 158
Cdd:PRK14243 99 KPNPFPKSIYDNIAYgaRINGYKGD----MDELVERSLRQAALWDEVKDKLKqsglSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2019142000 159 LDEPTAGVDIELRRSMWEFLKQINSQgITIILTTHYLEEA 198
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQA 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-225 |
4.90e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 90.02 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 13 YAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGLVPQE---FNF 88
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIrTVTRASLRRNIAVVFQDaglFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 89 N---------PFETVEQIVmqqagyygvsrtLAKERAEKyltqLDLWEKRK--------ERARNLSGGMKRRLMIARALM 151
Cdd:PRK13657 424 SiednirvgrPDATDEEMR------------AAAERAQA----HDFIERKPdgydtvvgERGRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 152 HEPQLLILDEPTAGVDIELRRSMWEFLKQInSQGITIILTTHYL---EEAEMlcrhIGIINRGELIENTTMKGLLGK 225
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLstvRNADR----ILVFDNGRVVESGSFDELVAR 559
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-233 |
5.06e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.74 E-value: 5.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGhnIDT----HLEQAKQHL 79
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTgdfsKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 80 GLVPQefnfNP-----FETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:PRK13644 80 GIVFQ----NPetqfvGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 155 QLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIgIINRGELIENTTMKGLLGKLHVETFIL 233
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRII-VMDRGKIVLEGEPENVLSDVSLQTLGL 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-199 |
5.72e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 86.00 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGfEALKGVSLTVNKGDFYALLGPNGAGKST----TIGIISSLVNkTSGTVKVFGHNIDThLEQAKQHL 79
Cdd:COG4136 2 LSLENLTITLGGR-PLLAPLSLTVAPGEILTLMGPSGSGKSTllaaIAGTLSPAFS-ASGEVLLNGRRLTA-LPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 80 GLVPQEFNFNPFETVEQ-IVMQQAGyyGVSRTLAKERAEKYLTQLDLwEKRKERARN-LSGGMKRRLMIARALMHEPQLL 157
Cdd:COG4136 79 GILFQDDLLFPHLSVGEnLAFALPP--TIGRAQRRARVEQALEEAGL-AGFADRDPAtLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2019142000 158 ILDEPTAGVDIELRRSMWEF-LKQINSQGITIILTTHYLEEAE 199
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTHDEEDAP 198
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-215 |
6.61e-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: 86.01 E-value: 6.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFE-ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT-HLEQAKQHLGL 81
Cdd:cd03244 3 IEFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQE---------FNFNPFETVEQIVMQQAgyygVSRTLAKERAEKYLTQLDLweKRKERARNLSGGMKRRLMIARALMH 152
Cdd:cd03244 83 IPQDpvlfsgtirSNLDPFGEYSDEELWQA----LERVGLKEFVESLPGGLDT--VVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 153 EPQLLILDEPTAGVDIELRRSMWEFLKQiNSQGITIILTTHYLeEAEMLCRHIGIINRGELIE 215
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRL-DTIIDSDRILVLDKGRVVE 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-214 |
8.45e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.16 E-value: 8.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAGGFE-ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLV-----NKTSGTVKVFGHNIDTHLEqAK 76
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpddnPNSKITVDGITLTAKTVWD-IR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 77 QHLGLVPQEFNfNPF--ETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:PRK13640 84 EKVGIVFQNPD-NQFvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 155 QLLILDEPTAGVDIELRRSMWEFLKQI-NSQGITIILTTHYLEEAEMlCRHIGIINRGELI 214
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANM-ADQVLVLDDGKLL 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-214 |
8.65e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.31 E-value: 8.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTyaggfEALKGVSLTVNKGD---FYALLGpngAGKSTTIGIISSLVNKTSGTVKVFGHNID-THLEQAKQH 78
Cdd:COG1129 256 VLEVEGLSVG-----GVVRDVSFSVRAGEilgIAGLVG---AGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIRA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 79 -LGLVP---QEFNFNPFETVEQ-IVMQQAGYYG----VSRTLAKERAEKYLTQLDLweK---RKERARNLSGGMKRRLMI 146
Cdd:COG1129 328 gIAYVPedrKGEGLVLDLSIREnITLASLDRLSrgglLDRRRERALAEEYIKRLRI--KtpsPEQPVGNLSGGNQQKVVL 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 147 ARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:COG1129 406 AKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
18-196 |
1.73e-19 |
|
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: 85.39 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 18 EALKGVSLTVNKGDFYALLGPNGAGKSTTIGII----SSLVnkTSGTVKVFGHNIDTHLEQAKQHLGLvpqefnFNPFET 93
Cdd:TIGR01978 14 EILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghpSYEV--TSGTILFKGQDLLELEPDERARAGL------FLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 94 VEQIVmqqagyyGVS-----RT-LAKERAEKYLTQLDLWEKRKE--------------RARNL----SGGMKRRLMIARA 149
Cdd:TIGR01978 86 PEEIP-------GVSnleflRSaLNARRSARGEEPLDLLDFEKLlkeklalldmdeefLNRSVnegfSGGEKKRNEILQM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2019142000 150 LMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLE 196
Cdd:TIGR01978 159 ALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQR 205
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-227 |
1.87e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.89 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYAGG--------FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT-H 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 72 LEQAKQHLGLVPQEFN-----FNPFETVEQIVMQQAGYY-GVSRTLAKERAEKYLTQLDL-WEKRKERARNLSGGMKRRL 144
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQdsisaVNPRKTVREIIREPLRHLlSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 145 MIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLL 223
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKL 240
|
....
gi 2019142000 224 GKLH 227
Cdd:PRK10419 241 TFSS 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-222 |
2.08e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.06 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTS--------GTVKVFGHNIDThl 72
Cdd:PRK13549 3 EYLLEMKNITKTF-GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyegeiifeGEELQASNIRDT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 73 EQA-----KQHLGLVPQ----EFNFNPFETVEQIVMQQAGYYgvsrtlakERAEKYLTQLDLWEKRKERARNLSGGMKRR 143
Cdd:PRK13549 80 ERAgiaiiHQELALVKElsvlENIFLGNEITPGGIMDYDAMY--------LRAQKLLAQLKLDINPATPVGNLGLGQQQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 144 LMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGL 222
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-223 |
3.51e-19 |
|
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: 87.87 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGH---NIDTHleQAKQHLG 80
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkDIDRH--TLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEfnfnPF---------------ETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLdlwekrKERARNLSGGMKRRLM 145
Cdd:TIGR01193 552 YLPQE----PYifsgsilenlllgakENVSQDEIWAACEIAEIKDDIENMPLGYQTEL------SEEGSSISGGQKQRIA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 146 IARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQgiTIILTTHYLEEAEMLCRhIGIINRGELIENTTMKGLL 223
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQSDK-IIVLDHGKIIEQGSHDELL 696
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-215 |
4.68e-19 |
|
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: 87.05 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLR---KTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTT----IGIISSLVNKTSGTVKVFGHNIDTHLEQAK 76
Cdd:COG4172 7 LSVEDLSvafGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 77 QHL-----GLVPQE--FNFNPFETVE-QI--VMQQagYYGVSRTLAKERAEKYLTQLDLWEKRKeRAR----NLSGGMKR 142
Cdd:COG4172 87 RRIrgnriAMIFQEpmTSLNPLHTIGkQIaeVLRL--HRGLSGAAARARALELLERVGIPDPER-RLDayphQLSGGQRQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019142000 143 RLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVE 237
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
23-222 |
5.17e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 85.93 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 23 VSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAKQHLGLVPQEFNFNPFETVEQIVmqqa 102
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRDICMVFQSYALFPHMSLGENV---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 103 GY----YGVSRTLAKERAEKYLTQLDL--WEKRkeRARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWE 176
Cdd:PRK11432 100 GYglkmLGVPKEERKQRVKEALELVDLagFEDR--YVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2019142000 177 FLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGL 222
Cdd:PRK11432 178 KIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-215 |
6.52e-19 |
|
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: 82.36 E-value: 6.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFE-ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLV 82
Cdd:cd03247 1 LSINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQEFnfnpfetveqivmqqagyYGVSRTLakeraekyltqldlwekRKERARNLSGGMKRRLMIARALMHEPQLLILDEP 162
Cdd:cd03247 81 NQRP------------------YLFDTTL-----------------RNNLGRRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 163 TAGVD----IELRRSMWEFLKqinsqGITIILTTHYLEEAEMLCRhIGIINRGELIE 215
Cdd:cd03247 126 TVGLDpiteRQLLSLIFEVLK-----DKTLIWITHHLTGIEHMDK-ILFLENGKIIM 176
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-225 |
1.25e-18 |
|
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: 82.92 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 14 AGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT-HLEQAKQHLGLVPQE---FN-- 87
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQEnvlFNrs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 88 -------FNPFETVEQIVmqQAGYYGVSRTLAKERAEKYLTQLDlwekrkERARNLSGGMKRRLMIARALMHEPQLLILD 160
Cdd:cd03252 92 irdnialADPGMSMERVI--EAAKLAGAHDFISELPEGYDTIVG------EQGAGLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019142000 161 EPTAGVDIELRRSMWEFLKQInSQGITIILTTHYLeEAEMLCRHIGIINRGELIENTTMKGLLGK 225
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-215 |
1.41e-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: 83.34 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGfEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH----LEQAKQHL 79
Cdd:TIGR02323 4 LQVSGLSKSYGGG-KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELelyqLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 80 gLVPQEFNF---NPFETV-----------EQIVMQQAGYYGVSRtlakERAEKYLTQLDLWEKR-KERARNLSGGMKRRL 144
Cdd:TIGR02323 83 -LMRTEWGFvhqNPRDGLrmrvsaganigERLMAIGARHYGNIR----ATAQDWLEEVEIDPTRiDDLPRAFSGGMQQRL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019142000 145 MIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQ-INSQGITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGlVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-229 |
1.74e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.52 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 6 IDQLRKTYAGG----FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQ---- 77
Cdd:PRK13645 9 LDNVSYTYAKKtpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEvkrl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 78 --HLGLVpqeFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQL-DLWEKRKERAR----NLSGGMKRRLMIARAL 150
Cdd:PRK13645 89 rkEIGLV---FQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELlKLVQLPEDYVKrspfELSGGQKRRVALAGII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 151 MHEPQLLILDEPTAGVDIELRRSMWEFLKQIN-SQGITIILTTHYLEEA-----EMLCRHIG-IINRGELIENTTMKGLL 223
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNkEYKKRIIMVTHNMDQVlriadEVIVMHEGkVISIGSPFEIFSNQELL 245
|
....*.
gi 2019142000 224 GKLHVE 229
Cdd:PRK13645 246 TKIEID 251
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-230 |
2.68e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.84 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 15 GGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSG-----TVKVFGHNIDTHLE--QAKQHLGLVPQEFN 87
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDvlEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 88 FNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARN----LSGGMKRRLMIARALMHEPQLLILDEPT 163
Cdd:PRK14271 112 PFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 164 AGVDIELRRSMWEFLKQINSQgITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLGK-LHVET 230
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSpKHAET 258
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-193 |
2.85e-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: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKST----TIGIISSlvnkTSGTVKVFGHNIDT-HLEQAKQHLGLVPQEFNFnpFE-T 93
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTlarlLVGVWPP----TAGSVRLDGADLSQwDREELGRHIGYLPQDVEL--FDgT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 94 V------------EQIVM--QQAGYYGVSRTLAKeraeKYLTQLDlwekrkERARNLSGGMKRRLMIARALMHEPQLLIL 159
Cdd:COG4618 422 IaeniarfgdadpEKVVAaaKLAGVHEMILRLPD----GYDTRIG------EGGARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190
....*....|....*....|....*....|....
gi 2019142000 160 DEPTAGVDIELRRSMWEFLKQINSQGITIILTTH 193
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKARGATVVVITH 525
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-236 |
3.94e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.93 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 19 ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI----DTHLEQAK-QHLGLVPQEFNFNPFET 93
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisDAELREVRrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 94 VEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRS 173
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 174 MWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLGKL---HVETFILDID 236
Cdd:PRK10070 203 MQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPandYVRTFFRGVD 269
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-214 |
6.49e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.59 E-value: 6.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 18 EALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH---LEQAKQHLGLVPQEFNFNPFET- 93
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSkrgLLALRQQVATVFQDPEQQIFYTd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 94 VEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRS 173
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2019142000 174 MWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:PRK13638 175 MIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-167 |
1.27e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 81.70 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTY--AGGF--------EALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLE 73
Cdd:COG4608 8 LEVRDLKKHFpvRGGLfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI-TGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 74 QAK-----QHLGLVPQefnfNPFE------TVEQIVMQQAGYYGV-SRTLAKERAEKYLTQLDLwekRKERARN----LS 137
Cdd:COG4608 87 GRElrplrRRMQMVFQ----DPYAslnprmTVGDIIAEPLRIHGLaSKAERRERVAELLELVGL---RPEHADRypheFS 159
|
170 180 190
....*....|....*....|....*....|
gi 2019142000 138 GGMKRRLMIARALMHEPQLLILDEPTAGVD 167
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-215 |
1.41e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.91 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYA--GGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT-HLEQAKQHLG 80
Cdd:PRK13642 5 LEVENLVFKYEkeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAeNVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNfNPF--ETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLI 158
Cdd:PRK13642 85 MVFQNPD-NQFvgATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 159 LDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRhIGIINRGELIE 215
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAASSDR-ILVMKAGEIIK 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-214 |
3.23e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 79.65 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 7 DQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHL-EQAKQHLGLVPQE 85
Cdd:PRK10253 11 EQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAsKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 86 FNFNPFETVEQIVMQqaGYYGVSRTLAKERAE------KYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLIL 159
Cdd:PRK10253 90 ATTPGDITVQELVAR--GRYPHQPLFTRWRKEdeeavtKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2019142000 160 DEPTAGVDIELRRSMWEFLKQIN-SQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
22-222 |
3.52e-17 |
|
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: 78.95 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 22 GVSLTVNKGDFYALLGPNGAGKSTT----IGIISSLVNKTSGTVKVFGHNIDThLEQAKQHLGLVPQE--FNFNPFETVE 95
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTclaiLGLLPPGLTQTSGEILLDGRPLLP-LSIRGRHIATIMQNprTAFNPLFTMG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 96 QIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKR---KERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRR 172
Cdd:TIGR02770 83 NHAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 173 SMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGL 222
Cdd:TIGR02770 163 RVLKLLRELRQLfGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEI 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-212 |
4.13e-17 |
|
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: 77.89 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 19 ALKGVSLTVNKGDFYALLGPNGAGKSTtigIISSL---VNKTSGTVKVFGHnidthleqakqhLGLVPQEfnfnPF---E 92
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSVSVPGS------------IAYVSQE----PWiqnG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 93 TV-EQIVMqqagyygvSRTLAKERAEKYL------TQLDLWEKRK-----ERARNLSGGMKRRLMIARALMHEPQLLILD 160
Cdd:cd03250 81 TIrENILF--------GKPFDEERYEKVIkacalePDLEILPDGDlteigEKGINLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2019142000 161 EPTAGVDIELRRSMWE-FLKQINSQGITIILTTH---YLEEAEmlcrHIGIINRGE 212
Cdd:cd03250 153 DPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHqlqLLPHAD----QIVVLDNGR 204
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-194 |
5.38e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 78.92 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTyAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISS--LVNKTSGTVKVFGHNIDTHLEQAKQHLGL 81
Cdd:CHL00131 8 LEIKNLHAS-VNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VpqeFNF-NPFET--VEQIVMQQAGYygvsRTLAKERAEKYLTQLDLWEKRKER-----------ARNL----SGGMKRR 143
Cdd:CHL00131 87 F---LAFqYPIEIpgVSNADFLRLAY----NSKRKFQGLPELDPLEFLEIINEKlklvgmdpsflSRNVnegfSGGEKKR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 144 LMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHY 194
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHY 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-215 |
7.15e-17 |
|
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: 80.50 E-value: 7.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTY----------AGGFEALKGVSLTVNKGDFYALLGPNGAGKSTT----IGIISSlvnktSGTVKVFGHNID 69
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 70 THLEQA----KQHLGLVPQE-FN-FNPFETVEQIVMQ--QAGYYGVSRTLAKERAEKYLTQLDLwekrKERARN-----L 136
Cdd:COG4172 351 GLSRRAlrplRRRMQVVFQDpFGsLSPRMTVGQIIAEglRVHGPGLSAAERRARVAEALEEVGL----DPAARHrypheF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 137 SGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-215 |
9.40e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 78.04 E-value: 9.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG-----HNIDTHLEQAKQH 78
Cdd:PRK11701 7 LSVRGLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 79 L-----GLVPQefnfNPFE----TV-------EQIVMQQAGYYGVSRtlakERAEKYLTQLDLWEKR-KERARNLSGGMK 141
Cdd:PRK11701 86 LlrtewGFVHQ----HPRDglrmQVsaggnigERLMAVGARHYGDIR----ATAGDWLERVEIDAARiDDLPTTFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019142000 142 RRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQ-INSQGITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-201 |
9.72e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.22 E-value: 9.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 15 GGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGlvPQEFnFNPFET 93
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIdDPDVAEACHYLG--HRNA-MKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 94 VEQIVMQQAGYYGVSRTLAKERAEKYltQLDLWEKRKerARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIE---- 169
Cdd:PRK13539 90 VAENLEFWAAFLGGEELDIAAALEAV--GLAPLAHLP--FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAaval 165
|
170 180 190
....*....|....*....|....*....|....*
gi 2019142000 170 LRRSMWEFLKqinsQGITIILTTHY---LEEAEML 201
Cdd:PRK13539 166 FAELIRAHLA----QGGIVIAATHIplgLPGAREL 196
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-201 |
9.75e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.15 E-value: 9.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVN-----KTSGTVKVFGHNI---DTHLEQAKQHLGLVPQEFNFNPF 91
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyerRVNLNRLRRQVSMVHPKPNLFPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 92 ETVEQIVmqqagyYGVS------RTLAKERAEKYLTQLDLWEKRKER----ARNLSGGMKRRLMIARALMHEPQLLILDE 161
Cdd:PRK14258 103 SVYDNVA------YGVKivgwrpKLEIDDIVESALKDADLWDEIKHKihksALDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2019142000 162 PTAGVDIELRRSMWEFLKQINSQG-ITIILTTHYLEEAEML 201
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRL 217
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-225 |
1.64e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.68 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFE-ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGL 81
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQEFN-FNpfETV-EQIVMQQAGYYgvSRTlAKERAEKYLTQLDLWEKRK--------ERARNLSGGMKRRLMIARALM 151
Cdd:PRK11176 422 VSQNVHlFN--DTIaNNIAYARTEQY--SRE-QIEEAARMAYAMDFINKMDngldtvigENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 152 HEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGiTIILTTHYL---EEAEMlcrhIGIINRGELIENTTMKGLLGK 225
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLstiEKADE----ILVVEDGEIVERGTHAELLAQ 568
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-215 |
2.26e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 78.90 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 24 SLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGT-VKVFGHNIDTHLEQAKQhlgLVPQEFNFN------PFE---- 92
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErQSQFSHITRLSFEQLQK---LVSDEWQRNntdmlsPGEddtg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 93 -TVEQIVMQQagyygvsrTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELR 171
Cdd:PRK10938 100 rTTAEIIQDE--------VKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2019142000 172 RSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:PRK10938 172 QQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAE 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-198 |
3.82e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.77 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 24 SLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNiDTHLEQAKQHLGLVPQEFNFNPFETVEQ-IVMqqa 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQENNLFSHLTVAQnIGL--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 103 gyyGVSRTLAKERAEKyltqldlwEKRKERARN-------------LSGGMKRRLMIARALMHEPQLLILDEPTAGVDIE 169
Cdd:PRK10771 95 ---GLNPGLKLNAAQR--------EKLHAIARQmgiedllarlpgqLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190
....*....|....*....|....*....|
gi 2019142000 170 LRRSMWEFLKQI-NSQGITIILTTHYLEEA 198
Cdd:PRK10771 164 LRQEMLTLVSQVcQERQLTLLMVSHSLEDA 193
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-215 |
4.26e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.41 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGgFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG--HNIDTHLEQAKQHLGL 81
Cdd:PRK11288 5 LSFDGIGKTFPG-VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqeMRFASTTAALAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQEFNFNPFETV-EQIVMQQ----AGYygVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQL 156
Cdd:PRK11288 84 IYQELHLVPEMTVaENLYLGQlphkGGI--VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 157 LILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-222 |
5.30e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 77.94 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLV--NKTSGTVKVFGHNIDTH--LEQAKQHL 79
Cdd:TIGR02633 2 LEMKGIVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASniRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 80 GLVPQEFNFNPFETV-EQIVMQQAGYYGVSRT---LAKERAEKYLTQLDLWEKRKERA-RNLSGGMKRRLMIARALMHEP 154
Cdd:TIGR02633 81 VIIHQELTLVPELSVaENIFLGNEITLPGGRMaynAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 155 QLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGL 222
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-215 |
8.68e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.58 E-value: 8.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 23 VSLTVNKGDFYALLGPNGAGKSttigiisSLVN------KTSGTVKVFG---HNIDthLEQAKQHLGLVPQefnfNP--F 91
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKT-------SLLNallgflPYQGSLKINGielRELD--PESWRKHLSWVGQ----NPqlP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 92 E-TV-EQIVM--QQAGYYGVSRTLAKERAEKYLTQLD--LWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAG 165
Cdd:PRK11174 436 HgTLrDNVLLgnPDASDEQLQQALENAWVSEFLPLLPqgLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2019142000 166 VDIELRRSMWEFLKQiNSQGITIILTTHYLEEAEMlCRHIGIINRGELIE 215
Cdd:PRK11174 516 LDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQ 563
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-226 |
9.26e-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: 77.15 E-value: 9.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYA----GGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKV-FGHN-ID-THLE--- 73
Cdd:TIGR03269 280 IKVRNVSKRYIsvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEwVDmTKPGpdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 74 --QAKQHLGLVPQEFNFNPFETVEQIVMQQAGyYGVSRTLAKERAEKYLTQLDLWEKRKERARN-----LSGGMKRRLMI 146
Cdd:TIGR03269 360 rgRAKRYIGILHQEYDLYPHRTVLDNLTEAIG-LELPDELARMKAVITLKMVGFDEEKAEEILDkypdeLSEGERHRVAL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 147 ARALMHEPQLLILDEPTAGVDIELRRSMWE-FLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLGK 225
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
.
gi 2019142000 226 L 226
Cdd:TIGR03269 519 L 519
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-193 |
1.15e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 76.90 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 2 YALEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfghnidthleQAKQHLGL 81
Cdd:TIGR03719 3 YIYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP----------QPGIKVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQEFNFNPFETVEQIVMQ--------QAGYYGVS----------RTLAKERAE--KYLTQLDLW--EKRKERA------ 133
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENVEEgvaeikdaLDRFNEISakyaepdadfDKLAAEQAElqEIIDAADAWdlDSQLEIAmdalrc 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 134 -------RNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIE----LRRSMWEFlkqinsQGiTIILTTH 193
Cdd:TIGR03719 153 ppwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsvawLERHLQEY------PG-TVVAVTH 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-213 |
1.36e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 18 EALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLV--PQEfnfnpfetve 95
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylPED---------- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 96 qivMQQAGYY-----------------GVSRTLAKERA--EKYLTQLDL-WEKRKERARNLSGGMKRRLMIARALMHEPQ 155
Cdd:PRK15439 347 ---RQSSGLYldaplawnvcalthnrrGFWIKPARENAvlERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQ 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 156 LLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGEL 213
Cdd:PRK15439 424 LLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-193 |
1.88e-15 |
|
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: 73.16 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLrkTYA-GGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLV 82
Cdd:TIGR01189 1 LAARNL--ACSrGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQEFNFNPFETV-EQIVMQQAGYYGVSRTLakeraEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDE 161
Cdd:TIGR01189 79 GHLPGLKPELSAlENLHFWAAIHGGAQRTI-----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|...
gi 2019142000 162 PTAGVDIE-LRRSMWEFLKQINSQGItIILTTH 193
Cdd:TIGR01189 154 PTTALDKAgVALLAGLLRAHLARGGI-VLLTTH 185
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-215 |
2.02e-15 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 73.60 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGF-EALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT-HLEQAKQHLGL 81
Cdd:cd03369 7 IEVENLSVRYAPDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQE---------FNFNPFE--TVEQIvmqqagyYGVSRTlakeraekyltqldlwekrKERARNLSGGMKRRLMIARAL 150
Cdd:cd03369 87 IPQDptlfsgtirSNLDPFDeySDEEI-------YGALRV-------------------SEGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019142000 151 MHEPQLLILDEPTAGVDIELRRSMWEFLKQiNSQGITIILTTHYLEEAeMLCRHIGIINRGELIE 215
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIRE-EFTNSTILTIAHRLRTI-IDYDKILVMDAGEVKE 203
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-214 |
2.21e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.20 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGgFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQH--LGL 81
Cdd:PRK10762 5 LQLKGIDKAFPG-VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEagIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQEFNFNPFETV-EQIVMQQAGYYGVSRTLAKE---RAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLL 157
Cdd:PRK10762 84 IHQELNLIPQLTIaENIFLGREFVNRFGRIDWKKmyaEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 158 ILDEPT-AGVDIElRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:PRK10762 164 IMDEPTdALTDTE-TESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-221 |
2.58e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.98 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTS--------GTVKVFGHNIDThlEQA 75
Cdd:NF040905 2 LEMRGITKTF-PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyegeilfdGEVCRFKDIRDS--EAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 76 -----KQHLGLVPQ----EfnfNPFETVEQivmqqaGYYGV-SRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLM 145
Cdd:NF040905 79 giviiHQELALIPYlsiaE---NIFLGNER------AKRGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2019142000 146 IARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKG 221
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRA 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
4-195 |
2.75e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.15 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYA---GGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNK---TSGTVKVFGHNI----DTHLE 73
Cdd:PRK09473 13 LDVKDLRVTFStpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 74 Q--AKQhLGLVPQE--FNFNPFETV-EQI--VMQQagYYGVSRTLAKERAEKYLTQLDLWEKRKeRAR----NLSGGMKR 142
Cdd:PRK09473 93 KlrAEQ-ISMIFQDpmTSLNPYMRVgEQLmeVLML--HKGMSKAEAFEESVRMLDAVKMPEARK-RMKmyphEFSGGMRQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2019142000 143 RLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYL 195
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDL 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-215 |
2.89e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.78 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLRKTYAGG---FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVN---KTSGTVKVF-GHNIDTHLE 73
Cdd:PRK11022 1 MALLNVDKLSVHFGDEsapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgRVMAEKLEFnGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 74 QAKQHL-----GLVPQE--FNFNP-----FETVEQIVMQQAGyygvSRTLAKERAEKYLTQL---DLWEKRKERARNLSG 138
Cdd:PRK11022 81 KERRNLvgaevAMIFQDpmTSLNPcytvgFQIMEAIKVHQGG----NKKTRRQRAIDLLNQVgipDPASRLDVYPHQLSG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 139 GMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-214 |
3.04e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.83 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQAK------ 76
Cdd:COG3845 257 VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-TGLSPRErrrlgv 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 77 -------QHLGLVPqefnfnPFETVEQIVMQQAGYYGVSRTL------AKERAEKYLTQLDLwekR----KERARNLSGG 139
Cdd:COG3845 336 ayipedrLGRGLVP------DMSVAENLILGRYRRPPFSRGGfldrkaIRAFAEELIEEFDV---RtpgpDTPARSLSGG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019142000 140 MKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-213 |
3.28e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.07 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 11 KTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDtHLEQAKQHLGLVPQEFNFNP 90
Cdd:PRK11000 11 KAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-DVPPAERGVGMVFQSYALYP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 91 FETVEQIVMQQAGYYGVSRTLAKERAEKY--LTQLDLWEKRKERArnLSGGMKRRLMIARALMHEPQLLILDEPTAGVDI 168
Cdd:PRK11000 89 HLSVAENMSFGLKLAGAKKEEINQRVNQVaeVLQLAHLLDRKPKA--LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2019142000 169 ELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGEL 213
Cdd:PRK11000 167 ALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-215 |
4.84e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.13 E-value: 4.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 19 ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNkTSGTVKVFGHNIdtHLEQAKQHLGL------VPQEFN--FNP 90
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPL--HNLNRRQLLPVrhriqvVFQDPNssLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 91 FETVEQIVMQ--QAGYYGVSRTLAKERAEKYLTQLDL-WEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVD 167
Cdd:PRK15134 378 RLNVLQIIEEglRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2019142000 168 IELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:PRK15134 458 KTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-215 |
6.97e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 74.84 E-value: 6.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSL--VNKTSGTV-------------------- 61
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 62 ---KVFGHNI-----------DTHLEQAKQHLGLVPQE-FNFNPFETVEQIVMQ---QAGYYGVSrtlAKERAEKYLTQL 123
Cdd:TIGR03269 80 epcPVCGGTLepeevdfwnlsDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEaleEIGYEGKE---AVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 124 DLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQ-INSQGITIILTTHYLEEAEMLC 202
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIEDLS 236
|
250
....*....|...
gi 2019142000 203 RHIGIINRGELIE 215
Cdd:TIGR03269 237 DKAIWLENGEIKE 249
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-214 |
8.59e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 73.76 E-value: 8.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 34 ALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHN-IDTH----LEQAKQHLGLVPQEFNFNPFETVEqivmqqaG--YYG 106
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEkgicLPPEKRRIGYVFQDARLFPHYKVR-------GnlRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 107 VSRTLAKERAekYLTQLDLWEKRKER-ARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFL----KQI 181
Cdd:PRK11144 101 MAKSMVAQFD--KIVALLGIEPLLDRyPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLerlaREI 178
|
170 180 190
....*....|....*....|....*....|...
gi 2019142000 182 NsqgITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:PRK11144 179 N---IPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-214 |
1.07e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.18 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVnKTSGTVKVFGHNIDT-HLEQAKQHLGLVPQEFNFNPFETVEQIV 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 99 mqQAGYYGVSRTLAKERAEKYLTQ-LDLWEKRKERARNLSGGMKRRLMIARALMH-------EPQLLILDEPTAGVDIEL 170
Cdd:COG4138 91 --ALHQPAGASSEAVEQLLAQLAEaLGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2019142000 171 RRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:COG4138 169 QAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-195 |
1.27e-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: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIdTHLEQA--KQHLG 80
Cdd:COG5265 357 EVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-RDVTQAslRAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQE---FN----FN-----PFETVEQIVmqqagyygvsrtLAKERA----------EKYLTQLDlwekrkERARNLSG 138
Cdd:COG5265 436 IVPQDtvlFNdtiaYNiaygrPDASEEEVE------------AAARAAqihdfieslpDGYDTRVG------ERGLKLSG 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 139 GMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQInSQGITIILTTHYL 195
Cdd:COG5265 498 GEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGRTTLVIAHRL 553
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-193 |
1.29e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.67 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 14 AGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT-HLEQAKQHLGL---VPQEFNfn 89
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYcaqTPTLFG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 90 pfETVE-------QIVMQQAGYYGVSRTLAK-ERAEKYLTQldlwekrkeRARNLSGGMKRRLMIARALMHEPQLLILDE 161
Cdd:PRK10247 95 --DTVYdnlifpwQIRNQQPDPAIFLDDLERfALPDTILTK---------NIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|...
gi 2019142000 162 PTAGVDIELRRSMWEFLKQINS-QGITIILTTH 193
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVReQNIAVLWVTH 196
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-205 |
2.46e-14 |
|
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: 70.21 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLrkTYAGGFEAL-KGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT------------ 70
Cdd:cd03231 1 LEADEL--TCERDGRALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFqrdsiargllyl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 71 -HLEQAKQHLGLVPQEFNFNPFETVEQIvmqqagyygvsrtlakeraEKYLTQLDLWEKRKERARNLSGGMKRRLMIARA 149
Cdd:cd03231 79 gHAPGIKTTLSVLENLRFWHADHSDEQV-------------------EEALARVGLNGFEDRPVAQLSAGQQRRVALARL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 150 LMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHY-LEEAEMLCRHI 205
Cdd:cd03231 140 LLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQdLGLSEAGAREL 196
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-195 |
2.49e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.05 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 19 ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI----DTHLEQAKQHLGLVPQE--FNFNPFE 92
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRAVRSDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 93 TVEQIVMQ--QAGYYGVSRTLAKERAEKYLTQLDLWEKRKER-ARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIE 169
Cdd:PRK15079 116 TIGEIIAEplRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180
....*....|....*....|....*..
gi 2019142000 170 LRRSMWEFLKQINSQ-GITIILTTHYL 195
Cdd:PRK15079 196 IQAQVVNLLQQLQREmGLSLIFIAHDL 222
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-215 |
2.66e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.27 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGgfEALKGVSLTVNKGDFYALLGPNGAGKSTT----IGIISSLVNKTSGTVKVFGHNIdtHLEQAK-QH 78
Cdd:PRK10418 5 IELRNIALQAAQ--PLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPV--APCALRgRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 79 LGLVPQefN----FNPFETVEQIVMQQAGYYGVSRTLAKERAEkyLTQLDLWEKR---KERARNLSGGMKRRLMIARALM 151
Cdd:PRK10418 81 IATIMQ--NprsaFNPLHTMHTHARETCLALGKPADDATLTAA--LEAVGLENAArvlKLYPFEMSGGMLQRMMIALALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019142000 152 HEPQLLILDEPTAGVDIELRRSMWEFLKQI-NSQGITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
4-171 |
3.59e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 71.53 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYA---GGF------EALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQ 74
Cdd:PRK11308 6 LQAIDLKKHYPvkrGLFkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 75 A----KQHLGLVPQefN----FNPFETVEQIVMQQagyYGVSRTL-AKERAEKYLTQLDLWEKRKERARN----LSGGMK 141
Cdd:PRK11308 86 AqkllRQKIQIVFQ--NpygsLNPRKKVGQILEEP---LLINTSLsAAERREKALAMMAKVGLRPEHYDRyphmFSGGQR 160
|
170 180 190
....*....|....*....|....*....|
gi 2019142000 142 RRLMIARALMHEPQLLILDEPTAGVDIELR 171
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-225 |
5.30e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.06 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQA-KQHLGL 81
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQefnfnpfetvEQIVMQQAGYYGVS--RTLAKERAEKYLTQLDLWEKRK-----------ERARNLSGGMKRRLMIAR 148
Cdd:PRK10790 420 VQQ----------DPVVLADTFLANVTlgRDISEEQVWQALETVQLAELARslpdglytplgEQGNNLSVGQKQLLALAR 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 149 ALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQgITIILTTHYLE---EAEmlcrHIGIINRGELIENTTMKGLLGK 225
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLStivEAD----TILVLHRGQAVEQGTHQQLLAA 564
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-193 |
5.76e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.07 E-value: 5.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 9 LRKTYAGGFEALKGVSLTvnkgdFY-----ALLGPNGAGKSTTIGIISSLVNKTSGTVKVF-GHNIdthleqakqhlGLV 82
Cdd:PRK11819 12 VSKVVPPKKQILKDISLS-----FFpgakiGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKV-----------GYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQEFNFNPFETVEQIVMQqagyyGVSRTLAK-----ERAEKY--------------------LTQLDLW--EKRKERA-- 133
Cdd:PRK11819 76 PQEPQLDPEKTVRENVEE-----GVAEVKAAldrfnEIYAAYaepdadfdalaaeqgelqeiIDAADAWdlDSQLEIAmd 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019142000 134 -----------RNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIE----LRRsmweFLKQInsQGiTIILTTH 193
Cdd:PRK11819 151 alrcppwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAEsvawLEQ----FLHDY--PG-TVVAVTH 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-193 |
7.37e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.82 E-value: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLVPQEFNFNPFETveqivM 99
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLT-----L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 100 QQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDielRRSMWEFLK 179
Cdd:PRK13540 92 RENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELSLLTIIT 168
|
170
....*....|....*..
gi 2019142000 180 QINS---QGITIILTTH 193
Cdd:PRK13540 169 KIQEhraKGGAVLLTSH 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-193 |
8.26e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.52 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfghniDTHLEQA--KQHlglvpqEFNFNPFETVE-- 95
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-----GTKLEVAyfDQH------RAELDPEKTVMdn 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 96 -----QIVMQQagyyGVSRtlakeRAEKYLtQLDLWEKRKERA--RNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDI 168
Cdd:PRK11147 404 laegkQEVMVN----GRPR-----HVLGYL-QDFLFHPKRAMTpvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
|
170 180
....*....|....*....|....*..
gi 2019142000 169 ElrrsMWEFLKQI--NSQGiTIILTTH 193
Cdd:PRK11147 474 E----TLELLEELldSYQG-TVLLVSH 495
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-220 |
9.94e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 9.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 17 FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFG--------HNIDTHLEQAKQ-------HLGL 81
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrQVIELSEQSAAQmrhvrgaDMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 82 VPQE--FNFNPFETV-EQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERAR---NLSGGMKRRLMIARALMHEPQ 155
Cdd:PRK10261 109 IFQEpmTSLNPVFTVgEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRyphQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2019142000 156 LLILDEPTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMK 220
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVE 254
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-222 |
1.49e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.53 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 16 GFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNID--THLEQAKQHLGLVPQEFNfnpfET 93
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfkSSKEALENGISMVHQELN----LV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 94 VEQIVMQQA--GYYG-----VSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGV 166
Cdd:PRK10982 86 LQRSVMDNMwlGRYPtkgmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2019142000 167 DIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGL 222
Cdd:PRK10982 166 TEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-193 |
2.79e-13 |
|
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: 67.27 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSlvNKTSGTVK----VFGHNIDTHLEQAkqhLGLVPQEFNFNPFETVE 95
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITgeilINGRPLDKNFQRS---TGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 96 QIVMQQAgyygvsrtlakeraekYLtqldlwekrkeraRNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMW 175
Cdd:cd03232 98 EALRFSA----------------LL-------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148
|
170
....*....|....*...
gi 2019142000 176 EFLKQINSQGITIILTTH 193
Cdd:cd03232 149 RFLKKLADSGQAILCTIH 166
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-212 |
3.73e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.74 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 19 ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGLVPQE-FNF-------- 88
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtKLQLDSWRSRLAVVSQTpFLFsdtvanni 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 89 ---NPFETVEQIvMQQAGYYGVSRTLAKeRAEKYLTQLDlwekrkERARNLSGGMKRRLMIARALMHEPQLLILDEPTAG 165
Cdd:PRK10789 410 algRPDATQQEI-EHVARLASVHDDILR-LPQGYDTEVG------ERGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2019142000 166 VDIELRRSMWEFLKQInSQGITIILTTHYL----EEAEMLC-RHIGIINRGE 212
Cdd:PRK10789 482 VDGRTEHQILHNLRQW-GEGRTVIISAHRLsaltEASEILVmQHGHIAQRGN 532
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-275 |
4.95e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.96 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 22 GVSLTVNKGDFYALLGPNGAGKSTTIGII-----SSLVNKTSGTVKVFGHNIDTHLEQAKQHL-----GLVPQE--FNFN 89
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSIlrllpSPPVVYPSGDIRFHGESLLHASEQTLRGVrgnkiAMIFQEpmVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 90 PFETVEQivmQQAGYYGVSRTLAKE--RAEkYLTQLDLWEKRKERAR------NLSGGMKRRLMIARALMHEPQLLILDE 161
Cdd:PRK15134 107 PLHTLEK---QLYEVLSLHRGMRREaaRGE-ILNCLDRVGIRQAAKRltdyphQLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 162 PTAGVDIELRRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLGK-LHVET-FILDIDNE 238
Cdd:PRK15134 183 PTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSApTHPYTqKLLNSEPS 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2019142000 239 -------EKLQPLTDVVSQRVvdgSLEIE---LEKTQGMNHVFTQLS 275
Cdd:PRK15134 263 gdpvplpEPASPLLDVEQLQV---AFPIRkgiLKRTVDHNVVVKNIS 306
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-193 |
7.22e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.75 E-value: 7.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNiDTHLEQAKQHLGLVPQEFNFNPFETVEQIVM 99
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQILKRTGFVTQDDILYPHLTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 100 QQAgYYGVSRTLAKER----AEKYLTQLDLWEKRK-----ERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIEL 170
Cdd:PLN03211 163 FCS-LLRLPKSLTKQEkilvAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180
....*....|....*....|...
gi 2019142000 171 RRSMWEFLKQINSQGITIILTTH 193
Cdd:PLN03211 242 AYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-193 |
2.06e-12 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 64.10 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNidthleqakqHLGLVPQEfnfnPfetveqivm 99
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----------DLLFLPQR----P--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 100 qqagyygvsrtlakeraekYLTQLDL-------WEkrkeraRNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRR 172
Cdd:cd03223 74 -------------------YLPLGTLreqliypWD------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|.
gi 2019142000 173 SMWEFLKQinsQGITIILTTH 193
Cdd:cd03223 129 RLYQLLKE---LGITVISVGH 146
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-227 |
2.08e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.97 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTY---AGGF-----EALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNI---DTHL 72
Cdd:PRK15112 5 LEVRNLSKTFryrTGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 73 EQAKQHLGLVPQEFNFNPFETVEQIVmqQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERA----RNLSGGMKRRLMIAR 148
Cdd:PRK15112 85 RSQRIRMIFQDPSTSLNPRQRISQIL--DFPLRLNTDLEPEQREKQIIETLRQVGLLPDHAsyypHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 149 ALMHEPQLLILDEPTAGVDIELRRSMWEFLKQIN-SQGITIILTTHYLEEAEMLCRHIGIINRGELIE-NTTMKGLLGKL 226
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVErGSTADVLASPL 242
|
.
gi 2019142000 227 H 227
Cdd:PRK15112 243 H 243
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-193 |
5.18e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.98 E-value: 5.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDfyALL--GPNGAGKSTTIGIISSLVNKTSGTVkvfghnidtHLEQAKQHLgLVPQEfnfnPF------ 91
Cdd:COG4178 379 LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRI---------ARPAGARVL-FLPQR----PYlplgtl 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 92 -------ETVEQIVMQQagyygVSRTLAKERAEKYLTQLDL---WEKRkerarnLSGGMKRRLMIARALMHEPQLLILDE 161
Cdd:COG4178 443 reallypATAEAFSDAE-----LREALEAVGLGHLAERLDEeadWDQV------LSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|..
gi 2019142000 162 PTAGVDIELRRSMWEFLKQiNSQGITIILTTH 193
Cdd:COG4178 512 ATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-195 |
8.43e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.80 E-value: 8.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 23 VSLTVNKGDFYALLGPNGAGKSTTIGIISSLVnKTSGTVKVFGHNIDT--HLEQAKQHLGLVPQE---FNFNPFETVEqi 97
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsAAELARHRAYLSQQQtppFAMPVFQYLT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 98 VMQQAGyygvSRTLAKERAEKYLTQ-LDLWEKRKERARNLSGGMKRR-------LMIARALMHEPQLLILDEPTAGVDIE 169
Cdd:PRK03695 92 LHQPDK----TRTEAVASALNEVAEaLGLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLDVA 167
|
170 180
....*....|....*....|....*.
gi 2019142000 170 LRRSMWEFLKQINSQGITIILTTHYL 195
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSSHDL 193
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-190 |
9.13e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQA------------KQHLGLVpqeFN 87
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyisedRKRDGLV---LG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 88 FNPFETVEQIVMQQAGYYGVSRTLAKER--AEKYLTQLDL-WEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTA 164
Cdd:PRK10762 345 MSVKENMSLTALRYFSRAGGSLKHADEQqaVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180
....*....|....*....|....*.
gi 2019142000 165 GVDIELRRSMWEFLKQINSQGITIIL 190
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAEGLSIIL 450
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-215 |
9.90e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.26 E-value: 9.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 19 ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT----HLEQAKQHLGLVPQE--FNFNPFE 92
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQDpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 93 TVEQIVMQQAGYYGVSR-TLAKERAEKYLTQLDLWEKRKER-ARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIEL 170
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2019142000 171 RRSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:PRK10261 499 RGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-198 |
1.10e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.04 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIIS-----------SLVNKTSGTvkvfGHNIdthlEQAKQHLGLVP----Q 84
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysndlTLFGRRRGS----GETI----WDIKKHIGYVSsslhL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 85 EFNFNpfETVEQIVMqqAGYY---GVSRTLA---KERAEKYLTQLDLwEKRKERA--RNLSGGMKRRLMIARALMHEPQL 156
Cdd:PRK10938 348 DYRVS--TSVRNVIL--SGFFdsiGIYQAVSdrqQKLAQQWLDILGI-DKRTADApfHSLSWGQQRLALIVRALVKHPTL 422
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2019142000 157 LILDEPTAGVDIELRRSMWEFLKQINSQGITIIL-TTHYLEEA 198
Cdd:PRK10938 423 LILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHHAEDA 465
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-227 |
1.29e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.16 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDqlrkTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTtigIISSLVNKTSGTVKV-----FGHNID----THLEQ 74
Cdd:COG4170 11 IEID----TPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSL---IAKAICGITKDNWHVtadrfRWNGIDllklSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 75 AK---QHLGLVPQEFN--FNPFETVEQIVMQqagyygvsrTLAKERAEKYLTQLDLWekRKERARNL------------- 136
Cdd:COG4170 84 RKiigREIAMIFQEPSscLDPSAKIGDQLIE---------AIPSWTFKGKWWQRFKW--RKKRAIELlhrvgikdhkdim 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 137 -------SGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQIN-SQGITIILTTHYLEEAEMLCRHIGII 208
Cdd:COG4170 153 nsyphelTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNqLQGTSILLISHDLESISQWADTITVL 232
|
250
....*....|....*....
gi 2019142000 209 NRGELIENTTMKGLLGKLH 227
Cdd:COG4170 233 YCGQTVESGPTEQILKSPH 251
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-222 |
1.48e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 63.63 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 23 VSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDT----HLEQAKQHLGLVPQE----FNFNPFETV 94
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsRLYTVRKRMSMLFQSgalfTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 95 EQIVMQQAGyygVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSM 174
Cdd:PRK11831 106 AYPLREHTQ---LPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2019142000 175 WEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGL 222
Cdd:PRK11831 183 VKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-215 |
1.58e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.42 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 21 KGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNID--THLEQAKQHLGLVPQ---EFNFNP-FETV 94
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprSPLDAVKKGMAYITEsrrDNGFFPnFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 95 EQIVMQQA---GYYGVSRTLAKERAEKYLTQldlwEKRKERA----------RNLSGGMKRRLMIARALMHEPQLLILDE 161
Cdd:PRK09700 360 QNMAISRSlkdGGYKGAMGLFHEVDEQRTAE----NQRELLAlkchsvnqniTELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2019142000 162 PTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIE 215
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-287 |
2.11e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 18 EALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVF-GHNI-DTHLEQAKQHLGLVPQE---------- 85
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLkDINLKWWRSKIGVVSQDpllfsnsikn 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 86 ------FNFNPFETVEQIVMQ-----QAGYYGVSRTLAKERAE-----KYLTQLDLWEKRKE------------------ 131
Cdd:PTZ00265 479 nikyslYSLKDLEALSNYYNEdgndsQENKNKRNSCRAKCAGDlndmsNTTDSNELIEMRKNyqtikdsevvdvskkvli 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 132 -----------------RARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDielRRSMWEFLKQINS-----QGITII 189
Cdd:PTZ00265 559 hdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD---NKSEYLVQKTINNlkgneNRITII 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 190 LtTHYLEEAEMLCRHIGIINRgeliENTTmkgllgklhveTFILDIDNEEKLQPLTDVVSQRVVDGSLEIELEKTQGMNH 269
Cdd:PTZ00265 636 I-AHRLSTIRYANTIFVLSNR----ERGS-----------TVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINN 699
|
330
....*....|....*...
gi 2019142000 270 VFTQLSEQGVNVMSMRNK 287
Cdd:PTZ00265 700 AGSYIIEQGTHDALMKNK 717
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-171 |
3.18e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFealkgvSLTVNKGDFYA-----LLGPNGAGKSTTIGIISSLVNKTSGTVkvfghniDTHLEQA-Kq 77
Cdd:PRK13409 341 VEYPDLTKKL-GDF------SLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEV-------DPELKISyK- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 78 hlglvPQEFNFNPFETVEQIVMQQAGYYGVS-------RTLAKERaekyltqldLWEKRkerARNLSGGMKRRLMIARAL 150
Cdd:PRK13409 406 -----PQYIKPDYDGTVEDLLRSITDDLGSSyykseiiKPLQLER---------LLDKN---VKDLSGGELQRVAIAACL 468
|
170 180
....*....|....*....|.
gi 2019142000 151 MHEPQLLILDEPTAGVDIELR 171
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDVEQR 489
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-223 |
4.53e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.78 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 11 KTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNkTSGTVKVFGHNIDT-HLEQAKQHLGLVPQEF--- 86
Cdd:TIGR01271 1226 KYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSvTLQTWRKAFGVIPQKVfif 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 87 ------NFNPFE--TVEQI--VMQQAGYygvsrtlaKERAEKYLTQLDLweKRKERARNLSGGMKRRLMIARALMHEPQL 156
Cdd:TIGR01271 1305 sgtfrkNLDPYEqwSDEEIwkVAEEVGL--------KSVIEQFPDKLDF--VLVDGGYVLSNGHKQLMCLARSILSKAKI 1374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 157 LILDEPTAGVDIELRRSMWEFLKQINSQgITIILTTHYLeEAEMLCRHIGIINRGELIENTTMKGLL 223
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQIIRKTLKQSFSN-CTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
17-193 |
7.16e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.59 E-value: 7.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 17 FEALkgvSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQ------HLGLVPQEFNfnP 90
Cdd:PRK13538 17 FSGL---SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQdllylgHQPGIKTELT--A 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 91 FETVeQIVMQQAGYYGvsrtlaKERAEKYLTQLDLweKRKER--ARNLSGGMKRRLMIARALMHEPQLLILDEP-----T 163
Cdd:PRK13538 92 LENL-RFYQRLHGPGD------DEALWEALAQVGL--AGFEDvpVRQLSAGQQRRVALARLWLTRAPLWILDEPftaidK 162
|
170 180 190
....*....|....*....|....*....|
gi 2019142000 164 AGVDiELRRSMWEFLkqinSQGITIILTTH 193
Cdd:PRK13538 163 QGVA-RLEALLAQHA----EQGGMVILTTH 187
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-214 |
8.12e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.34 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQA-KQHLGLVPQEFNFNPFETVEQIV 98
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfARKVAYLPQQLPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 99 M-------QQAGYYGVSRtlaKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELR 171
Cdd:PRK10575 107 AigrypwhGALGRFGAAD---REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2019142000 172 RSMWEFLKQINSQ-GITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:PRK10575 184 VDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-193 |
2.31e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 25 LTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKqhlglvPQEFNFNPFETVEQIVMQQAG- 103
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDP------PRNVEGTVYDFVAEGIEEQAEy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 104 ---YYGVSRTLAKERAEKYLTQL----------DLW--EKR------------KERARNLSGGMKRRLMIARALMHEPQL 156
Cdd:PRK11147 98 lkrYHDISHLVETDPSEKNLNELaklqeqldhhNLWqlENRinevlaqlgldpDAALSSLSGGWLRKAALGRALVSNPDV 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 2019142000 157 LILDEPTAGVDIELRRSMWEFLKqiNSQGiTIILTTH 193
Cdd:PRK11147 178 LLLDEPTNHLDIETIEWLEGFLK--TFQG-SIIFISH 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-213 |
2.33e-10 |
|
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: 60.99 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 23 VSLTVNKGDFYALLGPNGAGKSTTI-GIISSLVNKTSGTVKVFGHNIDTH--LEQAKQHLGLVPQEfnfnpfETVEQIVM 99
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVqALFGAYPGKFEGNVFINGKPVDIRnpAQAIRAGIAMVPED------RKRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 100 QQAgyYGVSRTLAKERAEKYLTQLD----LWEKRKERAR-------------NLSGGMKRRLMIARALMHEPQLLILDEP 162
Cdd:TIGR02633 353 ILG--VGKNITLSVLKSFCFKMRIDaaaeLQIIGSAIQRlkvktaspflpigRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 163 TAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGEL 213
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-227 |
2.70e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.20 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQLR---KTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSlVNKTSGTV---------------- 61
Cdd:PRK15093 1 MPLLDIRNLTiefKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVtadrmrfddidllrls 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 62 -----KVFGHNIDTHLEQakqhlglvPQEFnFNPFETVEQIVMQQ------AGYYGVSRTLAKERAEKYLTQLDLwEKRK 130
Cdd:PRK15093 80 prerrKLVGHNVSMIFQE--------PQSC-LDPSERVGRQLMQNipgwtyKGRWWQRFGWRKRRAIELLHRVGI-KDHK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 131 ERARN----LSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQIN-SQGITIILTTHYLEEAEMLCRHI 205
Cdd:PRK15093 150 DAMRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqNNNTTILLISHDLQMLSQWADKI 229
|
250 260
....*....|....*....|..
gi 2019142000 206 GIINRGELIENTTMKGLLGKLH 227
Cdd:PRK15093 230 NVLYCGQTVETAPSKELVTTPH 251
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-169 |
2.82e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.68 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 3 ALEIDQLRKTYAGGfEALKGVSLTVNKGDFYALLGPNGAGKSTtigIISSLVNK---TSGTVKvfghnidtHLEQAKqhL 79
Cdd:PRK15064 319 ALEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTT---LLRTLVGElepDSGTVK--------WSENAN--I 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 80 GLVPQ--EFNFNPFETV-------------EQIVMqqaGYYGvsRTLakeraekyLTQLDLwekrKERARNLSGGMKRRL 144
Cdd:PRK15064 385 GYYAQdhAYDFENDLTLfdwmsqwrqegddEQAVR---GTLG--RLL--------FSQDDI----KKSVKVLSGGEKGRM 447
|
170 180
....*....|....*....|....*
gi 2019142000 145 MIARALMHEPQLLILDEPTAGVDIE 169
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDME 472
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-215 |
3.03e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.76 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLglvp 83
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 qeFN--FNPFETVEQiVMQQAGYygvsrTLAKERAEKYLTQLDLWEKRKE---RARN--LSGGMKRRLMIARALMHEPQL 156
Cdd:PRK10522 399 --FSavFTDFHLFDQ-LLGPEGK-----PANPALVEKWLERLKMAHKLELedgRISNlkLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 157 LILDEPTAGVDIELRRSMW-EFLKQINSQGITIILTTH---YLEEAEMLCRhigiINRGELIE 215
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYqVLLPLLQEMGKTIFAISHddhYFIHADRLLE----MRNGQLSE 529
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-225 |
5.05e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH-LEQAKQHLGLVPQ---------EFNFN 89
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFgLTDLRRVLSIIPQspvlfsgtvRFNID 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 90 PFETVEQIVMQQAgyygVSRTLAKERAEKYLTQLDlwEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIE 169
Cdd:PLN03232 1332 PFSEHNDADLWEA----LERAHIKDVIDRNPFGLD--AEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 170 ----LRRSMWEFLKQinsqgITIILTTHYLEEAeMLCRHIGIINRGELIENTTMKGLLGK 225
Cdd:PLN03232 1406 tdslIQRTIREEFKS-----CTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
24-193 |
6.25e-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: 59.76 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 24 SLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfghnidthleQAKQHLGLVPQEfnfnPFETV----EQIVM 99
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK----------PAKGKLFYVPQR----PYMTLgtlrDQIIY 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 100 QQAGYYGVSRTLAKERAEKYLTQLDL---------WEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIEL 170
Cdd:TIGR00954 538 PDSSEDMKRRGLSDKDLEQILDNVQLthilereggWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
|
170 180
....*....|....*....|...
gi 2019142000 171 RRSMWEFLKQInsqGITIILTTH 193
Cdd:TIGR00954 618 EGYMYRLCREF---GITLFSVSH 637
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-193 |
9.63e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.03 E-value: 9.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFealkgvSLTVNKGDFY-----ALLGPNGAGKSTTIGIISSLVNKTSGtvkvfghNIDTHLEQA-Kq 77
Cdd:COG1245 342 VEYPDLTKSY-GGF------SLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEG-------EVDEDLKISyK- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 78 hlglvPQEFNFNPFETVEQIVMQQAG-YYGVSrtLAKERAEKYLtQLD-LWEKRkerARNLSGGMKRRLMIARALMHEPQ 155
Cdd:COG1245 407 -----PQYISPDYDGTVEEFLRSANTdDFGSS--YYKTEIIKPL-GLEkLLDKN---VKDLSGGELQRVAIAACLSRDAD 475
|
170 180 190
....*....|....*....|....*....|....*....
gi 2019142000 156 LLILDEPTAGVDIELRRSMWEFLKQI-NSQGITIILTTH 193
Cdd:COG1245 476 LYLLDEPSAHLDVEQRLAVAKAIRRFaENRGKTAMVVDH 514
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-193 |
1.17e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.28 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 17 FEALKGVSLTVNKGDFYALLGPNGAGKST----TIGIISSLvnKTSGTVKVFGHNID---THLEQakqhlglVPQEFNFN 89
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTllrlLAGALKGT--PVAGCVDVPDNQFGreaSLIDA-------IGRKGDFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 90 pfETVEqiVMQQAGYygvsrtlakerAEKYLtqldlWekrKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIE 169
Cdd:COG2401 114 --DAVE--LLNAVGL-----------SDAVL-----W---LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*
gi 2019142000 170 L-RRSMWEFLKQINSQGITIILTTH 193
Cdd:COG2401 171 TaKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
135-213 |
1.56e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.40 E-value: 1.56e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 135 NLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGEL 213
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
15-223 |
1.65e-09 |
|
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: 57.56 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 15 GGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNkTSGTVKVFGHNIDT-HLEQAKQHLGLVPQEF------- 86
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvPLQKWRKAFGVIPQKVfifsgtf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 87 --NFNPFE--TVEQI--VMQQAGYygvsrtlaKERAEKYLTQLDLweKRKERARNLSGGMKRRLMIARALMHEPQLLILD 160
Cdd:cd03289 94 rkNLDPYGkwSDEEIwkVAEEVGL--------KSVIEQFPGQLDF--VLVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 161 EPTAGVDIELRRSMWEFLKQINSqGITIILTTHYLeEAEMLCRHIGIINRGELIENTTMKGLL 223
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLKQAFA-DCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLL 224
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-193 |
2.29e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.40 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 27 VNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNiDTHLEQAK-----QHLGLVPQEFNfnpfeTVEQIVMQQ 101
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-ATRGDRSRfmaylGHLPGLKADLS-----TLENLHFLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 102 A--GYYgvsrtlAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIE---LRRSMwe 176
Cdd:PRK13543 108 GlhGRR------AKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEgitLVNRM-- 179
|
170
....*....|....*..
gi 2019142000 177 FLKQINSQGITiILTTH 193
Cdd:PRK13543 180 ISAHLRGGGAA-LVTTH 195
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
14-167 |
4.00e-09 |
|
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: 55.35 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 14 AGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVN---KTSGTVKVFGHNIDTHLEQAKQHLGLVPQEFNFNP 90
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 91 FETVEQIVmqqagyygvsRTLAKERAEKYLtqldlwekrkeraRNLSGGMKRRLMIARALMHEPQLLILDEPTAGVD 167
Cdd:cd03233 97 TLTVRETL----------DFALRCKGNEFV-------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-194 |
4.08e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.95 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYAGGfEALKGVSLTVNKGDFYALLGPNGAGKSTtigIISSLVNK-----TSGTVKVFGHNIdTHLE----- 73
Cdd:PRK09580 2 LSIKDLHVSVEDK-AILRGLNLEVRPGEVHAIMGPNGSGKST---LSATLAGRedyevTGGTVEFKGKDL-LELSpedra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 74 -----QAKQHLGLVPQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLWEKRKERARNL--SGGMKRRLMI 146
Cdd:PRK09580 77 gegifMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2019142000 147 ARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHY 194
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHY 204
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-169 |
5.58e-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: 57.26 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKST-TIGIISsLVNKTSGTVKVFGHNI-DTHLEQAKQHLGLVPQE---------FNF 88
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSlTLGLFR-INESAEGEIIIDGLNIaKIGLHDLRFKITIIPQDpvlfsgslrMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 89 NPFETV--EQIVMqqagyygvsrTLAKERAEKYLTQL--DLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTA 164
Cdd:TIGR00957 1381 DPFSQYsdEEVWW----------ALELAHLKTFVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
....*
gi 2019142000 165 GVDIE 169
Cdd:TIGR00957 1451 AVDLE 1455
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
8-171 |
1.01e-08 |
|
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: 54.72 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 8 QLRKTYaGGFealkgvSLTVNKGDFY-----ALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHleqakqhlglv 82
Cdd:cd03237 5 TMKKTL-GEF------TLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 PQEFNFNPFETVEQIVMQQAGYYGVSRTLAKERAeKYLTQLDLWEKRkerARNLSGGMKRRLMIARALMHEPQLLILDEP 162
Cdd:cd03237 67 PQYIKADYEGTVRDLLSSITKDFYTHPYFKTEIA-KPLQIEQILDRE---VPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
....*....
gi 2019142000 163 TAGVDIELR 171
Cdd:cd03237 143 SAYLDVEQR 151
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-193 |
1.22e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKST---------TIGIIsslvnkTSGTVKVFGHNIDTHLEQAkqhLGLVPQEFNFNP 90
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTllnvlaervTTGVI------TGGDRLVNGRPLDSSFQRS---IGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 91 FETVEQiVMQQAGYYGVSRTLAKERAEKYLTQ-LDLWEKRK-------ERARNLSGGMKRRLMIARALMHEPQLLI-LDE 161
Cdd:TIGR00956 850 TSTVRE-SLRFSAYLRQPKSVSKSEKMEYVEEvIKLLEMESyadavvgVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDE 928
|
170 180 190
....*....|....*....|....*....|..
gi 2019142000 162 PTAGVDIELRRSMWEFLKQINSQGITIILTTH 193
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-242 |
1.68e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.44 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 17 FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGH----NIDTHLEqaKQHLGLVPQEFnfnpfe 92
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvsviAISAGLS--GQLTGIENIEF------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 93 tvEQIVMqqagyyGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRR 172
Cdd:PRK13546 109 --KMLCM------GFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 173 SMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELIENTTMKGLLGklHVETFILDIDNEEKLQ 242
Cdd:PRK13546 181 KCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLP--KYEAFLNDFKKKSKAE 248
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-178 |
1.90e-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: 55.33 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfGHNID-THLEQAKQHLglv 82
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKlAYVDQSRDAL--- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 83 pqefnfNPFETV-EQI-----VMQQAGYYGVSRTlakeraekYLTQLDL-WEKRKERARNLSGGMKRRLMIARALMHEPQ 155
Cdd:TIGR03719 398 ------DPNKTVwEEIsggldIIKLGKREIPSRA--------YVGRFNFkGSDQQKKVGQLSGGERNRVHLAKTLKSGGN 463
|
170 180
....*....|....*....|...
gi 2019142000 156 LLILDEPTAGVDIELRRSMWEFL 178
Cdd:TIGR03719 464 VLLLDEPTNDLDVETLRALEEAL 486
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-168 |
1.98e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH-LEQAKQHLGLVPQ---------EFNFN 89
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFgLMDLRKVLGIIPQapvlfsgtvRFNLD 1334
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019142000 90 PFETVEQIVMQQAgyygVSRTLAKERAEKYLTQLDlwEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDI 168
Cdd:PLN03130 1335 PFNEHNDADLWES----LERAHLKDVIRRNSLGLD--AEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-213 |
4.21e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 23 VSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVkvfghNIDTHLEQAKqhlgLVPQEFNFNPFETVEQIVMQQA 102
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV-----SLDPNERLGK----LRQDQFAFEEFTVLDTVIMGHT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 103 GYYGVsrtlAKER----------AEKYLTQLDLWEKRKE--------RA------------------RNLSGGMKRRLMI 146
Cdd:PRK15064 91 ELWEV----KQERdriyalpemsEEDGMKVADLEVKFAEmdgytaeaRAgelllgvgipeeqhyglmSEVAPGWKLRVLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 147 ARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLeeaEMLCRHIGIINRGEL 213
Cdd:PRK15064 167 AQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFL---NSVCTHMADLDYGEL 230
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-178 |
6.10e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKV-----FGHNIDTHLEQAK------QHLG-LVPQEfn 87
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLakgikLGYFAQHQLEFLRadesplQHLArLAPQE-- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 88 fnpfetVEQIVMQQAGYYGVSRtlakeraekyltqldlwEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVD 167
Cdd:PRK10636 406 ------LEQKLRDYLGGFGFQG-----------------DKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
170
....*....|.
gi 2019142000 168 IELRRSMWEFL 178
Cdd:PRK10636 463 LDMRQALTEAL 473
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-225 |
6.51e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.80 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 2 YALEIDQLRKTYAGGFE-ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfghnidthleqaKQHLG 80
Cdd:TIGR00957 635 NSITVHNATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM------------KGSVA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 81 LVPQEFNFNPFETVEQIV----MQQAGYYGVSRTLAKERAEKYLTQLDLWEKrKERARNLSGGMKRRLMIARALMHEPQL 156
Cdd:TIGR00957 703 YVPQQAWIQNDSLRENILfgkaLNEKYYQQVLEACALLPDLEILPSGDRTEI-GEKGVNLSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2019142000 157 LILDEPTAGVDIELRRSMWEflKQINSQGI----TIILTTH---YLEEAEMlcrhIGIINRGELIENTTMKGLLGK 225
Cdd:TIGR00957 782 YLFDDPLSAVDAHVGKHIFE--HVIGPEGVlknkTRILVTHgisYLPQVDV----IIVMSGGKISEMGSYQELLQR 851
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-169 |
8.18e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 13 YAGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTV--------KVFG-HNIDthleqaKQHLGLVP 83
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmAVFSqHHVD------GLDLSSNP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 QEFNFNPFETV-EQIVMQQAGYYGVSRTLAKERAekyltqldlwekrkeraRNLSGGMKRRLMIARALMHEPQLLILDEP 162
Cdd:PLN03073 592 LLYMMRCFPGVpEQKLRAHLGSFGVTGNLALQPM-----------------YTLSGGQKSRVAFAKITFKKPHILLLDEP 654
|
....*..
gi 2019142000 163 TAGVDIE 169
Cdd:PLN03073 655 SNHLDLD 661
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
51-167 |
9.39e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 9.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 51 SSLVNKTSGTVKVFGHNI-DTHLEQAKQHLGLVPQE---FNFNPFE---------TVEQIvmQQAGYYGVSRTLAKERAE 117
Cdd:PTZ00265 1269 DSTVFKNSGKILLDGVDIcDYNLKDLRNLFSIVSQEpmlFNMSIYEnikfgkedaTREDV--KRACKFAAIDEFIESLPN 1346
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2019142000 118 KYLTQLDLWEKrkerarNLSGGMKRRLMIARALMHEPQLLILDEPTAGVD 167
Cdd:PTZ00265 1347 KYDTNVGPYGK------SLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
131-196 |
1.57e-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: 51.18 E-value: 1.57e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 131 ERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWE--FLKQINSQGITIILTTHYLE 196
Cdd:cd03290 136 ERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-213 |
1.86e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 23 VSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGH--NIDTHLEQAKQHLGLVPQEFNFN---PFETV-EQ 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGIMLCPEDRKAEgiiPVHSVaDN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 97 IVMQ------QAGYYgVSRTLAKERAEKYLTQLDLweK---RKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVD 167
Cdd:PRK11288 352 INISarrhhlRAGCL-INNRWEAENADRFIRSLNI--KtpsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2019142000 168 IELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGEL 213
Cdd:PRK11288 429 VGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-202 |
2.02e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.20 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 1 MYALEIDQL----RKTYAGGFE-ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGhnidthleqa 75
Cdd:PRK13545 16 MYNKPFDKLkdlfFRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 76 KQHLGLVPQEFNfNPFETVEQIVMQQAgYYGVSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQ 155
Cdd:PRK13545 86 SAALIAISSGLN-GQLTGIENIELKGL-MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2019142000 156 LLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLC 202
Cdd:PRK13545 164 ILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFC 210
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-207 |
2.11e-07 |
|
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: 49.68 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 29 KGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFghNIDTHLEQAKQHLGLVPqefnfnpfetveqivmqqagyygvs 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI--DGEDILEEVLDQLLLII------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 109 rtlakeraekyltqldlwekRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWE------FLKQIN 182
Cdd:smart00382 54 --------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLLLLKS 113
|
170 180 190
....*....|....*....|....*....|.
gi 2019142000 183 SQGITIILTTHYLEE------AEMLCRHIGI 207
Cdd:smart00382 114 EKNLTVILTTNDEKDlgpallRRRFDRRIVL 144
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
129-193 |
2.16e-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: 51.24 E-value: 2.16e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 129 RKERARNLSGGMKR---RLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTH 193
Cdd:pfam13304 230 GELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-208 |
3.68e-07 |
|
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: 50.44 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 30 GDFYALLGPNGAGKSTTIGIISSLVNKTSGT----------VKVF-GHNIDTHLEQAK----------QHLGLVPQEFNF 88
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeiLDEFrGSELQNYFTKLLegdvkvivkpQYVDLIPKAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 89 NpfetVEQIVmqqagyygvSRTLAKERAEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDI 168
Cdd:cd03236 106 K----VGELL---------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2019142000 169 ELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGII 208
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
16-193 |
4.66e-07 |
|
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: 50.77 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 16 GFEALKGVSLTVNKgDFYALLGPNGAGKSTTIGIISsLVNKTSGTVKV---------------------FG--------- 65
Cdd:COG3593 10 NFRSIKDLSIELSD-DLTVLVGENNSGKSSILEALR-LLLGPSSSRKFdeedfylgddpdlpeieieltFGsllsrllrl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 66 -------HNIDTHLEQAKQHLGLVPQEFNfnpfETVEQIVMQQAGYYGVSRTLAKERAEKYLTQLDLW--EKRKERARNL 136
Cdd:COG3593 88 llkeedkEELEEALEELNEELKEALKALN----ELLSEYLKELLDGLDLELELSLDELEDLLKSLSLRieDGKELPLDRL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019142000 137 SGGMKRRLMIA--RALMH-----EPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTH 193
Cdd:COG3593 164 GSGFQRLILLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
15-207 |
1.50e-06 |
|
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: 47.35 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 15 GGFE-ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNktsgtvkvfghnidthLEQAKQHLGLVPQEFNFNPFET 93
Cdd:cd03227 5 GRFPsYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALG----------------GAQSATRRRSGVKAGCIVAAVS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 94 VEQIVMqqagyygvsrtlakeraekyLTQLdlwekrkerarnlSGGMKRRLMIARALMH----EPQLLILDEPTAGVDIE 169
Cdd:cd03227 69 AELIFT--------------------RLQL-------------SGGEKELSALALILALaslkPRPLYILDEIDRGLDPR 115
|
170 180 190
....*....|....*....|....*....|....*...
gi 2019142000 170 LRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGI 207
Cdd:cd03227 116 DGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-168 |
2.44e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 15 GGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISslVNKTSGTVK----------VFGHNI-------DTHLEQAK- 76
Cdd:PLN03073 188 GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDGIPKncqilhveqeVVGDDTtalqcvlNTDIERTQl 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 77 --QHLGLVPQEFNFNPFETVEQIVMQQAGyyGVSRTLAKERAE---KYLTQLDLW-----------------EKRKERAR 134
Cdd:PLN03073 266 leEEAQLVAQQRELEFETETGKGKGANKD--GVDKDAVSQRLEeiyKRLELIDAYtaearaasilaglsftpEMQVKATK 343
|
170 180 190
....*....|....*....|....*....|....
gi 2019142000 135 NLSGGMKRRLMIARALMHEPQLLILDEPTAGVDI 168
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-171 |
2.71e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 26 TVNKGDFYALLGPNGAGKSTTIGIIS-----SLVNKTSGT-----VKVF-GHNIDTHLEQ-AKQHLGLV--PQEfnfnpf 91
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSgelipNLGDYEEEPswdevLKRFrGTELQNYFKKlYNGEIKVVhkPQY------ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 92 etVEQIVMQQAGyyGVSRTLAK--ER--AEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVD 167
Cdd:PRK13409 169 --VDLIPKVFKG--KVRELLKKvdERgkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
....
gi 2019142000 168 IELR 171
Cdd:PRK13409 245 IRQR 248
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-223 |
3.12e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 19 ALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTH--LEQAKQHLGLVPQE----------- 85
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHnaNEAINHGFALVTEErrstgiyayld 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 86 FNFNpfetveQIVMQQAGYYGVSRTLAKERAEKYlTQldlWEKRKERAR---------NLSGGMKRRLMIARALMHEPQL 156
Cdd:PRK10982 343 IGFN------SLISNIRNYKNKVGLLDNSRMKSD-TQ---WVIDSMRVKtpghrtqigSLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019142000 157 LILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHylEEAEMLcrhiGIINRGELIENTTMKGLL 223
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISS--EMPELL----GITDRILVMSNGLVAGIV 473
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-195 |
7.10e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.47 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 29 KGDFYALLGPNGAGKSTTIGIIS-----------------SLVNKTSGTVkvfghnIDTHLEQ-AKQHLGLV--PQEfnf 88
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSgelkpnlgdydeepswdEVLKRFRGTE------LQDYFKKlANGEIKVAhkPQY--- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 89 npfetVEQIVMQqagYYGVSRTLAK---ER--AEKYLTQLDLWEKRKERARNLSGGMKRRLMIARALMHEPQLLILDEPT 163
Cdd:COG1245 169 -----VDLIPKV---FKGTVRELLEkvdERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|..
gi 2019142000 164 AGVDIELRRSMWEFLKQINSQGITIILTTHYL 195
Cdd:COG1245 241 SYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-193 |
7.12e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 37 GPNGAGKSTTIGIISSLVNKTSGtvKVFGHNIDTHlEQAKQHLGLVPQEFNFNPFETVEQIVMQQAGYYGVSRTLakERA 116
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSG--NIYYKNCNIN-NIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETL--YAA 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 117 EKYLTQLDLWEkrkERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRRSMWEFL-KQINSQGItIILTTH 193
Cdd:PRK13541 108 IHYFKLHDLLD---EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIvMKANSGGI-VLLSSH 181
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-173 |
9.39e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 4 LEIDQLRKTYaGGFEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVfGhniDT----HLEQAKQHL 79
Cdd:PRK11819 325 IEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G---ETvklaYVDQSRDAL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 80 glvpqefnfNPFETVEQIVMQQAGYYGVSRTLAKERAekYLTQL-----DlwekRKERARNLSGGMKRRLMIARALMHEP 154
Cdd:PRK11819 400 ---------DPNKTVWEEISGGLDIIKVGNREIPSRA--YVGRFnfkggD----QQKKVGVLSGGERNRLHLAKTLKQGG 464
|
170
....*....|....*....
gi 2019142000 155 QLLILDEPTAGVDIELRRS 173
Cdd:PRK11819 465 NVLLLDEPTNDLDVETLRA 483
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-214 |
1.29e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKstTIGIIS----SLVNKTSGTVKVFGHNIDTH-LEQA-----------KQHLGLvp 83
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGR--TELAMSvfgrSYGRNISGTVFKDGKEVDVStVSDAidaglayvtedRKGYGL-- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 84 qefnfNPFETV-EQIVMqqAGYYGVSRT----LAKER--AEKYLTQL-----DLWEKrkerARNLSGGMKRRLMIARALM 151
Cdd:NF040905 352 -----NLIDDIkRNITL--ANLGKVSRRgvidENEEIkvAEEYRKKMniktpSVFQK----VGNLSGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 152 HEPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLEEAEMLCRHIGIINRGELI 214
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-199 |
1.93e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTtigIISSLVNKTSgtvkvfghnidtHLEQA----KQHLGLVPQ-EFNFNPfeTV 94
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTS---LISAMLGELS------------HAETSsvviRGSVAYVPQvSWIFNA--TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 95 EQIVMQQAGYYGvSRTLAKERAEKYLTQLDLWEKRK-----ERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIE 169
Cdd:PLN03232 696 RENILFGSDFES-ERYWRAIDVTALQHDLDLLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170 180 190
....*....|....*....|....*....|...
gi 2019142000 170 LRRSMWEFLKQINSQGITIILTT---HYLEEAE 199
Cdd:PLN03232 775 VAHQVFDSCMKDELKGKTRVLVTnqlHFLPLMD 807
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-222 |
1.25e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.57 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTI-GIISSLVNKTSGTVKVFGHnidthleqakqhLGLVPQ-EFNFNPfeTVEQI 97
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLIsAMLGELPPRSDASVVIRGT------------VAYVPQvSWIFNA--TVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 98 VM-----QQAGYYGVSRTLAKERAEKYLTQLDLWEKrKERARNLSGGMKRRLMIARALMHEPQLLILDEPTAGVDIELRR 172
Cdd:PLN03130 699 ILfgspfDPERYERAIDVTALQHDLDLLPGGDLTEI-GERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGR 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2019142000 173 SMWEFLKQINSQGITIILTT---HYLEEAEmlcrHIGIINRGELIENTTMKGL 222
Cdd:PLN03130 778 QVFDKCIKDELRGKTRVLVTnqlHFLSQVD----RIILVHEGMIKEEGTYEEL 826
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-167 |
1.72e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 17 FEALKGVSLTVNKGDFYALLGPNGAGKSTTIGIISS-----LVNKTsGTVKVFGHNIDthlEQAKQHLGLV----PQEFN 87
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgfHIGVE-GVITYDGITPE---EIKKHYRGDVvynaETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 88 FnPFETVEQ-----IVMQ--QAGYYGVSR-TLAKERAEKYLTQLDLWEKR-----KERARNLSGGMKRRLMIARALMHEP 154
Cdd:TIGR00956 150 F-PHLTVGEtldfaARCKtpQNRPDGVSReEYAKHIADVYMATYGLSHTRntkvgNDFVRGVSGGERKRVSIAEASLGGA 228
|
170
....*....|...
gi 2019142000 155 QLLILDEPTAGVD 167
Cdd:TIGR00956 229 KIQCWDNATRGLD 241
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-193 |
2.57e-04 |
|
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: 41.44 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 37 GPNGAGKSTTIGIIS-SLVNKTSGTVKVFGHniDTHLEQAKQHLGLVPQEFNFNPFETveqivmqqagyYGVSRTLAKER 115
Cdd:cd03240 29 GQNGAGKTTIIEALKyALTGELPPNSKGGAH--DPKLIREGEVRAQVKLAFENANGKK-----------YTITRSLAILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 116 AEKYLTQLDL-WEKRKERARnLSGGMKR------RLMIARALMHEPQLLILDEPTAGVDIE-LRRSMWEFLKQINSQGI- 186
Cdd:cd03240 96 NVIFCHQGESnWPLLDMRGR-CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLAEIIEERKSQKNf 174
|
....*..
gi 2019142000 187 TIILTTH 193
Cdd:cd03240 175 QLIVITH 181
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
136-211 |
2.84e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.77 E-value: 2.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 136 LSGGMKRRLMIARALMHEPQ--LLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYLeeaEMLCRHIGIINRG 211
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL---DVLSSADWIIDFG 162
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-193 |
3.51e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 20 LKGVSLTVNKGDFYALLGPNGAGKSTTIGIISSLVNKTSGTVKVFGHNIDTHLEQAKQHLGLVPQEF------NFNPFET 93
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYvidgdrEYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 94 VEQIVMQQ------AGYYGVSRTLA----KERAEKYLTQLDLWEKRKER-ARNLSGGMKRRLMIARALMHEPQLLILDEP 162
Cdd:PRK10636 97 QLHDANERndghaiATIHGKLDAIDawtiRSRAASLLHGLGFSNEQLERpVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
170 180 190
....*....|....*....|....*....|.
gi 2019142000 163 TAGVDIELRRSMWEFLKqiNSQGiTIILTTH 193
Cdd:PRK10636 177 TNHLDLDAVIWLEKWLK--SYQG-TLILISH 204
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
106-196 |
1.75e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 39.64 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019142000 106 GVSRTLAKERAEKYLTQLDLWEKRKERARNL-----SGGMKRRLMIARALM---HEPQLLILDEPTAGVDIELRRSMWE- 176
Cdd:COG1106 168 GIEDIEVEEEEIEDLVERKLIFKHKGGNVPLplseeSDGTKRLLALAGALLdalAKGGVLLIDEIEASLHPSLLRKLLKl 247
|
90 100
....*....|....*....|
gi 2019142000 177 FLKQINSQGITIILTTHYLE 196
Cdd:COG1106 248 FLDLANKNNAQLIFTTHSTE 267
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
126-180 |
3.23e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.06 E-value: 3.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019142000 126 WEKRKERARNLSGGMKRRLM---IARALM----------HEPQLLILDEPTAGVDIELRRSMWEFLKQ 180
Cdd:pfam13558 23 EVETYRRSGGLSGGEKQLLAylpLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-193 |
6.66e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 6.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019142000 136 LSGGMKRRLMIARALMH---EPQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTH 193
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-195 |
7.84e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 7.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2019142000 133 ARNLSGGMKRRLMIARALMHE---PQLLILDEPTAGVDIELRRSMWEFLKQINSQGITIILTTHYL 195
Cdd:TIGR00630 827 ATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| |
